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Year of Paper
int64
1.99k
2.02k
Link to PubMed Entry
stringlengths
40
154
Journals
stringclasses
173 values
Journal DOI
stringlengths
13
82
Citation
stringlengths
132
505
Type of Nucleic Acid
stringclasses
13 values
Name of Aptamer
stringlengths
1
102
Target
stringlengths
4
128
Aptamer Sequence
stringlengths
19
316
Sequence Length
int64
15
312
GC Content
float64
0.3
0.83
Affinity
stringlengths
3
186
Kd (nM)
float64
0
208M
Pool Type
stringlengths
3
360
Pool Random Region
float64
0
120
Binding Buffer/Conditions
stringlengths
3
291
Divalent Salt
stringclasses
4 values
Type of the buffer
stringclasses
4 values
pH
float64
3.6
9.6
Molecular weight of target
stringclasses
84 values
Application as quoted in the referenced paper
stringlengths
3
1.13k
Post-selex modifications to the aptamer
stringclasses
134 values
Additional Information
stringlengths
3
1.22k
Serial Number
int64
10M
10M
Parent sequence serial number
float64
10M
10M
Corresponding Author Name, email address
stringlengths
3
118
Aptagen Cross Referencing(Check Aptamer Chemistry, Affinity, Length, GC content, sequence)
stringclasses
75 values
1,990
https://pubmed.ncbi.nlm.nih.gov/1697402/
Nature
https://doi.org/10.1038/346818a0
Ellington, A. D., & Szostak, J. W. (1990). In vitro selection of RNA molecules that bind specific ligands. Nature, 346(6287), 818–822. https://doi.org/10.1038/346818a0
ssRNA
CB-42
Cibacron Blue 3GA
5'GGGAGAAUUCCCGCGGCAGAAGCCCACCUGGCUUUGAACUCUAUGUUAUUGGGUGGGGGAAACUUAAGAAAACUACCACCCUUCAACAUUACCGCCCUUCAGCCUGCCAGCGCCCUGCAGCCCGGGAAGCUU3'
132
0.560606
Kd~600µM
600,000
5'-GGGAGAATTCCCGCGG-N98-CTGCAGCCCGGGAAGCTT-3'
98
0.6 ml of 0.5 M LiCI, 20 mM Tris-HCI, pH 7.6, 1 mM MgCl2
MgCl
Tris Buffers
7.6
Not reported
Detection: " Isolate RNAs that bind to several dyes that appear to mimic metabolic cofactors. For example, Cibacron Blue binds tightly to the NADbinding site of many dehydrogenases and Cibacron Blue columns have been used for purification of these proteins by affinity chromatography. The experiments described here used Cibacron Blue 3GA (CB), Reactive Red 120 (R), Reactive Yellow 86 (Y), Reactive Brown 10 (BR), Reactive Green 19 (GR) and Reactive Blue 4 (B4) attached to cross-linked, beaded agarose. We chose these molecules because they have many possible hydrogen-bond donor and acceptor groups as well as planar surfaces for stacking interactions."
Not applicable
The aptamer was reported in DNA (include thymine nucleotide, instead of Uridine). The T was changed to U to match the discription of paper content. DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,000
null
Szostak JW
null
1,990
https://pubmed.ncbi.nlm.nih.gov/1697402/
Nature
https://doi.org/10.1038/346818a0
Ellington, A. D., & Szostak, J. W. (1990). In vitro selection of RNA molecules that bind specific ligands. Nature, 346(6287), 818–822. https://doi.org/10.1038/346818a0
ssRNA
B4-25
Reactive Blue 4
5'GGGAGAAUUCCCGCGGCGUUGGCCCAGGAUAAUAGGACGAAAUCCGAAAAAUCCGUACCCAACAUAGAACCCCCCCAGCGCUCACACGGACGCCCCAUUACGGCUAACCGAACGCCUGCAGCCCGGGAAGCUU3'
133
0.593985
Kd<100µM
100,000
5'-GGGAGAATTCCCGCGG-N97-CTGCAGCCCGGAAGCTT-3'
97
0.6 ml of 0.5 M LiCI, 20 mM Tris-HCI, pH 7.6, 1 mM MgCl3
MgCl
Tris Buffers
7.6
Not reported
Detection: " Isolate RNAs that bind to several dyes that appear to mimic metabolic cofactors. For example, Cibacron Blue binds tightly to the NADbinding site of many dehydrogenases and Cibacron Blue columns have been used for purification of these proteins by affinity chromatography. The experiments described here used Cibacron Blue 3GA (CB), Reactive Red 120 (R), Reactive Yellow 86 (Y), Reactive Brown 10 (BR), Reactive Green 19 (GR) and Reactive Blue 4 (B4) attached to cross-linked, beaded agarose. We chose these molecules because they have many possible hydrogen-bond donor and acceptor groups as well as planar surfaces for stacking interactions."
Not applicable
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,001
null
Szostak JW
null
1,990
https://pubmed.ncbi.nlm.nih.gov/2200121/
Science
https://doi.org/10.1126/science.2200121
Tuerk, C., & Gold, L. (1990). Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science (New York, N.Y.), 249(4968), 505–510. https://doi.org/10.1126/science.2200121
ssRNA
wild type
T4 DNA polymerase (gp43)
5'GAAUUGUGGUGUUGGCUCCCUAUAGUGAGUCGUAUUAAUAUUCCUUAGUUUUAUAGCCCAAUAACUCAGGCUCUUGAUUGGUUUUCAAUAGAGAUAUAAAAUUCUUUUCAUAG3'
113
0.336283
Kd: 4.8 nM
4.8
5'-GAATTGTGGTGTTGGCTCCCTATAGTGAGTCGTATTA-ATATTCCTTAGTTTTATAGCCC-N9-AGGCTCTTGATTG-GTTTTCAATAGAGATATAAAATTCTTTTCATAG-3'
9
Not reported
null
Not Reported
null
Not reported
Detection: " We have previously shown that the RNA target of T4 DNA polymerase selectively inhibits its replicative function.Thus,the products of SELEX can affect the activity of the protein to which they have been fit. We expect that, at the very least,nucleic acid ligands that inhibit replicative proteins of epidemiologically important infections can be likewise evolved."
Not applicable
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,002
null
Gold L
null
1,990
https://pubmed.ncbi.nlm.nih.gov/2200121/
Science
https://doi.org/10.1126/science.2200121
Tuerk, C., & Gold, L. (1990). Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science (New York, N.Y.), 249(4968), 505–510. https://doi.org/10.1126/science.2200121
ssRNA
major variant
T4 DNA polymerase (gp43)
5'GAAUUGUGGUGUUGGCUCCCUAUAGUGAGUCGUAUUAAUAUUCCUUAGUUUUAUAGCCCAGCAACCUAGGCUCUUGAUUGGUUUUCAAUAGAGAUAUAAAAUUCUUUUCAUAG3'
113
0.353982
Kd: 4.8 nM
4.8
5'-GAATTGTGGTGTTGGCTCCCTATAGTGAGTCGTATTA-ATATTCCTTAGTTTTATAGCCC-N9-AGGCTCTTGATTG-GTTTTCAATAGAGATATAAAATTCTTTTCATAG-3'
9
Not reported
null
Not Reported
null
Not reported
Detection: " We have previously shown that the RNA target of T4 DNA polymerase selectively inhibits its replicative function.Thus,the products of SELEX can affect the activity of the protein to which they have been fit. We expect that, at the very least,nucleic acid ligands that inhibit replicative proteins of epidemiologically important infections can be likewise evolved."
Not applicable
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,003
null
Gold L
null
1,992
https://pubmed.ncbi.nlm.nih.gov/1741036/
Nature
https://doi.org/10.1038/355564a0
Bock, L. C., Griffin, L. C., Latham, J. A., Vermaas, E. H., & Toole, J. J. (1992). Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature, 355(6360), 564–566. https://doi.org/10.1038/355564a0
ssDNA
15 mer (colloquially known as Bock DNA Aptamer)
Thrombin (Sigma), Human
5'GGTTGGTGTGGTTGG3'
15
0.6
Kd: 25-200 nM
112.5
5'-CGTACGGTCGACGCTAGC-60N-CACGTGGAGCTCGGATCC-3'
60
19 mM Tris-acetate, pH 7.4, 140 mM NaCI, 5 mM KCI, 1 mM CaCI2, 1 mM MgCI2
MgCl
Tris Buffers
7.4
Not reported
Diagnostic and therapeutic: "We are at present investigating the aptamer-binding site on thrombin and analysing the binding sequences of individual aptamers in an effort to understand the base relationships that mediate binding and inhibition, our long-term interest being to develop diagnostics and therapeutic agents."
Not applicable
Presumed minimized variant was found
10,000,004
null
Toole JJ
null
1,992
https://pubmed.ncbi.nlm.nih.gov/1379730/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.89.15.6988
Tuerk, C., MacDougal, S., & Gold, L. (1992). RNA pseudoknots that inhibit human immunodeficiency virus type 1 reverse transcriptase. Proceedings of the National Academy of Sciences of the United States of America, 89(15), 6988–6992. https://doi.org/10.1073/pnas.89.15.6988
ssRNA
ligand 1.1
Human imunnodeficiency virus type 1 reverse transcriptase (HIV-1-RT)
5'GGGAGCAUCAGACUUUUAAUCUGACAAUCAAGAAUUCCGUUUUCAGUCGGGAAAAACUGAACAAUCUAUGAAAGAAUUUUAUAUCUCUAUUGAAAC3'
96
0.333333
Kd: 5 nM
5
5'-GGGAGCAUCAGACUUUUAAUCUGACAAUCAAG-N32-AUCUAUGAAAGAAUUUUAUAUCUCUAUUGAAAC-3'
32
200 mM KOAc/50 mM Tris-HCI, pH 7.7/10 mM dithiothreitol
null
Tris Buffers
7.7
Not reported
Therapeutic: " Demonstrated that at least one of the ligands inhibits cDNA synthesis by HIV reverse transcriptase but falls to inhibit other reverse transcriptases. These exeriments highlight the power of SELEX to yield hlghiy spedfc ligands that reduce the activity of target proteins. Such ligands may provide therapeutic reagents for viral and' other dies."
Not applicable
null
10,000,006
null
Gold L
null
1,992
https://pubmed.ncbi.nlm.nih.gov/1379730/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.89.15.6988
Tuerk, C., MacDougal, S., & Gold, L. (1992). RNA pseudoknots that inhibit human immunodeficiency virus type 1 reverse transcriptase. Proceedings of the National Academy of Sciences of the United States of America, 89(15), 6988–6992. https://doi.org/10.1073/pnas.89.15.6988
ssRNA
ligand 1.3a
Human imunnodeficiency virus type 1 reverse transcriptase (HIV-1-RT)
5'GGGAGCAUCAGACUUUUAAUCUGACAAUCAAGAAUAUCUUCCGAAGCCGAACGGGAAAACCGGCAUCUAUGAAAGAAUUUUAUCUCUAUUGAAAC3'
95
0.389474
Kd: 5 nM
5
5'-GGGAGCAUCAGACUUUUAAUCUGACAAUCAA-N32-AUCUAUGAAAGAAUUUUAUCUCUAUUGAAAC-3'
32
200 mM KOAc/50 mM Tris-HCI, pH 7.7/10 mM dithiothreitol
null
Tris Buffers
7.7
Not reported
Therapeutic: " Demonstrated that at least one of the ligands inhibits cDNA synthesis by HIV reverse transcriptase but falls to inhibit other reverse transcriptases. These exeriments highlight the power of SELEX to yield hlghiy spedfc ligands that reduce the activity of target proteins. Such ligands may provide therapeutic reagents for viral and' other dies."
Not applicable
null
10,000,007
null
Gold L
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
5A
Basic fibroblast growth factor (bFGF)
5'GGGAGCUCAGAAUAAACGCUCAAAUCUCCUCCCGUCGAAGCUAACCUGGCCACUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.584416
Kd: 23 ± 3 nM
23
5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18000 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,008
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
7A
Basic fibroblast growth factor (bFGF)
5'GGGAGCUCAGAAUAAACGCUCAAUCGGCGAGCUAACCAAGACACUCGCUGCACUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.584416
Kd: 5.0 ± 0.5 nM
5
5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18001 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,009
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
13A
Basic fibroblast growth factor (bFGF)
5'GGGAGCUCAGAAUAAACGCUCAAACCCGCGGCCUCCGAAGCUAACCAGGACACUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.61039
Kd: 3.2 ± 0.5 nM
3.2
5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18002 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,010
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
14A
Basic fibroblast growth factor (bFGF)
5'GGGAGCUCAGAAUAAACGCUCAAUGGGUGCUAACCAGGACACACCCACGCUGUUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.584416
Kd: 3.0 ± 0.5 nM
3
5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18003 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,011
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
21A
Basic fibroblast growth factor (bFGF)
5'GGGAGCUCAGAAUAAACGCUCAAUGGGUGCUUAACCAGGCCACACCCUGCUGUUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.584416
Kd: 8.1 ± 0.8 nM
8.1
5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18004 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,012
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
12A
Basic fibroblast growth factor (bFGF)
5'GGGAGAUGCCUGUCGAGCAUGCUGGGGGCAACGCUACAGACAAGUGCACCCAACGUAGCUAAACAGCUUUGUCGACGGG3'
79
0.582278
Kd: exhibits biphasic binding, 0.51 ± 0.13 nM, 60 ± 52 nM
0.51
5'-GGGAGAUGCCUGUCGAGCAUGCUG-N30-GUAGCUAAACAGCUUUGUCGACGGG-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18005 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,013
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
26At
Basic fibroblast growth factor (bFGF)
5'GGUGAAGGCAACGUAUAGGCAAGCACACUUCACC3'
34
0.529412
Kd: ~0.19 ± 0.02 nM
0.19
5'-GGGAGAUGCCUGUCGAGCAUGCUG-N30-GUAGCUAAACAGCUUUGUCGACGGG-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18006 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Truncated
null
10,000,014
null
Janjić N
5'rGprGprUprGprAprAprGprGprCprAprAprCprGprUprAprUprAprGprGprCprAprAprGprCprAprCprAprCprUprUprCprAprCprCp3' https://www.aptagen.com/aptamer-details/?id=136
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
26A
Basic fibroblast growth factor (bFGF)
5'GGGAGAUGCCUGUCGAGCAUGCUGCGUCAGAAGGCAACGUAUAGGCAAGCACACGUAGCUAAACAGCUUUGUCGACGGG3'
79
0.556962
Kd: exhibits biphasic binding, 0.19 ± 0.02 nM, 49 ± 26 nM
0.19
5'-GGGAGAUGCCUGUCGAGCAUGCUG-N30-GUAGCUAAACAGCUUUGUCGACGGG-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18006 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,015
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7504300/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.90.23.11227
Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
ssRNA
28B
Basic fibroblast growth factor (bFGF)
5'GGGAGAUGCCUGUCGAGCAUGCUGAGGGUAACGUAUAGUCAAGACACCUCAAGUGUAGCUAAACAGCUUUGUCGACGGG3'
79
0.518987
Kd: exhibits biphasic binding, 0.32 ± 0.07 nM, 140 ± 80 nM
0.32
5'-GGGAGAUGCCUGUCGAGCAUGCUG-N30-GUAGCUAAACAGCUUUGUCGACGGG-3'
30
PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
null
PBS/phosphate buffers
7.4
18008 Da
Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Not applicable
null
10,000,017
null
Janjić N
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
9
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGGCGCAGCCUCAAUGAGGCUGGUGGUGCAAG3'
38
0.631579
Kd: 1.9 ± 0.21*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units. Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,018
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
18
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGGCGCAGCCUCAAUGAGGCUGGAGGUACAAG3'
38
0.605263
Kd: 2.0*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,019
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
19
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGGCACAGCCUCAAUGAGGCUGGUGGUACAAG3'
38
0.578947
Kd: 1.2 ± 0.08*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,020
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
6
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGACACAGCCUCAAUGAGGCUGCAGAUACAAG3'
38
0.526316
Kd: 3.1 ± 0.26*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,021
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
116
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGACACAGCUGCUGCAGAUACAAG3'
30
0.533333
Kd: 2.1*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,022
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
126
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGACACAGCCUCAAUGAGGCUGCAGAAACAAG3'
38
0.526316
Kd: 2.7 ± 0.29*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,023
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
15
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'GCUCUUGGCCGCAGCCUCAAUGAGGCUGAUGAUACAAG3'
38
0.552632
Kd: 1.7*
null
5'-GCUCUUG-N4-CAGCCUCAAUGAGGCUG-N6-CAAG-3'
10
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units Sequences at the defined 5' and 3' ends of the 76.6 DNA pool are, respectively, 5'-GGTAATACGATCACTATAGGG4ACTC_x0002_GATGAAGCGAGCT-3' and 5'-TACTGACT7CGGCATCCCTGC- -(3')
10,000,024
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
1
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUACUCCGUACGCAAGUACGGUCGAGAAACAG3'
37
0.486486
Kd: 4.3*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,025
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
2
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUUUAGGACUCGUACGCAAGUACUGAGAUACUACAG3'
41
0.414634
Kd: 2.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,026
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
14
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACUCGUACGCAAGUACUGGAGAAACAG3'
34
0.470588
Kd: 5.4 ± 0.05*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,028
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
23
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGGACUCGUACGCAAGUACUUGAGAUACACG3'
37
0.459459
Kd: 3.1*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,029
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
50
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGUCUCGUACGCAAGUACUGAGAAACGACAG3'
36
0.472222
Kd: 0.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,030
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
63
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACUCCGUAUGCAAGUACGUUGAGCAACAG3'
36
0.472222
Kd: 7.7, 9.5, 9.6*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,031
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
74
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUAGACUCGUACGCAAGUACUCGAGAUAUACAG3'
38
0.421053
Kd: 4.2*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,032
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
83
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGGACUCGUACGCAAGUACUGAGAAACACCG3'
37
0.486486
Kd: 3.6*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,034
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
88
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGACUCUUUGUACGCAAGUACAGAGUGAUACAG3'
39
0.410256
Kd: 1.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,035
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
15
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACGCGUACGCAAGUACUGUGAUACAG3'
33
0.484848
Kd: 4.1*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,036
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
17
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACGCGCUGGUACGCAAGUACGGCUGUGAUACAG3'
40
0.55
Kd: 3.9*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,037
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
20
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUACUCUCGUACGCAAGUACGAUCGAGACACAG3'
38
0.473684
Kd: 2.6*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,039
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
51
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGAGCUCGUACGCAAGUACUCGAGGUACAG3'
36
0.5
Kd: 1.0*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,040
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
58
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUACUCCUGUACGCAAGUACGGUUGAGACACAG3'
38
0.473684
Kd: 3.2*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,042
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
72
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUAUGAGAGUAGCAAGUACCGGACUCUACAG3'
36
0.444444
Kd: 0.3*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,043
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
73
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGCUCGUGUACGCAAGUACGCUUGAGGAACAG3'
38
0.5
Kd: 1.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,044
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
86
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGUAGAGGUACGCAAGUACGCGCUCCACAG3'
36
0.527778
Kd: 6.4, 6.5, 7.4, 9.7*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,045
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
92
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGUGUAGAGGUACGCAAGUAAGCGGCUCCACAG3'
37
0.513514
Kd: 7.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,047
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
22
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGUACGUUGUACGCAAGUACACGGGUUACAG3'
36
0.472222
Kd: 0.7*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,048
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
59
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGCUUCGUACGCAAGUAUGAUGAUACAG3'
33
0.424242
Kd: 0.2*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,049
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
61
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACAUCGUACGCAAGUACCUUGAAACAG3'
34
0.441176
Kd: 4.6*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,050
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
76
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACUUCGGUACGCAAUUACCGACUGACACAG3'
37
0.486486
Kd: 2.4*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,051
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
79
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCUGGACAUUUGUACGCAAGUACGUUUGAUACAG3'
36
0.388889
Kd: 3.9*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,052
null
Ellington AD
null
1,993
https://pubmed.ncbi.nlm.nih.gov/7505429/
Nucleic Acids Res
https://doi.org/10.1093/nar/21.23.5509
Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
ssRNA
18
Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
5'AUUCGGUAGCAUCUUGUACGCAAGUACGAGAGAGCAACAG3'
40
0.475
Kd: 0.5*
null
5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
15
50 mM KCl, 50 mM Tris-Cl, pH 8.0
null
Tris Buffers
8
Not reported
Therapeutic: " A population of improved Rev-binding aptamers can be used to inhibit viral replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Not applicable
*Activity values are described as "representing relative Kd's" with no units 6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length. Sequences at the defined 5' and 3' ends of the 79.9 pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
10,000,053
null
Ellington AD
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7518917/
Nucleic Acids Res
https://doi.org/10.1093/nar/22.13.2619
Kubik, M. F., Stephens, A. W., Schneider, D., Marlar, R. A., & Tasset, D. (1994). High-affinity RNA ligands to human alpha-thrombin. Nucleic acids research, 22(13), 2619–2626. https://doi.org/10.1093/nar/22.13.2619
ssRNA
16
α-Thrombin, Human
5'GGGAGAUGCCUGUCGAGCAUGCUGCAUCCGGAUCGAAGUUAGUAGGCGGAGUGGUAGCUAAACAGCUUUGUCGACGGG3'
78
0.564103
Kd: 37 ± 3.5 nM
37
5'-CCCGTCGACAAAGCTGTTTAGCTAC-N30-CAGCATGCTCGACAGGCATCT-3'
30
50 mM Tris-HCl, pH 7.7, 100 mM NaCl, 1 mM DTT, and 1 mM MgCl2
MgCl
Tris Buffers
7.7
Not reported
Therapeutic: " These sequences can be used as a molecular anchor to select for a larger RNA with more extensive protein interactions, including the active site. One can also envision development of a heparin mimic that could be more specific for the ATIE-mediated inhibition of thrombin. It is clear from this work and related work that oligonucleotides have great potential as antithrombotic agents."
Minimum sequence requirements for high affinity binding derived from clone 16 (truncated)
5' and 3' fixed regions differ than pool non-random regions. DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,054
null
Tasset D
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7518917/
Nucleic Acids Res
https://doi.org/10.1093/nar/22.13.2619
Kubik, M. F., Stephens, A. W., Schneider, D., Marlar, R. A., & Tasset, D. (1994). High-affinity RNA ligands to human alpha-thrombin. Nucleic acids research, 22(13), 2619–2626. https://doi.org/10.1093/nar/22.13.2619
ssRNA
27
α-Thrombin, Human
5'GGGAGAUGCCUGUCGAGCAUGCUGGUGCGGCUUUGGGCGCCGUGCUUGACGUAGCUAAACAGCUUUGUCGACGGG3'
75
0.613333
Kd: 114 ± 2.0 nM
114
5'-CCCGTCGACAAAGCTGTTTAGCTAC-N30-CAGCATGCTCGACAGGCATCT-3'
30
50 mM Tris-HCl, pH 7.7, 100 mM NaCl, 1 mM DTT, and 1 mM MgCl2
MgCl
Tris Buffers
7.7
Not reported
Therapeutic: " These sequences can be used as a molecular anchor to select for a larger RNA with more extensive protein interactions, including the active site. One can also envision development of a heparin mimic that could be more specific for the ATIE-mediated inhibition of thrombin. It is clear from this work and related work that oligonucleotides have great potential as antithrombotic agents."
Minimum sequence requirements for high affinity binding derived from clone 16 (truncated)
5' and 3' fixed regions differ than pool non-random regions. DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,055
null
Tasset D
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7518917/
Nucleic Acids Res
https://doi.org/10.1093/nar/22.13.2619
Kubik, M. F., Stephens, A. W., Schneider, D., Marlar, R. A., & Tasset, D. (1994). High-affinity RNA ligands to human alpha-thrombin. Nucleic acids research, 22(13), 2619–2626. https://doi.org/10.1093/nar/22.13.2619
ssRNA
16.24
α-Thrombin, Human
5'UCCGGAUCGAAGUUAGUAGGCGGA3'
24
0.541667
Kd: 9.3 ± 1.0 nM
9.3
5'-CCCGTCGACAAAGCTGTTTAGCTAC-N30-CAGCATGCTCGACAGGCATCT-3'
30
50 mM Tris-HCl, pH 7.7, 100 mM NaCl, 1 mM DTT, and 1 mM MgCl2
MgCl
Tris Buffers
7.7
Not reported
Therapeutic: " These sequences can be used as a molecular anchor to select for a larger RNA with more extensive protein interactions, including the active site. One can also envision development of a heparin mimic that could be more specific for the ATIE-mediated inhibition of thrombin. It is clear from this work and related work that oligonucleotides have great potential as antithrombotic agents."
Minimum sequence requirements for high affinity binding derived from clone 16 (truncated)
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,056
null
Tasset D
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7518917/
Nucleic Acids Res
https://doi.org/10.1093/nar/22.13.2619
Kubik, M. F., Stephens, A. W., Schneider, D., Marlar, R. A., & Tasset, D. (1994). High-affinity RNA ligands to human alpha-thrombin. Nucleic acids research, 22(13), 2619–2626. https://doi.org/10.1093/nar/22.13.2619
ssRNA
27.33
α-Thrombin, Human
5'GAGCAUGCUGGUGCGGCUUUGGGCGCCGUGCUU3'
33
0.666667
Kd: 155 ± 9.0 nM
155
5'-CCCGTCGACAAAGCTGTTTAGCTAC-N30-CAGCATGCTCGACAGGCATCT-3'
30
50 mM Tris-HCl, pH 7.7, 100 mM NaCl, 1 mM DTT, and 1 mM MgCl2
MgCl
Tris Buffers
7.7
Not reported
Therapeutic: " These sequences can be used as a molecular anchor to select for a larger RNA with more extensive protein interactions, including the active site. One can also envision development of a heparin mimic that could be more specific for the ATIE-mediated inhibition of thrombin. It is clear from this work and related work that oligonucleotides have great potential as antithrombotic agents."
Minimum sequence requirements for high affinity binding derived from clone 27 (truncated)
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,057
null
Tasset D
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
DOPE. 40
Cyanocobalamin (vitamin B12)
5'GUCGGCCUAUCCGACAGGCACCGCGAGAGGACCAUUAUAGUGCGCAUAACCACUUCAGUGCGAGCAAAAAUUUGG3'
75
0.533333
Kd: 88 ± 19 nM
88
Original random pool: 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.) mutagenized pool( 30% dopped pool): 5'-GGAACCTCTAGGTCATTA-GGAACACTATCCGACTGGCACCGCCAGCGGACAAATCCGGTGCGCATAACCACCTCAGTGCGAGCAACGATGGCC-ACGTCAGAAGGATCCAAG-3' (inside the dash are sequence of original aptamer B12.9)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer
Using a doped pool for the region inside the "- -", 32P-labeled RNA was used to follow all selections. DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection. The total length of the pool RNA the paper mentioned "was 111 bases (including two new primer binding sites), with 75 mutagenized bases, and a sequence complexity of approximately 5 X 1014 molecules." However, it did not mentioed the sequence of the new primers
10,000,061
null
Szostak JW
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
DOPE. 40
Cobinamide dicyanide
5'GUCGGCCUAUCCGACAGGCACCGCGAGAGGACCAUUAUAGUGCGCAUAACCACUUCAGUGCGAGCAAAAAUUUGG3'
75
0.533333
Kd: 20 ± 9 uM
20,000
Original random pool: 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.) mutagenized pool( 30% dopped pool): 5'-GGAACCTCTAGGTCATTA-GGAACACTATCCGACTGGCACCGCCAGCGGACAAATCCGGTGCGCATAACCACCTCAGTGCGAGCAACGATGGCC-ACGTCAGAAGGATCCAAG-3' (inside the dash are sequence of original aptamer B12.9)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer
Using a doped pool for the region inside the "- -", 32P-labeled RNA was used to follow all selections. DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,061
null
Szostak JW
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
B12.9
Cobinamide dicyanide
5'AACACUAUCCGACUGGCACCGCCAGCGGACAAAUCCGGUGCGCAUAACCACCUCAGUGCGAGCAACGAUGGCCUUUCUACCCAAAGAUUUUCCUUGGUCAUUAGGAUCC3'
109
0.53211
Kd: 8.8 ± 0.5 uM
8,800
Original random pool 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,062
null
Szostak JW
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
B12.9
Cyanocobalamin (vitamin B12)
5'AACACUAUCCGACUGGCACCGCCAGCGGACAAAUCCGGUGCGCAUAACCACCUCAGUGCGAGCAACGAUGGCCUUUCUACCCAAAGAUUUUCCUUGGUCAUUAGGAUCC3'
109
0.53211
Kd: 320 ± 90 nM
320
Original random pool 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,062
null
Szostak JW
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
35-mer aptamer
Cyanocobalamin (vitamin B12)
5'GGAACCGGUGCGCAUAACCACCUCAGUGCGAGCAA3'
35
0.6
Kd: 88 ± 19 nM
87
Original random pool 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer Based on the sequence data from the mutagenized pool selection, a smaller aptamer (35 nucleotides long) was made by run-off transcription of a synthetic DNA oligonucleotide (Truncation/minimal sequence)
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,063
null
Szostak JW
5'rCprCprGprGprUprGprCprGprCprAprUprAprAprCprCprAprCprCprUprCprAprGprUprGprCprGprAprGprCprAprAprGprGprAprAp3' https://www.aptagen.com/aptamer-details/?id=105
1,994
https://pubmed.ncbi.nlm.nih.gov/7508262/
Biochemistry
https://doi.org/10.1021/bi00170a016
Lorsch, J. R., & Szostak, J. W. (1994). In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry, 33(4), 973–982. https://doi.org/10.1021/bi00170a016
ssRNA
35-mer aptamer
Cobinamide dicyanide
5'GGAACCGGUGCGCAUAACCACCUCAGUGCGAGCAA3'
35
0.6
Kd: 19.7 ± 8.7 uM
19,700
Original random pool 5'-AACACTATCCGACTG-GCACC-N72-CCTTGGTCATTAGGATCC-3' (source --> Bartel, D. P., & Szostak, J. W. (1993) Science 261,1411-1418.)
72
1 M LiCl, 5 mM MgCl2, and 25 mM HEPES (pH 7.4)
MgCl
Other Buffers
7.4
Not reported
Detection: " The aptamers we have selected may also serve as a starting point for the in vitro evolution of cobalamindependent ribozymes. A number of other biologically important reactions are carried out by cobalamin-dependent enzymes, including methyl group transfers, carbon skeletal rearrangements, and diol dehydrations"
DMS modification for probing the tertiary interaction in aptamer Based on the sequence data from the mutagenized pool selection, a smaller aptamer (35 nucleotides long) was made by run-off transcription of a synthetic DNA oligonucleotide (Truncation/minimal sequence)
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,063
null
Szostak JW
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7519769/
Nucleic Acids Res
https://doi.org/10.1093/nar/22.14.2817
Latham, J. A., Johnson, R., & Toole, J. J. (1994). The application of a modified nucleotide in aptamer selection: novel thrombin aptamers containing 5-(1-pentynyl)-2'-deoxyuridine. Nucleic acids research, 22(14), 2817–2822. https://doi.org/10.1093/nar/22.14.2817
5-uracil-modified-DNA
Clone 3
Thrombin, Human
5'TAGAATACTCAAGCTTCGACGCAGAXACAGGCCAXGXGCAGTTTGGATCCCCGGGTAC3'
55
0.545455
Kd: 800 nM
800
5'-TAGAATACTCAAGCTTCGACG-N20-AGTTTGGATCCCCGGGTAC-3'
20
20 mM Tris—acetate pH 7.4, 140 mM NaCl, 5 mM KC1, 1 mM MgCl2, 1 mM CaCl2
MgCl/CaCl
Tris Buffers
7.4
Not reported
Therapeutic: " We demonstrate that the incorporation of this hydrophobic group into the random oligonucleotide library signficantly alters the outcome of the selection process against human thrombin. The isolated aptamers display enrichment for molecules containing extensive substitution with this modified nucleotide. Binding and anticoagulant activity of the isolated aptamers are discussed."
Not applicable
X denotes pentynyl dU as determined via sequencing. 5-(1-pentynyl)-2'-deoxyuridine used instead of thymidine ("X" in sequences) it is also called 5-pentynyl-dU
10,000,064
null
Latham, J. A.
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7510417/
Science
https://doi.org/10.1126/science.7510417
Jenison, R. D., Gill, S. C., Pardi, A., & Polisky, B. (1994). High-resolution molecular discrimination by RNA. Science (New York, N.Y.), 263(5152), 1425–1429. https://doi.org/10.1126/science.7510417
ssRNA
mTCT8-4
Bronchodilator theophylline
5'AGUGAUACCAGCAUCGUCUUGAUGCCCUUGGCAGCACU3'
38
0.526316
Kd: 0.1 μM
100
Not reported (N40)
40
Sepharose column conditions: 60 mg of N-hydroxysuccinimide and 190 mg of 1 -ethyl-3,3-dimethylaminopropyl carbodiimide in a 5-mi 1:1 mixture of dioxane and phosphatebuffered saline (pH 7.2)
null
PBS/phosphate buffers
7.2
Not reported
Diagnostic: " One of the selected RNAs shows binding discrimination between theophylline and caffeine that is 10-fold better than that for available antibodies. In addition, this RNA possesses a binding affinity to theophylline over 100-fold greater than that to other oligonucleotides that have been selected to bind to small molecule targets. These results illustrate that small RNAs can display molecular recognition and specificity with extremely high resolution and illustrate the potential utility of oligonucleotides as diagnostic reagents."
38-nucleotide truncated version of the TCT8-4 aptamer.
Alternative sequence report: (Nx)AUACCA(Nx)CCUUGG(C/A)AG(Nx)
10,000,067
null
Polisky, B
5'rAprGprUprGprAprUprAprCprCprAprGprCprAprUprCprGprUprCprUprUprGprAprUprGprCprCprCprUprUprGprGprCprAprGprCprAprCprUp3 https://www.aptagen.com/aptamer-details/?id=150
1,994
https://pubmed.ncbi.nlm.nih.gov/7510417/
Science
https://doi.org/10.1126/science.7510417
Jenison, R. D., Gill, S. C., Pardi, A., & Polisky, B. (1994). High-resolution molecular discrimination by RNA. Science (New York, N.Y.), 263(5152), 1425–1429. https://doi.org/10.1126/science.7510417
ssRNA
TCT8-4
Bronchodilator theophylline
5'AAGUGAUACCAGCAUCGUCUUGAUGCCCUUGGCAGCACUUCA3'
42
0.5
Kd: 0.6 μM
600
Not reported (N40)
40
Sepharose column conditions: 60 mg of N-hydroxysuccinimide and 190 mg of 1 -ethyl-3,3-dimethylaminopropyl carbodiimide in a 5-mi 1:1 mixture of dioxane and phosphatebuffered saline (pH 7.2)
null
PBS/phosphate buffers
7.2
Not reported
Diagnostic: " One of the selected RNAs shows binding discrimination between theophylline and caffeine that is 10-fold better than that for available antibodies. In addition, this RNA possesses a binding affinity to theophylline over 100-fold greater than that to other oligonucleotides that have been selected to bind to small molecule targets. These results illustrate that small RNAs can display molecular recognition and specificity with extremely high resolution and illustrate the potential utility of oligonucleotides as diagnostic reagents."
Not applicable
Alternative sequence report: (Nx)AUACCA(Nx)CCUUGG(C/A)AG(Nx)
10,000,068
null
Polisky, B
null
1,994
https://pubmed.ncbi.nlm.nih.gov/10786843/
RNA
https://doi.org/10.1021/ja00084a010
Famulok, M. (1994). Molecular recognition of amino acids by RNA-aptamers: An L-citrulline binding RNA motif and its evolution into an L-arginine binder. Journal of the American Chemical Society, 116(5), 1698–1706. https://doi.org/10.1021/ja00084a010
ssRNA
44.Cit11
L-citrulline [L-(+)-2-amino-5-ureidovaleric acid]
5'GACGAGAAGGAGUGCUGGUUAUACUAGCGGUUAGGUCACUCGUC3'
44
0.522727
Kd: 62-68 µM
62,000
5'-GGAGCTCAGCCTTCACTGC-N74-GGCACCACGGTCGGATCC-3'
74
250 mM NaCl; 50 mM Tris-HCl, pH = 7.6; 5 mM MgCl2
MgCl
Tris Buffers
7.6
Not reported
Research: " We now report the isolation of RNAs able to bind the amino acid L-tyrosine+ The tyrosine aptamers were obtained by in vitro evolution of a previously selected dopamine aptamer. Tyrosine-binding sites are characterized by the presence of both tyrosine (UAU and UAC) and termination (UAG and UAA) triplets."
On the basis of the similarities of the individual sequences, a 44-mer RNA was constructed
extended descriptions of the aptamer structures can be found here: https://doi.org/10.1093/nar/23.23.4769 DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,069
null
Famulok, M
5'rGprAprCprGprAprGprAprAprGprGprAprGprUprGprCprUprGprGprUprUprAprUprAprCprUprAprGprCprGprGprUprUprAprGprGprUprCprAprCprUprCprGprUprCp3' https://www.aptagen.com/aptamer-details/?id=109
1,994
https://pubmed.ncbi.nlm.nih.gov/10786843/
RNA
https://doi.org/10.1021/ja00084a010
Famulok, M. (1994). Molecular Recognition of Amino Acids by RNA-Aptamers: An L-Citrulline Binding RNA Motif and Its Evolution into an L-Arginine Binder. Journal of the American Chemical Society, 116(5), 1698–1706. https://doi.org/10.1021/ja00084a010
ssRNA
44.Arg11
L-arginine
5'GACGAGAAGGAGCGCUGGUUCUACUAGCAGGUAGGUCACUCGUC3'
44
0.568182
Kd: 56-76 µM
56,000
5'-GGAGCTCAGCCTTCACTGC-N74-GGCACCACGGTCGGATCC-3'
74
250 mM NaCl; 50 mM Tris-HCl, pH = 7.6; 5 mM MgCl2
MgCl
Tris Buffers
7.6
Not reported
Research: " We now report the isolation of RNAs able to bind the amino acid L-tyrosine+ The tyrosine aptamers were obtained by in vitro evolution of a previously selected dopamine aptamer. Tyrosine-binding sites are characterized by the presence of both tyrosine (UAU and UAC) and termination (UAG and UAA) triplets."
On the basis of the similarities of the individual sequences, a 44-mer RNA was constructed
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,070
null
Famulok, M
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7528207/
J Biol Chem
PMID: 7528207
Conrad, R., Keranen, L. M., Ellington, A. D., & Newton, A. C. (1994). Isozyme-specific inhibition of protein kinase C by RNA aptamers. The Journal of biological chemistry, 269(51), 32051–32054.
ssRNA
Clone 6
Protein kinase C beta II (protein kinase C βII)
5'GGGAGAAUUCCGACCAGAGGCUUACAGAGUGUGCGUAAUGGCGUUCCCAAAUUCGGGCUGGGAACCGUUCGUUCGUGUUAUGCCCGUAGAUAUGGCAAGUCGCGGAUGCUCAGUACUACACUCUUGUGGUCAGUCACAUAUGUGCGUCUACAUGGAUCCUCA3'
162
0.518519
Kd: 7 nM
7
5'-GGGAGAAUUCCGACCAGAGGCUU-N120-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
120
20 mM HEPES, pH 7.5, 10 mM MgCl,, 0.3 m~ CaCl,, 1 mM DTT, 0.05 m~ ATP
MgCl/CaCl
Other Buffers
7.5
Not reported
Detection: " This work opens the possibility that the substrate recognition properties conferred on most proteins by natural selection can be mimicked by artificial evolution and that new allosteric inhibitors and activators of enzymes may be found using in vitro selection. As a practical example, expression of these aptamers in cells should now allow inhibition of one specific protein kinase C isozyme, thus opening the possibility for dissecting the roles of protein kinase C isozymes in signal transduction."
Not applicable
Paper says RNA aptamers but reports the sequences in DNA so T's were changed to U's in the spreadsheet DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,071
null
Newton AC
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7528207/
J Biol Chem
PMID: 7528207
Conrad R, Keranen LM, Ellington AD, Newton AC. Isozyme-specific inhibition of protein kinase C by RNA aptamers. J Biol Chem. 1994 Dec 23;269(51):32051-4. PMID: 7528207
ssRNA
Clone 10
Protein kinase C beta II (protein kinase C βII)
5'GGGAGAAUUCCGACCAGAGGUUGUUAAGUGCGAGUUGUUUUACUCCGAUGAUACGGGGAGCGUUAGAGUCUUAUGACCUUGUUCUCCACGUCACUGUCCAAGUCACUCCGCGUCAUAGCAGUCGGAUCCUGUACAUAUGUGCGUCUACAUGGAUCCUCA3'
159
0.496855
Kd: 7 nM
7
5'-GGGAGAAUUCCGACCAGAGGCUU-N120-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
120
20 mM HEPES, pH 7.5, 10 mM MgCl,, 0.3 m~ CaCl,, 1 mM DTT, 0.05 m~ ATP
MgCl/CaCl
Other Buffers
7.5
Not reported
Detection: " This work opens the possibility that the substrate recognition properties conferred on most proteins by natural selection can be mimicked by artificial evolution and that new allosteric inhibitors and activators of enzymes may be found using in vitro selection. As a practical example, expression of these aptamers in cells should now allow inhibition of one specific protein kinase C isozyme, thus opening the possibility for dissecting the roles of protein kinase C isozymes in signal transduction."
Not applicable
Paper says RNA aptamers but reports the sequences in DNA so T's were changed to U's in the spreadsheet DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,072
null
Newton AC
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
100
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAACCGGUAGUCGCAUGGCCCAUCGCGCCCGGUUCGACAUGAGGCCCGGAUCCGGC3'
76
0.644737
Kd1: 0.20 ± 0.02 nM Kd2: 42 ± 30 nM
0.2
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,073
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
100t
Vascular Endothelial Growth Factor (VEGF)
5'GGCCGGUAGUCGCAUGGCCCAUCGCGCCCGG3'
31
0.774194
Kd1: 0.42 ± 0.04 nM Kd2: 182 ±94 nM
0.42
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,074
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
44t
Vascular Endothelial Growth Factor (VEGF)
5'GGAAGCUUGAUGGGUGACACACGUCAUGCCGAGCU3'
35
0.571429
Kd1: 0.48 ± 0.04 nM Kd2: 82 ± 23 nM
0.48
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,075
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
12t
Vascular Endothelial Growth Factor (VEGF)
5'GGAAGGGAACCUGCGUCUCGGCACCUUCG3'
29
0.655172
Kd1: 1.1 ±0.2 nM Kd2: 180 ± 160 nM
1.1
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,076
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
40t
Vascular Endothelial Growth Factor (VEGF)
5'GGUCAACGGUUGAGUCUGUCCCGUUCGAC3'
29
0.586207
Kd1: 20 ± 1 nM
20
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,077
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
84t
Vascular Endothelial Growth Factor (VEGF)
5'GGCUCAAUAGUUGGAGGCCUGUCCUCGCCGUAGAGC3'
36
0.611111
Kd1:1.8 ±0.4 nM Kd2: 31 ± 10 nM
1.8
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,078
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
126t
Vascular Endothelial Growth Factor (VEGF)
5'GGAACGGUUCUGUGUGUGGACUAGCCGCGGCCGUU3'
35
0.628571
Kd1: 1.4 ±0.2 nM Kd2: 181 ± 57 nM
1.4
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Truncated
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,079
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
44
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAAAGCUUGAUGGGUGACACACGUCAUGCCGAGCUUUUCGACAUGAGGCCCGGAUCCGGC3'
80
0.5625
Kd1: 1.7 ±0.5 nM Kd2: 38 ±32 nM
1.7
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,080
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
12
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAAGCAGACGAAGGGAACCUGCGUCUCGGCACCUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.61039
Kd1: 0.48 ± 0.07 nM Kd2: 21 ±5 nM
0.48
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,081
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
40
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAAGCUUGAUGGGUGACACACGUCAUGCCGAGCUUCGACAUGAGGCCCGGAUCCGGC3'
77
0.584416
Kd1: 0.19 ±0.09 nM Kd2: 10 ± 1 nM
0.19
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,082
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
84
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAAGCUCAAUAGUUGGAGGCCUGUCCUCGCCGUAGAGCGUUCGACAUGAGGCCCGGAUCCGGC3'
83
0.590361
Kd1: 0.82 ±0.2 nM Kd2: 21 ± 5 nM
0.82
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,083
null
Janjić, N
null
1,994
https://pubmed.ncbi.nlm.nih.gov/7520755/
Biochemistry
https://doi.org/10.1021/bi00200a028
Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
ssRNA
126
Vascular Endothelial Growth Factor (VEGF)
5'GGGAGCUCAGAAUAAACGCUCAAAACGGUUCUGUGUGUGGACUAGCCGCGGCCGUUUUCGACAUGAGGCCCGGAUCCGGC3'
80
0.5875
Kd1: 0.14 ±0.04 nM Kd2: 11 ± 3 nM
0.14
5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
30
Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
null
PBS/phosphate buffers
7.4
Not reported
Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
null
Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
10,000,084
null
Janjić, N
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7819261/
Biochemistry
https://doi.org/10.1021/bi00002a033
Huizenga, D. E., & Szostak, J. W. (1995). A DNA aptamer that binds adenosine and ATP. Biochemistry, 34(2), 656–665. https://doi.org/10.1021/bi00002a033
ssDNA
DH25.42
Adenosine and Adenosine Triphosphate (ATP)
5'CCTGGGGGAGTATTGCGGAGGAAGG3'
25
0.64
Not reported
null
5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCC -3'
72
300 mM NaCl, 5 mM MgCl2, 20 mM Tris, pH 7.6
MgCl
Tris Buffers
7.6
Not reported
Research: " The specificity of ATP binding exhibited by the DNA aptamer raises the possibility that some DNA sequences might be able to stabilize reaction transition states with respect to ground state structures and, thus, exhibit catalytic function. Furthermore, the RNA aptamer for ATP has been used as a starting point for the selection of ribozymes with polynucleotide kinase activity (Lorsch & Szostak, 1994b). Now that a DNA aptamer for ATP has been isolated, similar selections for catalytic DNAs can also be attempted"
To see if the conserved and covarying sequences were sufficient for ATP binding, a 25 base oligonucleotide (DH25.42; Figure 5 A) that contained only these regions was synthesized. When this oligonucleotide was assayed for ATP binding, greater then 90% of the DNA remained on the ATP-agarose column after washing with 10 column vol_x0002_umes of buffer and was specifically eluted by ATP
The pool of random-sequence RNA molecules that was used in this work has been previously described (Bartel & Szostak,1993).The mutagenized pool used in the secondary selection was based on the sequence 5'-GTGCTTGGGGGAGTATTGCGGAGGAAAGCGGCCCTGCTGAAG-3', flanked by the same primer binding sites as in the original random-sequence pool.
10,000,085
null
Szostak, J. W
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7819261/
Biochemistry
https://doi.org/10.1021/bi00002a033
Huizenga, D. E., & Szostak, J. W. (1995). A DNA aptamer that binds adenosine and ATP. Biochemistry, 34(2), 656–665. https://doi.org/10.1021/bi00002a033
ssDNA
clone 16
Adenosine and Adenosine Triphosphate (ATP)
5'CTACCTGGGGGAGCATTGGGGAGGAAGGTAGCCGTGCGAAAA3'
42
0.595238
Kd: 6 ± 3 uM
6,000
5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCC -3'
72
300 mM NaCl, 5 mM MgCl2, 20 mM Tris, pH 7.6
MgCl
Tris Buffers
7.6
Not reported
Research: " The specificity of ATP binding exhibited by the DNA aptamer raises the possibility that some DNA sequences might be able to stabilize reaction transition states with respect to ground state structures and, thus, exhibit catalytic function. Furthermore, the RNA aptamer for ATP has been used as a starting point for the selection of ribozymes with polynucleotide kinase activity (Lorsch & Szostak, 1994b). Now that a DNA aptamer for ATP has been isolated, similar selections for catalytic DNAs can also be attempted"
The binding domain of this aptamer was localized to a 42 base sequence by deletion analysis. (Truncation)
The pool of random-sequence RNA molecules that was used in this work has been previously described (Bartel & Szostak,1993).The mutagenized pool used in the secondary selection was based on the sequence 5'-GTGCTTGGGGGAGTATTGCGGAGGAAAGCGGCCCTGCTGAAG-3', flanked by the same primer binding sites as in the original random-sequence pool.
10,000,086
null
Szostak, J. W
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT1
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTCAGAAGGATAAACTGTCCAGAACTTGGAATATATCAGTATCGCTAATCAGGCGGAT3'
81
0.444444
Kd: 1 nM; Ki: <0.3 nM
1
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,087
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT1t49
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTCAGAAGGATAAACTGTCCAGAACTTGGA3'
53
0.471698
Kd: 4 nM;
4
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Truncated
null
10,000,088
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT4
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTTTAGCAAAGTTGAAGCCGGACTAACAAGCTCTACGAGTATCGCTAATCAGGCGGAT3'
81
0.481481
Kd: 8 nM; Ki: 4 nM
8
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,089
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT6
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTCAGGCGTTAGGGAAGGGCGTCGAAAGCAGGGTGGGAGTATCGCTAATCAGGCGGAT3'
81
0.567901
Kd: 5 nM; Ki: 30 nM
5
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,090
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT10
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTTATTTGCCCCTGCAGGCCGCAGGAGTGCTAGCAGTAGTATCGCTAATCAGGCGGAT3'
81
0.54321
Kd: 11 nM; Ki: 62 nM
11
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,092
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT12
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTCGATTAGGTCCCCTGCCGCTAAACAGCGCCGCGGTAAGTATCGCTAATCAGGCGGAT3'
82
0.560976
Kd: 2 nM
2
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,093
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7542922/
Biochemistry
https://doi.org/10.1021/bi00029a037
Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
ssDNA
RT36
Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
5'CCCCTGCAGGTGATTTTGCTCAAGTAAGCTCTTAGTTGATGCGCGGTCAAAATTTAAGCTAGTATCGCTAATCAGGCGGAT3'
81
0.45679
Kd: 4 nM; Ki: 6.5 nM
4
5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
35
200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
MgCl
Tris Buffers
8
66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Not applicable
null
10,000,095
null
Gold L
null
1,995
https://pubmed.ncbi.nlm.nih.gov/7489503/
RNA
PMID: 7489503 or PMCID: PMC1369084
Tian, Y., Adya, N., Wagner, S., Giam, C. Z., Green, M. R., & Ellington, A. D. (1995). Dissecting protein:protein interactions between transcription factors with an RNA aptamer. RNA (New York, N.Y.), 1(3), 317–326.
ssRNA
YT1
Tax protein of the human T-cell lymphomatic virus (HTLV-1)
5'GGGAGAAUUCCGACCAGAAGCUUGGACUUAUUCUCGAGCCUGCAUGUGCUAGUCGACGUUGUUUCUGCAUCUUGAAAGAUGGGGCUGUGGGUGUGGUUACUUCUACGCGGUAUGCACUGUACGCCCCAUAUGUGCGUCUACAUGGAUCCUCA3'
152
0.513158
Kd: 70 nM
70
5'-GGGAGAATTCCGACCAGAAGCTT-N120-CATATGTGCGTCTACATGGATCCTCA-3'
120
20 mM Tris x Cl, pH 7.9, 80 mM KCl, 10% glycerol, 1 mM MgCl2, 0.2 mM EDTA, 10 microM DTT, 0.5 mM PMSF)
MgCl
Tris Buffers
7.9
Not reported
Therapeutic: " In order to develop reagents that could also be used to study protein:protein interactions, we have used in vitro selection to search for RNA aptamers that could interact with the transactivating protein Tax from human T-cell leukemia virus. The differential effects of our aptamer probe on protein:protein interactions suggest a model for how the transcription factor binding sites on the surface of the Tax protein are organized."
Not applicable
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
10,000,096
null
Ellington AD, adelling@ucs.indiana.edu
null
1,995
https://pubmed.ncbi.nlm.nih.gov/9383430/
Chem Biol
https://doi.org/10.1016/1074-5521(95)90047-0
Wang, Y., & Rando, R. R. (1995). Specific binding of aminoglycoside antibiotics to RNA. Chemistry & biology, 2(5), 281–290. https://doi.org/10.1016/1074-5521(95)90047-0
ssRNA
X1
Tobramycin
5'GGGAGAAUUCCGACCAGAAGCUUCUGGUUAGUUUUGCACAGUGGUCGAUGCUAGACUUGGUUUAGGUAAUGAGUCCAAUAGUCCAUAUGUGCGUCUACAUGGAUCCUCA3'
109
0.458716
Kd: 3 ± 1 nM (high affinity component); 15.9 ± 0.7 µM (low affinity component)
3
5'-GGGAGAAUUCCGACCAGAAGCUU-N60-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
60
140 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, and 20 mM Tris acetate at pH 7.4
MgCl/CaCl
Tris Buffers
7.4
Not reported
Therapeutic, Detection, and Research: "When coupled with the use of high-resolution NMR and X-ray spectroscopic studies, it ought to be possible to define the specific ways in which RNA molecules recognize aminoglycoside antibiotics.This information will be important in the design of novel molecules that will bind to and interfere with the function of specific RNA structures. Molecules of this type could be useful as paradigms for the design of novel drugs."
Not applicable
null
10,000,098
null
Rando, R. R.
null
1,995
https://pubmed.ncbi.nlm.nih.gov/9383430/
Chem Biol
https://doi.org/10.1016/1074-5521(95)90047-0
Wang, Y., & Rando, R. R. (1995). Specific binding of aminoglycoside antibiotics to RNA. Chemistry & biology, 2(5), 281–290. https://doi.org/10.1016/1074-5521(95)90047-0
ssRNA
J6
Tobramycin
5'GGGAGAAUUCCGACCAGAAGCUUAGUAUAGCGAGGUUUAGCUACACUCGUGCUGAUCGUUUGGUACGGGACCUGCGUGUAGCCCAUAUGUGCGUCUACAUGGAUCCUCA3'
109
0.513761
Kd: 2 ± 1 nM (high affinity component); 6.0 ± 0.4 µM (low affinity component)
2
5'-GGGAGAAUUCCGACCAGAAGCUU-N60-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
60
140 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, and 20 mM Tris acetate at pH 7.4
MgCl/CaCl
Tris Buffers
7.4
Not reported
Therapeutic, Detection, and Research: "When coupled with the use of high-resolution NMR and X-ray spectroscopic studies, it ought to be possible to define the specific ways in which RNA molecules recognize aminoglycoside antibiotics.This information will be important in the design of novel molecules that will bind to and interfere with the function of specific RNA structures. Molecules of this type could be useful as paradigms for the design of novel drugs."
Not applicable
null
10,000,099
null
Rando, R. R.
5'rGprGprGprAprGprAprAprUprUprCprCprGprAprCprCprAprGprAprAprGprCprUprUprAprGprUprAprUprAprGprCprGprAprGprGprUprUprUprAprGprCprUprAprCprAprCprUprCprGprUprGprCprUprGprAprUprCprGprUprUprUprGprGprUprAprCprGprGprGprAprCprCprUprGprCprGprUprGprUprAprGprCprCprCprAprUprAprUprGprUprGprCprGprUprCprUprAprCprAprUprGprGprAprUprCprCprUprCprAp3' https://www.aptagen.com/aptamer-details/?id=41
1,995
https://pubmed.ncbi.nlm.nih.gov/8524793/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.92.25.11509
Pan, W., Craven, R. C., Qiu, Q., Wilson, C. B., Wills, J. W., Golovine, S., & Wang, J. F. (1995). Isolation of virus-neutralizing RNAs from a large pool of random sequences. Proceedings of the National Academy of Sciences of the United States of America, 92(25), 11509–11513. https://doi.org/10.1073/pnas.92.25.11509
2'-fluoro-RNA
B
Rous sarcoma virus (RSV)
5'GGGAGCUCAGAAUAAACGCUCAAUGCCUCGUGUCGAAGAAGGGUGGCGCGAGGGUAGGGUUUCGACAUGAGGCCCGGAUCCGGC3'
84
0.607143
Kd: ~2-3 μg of viral protein per ml)
2,000
5'-GCCGGATCCGGGCCTCATGTCGAA-N40-TTGAGCGTTTATTCTGAGCTCCC-3'
40
2.5 mM MgCl2/100 mM NaCl/20 mM Tris HCl, pH 7.5
MgCl
Tris Buffers
7.5
Not reported
Therapeutic: " The selection of the anti-RSV RNA and RNA analogs by intact virions immediately suggests the potential application of this approach to develop RNA and RNA analogs as inhibitors of other viruses such as human immunodeficiency virus. Aptamers change the structures of viral surface proteins so that these proteins can no longer function in steps critical for viral infection, such as viral attachment and virus-cell membrane fusion. Alternatively, some of the structural changes may trigger pathways to inhibit the steps which normally occur after virus internalization, such as the uncoating and the expression of the virus genome."
Not applicable
2'F-RNA: 2'-F-CTP and 2'-F-UTP replaced CTP and UTP. Transcribed a pool of 2'-F-RNA from unmodified RNA after 9 cycles of selection by RSV
10,000,100
null
Wang JF
null
1,995
https://pubmed.ncbi.nlm.nih.gov/8524793/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.92.25.11509
Pan, W., Craven, R. C., Qiu, Q., Wilson, C. B., Wills, J. W., Golovine, S., & Wang, J. F. (1995). Isolation of virus-neutralizing RNAs from a large pool of random sequences. Proceedings of the National Academy of Sciences of the United States of America, 92(25), 11509–11513. https://doi.org/10.1073/pnas.92.25.11509
2'-fluoro-RNA
E
Rous sarcoma virus (RSV)
5'GGGAGCUCAGAAUAAACGCUCAAUGUAGUGAACAUUAAUGGAGAGAGGGAGGGUAGGGUUACGUUCGACAUGAGGCCCGGAUCCGGC3'
87
0.528736
Not reported
null
5'-GCCGGATCCGGGCCTCATGTCGAA-N40-TTGAGCGTTTATTCTGAGCTCCC-3'
40
2.5 mM MgCl2/100 mM NaCl/20 mM Tris HCl, pH 7.5
MgCl
Tris Buffers
7.5
Not reported
Therapeutic: " The selection of the anti-RSV RNA and RNA analogs by intact virions immediately suggests the potential application of this approach to develop RNA and RNA analogs as inhibitors of other viruses such as human immunodeficiency virus. Aptamers change the structures of viral surface proteins so that these proteins can no longer function in steps critical for viral infection, such as viral attachment and virus-cell membrane fusion. Alternatively, some of the structural changes may trigger pathways to inhibit the steps which normally occur after virus internalization, such as the uncoating and the expression of the virus genome."
Not applicable
2'F-RNA: 2'-F-CTP and 2'-F-UTP replaced CTP and UTP. Transcribed a pool of 2'-F-RNA from unmodified RNA after 9 cycles of selection by RSV
10,000,101
null
Wang JF
null
1,995
https://pubmed.ncbi.nlm.nih.gov/8524793/
Proc Natl Acad Sci U S A
https://doi.org/10.1073/pnas.92.25.11509
Pan, W., Craven, R. C., Qiu, Q., Wilson, C. B., Wills, J. W., Golovine, S., & Wang, J. F. (1995). Isolation of virus-neutralizing RNAs from a large pool of random sequences. Proceedings of the National Academy of Sciences of the United States of America, 92(25), 11509–11513. https://doi.org/10.1073/pnas.92.25.11509
2'-fluoro-RNA
F
Rous sarcoma virus (RSV)
5'GGGAGCUCAGAAUAAACGCUCAAAUUGUCUUGAACCCGUGGGAGGUGUGAGGGUAGGGGUGGUUCGACAUGAGGCCCGGAUCCGGC3'
86
0.581395
Not reported
null
5'-GCCGGATCCGGGCCTCATGTCGAA-N40-TTGAGCGTTTATTCTGAGCTCCC-3'
40
2.5 mM MgCl2/100 mM NaCl/20 mM Tris HCl, pH 7.5
MgCl
Tris Buffers
7.5
Not reported
Therapeutic: " The selection of the anti-RSV RNA and RNA analogs by intact virions immediately suggests the potential application of this approach to develop RNA and RNA analogs as inhibitors of other viruses such as human immunodeficiency virus. Aptamers change the structures of viral surface proteins so that these proteins can no longer function in steps critical for viral infection, such as viral attachment and virus-cell membrane fusion. Alternatively, some of the structural changes may trigger pathways to inhibit the steps which normally occur after virus internalization, such as the uncoating and the expression of the virus genome."
Not applicable
2'F-RNA: 2'-F-CTP and 2'-F-UTP replaced CTP and UTP. Transcribed a pool of 2'-F-RNA from unmodified RNA after 9 cycles of selection by RSV
10,000,102
null
Wang JF
null
End of preview. Expand in Data Studio

UT Aptamer Dataset

This is a collection of 1480 aptamer sequences from the University of Texas Aptamer Database as of 2023. This dataset is split into three subsets (train, test, and validation) based on clustering by CD-HIT.

Clustering

Clustering was conducting using the CD-HIT: Cluster Database at High Identity with Tolerance web browser using a 40% sequence identity threshold and word size of 2. To update this dataset with new reported aptamers, splits can be determined by re-clustering.

Quickstart Usage

Install HuggingFace Datasets package

Each subset can be loaded into python using the HuggingFace datasets library. First, from the command line install the datasets library

$ pip install datasets

Optionally set the cache directory, e.g.

$ HF_HOME=${HOME}/.cache/huggingface/
$ export HF_HOME

then, from within python load the datasets library

import datasets

Load model datasets

To load one of the UTexasAptamer model datasets, use datasets.load_dataset(...):

dataset = datasets.load_dataset(f"kysie/UTexasAptamer", "train")

and the dataset is loaded as a datasets.arrow_dataset.Dataset

>>> print(dataset)
DatasetDict({
    train: Dataset({
        features: ['Year of Paper', 'Link to PubMed Entry', 'Journals', 'Journal DOI', 'Citation', 'Type of Nucleic Acid', 'Name of Aptamer', 'Target', 'Aptamer Sequence', 'Sequence Length', 'GC Content', 'Affinity', 'Kd (nM)', 'Pool Type', 'Pool Random Region', 'Binding Buffer/Conditions', 'Divalent Salt', 'Type of the buffer', 'pH', 'Molecular weight of target', 'Application as quoted in the referenced paper', 'Post-selex modification to the aptamer', 'Additional Information', 'Serial Number', 'Parent sequence serial number', 'Corresponding Author Name, email address', 'Aptagen Cross Referencing(Check Aptamer Chemistry, Affinity, Length, GC content, sequence)'],
        num_rows: 1262
    })
    test: Dataset({
        features: ['Year of Paper', 'Link to PubMed Entry', 'Journals', 'Journal DOI', 'Citation', 'Type of Nucleic Acid', 'Name of Aptamer', 'Target', 'Aptamer Sequence', 'Sequence Length', 'GC Content', 'Affinity', 'Kd (nM)', 'Pool Type', 'Pool Random Region', 'Binding Buffer/Conditions', 'Divalent Salt', 'Type of the buffer', 'pH', 'Molecular weight of target', 'Application as quoted in the referenced paper', 'Post-selex modification to the aptamer', 'Additional Information', 'Serial Number', 'Parent sequence serial number', 'Corresponding Author Name, email address', 'Aptagen Cross Referencing(Check Aptamer Chemistry, Affinity, Length, GC content, sequence)'],
        num_rows: 154
    })
    validation: Dataset({
        features: ['Year of Paper', 'Link to PubMed Entry', 'Journals', 'Journal DOI', 'Citation', 'Type of Nucleic Acid', 'Name of Aptamer', 'Target', 'Aptamer Sequence', 'Sequence Length', 'GC Content', 'Affinity', 'Kd (nM)', 'Pool Type', 'Pool Random Region', 'Binding Buffer/Conditions', 'Divalent Salt', 'Type of the buffer', 'pH', 'Molecular weight of target', 'Application as quoted in the referenced paper', 'Post-selex modification to the aptamer', 'Additional Information', 'Serial Number', 'Parent sequence serial number', 'Corresponding Author Name, email address', 'Aptagen Cross Referencing(Check Aptamer Chemistry, Affinity, Length, GC content, sequence)'],
        num_rows: 64
    })
})

which is a column oriented format that can be accessed directly, converted in to a pandas.DataFrame, or parquet format, e.g.

dataset.data.column('<COLUMN NAME IN DATASET>')
dataset.to_pandas()
dataset.to_parquet("dataset.parquet")

Curation Rationale

This dataset has the potential for training models related to aptamer sequence and binding relationships, including prediction of binding affinities and design of aptamers.

Dataset Sources

  • Repository: https://zenodo.org/records/8387047
  • Paper: Ali Askari, Sumedha Kota, Hailey Ferrell, Shriya Swamy, Kayla S Goodman, Christine C Okoro, Isaiah C Spruell Crenshaw, Daniela K Hernandez, Taylor E Oliphant, Akshata A Badrayani, Andrew D Ellington, Gwendolyn M Stovall, UTexas Aptamer Database: the collection and long-term preservation of aptamer sequence information, Nucleic Acids Research, Volume 52, Issue D1, 5 January 2024, Pages D351–D359, https://doi.org/10.1093/nar/gkad959

Dataset Card Authors

  • Katie Sie katiesie/@/uw.edu

Acknowledgements: Askari, Ali; Kota, Sumedha; Ferrell, Hailey; Swamy, Shriya; Goodman, Kayla S.; Okoro, Christine C.; Spruell Crenshaw, Isaiah C.; Hernandez, Daniela K.; Oliphant, Taylor E.; Badrayani, Akshata A.; Ellington, Andrew D.; Stovall, Gwendolyn M.1 License: Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/)

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