Binding affinities (Kd) — source-verified (view)
Data license: CC BY 4.0 · Data source: apt-scout automated curation pipeline (E. Dohi, NCNP) — values harvested from public databases; raw source stored per target
- target_name_canonical
- Target as named in the source paper.
- target_type
- protein / cell-line+EV / glycan-conjugate. Filter to 'protein' for molecular targets.
- target_uniprot
- UniProt accession when a human protein (sparse for now; links to apt-scout target).
- aptamer_name
- Aptamer identifier as reported.
- kd_reported
- Kd value AS REPORTED in the paper (value + unit). Units are MIXED — do NOT compare this column directly.
- kd_log10_molar
- log10(Kd in molar). THE column to sort / compare / learn on (lower = tighter).
- measurement_class
- intrinsic = equilibrium vs purified target; non_intrinsic = apparent/cellular or avidity (NOT comparable to intrinsic).
- binding_constant_type
- Kd / apparent-Kd etc. as reported.
- assay_method
- SPR / filter binding / flow cytometry / ITC / BLI …
- assay_temperature_k
- Assay temperature (K) — a reason the same pair can have several rows.
- source_pmid
- PubMed ID of the source paper (links out).
- verbatim_quote
- The exact sentence the value was taken from.
- verification_level
- QC status (honest, growing): human_verified / human_corrected = a logged human verdict from the stratified-random sample; multi_agent_verified = passed independent multi-agent (L2) check; extraction_verified = extraction-pipeline verified; automated. Human verification is in progress: as of this release 0 records carry a logged human verdict — the published set is multi-agent-/extraction-verified, and human spot-checking is being added post-publication (version-tracked). No record is labelled human_verified without a logged human review.
- sequence_status
- Aptamer-sequence provenance: verified_in_text_or_SI = sequence verbatim-verified against the source text/SI (shown); pending_manual_supp / pending_supp_oa / pending_manual_figure = sequence reported only in a (often paywalled) SI or a figure, being curated post-submission; no_single_sequence_pool = a pool/library/primer, no single sequence exists.
- pi_provenance_flag
- PI manual-review flag: KEEP_seq_in_figure = valid record, sequence is in a 3D-structure figure; FLAG_cited_data = Kd may be a value cited from elsewhere, re-verify. (EXCLUDE rows are hidden from this view.)
- seq_source
- original (already in source DB) / backfill_text_verified (recovered from paper or SI text).
534 rows where target_type = "protein" and verification_level = "extraction_verified" sorted by kd_log10_molar
This data as json, CSV (advanced)
Suggested facets: source_origin, seq_source, pi_provenance_flag, assay_temperature_k, assay_ph, assay_cations, aptamer_chemistry, source_db
assay_method 18
- flow_cytometry 83
- SPR 53
- filter_binding 28
- BLI 24
- MST 20
- fluorescence 14
- CE-LIF 10
- ELISA 8
- ITC 8
- QCM 5
- BSI 4
- ELONA 2
- FACS 2
- mass_spectrometry 2
- microcantilever 2
- microscale thermophoresis 2
- qPCR 1
- qRT-PCR 1
sequence_status 5
measurement_class 2
- intrinsic 395
- non_intrinsic 139
verification_level 1
- extraction_verified · 534 ✖
tier 1
- Gold 534
target_type 1
- protein · 534 ✖
| id | target_name_canonical | target_type | target_uniprot | aptamer_name | aptamer_seq | kd_reported | kd_log10_molar ▼ | measurement_class | binding_constant_type | tier | source_origin | verification_level | sequence_status | seq_source | pi_provenance_flag | assay_method | assay_temperature_k | assay_ph | assay_buffer | assay_cations | aptamer_chemistry | aptamer_modifications | source_pmid | doi | verbatim_quote | source_db |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 188 | PDGF-BB | protein | P01127 | 36aApt | 0.036 pM | -13.444 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | ELISA | 298.0 | DNA | 28825469 | 10.1021/acscombsci.6b00163 | 36aApt | 0.036 ± 0.012 | - 18.33 | step2c_literal_v3 | |||||||
| 186 | PDGF-BB | protein | P01127 | 38aApt | 0.094 pM | -13.027 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | ELISA | 298.0 | DNA | 28825469 | 10.1021/acscombsci.6b00163 | 38aApt | 0.094 ± 0.008 | - 17.76 | step2c_literal_v3 | |||||||
| 44 | IL-8 | protein | P10145 | 8A-35 | GGGGGCUUAUCAUUCCAUUUAGUGUUAUGAUAACC | 1.72e-12 M | -11.764 | intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | original | SPR | 298.0 | 7.4 | HBST running buffer (10 mM HEPES, pH 7.4, 150 mM NaCl, and 0.005% Tween 20) | 2'F-RNA | 2'-fluoro-pyrimidine modified | 24129312 | 10.1016/j.biomaterials.2013.09.107 | | 8A-35 | 5.78 x 10 4 | 9.95 x 10 -8 | 1.72 x 10 -12 | 2.80 | 3.11 x 10 1 | | step2c_literal_v3 | ||
| 598 | human α-Thrombin | protein | P00734 | A1 | 2.0 pM | -11.699 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | Also for aptamer A1 we measured with MST KD values in the pico- and nanomolar range (2 pM and 52 nM). The lowest KD value is determined with MST (shown as bar) for aptamer A1, which is 2 pM. | elsevier_step2c | |||||||||
| 621 | nucleolin | protein | P19338 | Cy5-AT11-B0 | TGGTGGTGGTTGGTGGTGGTGGTGGT | 3.3e-12 M | -11.481 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 31301466 | 10.1016/j.ijpharm.2019.118511 | yielding K D values of 5.2 × 10 -12 and 3.3 × 10 -12 M for Cy5-AT11 G4 C8 and Cy5-AT11-B0 G4 C8 | elsevier_step2c | |||||||
| 620 | nucleolin | protein | P19338 | Cy5-AT11 | TGGTGGTGGTTGTTGTGGTGGTGGTGGT | 5.2e-12 M | -11.284 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 31301466 | 10.1016/j.ijpharm.2019.118511 | yielding K D values of 5.2 × 10 -12 and 3.3 × 10 -12 M for Cy5-AT11 G4 C8 and Cy5-AT11-B0 G4 C8 | elsevier_step2c | |||||||
| 184 | PDGF-BB | protein | P01127 | FullApt | 5.33 pM | -11.273 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | ELISA | 298.0 | DNA | 28825469 | 10.1021/acscombsci.6b00163 | FullApt | 5.33 ± 2.36 | - 15.37 | step2c_literal_v3 | |||||||
| 185 | PDGF-BB | protein | P01127 | 40Apt | 5.92 pM | -11.228 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | ELISA | 298.0 | DNA | 28825469 | 10.1021/acscombsci.6b00163 | 40Apt | 5.92 ± 1.13 | - 15.31 | step2c_literal_v3 | |||||||
| 187 | PDGF-BB | protein | P01127 | 38bApt | 7.03 pM | -11.153 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | ELISA | 298.0 | DNA | 28825469 | 10.1021/acscombsci.6b00163 | 38bApt | 7.03 ± 1.28 | - 15.21 | step2c_literal_v3 | |||||||
| 618 | nucleolin | protein | P19338 | Cy5-AT11 | TGGTGGTGGTTGTTGTGGTGGTGGTGGT | 9.1e-12 M | -11.041 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 31301466 | 10.1016/j.ijpharm.2019.118511 | K D values of 9.1 × 10 -12 and 9.5 × 10 -12 M for Cy5-AT11 G4 and Cy5-AT11-B0 G4 | elsevier_step2c | |||||||
| 619 | nucleolin | protein | P19338 | Cy5-AT11-B0 | TGGTGGTGGTTGGTGGTGGTGGTGGT | 9.5e-12 M | -11.022 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 31301466 | 10.1016/j.ijpharm.2019.118511 | K D values of 9.1 × 10 -12 and 9.5 × 10 -12 M for Cy5-AT11 G4 and Cy5-AT11-B0 G4 | elsevier_step2c | |||||||
| 269 | thrombin | protein | P00734 | HD1-12A-DAB | 13.1 pM | -10.883 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | filter_binding | selection buffer | DNA | 41053535 | 10.1002/advs.202509867 | HD1-12A-DAB EXACT inhibitor bound to thrombin and prothrombin with K D s of 13.1 pm | step2c_literal_v3 | |||||||
| 143 | P-selectin | protein | Q14242 | PF377 | 14.0 pM | -10.854 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377 | 14 | step2c_literal_v3 | ||||
| 147 | P-selectin | protein | Q14242 | PF377sl | 14.0 pM | -10.854 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 296.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377sl | 14 | step2c_literal_v3 | ||||
| 142 | P-selectin | protein | Q14242 | PF377 | 16.0 pM | -10.796 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377 | 16 | step2c_literal_v3 | ||||
| 144 | P-selectin | protein | Q14242 | PF377 | 18.0 pM | -10.745 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 277.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377 | 18 | step2c_literal_v3 | ||||
| 623 | Malate Synthase | protein | Q8N0X4 | MS10-Trunc | GGTGGTGGTGG | 19.0 pM | -10.721 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | abstract | 31704587 | 10.1016/j.omtn.2019.09.026 | MS10-Trunc aptamer exhibited high af fi nity for MS (equilibrium dissociation constant [KD] 19 pM) | elsevier_step2c | |||||||
| 140 | PDGF-C | protein | P01127 | α-PC | CTACTGTGTGATGTCTGAGAGCAGCGTCTAAACGAACAAGCGAACCTATGCACAGAGGACAGTACATCAGACAC | 20.0 pM | -10.699 | intrinsic | KD | Gold | v4 | extraction_verified | verified_in_text_or_SI | original | SPR | 7.4 | HBS-EP + (10-mM HEPES, 150-mM NaCl, 3-mM EDTA, and 0.05% Tween 20, pH 7.4) | DNA | PEG | 42138517 | 10.1167/iovs.67.5.36 | SPR analysis demonstrated that the α -PC aptamer bound tightly to PDGF-C with a dissociation constant ( KD ) of 20 pM | step2c_literal_v3 | |||
| 146 | P-selectin | protein | Q14242 | PF377sl | 29.0 pM | -10.538 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377sl | 29 | step2c_literal_v3 | ||||
| 669 | bevacizumab | protein | P31995 | A14#1 | GCGGTTGGTGGTAGTTACGTTCGC | 44.0 pM | -10.357 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | abstract | 35114463 | 10.1016/j.bios.2022.114027 | affinity of A14#1 to bevacizumab markedly increased at pH 4.7 ( K D = 44 pM) | elsevier_step2c | |||||||
| 145 | P-selectin | protein | Q14242 | PF377sl | 46.0 pM | -10.337 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377sl | 46 | step2c_literal_v3 | ||||
| 148 | P-selectin | protein | Q14242 | PF373sl | 56.0 pM | -10.252 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF373sl | 56 | step2c_literal_v3 | ||||
| 56 | von Willebrand factor A1-domain | protein | P04275 | Rn-DsDsDs-53mh | 61.3 pM | -10.213 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | 310.15 | 1 × PBS supplemented with 0.05% (w/v) Nonidet P-40 | DNA | Ds (7-(2-thienyl)imidazo[4,5b]pyridine); mini-hairpin DNA | 27966933 | 10.1021/jacs.6b10767 | RnDsDsDs-53mh ( K D = 61.3 pM) | step2c_literal_v3 | |||||
| 542 | Myoglobin | protein | P02144 | anti-Mb aptamer | 65.0 pM | -10.187 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 25957831 | 10.1016/j.bios.2015.04.089 | The corresponding af fi nity, K D, values calculated from the ratio between dissociation ( k d) and association ( k a ) was found to be 65 pM. | elsevier_step2c | |||||||||
| 53 | von Willebrand factor A1-domain | protein | P04275 | Rn-DsDsDs-44 | 74.9 pM | -10.126 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | 310.15 | 1 × PBS supplemented with 0.05% (w/v) Nonidet P-40 | DNA | Ds (7-(2-thienyl)imidazo[4,5b]pyridine) | 27966933 | 10.1021/jacs.6b10767 | Rn-DsDsDs-44 ( K D = 74.9 pM) exhibited the highest a ffi nity | step2c_literal_v3 | |||||
| 152 | PDGF-BB | protein | P01127 | PDGF-B aptamer | 0.1 nM | -10.0 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | DNA | 2'-fluoro; 2'-O-methyl; hexaethylene glycol spacer; inverted 3'-3' thymidine cap; 40-kd PEG conjugated | 9916931 | 10.1016/S0002-9440(10)65263-7 | the binding affinity of the aptamer used in the experiments described below ( K d ≈ 0.1 nM) | step2c_literal_v3 | |||||||
| 547 | ofloxacin | protein | Q9H015 | Q2 | ATACCAGCTTATTCAATTGCAGGGTATCTGAGGCTTGATCTACTAAATGTCGTGGGGCATTGCTATTGGCGTTGATACGTACAATCGTAATCAGTTAG | 0.11 nM | -9.959 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 26547431 | 10.1016/j.bios.2015.10.069 | Their K D values were calculated at K D 1⁄4 0.11 nM ( 7 0.06) for aptamer Q2 | elsevier_step2c | |||||||
| 245 | MPO | protein | P05164 | MPO-16 | GTCTGGAAACGACGAGGGCCACTGATTAACGTAGTTAATTGGTCTTGTCG | 166.0 pM | -9.78 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | backfill_text_verified | flow_cytometry | selection buffer (DPBS with 2.5 mM MgCl2 , 1 mM CaCl 2 , 0.01% TWEEN-20, 0.2% BSA) | 2.5 | DNA | 37277648 | 10.1038/s41557-023-01207-z | MPO16 revealed the highest binding affinity ( K d = 166 pM) | step2c_literal_v3 | ||||
| 149 | P-selectin | protein | Q14242 | PF398sl | 178.0 pM | -9.75 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | filter_binding | 310.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF398sl | 178 | step2c_literal_v3 | ||||
| 57 | von Willebrand factor A1-domain | protein | P04275 | Rn-DsDs-51mh2 | 182.0 pM | -9.74 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | 310.15 | 1 × PBS supplemented with 0.05% (w/v) Nonidet P-40 | DNA | Ds (7-(2-thienyl)imidazo[4,5b]pyridine); mini-hairpin DNA | 27966933 | 10.1021/jacs.6b10767 | Rn-DsDs-51mh2 ( K D = 182 pM) | step2c_literal_v3 | |||||
| 548 | ofloxacin | protein | Q9H015 | Q8 | ATACCAGCTTATTCAATTAGTTGTGTATTGAGGTTTGATCTAGGCATAGTCAACAGAGCACGATCGATCTGGCTTGTTCTACAATCGTAATCAGTTAG | 0.2 nM | -9.699 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 26547431 | 10.1016/j.bios.2015.10.069 | K D 1⁄4 0.20 nM ( 7 0.09) for aptamer Q8 | elsevier_step2c | |||||||
| 558 | OH-BDE47 | protein | BDE-A-8 | GACAGCCGGGGCATCAGAGCAGCCGATTGTCTGTTGTGCC | 0.2 nM | -9.699 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 27566357 | 10.1016/j.aca.2016.06.040 | The dissociation constant (Kd) of BDE-A-8 and BDE-A-12 were 0.20 nM (~0.08 ppb) and 1.53 nM (~0.8 ppb), respectively, in PBS buffer condition. | elsevier_step2c | ||||||||
| 234 | MPO | protein | P05164 | MPO-02 | TATGCGATTTCAAAAATGTTACGATGGATATTGACATTTAAATATGTCGG | 227.0 pM | -9.644 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | backfill_text_verified | flow_cytometry | selection buffer (DPBS with 2.5 mM MgCl2 , 1 mM CaCl 2 , 0.01% TWEEN-20, 0.2% BSA) | 2.5 | DNA | 37277648 | 10.1038/s41557-023-01207-z | MPO-02 ... 227 | step2c_literal_v3 | ||||
| 307 | P-selectin | protein | Q14242 | PF377sl | 250.0 pM | -9.602 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | flow_cytometry | 296.15 | 7.4 | SHMCK buffer | 1.0 | 2'F-RNA | 9743465 | 10.1089/oli.1.1998.8.265 | PF377sl | 250 | step2c_literal_v3 | ||||
| 639 | thrombin | protein | P00734 | 29-mer thrombin-specific aptamer | AGTCCGTGGTAGGGCAGGTTGGGGTGACT | 298.0 pM | -9.526 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 32570818 | 10.3390/s20123442 | The n-curve analysis provided a Kd of 298 pM ( + 111 / 81 pM) | elsevier_step2c | |||||||
| 660 | 20 Methyl Spirolide G | protein | SPX 7 | GGCGGTGTGGGTACCACGAGGTTTGGACGCGCGTAGCACCCCATTCAGC | 3e-10 M | -9.523 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | text | 34144421 | 10.1016/j.foodchem.2021.130332 | The present study, among the aptamers selected, the aptamer with highest affinity had a dissociation constant of 0.3 nM for SPX G | elsevier_step2c | ||||||||
| 554 | chimeric-tPA | protein | Chi-tPA 1 | TTCCAACGGTTGGTGGGTGGTT | 0.32 nM | -9.495 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | original | abstract | 26876003 | 10.1016/j.pep.2016.02.004 | selected aptamer having KD values of 0.320 nM | elsevier_step2c | ||||||||
| 55 | von Willebrand factor A1-domain | protein | P04275 | ARC1172-41 | 326.0 pM | -9.487 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | 310.15 | 1 × PBS supplemented with 0.05% (w/v) Nonidet P-40 | DNA | 27966933 | 10.1021/jacs.6b10767 | ARC1172-41 ( K D = 326 pM) | step2c_literal_v3 | ||||||
| 247 | Human thrombin | protein | P00734 | Lin08-08 | 0.4 nM | -9.398 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | KEEP_seq_in_figure | SPR | 7.4 | PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20 | DNA | 37621412 | 10.1016/j.omtn.2023.07.038 | Lin(08-08) | 1.63 10^6 | 6.94 10^-4 | 0.4 | step2c_literal_v3 | |||||
| 249 | Human thrombin | protein | P00734 | Pse08-08 | 0.4 nM | -9.398 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | KEEP_seq_in_figure | SPR | 7.4 | PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20 | DNA | 37621412 | 10.1016/j.omtn.2023.07.038 | Pse(08-08) | 1.19 10^6 | 5.10 10^-4 | 0.4 | step2c_literal_v3 | |||||
| 50 | PDGF-BB | protein | P01127 | PDGF-specific aptamer | 5e-10 M | -9.301 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_figure | microcantilever | 310.15 | 7.4 | PBSM buffer (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, and 1 mM MgCl2, pH 7.4) | 1.0 | DNA | 3'-3'-linked thymidine nucleotide ([3'T]); thiolated 5'-end | 24723743 | 10.1016/j.snb.2012.02.045 | K d , as shown in Fig. 10, decreased from approximately 12 × 10 -10 M to 5 × 10 -10 M as the temperature changed from 19 to 37 ◦ C. | step2c_literal_v3 | |||
| 173 | human α-thrombin | protein | P00734 | Apt29 | AGTCCGTGGTAGGGCAGGTTGGGGTGACT | 0.5 nM | -9.301 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | original | DNA | 28763192 | 10.1021/acs.analchem.7b02313 | a 29nucleotide aptamer (5 ′ -AGT CCG TGG TAG GGC AGG TTG GGG TGA CT-3 ′ , denoted as Apt29 here) binds to the heparin-binding site of human α -thrombin with a dissociation constant ( K d) around 0.5 nM. | step2c_literal_v3 | |||||||
| 205 | thrombin | protein | P00734 | TBA29 | 0.5 nM | -9.301 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | DNA | 31614078 | 10.1021/acs.analchem.9b03368 | The 29-nt TBA29 aptamer has a bimodular duplex-antiparallel G4 structure and binds to thrombin with a binding a ffi nity of 0.5 nM. 30 | step2c_literal_v3 | |||||||||
| 550 | Thrombin | protein | P00734 | TBA29 | 5e-10 M | -9.301 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 26643617 | 10.1016/j.jconrel.2015.11.028 | and TBA29 (~5 × 10 -10 M) | elsevier_step2c | |||||||||
| 530 | AGEs-HSA | protein | #9s | TCTGCCACCCTCCGACTAACATATCCGGCCTGAGACCA | 0.57 nM | -9.244 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | backfill_text_verified | abstract | 24012635 | 10.1016/j.mvr.2013.08.010 | Surface plasmon resonance analysis revealed that K D values of #4s, #7s and #9s were 0.63, 0.36, and 0.57 nM, respectively. | elsevier_step2c | ||||||||
| 175 | human α-thrombin | protein | P00734 | 5'-TMR-Apt15-T24 | GGTTGGTGTGGTTGG | 0.6 nM | -9.222 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | backfill_text_verified | CE-LIF | 298.15 | 7.5 | sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 5 mM KCl | DNA | TMR label at 5'-end; polyT tail (24 T) at 3'-end | 28763192 | 10.1021/acs.analchem.7b02313 | 0.6 nM for 5 ′ -TMR-Apt15-T24 | step2c_literal_v3 | ||
| 176 | human α-thrombin | protein | P00734 | 5'-TMR-Apt15-T25 | GGTTGGTGTGGTTGG | 0.6 nM | -9.222 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | backfill_text_verified | CE-LIF | 298.15 | 7.5 | sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 5 mM KCl | DNA | TMR label at 5'-end; polyT tail (25 T) at 3'-end | 28763192 | 10.1021/acs.analchem.7b02313 | 0.6 nM for 5 ′ -TMR-Apt15-T25 | step2c_literal_v3 | ||
| 303 | EGFR | protein | P00533 | Anti-EGF receptor aptamer | 0.62 nM | -9.208 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | DNA | 3' end sulfhydryl group (-SH) | 41877526 | 10.1021/acs.molpharmaceut.5c01966 | Anti-EGF receptor aptamers ( K d : 0.62 nM, DNA aptamers) | step2c_literal_v3 | ||||||||
| 529 | AGEs-HSA | protein | #4s | CAGAATCGGGGACCACGACACTGCACATACCTCGTACGAA | 0.63 nM | -9.201 | intrinsic | Kd | Gold | elsevier | extraction_verified | verified_in_text_or_SI | backfill_text_verified | abstract | 24012635 | 10.1016/j.mvr.2013.08.010 | Surface plasmon resonance analysis revealed that K D values of #4s, #7s and #9s were 0.63, 0.36, and 0.57 nM, respectively. | elsevier_step2c | ||||||||
| 154 | thrombin | protein | P00734 | HD1-22 | GGTTGGTGTGGTTGGAAAAAAAAAAAAGTCCGTGGTAGGGCAGGTTGGGGTGACT | 6.5e-10 M | -9.187 | non_intrinsic | Kd | Gold | v4 | extraction_verified | verified_in_text_or_SI | original | SPR | DNA | bivalent fusion; poly-dA linker | 18826387 | 10.1111/j.1538-7836.2008.03162.x | HD1-22 | Thrombin | K D ( M) | 6.5 · 10 ) 10 | step2c_literal_v3 |
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CREATE VIEW v_kd AS
SELECT k.id,
target_name_canonical,
CASE
WHEN target_name_canonical LIKE '%cell%' OR target_name_canonical LIKE '%vesicle%' OR target_name_canonical LIKE '%exosome%' THEN 'cell/EV'
WHEN target_name_canonical LIKE '%BSA%' OR target_name_canonical LIKE '%sLe%' OR target_name_canonical LIKE '%glycan%' OR target_name_canonical LIKE '% Le %' THEN 'glycan/conjugate'
ELSE 'protein'
END AS target_type,
target_uniprot, aptamer_name, aptamer_seq,
(COALESCE(kd_value,'') || CASE WHEN COALESCE(kd_unit,'')!='' THEN ' '||kd_unit ELSE '' END) AS kd_reported,
CAST(NULLIF(kd_log10_molar,'') AS REAL) AS kd_log10_molar,
measurement_class, binding_constant_type, 'Gold' AS tier, k.tier AS source_origin,
CASE
WHEN vh.verdict='confirmed' THEN 'human_verified'
WHEN vh.verdict='corrected' THEN 'human_corrected'
WHEN vh.verdict='rejected' THEN 'human_rejected'
WHEN k.verification_status='agent_verified_L2' THEN 'multi_agent_verified'
WHEN k.verification_status IN ('verified','CONFIRM') THEN 'extraction_verified'
ELSE 'automated'
END AS verification_level,
sequence_status, seq_source, pi_provenance_flag,
assay_method,
CAST(NULLIF(assay_temperature_k,'') AS REAL) AS assay_temperature_k,
CAST(NULLIF(assay_ph,'') AS REAL) AS assay_ph,
assay_buffer, assay_cations, aptamer_chemistry, aptamer_modifications,
source_pmid, doi, verbatim_quote, source_db
FROM kd_measurements k LEFT JOIN verification_human vh ON vh.row_id=k.source_record_id
WHERE LOWER(COALESCE(k.include_in_gold,''))='true';