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).
119 rows where measurement_class = "intrinsic", sequence_status = "pending_manual_supp" and verification_level = "extraction_verified" sorted by kd_log10_molar
This data as json, CSV (advanced)
Suggested facets: target_uniprot, source_origin, assay_temperature_k, assay_ph, assay_buffer, assay_cations, aptamer_modifications, source_db
assay_method 5
- BLI 12
- SPR 8
- ITC 5
- fluorescence 4
- ELONA 1
verification_level 1
- extraction_verified · 119 ✖
tier 1
- Gold 119
target_type 1
- protein 119
sequence_status 1
- pending_manual_supp · 119 ✖
measurement_class 1
- intrinsic · 119 ✖
binding_constant_type 1
- Kd 119
| 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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 | |||||||||
| 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 | |||||
| 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 | |||||
| 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 | ||||||
| 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 | |||||||||
| 536 | tetracycline | protein | Q14728 | TC aptamer | 770.0 pM | -9.114 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 25517161 | 10.1016/j.bpj.2014.11.001 | dissociation constant Kd of 770 pM ([Mg 2 þ ] 1⁄4 10 mM) | elsevier_step2c | |||||||||
| 54 | von Willebrand factor A1-domain | protein | P04275 | Pr-DsDsDs-40 | 1.03 nM | -8.987 | 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 | Pr-DsDsDs-40 ( K D = 1.03 nM) | step2c_literal_v3 | |||||
| 664 | PD-L1 | protein | Q9NZQ7 | 8-60 | 1.4 nM | -8.854 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 34711320 | 10.1016/j.aca.2021.339066 | 8 e 60, a representative aptamer with high af fi nity (KD 1⁄4 1.4 nM determined by SPR) | elsevier_step2c | |||||||||
| 108 | thrombin | protein | P00734 | T.7 | 1.5 nM | -8.824 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | binding buffer supplemented with 0.05% of Tween-20 | DNA | 37798416 | 10.1038/s41587-023-01973-8 | T.7 exhibited the strongest binding signal with a 1.5 nM K d | step2c_literal_v3 | |||||||
| 614 | human α-Thrombin | protein | P00734 | B1 | 3.4 nM | -8.469 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM) | elsevier_step2c | |||||||||
| 615 | human α-Thrombin | protein | P00734 | B2 | 5.0 nM | -8.301 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM) | elsevier_step2c | |||||||||
| 710 | sST2 | protein | P30874 | sS9_P | 5.6 nM | -8.252 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 37992929 | 10.1016/j.ijbiomac.2023.128295 | in case of sS9, parent aptamer has outperformed its truncated counterpart in terms of affinity as it has shown higher affinity (Kd ~5.6 nM). | elsevier_step2c | |||||||||
| 603 | human α-Thrombin | protein | P00734 | A2 | 6.3 nM | -8.201 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for SCORE (b-nd analysis) the best are A2 (6.3 nM) | elsevier_step2c | |||||||||
| 609 | human α-Thrombin | protein | P00734 | A3 | 6.9 nM | -8.161 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for SCORE (b-nd analysis) the best are A2 (6.3 nM) and A3 (6.9 nM) | elsevier_step2c | |||||||||
| 139 | PTK7 | protein | Q13308 | 4AsF | 7.2 nM | -8.143 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | SPR | 310.15 | 7.4 | 1 × DPBS | 5.0 | DNA | SF at positions A23, A24, A25, A26 | 41065179 | 10.1021/jacs.5c11823 | 4AsF, which exhibited a 10-fold reduction compared to 4APS (0.77 vs 7.20 nM) | step2c_literal_v3 | |||
| 556 | VEGF165 | protein | P15692 | cot-pega | 7.33 nM | -8.135 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 26956592 | 10.1016/j.jconrel.2016.03.006 | The K D of cot-pega for VEGF was 7.33 nM (Fig. 1b) | elsevier_step2c | |||||||||
| 616 | human α-Thrombin | protein | P00734 | B3 | 7.6 nM | -8.119 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM) | elsevier_step2c | |||||||||
| 605 | human α-Thrombin | protein | P00734 | A3 | 8.0 nM | -8.097 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | For BLI it was found that aptamer A3 (8 nM and 25.5 nM) is the best binder | elsevier_step2c | |||||||||
| 92 | Okadaic Acid | protein | O95232 | OA-LC2-TF | 8.735 nM | -8.059 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | 7.5 | 50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5) | 2.0 | DNA | terminal fixation with GC-rich sequences | 36322695 | 10.1021/acs.analchem.2c02653 | The terminal-fixed OA-LC2 (OA-LC2-TF) exhibited a K d of 8.735 ± 0.606 nM | step2c_literal_v3 | ||||
| 613 | human α-Thrombin | protein | P00734 | B1 | 9.2 nM | -8.036 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | For SCORE (Anabel analysis) the best is B1 (9.2 nM) | elsevier_step2c | |||||||||
| 557 | 25-HydroxyvitaminD3 | protein | A0A0C5B5G6 | VDBA14 | 11.0 nM | -7.959 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 27520502 | 10.1016/j.bios.2016.08.011 | the dissociation constants (Kd) of the VDBA14 was estimated to be 11 nM based on a non-linear regression method. | elsevier_step2c | |||||||||
| 572 | CTLA-4 | protein | P16410 | aptCTLA-4 | 11.84 nM | -7.927 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 28918052 | 10.1016/j.omtn.2017.08.006 | dissociation constant (Kd) being 11.84 nM | elsevier_step2c | |||||||||
| 101 | thrombin | protein | P00734 | Uyne A - AUyne | 12.16 nM | -7.915 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | buffer used for the bead-based selection, which contains Tween-20 | DNA | 5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end) | 37531184 | 10.1021/acschembio.3c00183 | U yne A - AUyne | 12.16 ± 0.02 | step2c_literal_v3 | ||||||
| 711 | sST2 | protein | P30874 | sS9_P | 13.0 nM | -7.886 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 37992929 | 10.1016/j.ijbiomac.2023.128295 | The best performing aptamer candidate sS9_P (80mer) has shown affinity in low nanomolar range (~5.6 nM in ALISA and ~13 nM in ITC) | elsevier_step2c | |||||||||
| 631 | Bisphenol A | protein | O75897 | 38-mer BPA aptamer | 13.17 nM | -7.88 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 32113141 | 10.1016/j.foodchem.2020.126459 | The K d values of the 63-mer, 38-mer, 12-mer and 23-mer aptamers were determined by using MST experiments, which were 491.69 nM, 13.17 nM, 27.05 nM and 1190.61 nM | elsevier_step2c | |||||||||
| 100 | thrombin | protein | P00734 | Uyne A - Uyne Uyne | 13.96 nM | -7.855 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | buffer used for the bead-based selection, which contains Tween-20 | DNA | 5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end) | 37531184 | 10.1021/acschembio.3c00183 | U yne A - U yne U yne | 13.96 ± 0.03 | step2c_literal_v3 | ||||||
| 641 | hexahistidine peptide | protein | AptHis-1 | 15.0 nM | -7.824 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 32739349 | 10.1016/j.ab.2020.113893 | the Kd was as low as 15 nM (Table S1) | elsevier_step2c | ||||||||||
| 642 | hexahistidine peptide | protein | AptHis-2 | 15.0 nM | -7.824 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 32739349 | 10.1016/j.ab.2020.113893 | the Kd was as low as 15 nM (Table S1) | elsevier_step2c | ||||||||||
| 643 | hexahistidine peptide | protein | AptHis-3 | 15.0 nM | -7.824 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 32739349 | 10.1016/j.ab.2020.113893 | the Kd was as low as 15 nM (Table S1) | elsevier_step2c | ||||||||||
| 95 | Dinophysistoxin | protein | DTX-SL1-TF | 15.45 nM | -7.811 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | 7.5 | 50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5) | 2.0 | DNA | terminal fixation | 36322695 | 10.1021/acs.analchem.2c02653 | DTX-SL1-TF showed a K d of 15.45 ± 1.92 nM | step2c_literal_v3 | |||||
| 612 | human α-Thrombin | protein | P00734 | B1 | 15.7 nM | -7.804 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM) | elsevier_step2c | |||||||||
| 604 | human α-Thrombin | protein | P00734 | A2 | 17.0 nM | -7.77 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM) | elsevier_step2c | |||||||||
| 617 | human α-Thrombin | protein | P00734 | B3 | 17.6 nM | -7.754 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM) | elsevier_step2c | |||||||||
| 551 | GTX1/4 | protein | GO18-T-d | 17.7 nM | -7.752 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | abstract | 26802576 | 10.1016/j.bios.2016.01.032 | we truncated GTX1/4 aptamer and obtained the aptamer core sequence with a higher K d of 17.7 nM. | elsevier_step2c | ||||||||||
| 94 | Dinophysistoxin | protein | DTX-SL1 | 21.75 nM | -7.663 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | 7.5 | 50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5) | 2.0 | DNA | 36322695 | 10.1021/acs.analchem.2c02653 | DTX-SL1 showed the lowest K d at 21.75 ± 1.42 nM | step2c_literal_v3 | ||||||
| 552 | GTX1/4 | protein | GO18-T-d | 21.9 nM | -7.66 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 26802576 | 10.1016/j.bios.2016.01.032 | Therefore, we further removed inactive nucleotides from GO18-T-a and obtained the core aptamer sequence GO18-T-d with a K d of 21.9 nM | elsevier_step2c | ||||||||||
| 707 | prometryn | protein | P60-1 | 23.0 nM | -7.638 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 37453395 | 10.1016/j.talanta.2023.124838 | The Kd value of P60-1 aptamer for prometryn was approximately 23 nM | elsevier_step2c | ||||||||||
| 665 | 16mer peptide from collagen XI alpha 1 chain | protein | D1 | 25.0 nM | -7.602 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 34815029 | 10.1016/j.aca.2021.339206 | The K d values were identical (about 25 nM) | elsevier_step2c | ||||||||||
| 666 | 16mer peptide from collagen XI alpha 1 chain | protein | C1 | 25.0 nM | -7.602 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 34815029 | 10.1016/j.aca.2021.339206 | The K d values were identical (about 25 nM) | elsevier_step2c | ||||||||||
| 606 | human α-Thrombin | protein | P00734 | A3 | 25.5 nM | -7.593 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | For BLI it was found that aptamer A3 (8 nM and 25.5 nM) is the best binder | elsevier_step2c | |||||||||
| 539 | Staphylococcal enterotoxin B | protein | P01911 | A2 | 26.0 nM | -7.585 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 25624325 | 10.1128/AAC.04414-14 | A2 and A11 both bound with high affinity to SEB, with dissociation constants of 26 nM and 64 nM, respectively | elsevier_step2c | |||||||||
| 602 | human α-Thrombin | protein | P00734 | A2 | 26.4 nM | -7.578 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | for iRIf aptamer A2 is the best (26.4 nM) | elsevier_step2c | |||||||||
| 632 | Bisphenol A | protein | O75897 | 12-mer BPA aptamer | 27.05 nM | -7.568 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 32113141 | 10.1016/j.foodchem.2020.126459 | The K d values of the 63-mer, 38-mer, 12-mer and 23-mer aptamers were determined by using MST experiments, which were 491.69 nM, 13.17 nM, 27.05 nM and 1190.61 nM | elsevier_step2c | |||||||||
| 608 | human α-Thrombin | protein | P00734 | A3 | 34.6 nM | -7.461 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | For SCORE (Anabel analysis) the best is B1 (9.2 nM) and the poorest A3 (34.6 nM) | elsevier_step2c | |||||||||
| 720 | Zearalenone | protein | Q6UWP2 | M1 | 35.83 nM | -7.446 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 38608399 | 10.1016/j.foodchem.2024.139127 | resulting in a slightly higher Kd value of 35.83 nM | elsevier_step2c | |||||||||
| 611 | human α-Thrombin | protein | P00734 | B1 | 37.0 nM | -7.432 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 31129134 | 10.1016/j.ab.2019.05.012 | and the poorest B1 (37 nM) | elsevier_step2c | |||||||||
| 731 | ceftiofur | protein | Apt-9 | 37.68 nM | -7.424 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_manual_supp | text | 40203705 | 10.1016/j.bios.2025.117446 | Kd values for the binding of Apt-9 to cefapirin, cefquizime, and ceftiofur were ... 37.68 nM | elsevier_step2c | ||||||||||
| 99 | thrombin | protein | P00734 | TA-AT | 38.7 nM | -7.412 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_manual_supp | BLI | buffer used for the bead-based selection, which contains Tween-20 | DNA | Biotin (5' end) | 37531184 | 10.1021/acschembio.3c00183 | TA - AT | 38.7 ± 0.5 | 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';