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).
49 rows where sequence_status = "pending_supp_oa" sorted by kd_log10_molar
This data as json, CSV (advanced)
Suggested facets: target_name_canonical, target_uniprot, source_origin, assay_temperature_k, assay_buffer, aptamer_modifications, source_pmid, doi, source_db
assay_method 6
- flow_cytometry 19
- BLI 9
- SPR 5
- ITC 1
- MST 1
- fluorescence 1
verification_level 2
measurement_class 2
- intrinsic 25
- non_intrinsic 24
tier 1
- Gold 49
sequence_status 1
- pending_supp_oa · 49 ✖
binding_constant_type 1
- Kd 49
| 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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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 | |||||
| 724 | Heparin-binding protein | protein | P21246 | Apt-13 | 1.04 nM | -8.983 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 38675537 | 10.3390/molecules29081717 | The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively | elsevier_step2c | |||||||||
| 328 | ATP | protein | P00846 | Huizenga-Szostak ATP aptamer | 1.3e-09 M | -8.886 | intrinsic | Kd | Gold | v4 | multi_agent_verified | pending_supp_oa | fluorescence | DNA | 25170558 | 10.1021/bc500286r | binding a ffi nity can be tuned over 4 orders of magnitude (1.3 nM -203 μ M) | step2c_acs_v1 | ||||||||
| 723 | Heparin-binding protein | protein | P21246 | Apt-02 | 1.44 nM | -8.842 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 38675537 | 10.3390/molecules29081717 | The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively | elsevier_step2c | |||||||||
| 202 | CD8a | protein | P01732 | A3 | 1.9 nM | -8.721 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9 nM, respectively | step2c_literal_v3 | ||||||||
| 203 | CD8a | protein | P01732 | A8 | 2.4 nM | -8.62 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9 nM, respectively | step2c_literal_v3 | ||||||||
| 226 | transferrin receptor 1 | protein | P02786 | JBA8.26 | 3.3 nM | -8.481 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 35875870 | 10.1021/jacs.2c05349 | JBA8.26 bound TfR1 hi H9 T-lymphoma cells with an apparent K D of 3.3 ± 0.6 nM | step2c_literal_v3 | ||||||||
| 250 | Mouse thrombin | protein | Pse08-08 | 4.2 nM | -8.377 | 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) | 7.35 10^5 | 3.06 10^-3 | 4.2 | step2c_literal_v3 | ||||||
| 224 | transferrin receptor 1 | protein | P02786 | JBA8.1 | 5.5 nM | -8.26 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | fluorescein-labeled | 35875870 | 10.1021/jacs.2c05349 | JBA8.1 has an apparent binding affinity (K D ) of 5.5 ± 1.2 nM | step2c_literal_v3 | |||||||
| 63 | CD8a | protein | P01732 | A8 | 5.59 nM | -8.253 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | binding buffer with 0.01% Tween 20 | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2, 14.7 ± 0.1 and 5.59 ± 0.11 nM, respectively | step2c_literal_v3 | ||||||
| 248 | Mouse thrombin | protein | Lin08-08 | 6.7 nM | -8.174 | 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) | 6.41 10^5 | 4.30 10^-3 | 6.7 | step2c_literal_v3 | ||||||
| 87 | transferrin receptor 1 | protein | P02786 | JBA8.26 | 6.87 nM | -8.163 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | DNA | 35875870 | 10.1021/jacs.2c05349 | Using BLI, JBA8.26 was found to bind immobilized TfR1 with a K D of 6.87 ± 0.04 nM | step2c_literal_v3 | ||||||||
| 689 | EN2 | protein | P19622 | EBA | 8.26 nM | -8.083 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35798816 | 10.1038/s41598-022-15556-1 | EBA had K d = 8.26 nM (R 2 = 0.971) | elsevier_step2c | |||||||||
| 225 | transferrin receptor 1 | protein | P02786 | tJBA8.1 | 10.9 nM | -7.963 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 35875870 | 10.1021/jacs.2c05349 | versus that of 10.9 ± 2.4 nM for tJBA8.1 | step2c_literal_v3 | ||||||||
| 697 | β-conglutin | protein | unmodified β-CBA II aptamer | 11.1 nM | -7.955 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 36354481 | 10.3390/bios12110972 | with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively. | elsevier_step2c | ||||||||||
| 62 | CD8a | protein | P01732 | A3 | 14.7 nM | -7.833 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | binding buffer with 0.01% Tween 20 | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2, 14.7 ± 0.1 and 5.59 ± 0.11 nM, respectively | step2c_literal_v3 | ||||||
| 201 | CD8a | protein | P01732 | A1 | 18.3 nM | -7.738 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9 nM, respectively | step2c_literal_v3 | ||||||||
| 698 | β-conglutin | protein | biotinylated dUTPs aptamer | 18.5 nM | -7.733 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 36354481 | 10.3390/bios12110972 | with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively. | elsevier_step2c | ||||||||||
| 61 | CD8a | protein | P01732 | A1 | 20.1 nM | -7.697 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | binding buffer with 0.01% Tween 20 | DNA | 31209354 | 10.1038/s41551-019-0411-6 | the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2, 14.7 ± 0.1 and 5.59 ± 0.11 nM, respectively | step2c_literal_v3 | ||||||
| 677 | saxitoxin | protein | O60939 | 45e | 21.2 nM | -7.674 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35324725 | 10.3390/toxins14030228 | aptamer 45e with a K d value of 21.2 nM | elsevier_step2c | |||||||||
| 128 | CD117 | protein | P10721 | Apta02 | 21.8 nM | -7.662 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b). | step2c_literal_v3 | |||||||
| 302 | prostate-cancer-derived small extracellular vesicles | cell/EV | Q99523 | seq25 | 24.02 nM | -7.619 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | SPR | PBST buffer | DNA | 5'-FAM | 41646885 | 10.1016/j.omtn.2026.102836 | The affinity of seq25 for positive selection was significantly higher than that of the other aptamers, with a KD of 24.02 nM | step2c_literal_v3 | ||||||
| 86 | transferrin receptor 1 | protein | P02786 | tJBA8.1 | 25.11 nM | -7.6 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | DNA | biotinylated | 35875870 | 10.1021/jacs.2c05349 | tJBA8.1 bound the TfR1 protein with a K D value of 25.11 ± 0.19 nM | step2c_literal_v3 | |||||||
| 227 | transferrin receptor 1 | protein | P02786 | tJBA8.1 | 25.6 nM | -7.592 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | DNA | 35875870 | 10.1021/jacs.2c05349 | compared to tJBA8.1's apparent K D of 25.6 ± 13.0 nM for these cells | step2c_literal_v3 | ||||||||
| 716 | Enrofloxacin | protein | P05177 | ENR-Apt 6 | 35.08 nM | -7.455 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 38540931 | 10.3390/foods13060941 | Figure 4A shows the non-linear fitting curve of ENR-Apt 6, with a Kd value of 35.08 nM. | elsevier_step2c | |||||||||
| 222 | CD20 | protein | P11836 | WB1-CD20 | 73.0 nM | -7.137 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 298.15 | Cell Suspension Buffer (CSB) | DNA | 5'-FAM | 35829681 | 10.1021/acs.biochem.2c00105 | The apparent affinities of WB1-CD20 and WB2-CD20 were calculated as 73 nM and 163 nM at 25°C, respectively | step2c_literal_v3 | |||||
| 97 | N-acetylneuraminic acid | protein | Q8NFW8 | Neu5Ac aptamer | 91.0 nM | -7.041 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | ITC | 310.15 | 7.4 | 1× aptamer binding buffer (50 mM Tris-HCl, 5 mM KCl, 100 mM NaCl and 1 mM MgCl2, pH 7.4) | 1.0 | DNA | 37217750 | 10.1038/s41587-023-01801-z | To validate ARPLA, we first determined the binding affinity ( K d ) of the Neu5Ac aptamer by isothermal titration calorimetry (ITC) as 91 nM (Extended Data Fig. 2a,b) | step2c_literal_v3 | ||||
| 687 | mouse IL-2 | protein | M20 | 91.0 nM | -7.041 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35756119 | 10.1016/j.heliyon.2022.e09721 | The results indicated that the af fi nity of the M20 aptamer was greater than the M15, and its predicted Kd was 91 nM | elsevier_step2c | ||||||||||
| 678 | saxitoxin | protein | O60939 | 75a | 136.0 nM | -6.866 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35324725 | 10.3390/toxins14030228 | aptamer 75a with a K d value of 136 nM | elsevier_step2c | |||||||||
| 220 | CD19 | protein | P15391 | WB15-CD19 | 153.0 nM | -6.815 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 298.15 | Cell Suspension Buffer (CSB) | DNA | 5'-FAM | 35829681 | 10.1021/acs.biochem.2c00105 | At 25 °C, WB15-CD19 showed an apparent affinity of 153 nM | step2c_literal_v3 | |||||
| 223 | CD20 | protein | P11836 | WB2-CD20 | 163.0 nM | -6.788 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 298.15 | Cell Suspension Buffer (CSB) | DNA | 5'-FAM | 35829681 | 10.1021/acs.biochem.2c00105 | The apparent affinities of WB1-CD20 and WB2-CD20 were calculated as 73 nM and 163 nM at 25°C, respectively | step2c_literal_v3 | |||||
| 221 | CD19 | protein | P15391 | WB17-CD19 | 187.0 nM | -6.728 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 298.15 | Cell Suspension Buffer (CSB) | DNA | 5'-FAM | 35829681 | 10.1021/acs.biochem.2c00105 | and WB17-CD19 showed an apparent affinity of 187 nM (Figure S12A-B). | step2c_literal_v3 | |||||
| 419 | cortisol | protein | P08185 | CSS.3 | 2.4000000000000003e-07 M | -6.62 | intrinsic | Kd | Gold | v4 | multi_agent_verified | pending_supp_oa | 38270529 | 10.1021/acssensors.3c02004 | Our own internal work confirmed that CSS.3 had the best binding affinity in binding buffer with a K D of 240 nM | step2c_acs_v1 | ||||||||||
| 673 | kanamycin | protein | Apt 1/Apt 2 (split aptamers) | 247.0 nM | -6.607 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35316405 | 10.1007/s00604-022-05235-3 | With the (GlcN)5 added in the binding buffer, the Kd was measured to be 247 nM | elsevier_step2c | ||||||||||
| 672 | kanamycin | protein | Apt 1/Apt 2 (split aptamers) | 304.0 nM | -6.517 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35316405 | 10.1007/s00604-022-05235-3 | The split aptamers exhibited high affinity towards the kanamycin, with an Kd of 304 nM. | elsevier_step2c | ||||||||||
| 263 | H-6 cells | cell/EV | O14756 | Apta25 | 0.42 µM | -6.377 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | H-6 cells showed binding with Apta25 ( K D value-0.42 ± 0.093 µ m) | step2c_literal_v3 | |||||||
| 688 | mouse IL-2 | protein | M15 | 600.0 nM | -6.222 | intrinsic | Kd | Gold | elsevier | extraction_verified | pending_supp_oa | text | 35756119 | 10.1016/j.heliyon.2022.e09721 | The calculation of the dissociation constant predicted 91 and 600 nM Kd for M20 and M15, respectively | elsevier_step2c | ||||||||||
| 261 | K-1 cells | cell/EV | O60814 | Apta30 | 0.66 µM | -6.18 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta30 ( K D -0.66 ± 0.12 µ m) | step2c_literal_v3 | |||||||
| 129 | CD117 | protein | P10721 | Apta04 | 1100.0 nM | -5.959 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b). | step2c_literal_v3 | |||||||
| 264 | H-6 cells | cell/EV | O14756 | Apta30 | 1.107 µM | -5.956 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | H-6 cells showed binding with ... Apta30 ( K D -1.107 ± 0.208 µ m) | step2c_literal_v3 | |||||||
| 131 | CD123 | protein | O75794 | Apta25 | 1.16 µM | -5.936 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | DNA | 40487293 | 10.1002/adfm.202425394 | BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information). | step2c_literal_v3 | |||||||
| 262 | K-1 cells | cell/EV | O60814 | Apta25 | 1.358 µM | -5.867 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta25 ( K D value-1.358 ± 0.201 µ m) | step2c_literal_v3 | |||||||
| 259 | K-1 cells | cell/EV | O60814 | Apta02 | 1.821 µM | -5.74 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta02 ( K D value-1.821 ± 0.117 µ m) | step2c_literal_v3 | |||||||
| 260 | K-1 cells | cell/EV | O60814 | Apta04 | 1.867 µM | -5.729 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | Apta04 ( K D value-1.867 ± 0.19 µ m) | step2c_literal_v3 | |||||||
| 121 | CTNNA1 | protein | P35221 | EA2 | 2.07 µM | -5.684 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | MST | DNA | biotinylated | 40265971 | 10.1002/advs.202411930 | The K d values (2.07 ± 0.60 µ M) obtained from MST assay (Figure 2l) further corroborated the specific binding between CTNNA1 and EA2. | step2c_literal_v3 | |||||||
| 265 | H-9 cells | cell/EV | Q8IVB4 | Apta02 | 4.93 µM | -5.307 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | H-9 cells showed binding with Apta02 ( K D value-4.93 ± 0.367 µ m) | step2c_literal_v3 | |||||||
| 266 | H-9 cells | cell/EV | Q8IVB4 | Apta04 | 5.402 µM | -5.267 | non_intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | flow_cytometry | 310.15 | DNA | 40487293 | 10.1002/adfm.202425394 | H-9 cells showed binding with ... Apta04 ( K D value-5.402 ± 0.795 µ m) | step2c_literal_v3 | |||||||
| 130 | CD123 | protein | O75794 | Apta30 | 15.6 µM | -4.807 | intrinsic | Kd | Gold | v4 | extraction_verified | pending_supp_oa | BLI | 298.15 | DNA | 40487293 | 10.1002/adfm.202425394 | BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information). | 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';