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
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
517,Hemagglutinin (HA) protein of AIV H5N1 (A/Vietnam/1203/04),protein,,Aptamer sequence (2),GTGTGCATGGATAGCACGTAACGGTGTAGTAGATACGTGCGGGTAGGAAGAAAGGGAAATAGTTGTCCTGTTG,4.65 nM,-8.333,intrinsic,KD,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,23523887,10.1016/j.jviromet.2013.03.006,"the KD (dissociation constants) was 4.65 nM, indicating strong binding between the HA protein and the selected aptamer.",elsevier_step2c
141,PDGF-C,protein,P01127,α-PC,CTACTGTGTGATGTCTGAGAGCAGCGTCTAAACGAACAAGCGAACCTATGCACAGAGGACAGTACATCAGACAC,33.0 nM,-7.481,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,,42138517,10.1167/iovs.67.5.36,SPR analysis demonstrated that the α -PC aptamer bound tightly to mouse PDGF-C with a high affinity ( KD = 33 nM,step2c_literal_v3