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Report error Found 592 of affinity data for UniProtKB/TrEMBL: Q13526
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184825(Ac-Lys(N-epsilon-biotinoyl)-Ala-Ala-Bth-D-Thr(PO3H...)
Affinity DataKi:  1.20nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184823(Ac-Lys(N-epsilon-biotinoyl)-Ala-Ala-Bip-Thr(PO3H2)...)
Affinity DataKi:  4.80nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314714((R)-N-(1-(3-fluorophenyl)-3-hydroxypropan-2-yl)ben...)
Affinity DataKi:  6nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34012(3-fluorophenylalanine derivative, 21b)
Affinity DataKi:  6nM ΔG°:  -45.4kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314706((R)-2-(2-naphthamido)-5-(3-fluorophenyl)pent-4-eno...)
Affinity DataKi:  6nMAssay Description:Inhibition of N-terminal His tagged human Pin1 expressed in Escherichia coli BL21 (DE3) using Suc-Ala-Glu-Pro-Phe-4-nitroanilide as substrate preincu...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34012(3-fluorophenylalanine derivative, 21b)
Affinity DataKi:  6nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34011(3-fluorophenylalanine derivative, 21a)
Affinity DataKi:  8nM ΔG°:  -44.7kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056217(CHEMBL3353369)
Affinity DataKi:  12nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184841(Ac-Phe-D-Thr(PO3H2)-Pip-Nal-Gln-NH2 | CHEMBL436759)
Affinity DataKi:  18.3nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50552327(CHEMBL4751817)
Affinity DataKi:  20nMAssay Description:Inhibition of GST-tagged Pin1 (unknown origin) using Suc-Ala-pSer-Pro-Phe-pNA as substrate preincubated with enzyme for 12 hrs followed by substrate ...More data for this Ligand-Target Pair
Ligand InfoPC cidPC sid
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34013(3-methylphenylalanine derivative, 22a)
Affinity DataKi:  32nM ΔG°:  -41.3kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50552328(CHEMBL4750217)
Affinity DataKi:  48nMAssay Description:Inhibition of GST-tagged Pin1 (unknown origin) using Suc-Ala-pSer-Pro-Phe-pNA as substrate preincubated with enzyme for 12 hrs followed by substrate ...More data for this Ligand-Target Pair
Ligand InfoPC cidPC sid
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50437704(CHEMBL2409078)
Affinity DataKi:  50nMAssay Description:Competitive inhibition of Pin1 (unknown origin) by Lineweaver-Burk plot analysisMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34014(3-methylphenylalanine derivative, 22b)
Affinity DataKi:  57nM ΔG°:  -40.0kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056216(CHEMBL3353368)
Affinity DataKi:  75nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056208(CHEMBL3322220)
Affinity DataKi:  76nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34015(2,3-difluorophenylalanine derivative, 23a)
Affinity DataKi:  78nM ΔG°:  -39.2kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056214(CHEMBL3322219)
Affinity DataKi:  80nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34016(2,3-difluorophenylalanine derivative, 23b)
Affinity DataKi:  89nM ΔG°:  -38.9kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34009(naphthalene carboxamide, 18a)
Affinity DataKi:  100nM ΔG°:  -38.6kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056211(CHEMBL3322225)
Affinity DataKi:  138nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056204(CHEMBL3322215)
Affinity DataKi:  173nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314715((R)-N-(1-hydroxy-3-phenylpropan-2-yl)benzo[b]thiop...)
Affinity DataKi:  179nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34010(benzothiophene carboxamide, 18b)
Affinity DataKi:  179nM ΔG°:  -37.2kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184830(Ac-Lys(N-epsilon-biotinoyl)-Ala-Ala-Bth-Thr(PO3H2)...)
Affinity DataKi:  183nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056205(CHEMBL3322216)
Affinity DataKi:  189nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056219(CHEMBL3322230)
Affinity DataKi:  196nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50381013(CHEMBL2017129)
Affinity DataKi:  200nMAssay Description:Inhibition of human Pin1More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50345548(CHEMBL1784538 | [13C,15N-Y,P,V]cyclic CRYPEVEIC | ...)
Affinity DataKi:  200nMAssay Description:Competitive inhibition of human GST-tagged-Pin1 PPIase activity using WFYpSPR-pNA as substrate by Michaelis-Menton equationMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184834(Ac-Bth-Thr(PO3H2)-Pip-Nal-Gln-NH2 | CHEMBL380685)
Affinity DataKi:  258nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056220(CHEMBL3322295)
Affinity DataKi:  320nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056215(CHEMBL3353367)
Affinity DataKi:  400nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056207(CHEMBL3322218)
Affinity DataKi:  424nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50345548(CHEMBL1784538 | [13C,15N-Y,P,V]cyclic CRYPEVEIC | ...)
Affinity DataKi:  520nMAssay Description:Inhibition of human GST-tagged-Pin1 PPIase activity using Suc-AEPF-pNA as substrate by Michaelis-Menton equationMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34008(amide, 17c)
Affinity DataKi:  525nM ΔG°:  -34.6kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50184838(Ac-Phe-Thr(PO3H2)-Pip-Nal-Gln-NH2 | CHEMBL383244)
Affinity DataKi:  547nMAssay Description:Inhibition of human Pin1 PPIase Activity by protease free PPIase assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056203(CHEMBL3322296)
Affinity DataKi:  580nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50518736(CHEMBL4526940)
Affinity DataKi:  625nMAssay Description:Inhibition of recombinant Pin1 (unknown origin) using Suc-AEPF-MCA as substrate preincubated followed by substrate addition and measured after 60 to ...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056206(CHEMBL3322217)
Affinity DataKi:  780nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34005(pipecolate deriv., 12b)
Affinity DataKi:  800nM ΔG°:  -33.6kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM31883(9-cis-retinoic acid (9cRA) | ALL-TRANS-RETINOIC AC...)
Affinity DataKi:  820nMAssay Description:Inhibition of GST-tagged Pin1 (unknown origin) using Suc-Ala-pSer-Pro-Phe-pNA, Suc-Ala-Glu-Pro-Phe-pNA or Suc-Ala-Ala-Pro-Phe-pNA as substrate preinc...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314706((R)-2-(2-naphthamido)-5-(3-fluorophenyl)pent-4-eno...)
Affinity DataKi:  890nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056210(CHEMBL3322222)
Affinity DataKi:  1.00E+3nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056218(CHEMBL3322229)
Affinity DataKi:  1.36E+3nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50518734(CHEMBL4467081)
Affinity DataKi:  1.37E+3nMAssay Description:Irreversible inhibition of Pin1 (unknown origin) using suc-Ala-Glu-Pro-Phe-pNA as substrate preincubated for 10 mins followed by substrate addition a...More data for this Ligand-Target Pair
Ligand InfoPC cidPC sid
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM34003(pipecolate deriv., 11)
Affinity DataKi:  1.70E+3nM ΔG°:  -31.8kJ/molepH: 7.5 T: 15°CAssay Description:The cis/trans conversion of cis-Suc-AEPFpNA peptide by the PPIase led to the cleavage of para nitroaniline by subtilisin which was monitored at 390 n...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314705((2R,4E)-2-[(naphthalen-2-ylcarbonyl)amino]-5-pheny...)
Affinity DataKi:  1.80E+3nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314682((R)-2-(2-naphthamido)-3-(3-(trifluoromethyl)phenyl...)
Affinity DataKi:  1.80E+3nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50314701((R)-2-(2-naphthamido)-5-(3-fluorophenyl)pent-4-yno...)
Affinity DataKi:  1.87E+3nMAssay Description:Displacement of WFYpSPFLE from human Pin1 catalytic domain after 10-20 mins by fluorescence polarization assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1(Human)
Max Planck Research Unit For Enzymology of Protein Folding

Curated by ChEMBL
LigandPNGBDBM50056212(CHEMBL3322224)
Affinity DataKi:  1.90E+3nMAssay Description:Inhibition of Pin1 (unknown origin)More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
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