Compile Data Set for Download or QSAR
Report error Found 10 of Enz. Inhib. data with enzyme = '72 kDa type IV collagenase' and Substrate = 'Fluorogenic Peptide Substrate'
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11551BDBM11551((3R)-N-hydroxy-2-{[4-(4-methoxyphenyl)phenyl]methy...)
Affinity DataKi:  0.400nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11554BDBM11554((3R)-N-hydroxy-1,1-dioxo-2-{[4-(pyridin-4-yl)pheny...)
Affinity DataKi:  1nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11553BDBM11553((3R)-2-[(4-tert-butyl-1,1-biphenyl-4-yl)methyl]-N-...)
Affinity DataKi:  3.20nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11552BDBM11552((3R)-2-[(4-chloro-1,1-biphenyl-4-yl)methyl]-N-hydr...)
Affinity DataKi: <3.30nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11548BDBM11548(CHEMBL100570 | N-hydroxy-2-[(4-methoxy-1,1-bipheny...)
Affinity DataKi:  3.80nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11546BDBM11546((3R)-N-hydroxy-1,1-dioxo-2-[(4-phenylphenyl)methyl...)
Affinity DataKi:  28.5nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11547BDBM11547(N-hydroxy-1,1-dioxo-2-[2-(4-phenylphenyl)ethyl]-1,...)
Affinity DataKi:  433nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11545BDBM11545(2-(1,1-biphenyl-4-yl)-N-hydroxyisothiazolidine-3-c...)
Affinity DataKi:  667nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11549BDBM11549(2-{[4-(3,5-dichlorophenyl)phenyl]methyl}-N-hydroxy...)
Affinity DataKi: >3.33E+3nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed
Target72 kDa type IV collagenase(Human)
Bristol Myers Squibb

LigandChemical structure of BindingDB Monomer ID 11550BDBM11550(N-hydroxy-2-[(2-methyl-1,1-biphenyl-4-yl)methyl]is...)
Affinity DataKi: >3.33E+3nMAssay Description:The enzymatic activities of MMPs were determined with recombinant human version catalytic domains and a fluorogenic peptide substrate. Fluorescence m...More data for this Ligand-Target Pair
In Depth
Date in BDB:
10/17/2006
Entry Details Article
PubMed