Analysis of the interaction of TIMP-2 and MMPs: engineering the changes.
School of Biological Sciences, University of East Anglia, Norwich, UK. m.hutton@uea.ac.uk
M
M
Hutton
G S
GS
Butler
B A
BA
Wattam
F
F
Willenbrock
R A
RA
Williamson
G
G
Murphy
D001665:Binding Sites; D017364:Collagenases / Q000378:metabolism; D018093:Gelatinases / Q000378:metabolism; D006801:Humans; D053509:Matrix Metalloproteinase 13; D020778:Matrix Metalloproteinase 2; D019278:Matrix Metalloproteinase 3 / Q000378:metabolism; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases / Q000737:chemistry / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D019716:Tissue Inhibitor of Metalloproteinase-2 / Q000737:chemistry* / Q000378:metabolism*
D011994:Recombinant Proteins; D019716:Tissue Inhibitor of Metalloproteinase-2; D017364:Collagenases; D018093:Gelatinases; C507079:MMP13 protein, human; D053509:Matrix Metalloproteinase 13; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2