W
William G. I. Moore
Researcher at University of Alabama at Birmingham
Publications - 7
Citations - 3241
William G. I. Moore is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Matrix metalloproteinase & Collagenase. The author has an hindex of 4, co-authored 7 publications receiving 3192 citations.
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Journal ArticleDOI
Matrix Metalloproteinases: A Review
Henning Birkedal-Hansen,William G. I. Moore,M.K. Bodden,L.J. Windsor,B. Birkedal-Hansen,Arthur A. Decarlo,Jeffrey A. Engler +6 more
TL;DR: The present review discusses in detail the primary structures and the overlapping yet distinct substrate specificities of MMPs as well as the mode of activation of the unique MMP precursors.
Journal ArticleDOI
Monoclonal antibodies to human fibroblast procollagenase. Inhibition of enzymatic activity, affinity purification of the enzyme, and evidence for clustering of epitopes in the NH2-terminal end of the activated enzyme.
B. Birkedal-Hansen,William G. I. Moore,Robert E. Taylor,Ajit S. Bhown,Henning Birkedal-Hansen +4 more
TL;DR: Assignment of epitopes to structural domains within the molecule based on immunoperoxidase staining of Western blots of collagenase and its autocatalytic fragments revealed that 9 of 11 epitopes were clustered in a 169-residue domain, which constitutes the NH2-terminal part of the Mr 46,000/42,000 active enzyme.
Journal ArticleDOI
Characteristics of a 95-kda matrix metalloproteinase produced by mammary carcinoma cells
J. Guy Lyons,B. Birkedal-Hansen,William G. I. Moore,Robert L. O'Grady,Henning Birkedal-Hansen +4 more
TL;DR: This suggests that expression of the Mr 95,000 MMP is regulated differently from that of interstitial collagenase, which is produced by the epithelial cells only in response to specific inductive factor(s) from the myoepithelial-like cells.
Journal ArticleDOI
Use of inhibitory (anti-catalytic) antibodies to study extracellular proteolysis.
Hanning Birkedal-Hansen,B. Birkedal-Hansen,Lester J. Windsor,Hong-Yea Lin,Robert E. Taylor,William G. I. Moore +5 more
TL;DR: The findings permit us to deduce that, at least in culture, the dissolution of fibrin by plasminogen-supplemented HT-1080 cells was mediated by plaeminogen-assisted proteolysis which entailed the extracellular conversion of pl asminogen to plAsmin by cell-derived u-PA, and that the dissolution Of reconstituted type I collagen fibrils by trypsin-supplementsed skin fibroblasts was