G
Gillian Murphy
Researcher at University of Cambridge
Publications - 375
Citations - 48833
Gillian Murphy is an academic researcher from University of Cambridge. The author has contributed to research in topics: Matrix metalloproteinase & Collagenase. The author has an hindex of 122, co-authored 373 publications receiving 47043 citations. Previous affiliations of Gillian Murphy include University of Miami & University of East Anglia.
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Journal ArticleDOI
Structure and function of matrix metalloproteinases and TIMPs
TL;DR: The members of the MMP family are introduced and their domain structure and function, proenyme activation, the mechanism of inhibition by TIMPs and their significance in physiology and pathology are discussed.
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Metalloproteinase inhibitors: biological actions and therapeutic opportunities.
TL;DR: The concept of the use of the natural inhibitors, such as the TIMPs, in gene based therapies is being assessed in animal models and should provide useful insights into the cell biology of degradative diseases.
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Biochemical Characterization of Human Collagenase-3
TL;DR: Analysis of the substrate specificity of collagenase-3 revealed that soluble type II collagen was preferentially hydrolyzed, while the enzyme was 5 or 6 times less efficient at cleaving type I or III collagen.
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Cellular Mechanisms for Human Procollagenase-3 (MMP-13) Activation EVIDENCE THAT MT1-MMP (MMP-14) AND GELATINASE A (MMP-2) ARE ABLE TO GENERATE ACTIVE ENZYME
Vera Knäuper,Horst Will,Carlos López-Otín,Bryan D. Smith,Susan J. Atkinson,Heather Stanton,Rosalind M. Hembry,Gillian Murphy +7 more
TL;DR: It is established that progelatinase A can considerably potentiate the activation rate of procollagenase-3 by crude plasma membrane preparations from concanavalin A-stimulated fibroblasts, thus confirming the results using purified progelasinase A and MT1-MMP.
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A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases.
TL;DR: In assays of the human matrix metalloproteinases, Mca‐Pro‐ Leu‐Gly‐Leu‐Dpa‐Ala‐Arg‐NH2 is about 50 to 100 times more sensitive than dinitrophenyl‐Pro •Leu •Gly •LeU‐Trp •Ala •d‐Arg •NH2 and continuous assays can be made at enzyme concentrations comparable to those used with macromolecular substrates.