B
Bryan D. Smith
Researcher at University of Wisconsin-Madison
Publications - 48
Citations - 4826
Bryan D. Smith is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Tumor microenvironment & Kinase. The author has an hindex of 21, co-authored 44 publications receiving 4459 citations. Previous affiliations of Bryan D. Smith include University of Nebraska–Lincoln & University of Texas MD Anderson Cancer Center.
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Journal ArticleDOI
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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The Soluble Catalytic Domain of Membrane Type 1 Matrix Metalloproteinase Cleaves the Propeptide of Progelatinase A and Initiates Autoproteolytic Activation REGULATION BY TIMP-2 AND TIMP-3
TL;DR: The basic mechanism of MT1-MMP action on progelatinase A is demonstrated and the reason for the lack of inhibition by TIMP-1 previously demonstrated in cell-based activation studies is demonstrated.
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Membrane‐Type Matrix Metalloproteinases 1 and 2 Exhibit Broad‐Spectrum Proteolytic Capacities Comparable to Many Matrix Metalloproteinases
Marie-Pia d'Ortho,Horst Will,Susan J. Atkinson,Georgina S. Butler,Anthea J. Messent,Jelena Gavrilovic,Bryan D. Smith,Rupert Timpl,Luciano Zardi,Gillian Murphy +9 more
TL;DR: Results demonstrate that, in addition to their ability to activate other MMP, MT-MMP degrade a number of extracellular matrix macromolecules, and their location at the surface of cells implies that they could play a significant role in the modulation of cell-matrix interactions.
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The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction.
Vera Knäuper,Susan Cowell,Bryan D. Smith,Carlos López-Otín,Mark O'Shea,Helen Morris,Luciano Zardi,Gillian Murphy +7 more
TL;DR: Kinetic analysis of the mechanism of inhibition of wild-type and Δ249-451 collagenase-3 by wild- type and mutant tissue inhibitors of metalloproteinase (TIMPs) revealed that the association rates for complex formation were influenced by both N- and C-terminal domain interactions.