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- W2013581203 abstract "CTRC-AACR San Antonio Breast Cancer Symposium: 2008 AbstractsAbstract #2063 Collagen serves as a structural scaffold and a barrier between tissues, and thus collagen catabolism (collagenolysis) is required to be a tightly regulated process in normal physiology. In turn, the destruction or damage of collagen during pathological states plays a role in tumor growth and invasion, cartilage degradation, or atherosclerotic plaque formation. Only a small number of proteases have been identified capable of efficient processing of triple-helical regions of collagens. Several members of the zinc metalloenzyme family, specifically matrix metalloproteinases (MMPs), possess collagenolytic activity, and at least one of these (MMP-1) has been strongly implicated in the progression of breast cancer. The present study has utilized triple-helical peptide (THP) substrates and inhibitors to dissect MMP-1 collagenolytic behavior. Analysis of MMP-1/THP interactions by hydrogen/deuterium exchange mass spectrometry (HDX MS) in combination with site-specific mutagenesis and enzyme kinetic assays have allowed us to identify non-catalytic sites in MMP-1 that participate in collagenolysis. As we have recently demonstrated [J. Am. Chem. Soc. 129, 10408 (2007)], non-catalytic sites can be utilized to create THP inhibitors that target proteases implicated in cancer progression while sparing proteases with host-beneficial functions.Citation Information: Cancer Res 2009;69(2 Suppl):Abstract nr 2063." @default.
- W2013581203 created "2016-06-24" @default.
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- W2013581203 date "2009-01-15" @default.
- W2013581203 modified "2023-09-27" @default.
- W2013581203 title "Identification of non-catalytic matrix metalloproteinase 1 residues that participate in collagenolysis." @default.
- W2013581203 doi "https://doi.org/10.1158/0008-5472.sabcs-2063" @default.
- W2013581203 hasPublicationYear "2009" @default.
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