M
Mark D. Sternlicht
Researcher at University of California, San Francisco
Publications - 21
Citations - 8435
Mark D. Sternlicht is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Metastasis & Matrix metalloproteinase. The author has an hindex of 21, co-authored 21 publications receiving 8028 citations.
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Journal ArticleDOI
How Matrix Metalloproteinases Regulate Cell Behavior
Mark D. Sternlicht,Zena Werb +1 more
TL;DR: Recent advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled.
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The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis.
Mark D. Sternlicht,André Lochter,Carolyn J. Sympson,Bing Huey,Jean-Philippe Rougier,Joe W. Gray,Daniel Pinkel,Mina J. Bissell,Zena Werb +8 more
TL;DR: P phenotypically normal mammary epithelial cells with tetracycline-regulated expression of MMP3/stromelysin-1 (Str1) form epithelial glandular structures in vivo without Str1 but form invasive mesenchymal-like tumors with Str1, indicating that Str1 influences tumor initiation and alters neoplastic risk.
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GATA-3 maintains the differentiation of the luminal cell fate in the mammary gland.
TL;DR: It is suggested that GATA-3 actively maintains luminal epithelial differentiation in the adult mammary gland, which raises important implications for the pathogenesis of breast cancer.
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Key stages in mammary gland development: the cues that regulate ductal branching morphogenesis.
TL;DR: A clearer understanding of the underlying endocrine and paracrine pathways that regulate mammary branching may shed light on how they contribute to cancer and how their ill effects might be overcome or entirely avoided.
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Matrix metalloproteinase-2 contributes to cancer cell migration on collagen.
TL;DR: Evidence is provided that MMP-2 is an important determinant of cancer cell behavior but is not inhibited by the collagen binding segment of fibronectin, as confirmed in competitive protein-protein binding assays.