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Susan Yamada

Researcher at National Institutes of Health

Publications -  15
Citations -  2967

Susan Yamada is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Matrix metalloproteinase & Extracellular matrix. The author has an hindex of 12, co-authored 15 publications receiving 2861 citations.

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MT1-MMP-Deficient Mice Develop Dwarfism, Osteopenia, Arthritis, and Connective Tissue Disease due to Inadequate Collagen Turnover

TL;DR: The findings demonstrate the pivotal function of MT1-MMP in connective tissue metabolism, and illustrate that modeling of the soft connective tissues matrix by resident cells is essential for the development and maintenance of the hard tissues of the skeleton.
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Novel function for beta 1 integrins in keratinocyte cell-cell interactions.

TL;DR: The results indicate that beta 1 integrins play roles in the maintenance of cell- cell contacts between keratinocytes and in the organization of intracellular microfilaments, and suggest that in epithelial cells Integrins can function in cell-cell interactions as well as incell- substrate adhesion.
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Localization of integrin receptors for fibronectin, collagen, and laminin in human skin. Variable expression in basal and squamous cell carcinomas.

TL;DR: VLA integrins in human skin were examined by indirect immunofluorescence utilizing antibodies recognizing the beta 1, alpha 2, alpha 3, or alpha 5 subunits and it is speculated that these receptors might have previously unrecognized functions in cell-cell interactions.
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The metalloproteinase MT1-MMP is required for normal development and maintenance of osteocyte processes in bone.

TL;DR: Osteocytogenesis is thus an active invasive process requiring cleavage of collagen for maintenance of the osteocyte phenotype, and collagenolytic activity and formation of osteocyte processes is dependent on matrix metalloproteinase activity.
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Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras.

TL;DR: The results indicate that information contained in the beta 1, beta 3, or beta 5 integrin intracellular domain is sufficient to stimulate integrin-mediated tyrosine phosphorylation of specific intrACEllular proteins and that integrin extracellular and transmembrane domains are not required for inducing tyrosinesineosphorylation.