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Vito Quaranta

Researcher at Vanderbilt University

Publications -  267
Citations -  20383

Vito Quaranta is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Integrin & Extracellular matrix. The author has an hindex of 70, co-authored 251 publications receiving 18726 citations. Previous affiliations of Vito Quaranta include Northwestern University & Torrey Pines Institute for Molecular Studies.

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Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5.

TL;DR: Cleavage of laminin-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.
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Tumor morphology and phenotypic evolution driven by selective pressure from the microenvironment.

TL;DR: The genetic make-up of a cancer cell may realize its invasive potential through a clonal evolution process driven by definable microenvironmental selective forces, and this mathematical model provides a theoretical/experimental framework to quantitatively characterize this selective pressure for invasion and test ways to eliminate it.
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Integrin cytoplasmic domains mediate inside-out signal transduction

TL;DR: Both cytoplasmic domains are required for energy-dependent, cell type-specific affinity modulation and mutations that disrupted a highly conserved alpha subunit GFFKR motif, resulted in high affinity binding of ligands to alpha IIb beta 3.
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Role of Cell Surface Metalloprotease Mt1-Mmp in Epithelial Cell Migration over Laminin-5

TL;DR: It is shown that exogenous addition of activated matrix metalloprotease (MMP) 2 stimulates migration onto Ln-5 in breast epithelial cells via cleavage of the γ2 subunit, and this model suggests a model whereby expression of MT1-MMP is the primary trigger for migration over LN-5, whereas MMP2, which is activated by MT1,MMP, may play an ancillary role, perhaps by amplifying the MT1