V
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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Journal ArticleDOI
Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5.
Gianluigi Giannelli,Jutta Falk-Marzillier,Oronzo Schiraldi,William G. Stetler-Stevenson,Vito Quaranta +4 more
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.
Journal ArticleDOI
A simplified laminin nomenclature
Monique Aumailley,Leena Bruckner-Tuderman,William G. Carter,Rainer Deutzmann,David Edgar,Peter Ekblom,Jürgen Engel,Eva Engvall,Erhard Hohenester,Jonathan C.R. Jones,Hynda K. Kleinman,M. Peter Marinkovich,George R. Martin,Ulrike Mayer,Guerrino Meneguzzi,Jeffrey H. Miner,Kaoru Miyazaki,Manuel Patarroyo,Mats Paulsson,Vito Quaranta,Joshua R. Sanes,Takako Sasaki,Kiyotoshi Sekiguchi,Lydia Sorokin,Jan F. Talts,Jan F. Talts,Karl Tryggvason,Jouni Uitto,Ismo Virtanen,Klaus von der Mark,Ulla M. Wewer,Yoshihiko Yamada,Peter D. Yurchenco +32 more
TL;DR: A new identification system for a trimer using three Arabic numerals, based on the alpha, beta and gamma chain numbers is introduced, which is introduced for laminin trimers.
Journal ArticleDOI
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.
Journal ArticleDOI
Integrin cytoplasmic domains mediate inside-out signal transduction
Timothy E. O'Toole,Yasuhiro Katagiri,Yasuhiro Katagiri,Randall J. Faull,Randall J. Faull,Karlheinz Peter,Karlheinz Peter,Richard N. Tamura,Vito Quaranta,Joseph C. Loftus,Sanford J. Shattil,Mark H. Ginsberg +11 more
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.
Journal ArticleDOI
Role of Cell Surface Metalloprotease Mt1-Mmp in Epithelial Cell Migration over Laminin-5
Naohiko Koshikawa,Naohiko Koshikawa,Gianluigi Giannelli,Vincenzo Cirulli,Kaoru Miyazaki,Vito Quaranta +5 more
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