J
James P. Quigley
Researcher at Scripps Research Institute
Publications - 178
Citations - 18680
James P. Quigley is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Plasminogen activator & Limulus. The author has an hindex of 65, co-authored 177 publications receiving 17748 citations. Previous affiliations of James P. Quigley include State University of New York System & Thomas Jefferson University.
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Matrix metalloproteinases and tumor metastasis
TL;DR: The major pieces of evidence that are most compelling and clearly determine the role and involvement of MMPs in the metastatic cascade are provided by molecular genetic studies employing knock-out or transgenic animals and tumor cell lines, modified to overexpress or downregulate a specific MMP.
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Localization of Matrix Metalloproteinase MMP-2 to the Surface of Invasive Cells by Interaction with Integrin αvβ3
Peter C. Brooks,Staffan Strömblad,Luraynne C. Sanders,Tami von Schalscha,Ronald T. Aimes,William G. Stetler-Stevenson,James P. Quigley,David A. Cheresh +7 more
TL;DR: These findings define a single cell-surface receptor that regulates both matrix degradation and motility, thereby facilitating directed cellular invasion.
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Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments.
Ronald T. Aimes,James P. Quigley +1 more
TL;DR: It is reported that both human and chicken MMP-2, free of tissue inhibitors of metalloproteinases (TIMPs) are capable of cleaving soluble, triple helical type I collagen generating the ¾- and ¼-length collagen fragments characteristic of vertebrate interstitial collagenases.
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An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses.
TL;DR: At least one step of the fibrinolytic process shows specificity resembling that of trypsin, and the sera of sarcoma-bearing chickens contain an inhibitor of thefibrinolysin, whereas normal chicken sera do not.
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Activation of Matrix Metalloproteinase-9 (MMP-9) via a Converging Plasmin/Stromelysin-1 Cascade Enhances Tumor Cell Invasion
Noemi RAMOS-DeSIMONE,Elizabeth Hahn-Dantona,John D. Sipley,Hideaki Nagase,Deborah L. French,James P. Quigley +5 more
TL;DR: The activated MMP-9 enhances the invasive phenotype of the cultured cells as their ability to both degrade extracellular matrix and transverse basement membrane is significantly increased following zymogen activation.