A
Alex Y. Strongin
Researcher at Discovery Institute
Publications - 177
Citations - 14746
Alex Y. Strongin is an academic researcher from Discovery Institute. The author has contributed to research in topics: Matrix metalloproteinase & Furin. The author has an hindex of 58, co-authored 176 publications receiving 13929 citations. Previous affiliations of Alex Y. Strongin include Sanford-Burnham Institute for Medical Research & Torrey Pines Institute for Molecular Studies.
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Journal ArticleDOI
Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase ISOLATION OF THE ACTIVATED FORM OF THE MEMBRANE METALLOPROTEASE
Alex Y. Strongin,Ivan E. Collier,Gregory A. Bannikov,Barry L. Marmer,Gregory A. Grant,Gregory I. Goldberg +5 more
TL;DR: Activation of 72T4Cl on the cell membrane provides a basic mechanism for spatially regulated extracellular proteolysis and presents a new target for prognosis and treatment of metastatic disease.
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Compensation mechanism in tumor cell migration: mesenchymal–amoeboid transition after blocking of pericellular proteolysis
Katarina Wolf,Irina B. Mazo,Harry Leung,Katharina Engelke,Ulrich H. von Andrian,Elena I. Deryugina,Alex Y. Strongin,Eva B. Bröcker,Peter Friedl +8 more
TL;DR: The transition from proteolytic mesenchymal toward nonproteolytic amoeboid movement highlights a supramolecular plasticity mechanism in cell migration and further represents a putative escape mechanism in tumor cell dissemination after abrogation of pericellular proteolysis.
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S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death.
Zezong Gu,Marcus Kaul,Boxu Yan,Steven J. Kridel,Jiankun Cui,Alex Y. Strongin,Jeffrey W. Smith,Robert C. Liddington,Stuart A. Lipton +8 more
TL;DR: Findings suggest a potential extracellular proteolysis pathway to neuronal cell death in which S-nitrosylation activates MMPs, and further oxidation results in a stable posttranslational modification with pathological activity.
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Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin.
TL;DR: It is demonstrated that in the absence of TIMP, 92-kDa Type IV procollagenase (92T4Cl) can form a covalent homodimer and a novel complex with ClI, suggesting a mechanism for cooperative action of two enzymes in reducing collagen fibrils to small peptides under physiologic conditions.
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A Highly Specific Inhibitor of Matrix Metalloproteinase-9 Rescues Laminin from Proteolysis and Neurons from Apoptosis in Transient Focal Cerebral Ischemia
Zezong Gu,Jiankun Cui,Stephen L. Brown,Rafael Fridman,Shahriar Mobashery,Alex Y. Strongin,Stuart A. Lipton +6 more
TL;DR: It is concluded that MMP-9 is a highly promising drug target and that SB-3CT derivatives have significant therapeutic potential in stroke patients.