R
Rafael Fridman
Researcher at Wayne State University
Publications - 29
Citations - 7151
Rafael Fridman is an academic researcher from Wayne State University. The author has contributed to research in topics: Matrigel & Cell culture. The author has an hindex of 25, co-authored 29 publications receiving 6908 citations. Previous affiliations of Rafael Fridman include National Institutes of Health.
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Journal ArticleDOI
Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix
Israel Vlodavsky,Judah Folkman,Robert K. P. Sullivan,Rafael Fridman,Rivka Ishai-Michaeli,Joachim Sasse,Michael Klagsbrun +6 more
TL;DR: It is suggested that endothelium can store growth factors capable of autocrine growth promotion in two ways: by sequestering growth factor within the cell and by incorporating it into the underlying extracellular matrix.
Journal ArticleDOI
Matrix metalloproteinases: structures, evolution, and diversification
TL;DR: Analysis indicates that a retrograde structure simplification may have accounted for the evolution of MMPs with simple domain constituents, such as matrilysin, from the larger and more elaborate enzymes.
Journal ArticleDOI
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.
Book ChapterDOI
Assessment of gelatinases (MMP-2 and MMP-9) by gelatin zymography.
TL;DR: This polyacrylamide gel electrophoresis-based method can provide a reliable assessment of the type of gelatinase, relative amount, and activation status (latent, compared with active enzyme forms) in cultured cells, tissues, and biological fluids.
Journal ArticleDOI
Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1.
TL;DR: It is reported that the 72-kDa gelatinase A (matrix metalloproteinase type 2, MMP2) can hydrolyze the Val368-Met369 peptide bond of the FGFR1 ectodomain, eight amino acids upstream of the transmembrane domain, thus releasing the entire extracellular domain.