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Mammalian metalloendopeptidases
International Journal of Biochemistry & Cell Biology, 1985Robert Beynon, Judith S Bond
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Structural aspects of the metzincin clan of metalloendopeptidases
Molecular Biotechnology, 2003 Metalloendopeptidases are present across all kingdoms of living organisms; they are ubiquitous and widely involved in metabolism regulation through their ability either to extensively degrade proteins or to selectively hydrolyze specific peptide bonds. They must be subjected to exquisite spatial and temporal control to prevent this vast potential from ...
F. Xavier Gomis-Rüth
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Commitment to expression of the metalloendopeptidases, collagenase and stromelysin: relationship of inducing events to changes in cytoskeletal architecture. [PDF]
Journal of Cell Biology, 1986 Agents that alter the morphology of rabbit synovial fibroblasts induce synthesis of the metalloendopeptidases, collagenase and stromelysin. We studied the relationship of cytoskeletal changes to the commitment to expression of these metalloendopeptidases.
Werb, Z +7 more
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[21] Snake venom metalloendopeptidases: Reprolysins
Methods in Enzymology, 1995 Jay W Fox +2 more
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[24] Snake venom hemorrhagic and nonhemorrhagic metalloendopeptidases
Methods in Enzymology, 1993 Norikazu Nishino +2 more
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[30] Tissue inhibitors of matrix metalloendopeptidases
Methods in Enzymology, 1995 F Willenbrock, Frances Willenbrock
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Extracellular metalloendopeptidase of Streptomyces rimosus
Archives of Microbiology, 2006Metalloendopeptidase was isolated from Streptomyces rimosus culture filtrates in a homogeneous form. It was determined to be a 15 kDa basic protein, most active around pH 7.5, and susceptible to inhibition by chelating agents, N-bromosuccinimide, thiorphan, and 10(-4) M zinc. The enzyme was highly specific for phenylalanine at the N-side of endopeptide
Vitale, Ljubinka +2 more
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