Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities.
about
Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzymeFibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domainMatrix metalloproteinases cleave at two distinct sites on human cartilage link proteinNeutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecanMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesFibrillin degradation by matrix metalloproteinases: implications for connective tissue remodellingHuman progelatinase A can be activated by matrilysinMetalloproteinase Activity Secreted by Fibrogenic Cells in the Processing of Prolysyl OxidaseMatrix metalloproteinases are not essential for aggrecan turnover during normal skeletal growth and development.Bioactive conformation of stromelysin inhibitors determined by transferred nuclear Overhauser effects.The role of plasminogen activators in the regulation of connective tissue metalloproteinases.The matrix metalloproteinases and their inhibitors.Mutations in the interglobular domain of aggrecan alter matrix metalloproteinase and aggrecanase cleavage patterns. Evidence that matrix metalloproteinase cleavage interferes with aggrecanase activity.Different susceptibility of small and large human tenascin-C isoforms to degradation by matrix metalloproteinases.Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP).The 45 kDa collagen-binding fragment of fibronectin induces matrix metalloproteinase-13 synthesis by chondrocytes and aggrecan degradation by aggrecanases.The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases.Direct activation of human neutrophil procollagenase by recombinant stromelysinGlial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?Development of a cleavage-site-specific monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fluids.Fragmentation of human polymorphonuclear-leucocyte collagenase.Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis.Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities.The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane componen
P2860
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P2860
Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Purification of recombinant hu ...... atural stromelysin activities.
@en
type
label
Purification of recombinant hu ...... atural stromelysin activities.
@en
prefLabel
Purification of recombinant hu ...... atural stromelysin activities.
@en
P2093
P2860
P356
P1433
P1476
Purification of recombinant hu ...... atural stromelysin activities.
@en
P2093
P2860
P304
P356
10.1042/BJ2760217
P407
P478
276 ( Pt 1)
P577
1991-05-01T00:00:00Z