Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.
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The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its functionBreast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathwayTissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranesActivation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13)A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis.Elevation of hemopexin-like fragment of matrix metalloproteinase-2 tissue levels inhibits ischemic wound healing and angiogenesis.Activation of human neutrophil procollagenase by stromelysin 2.Proteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.Suppression of angiogenesis by lentiviral delivery of PEX, a noncatalytic fragment of matrix metalloproteinase 2.Selective regulation of MMP and TIMP mRNA levels in tree shrew sclera during minus lens compensation and recoveryFilamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells.Control of matrix metalloproteinase catalytic activityLooking at the proteases from a simple perspective.Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases.The molecular biology of matrix metalloproteinases and tissue inhibitors of metalloproteinases in inflammatory bowel diseases.Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13.Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface.Interaction between tissue inhibitor of metalloproteinases-2 and progelatinase A: immunoreactivity analyses.Mechanisms of connective tissue matrix destruction in periodontitis.Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase A in human osteoarthritic cartilage.Endotoxemia shifts neutrophils with TIMP-free gelatinase B/MMP-9 from bone marrow to the periphery and induces systematic upregulation of TIMP-1.Distinct progression-associated expression of tumor and stromal MMPs in HaCaT skin SCCs correlates with onset of invasion.Activation of MMP-2 by human GCT23 giant cell tumour cells induced by osteopontin, bone sialoprotein and GRGDSP peptides is RGD and cell shape change dependent.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 componenEnhancement of matrix metalloproteinase (MMP)-2 activity in gingival tissue and cultured fibroblasts from Down's syndrome patients.
P2860
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P2860
Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@en
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@nl
type
label
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@en
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@nl
prefLabel
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@en
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@nl
P2093
P2860
P356
P1433
P1476
Cell surface-mediated activati ...... nase A by primary fibroblasts.
@en
P2093
P2860
P304
P356
10.1042/BJ3040263
P407
P478
304 ( Pt 1)
P577
1994-11-01T00:00:00Z