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.
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Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzymeCell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinasesThe cysteine-rich domain regulates ADAM protease function in vivo.MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cellsCrystal structure of the haemopexin-like C-terminal domain of gelatinase AThe C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its functionDomain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activationUtilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding theSpecific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodellingHuman progelatinase A can be activated by matrilysinIntermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranesImmunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis.The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.Clinically relevant doses of lidocaine and bupivacaine do not impair cutaneous wound healing in miceRole of the netrin-like domain of procollagen C-proteinase enhancer-1 in the control of metalloproteinase activity.17beta-estradiol inhibits wound healing in male mice via estrogen receptor-alpha.Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants.Brain-enriched hyaluronan binding (BEHAB)/brevican cleavage in a glioma cell line is mediated by a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family member.Proteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.Advances in animal cell recombinant protein production: GS-NS0 expression system.Proteolytic host cell enzymes in gingival crevice fluid.The matrix metalloproteinases and their inhibitors.Selective regulation of MMP and TIMP mRNA levels in tree shrew sclera during minus lens compensation and recoveryEarly changes in matrix metalloproteinases and inhibitors after in vitro laser treatment to the trabecular meshwork.Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation.Specialized podosome- or invadopodia-like structures (PILS) for focal trabecular meshwork extracellular matrix turnoverBinding of gelatinases A and B to type-I collagen and other matrix components.The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A).The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic efficiency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily.Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases.Nimbolide inhibits invasion and migration, and down-regulates uPAR chemokine gene expression, in two breast cancer cell lines.Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis.Structure-function studies of mouse tissue inhibitor of metalloproteinases-1.TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP.Matrix metalloproteases and lung disease.Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
P2860
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P2860
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.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The C-terminal domain of 72 kD ...... ibitors of metalloproteinases.
@en
type
label
The C-terminal domain of 72 kD ...... ibitors of metalloproteinases.
@en
prefLabel
The C-terminal domain of 72 kD ...... ibitors of metalloproteinases.
@en
P2093
P2860
P356
P1433
P1476
The C-terminal domain of 72 kD ...... ibitors of metalloproteinases.
@en
P2093
P2860
P304
P356
10.1042/BJ2830637
P407
P478
283 ( Pt 3)
P577
1992-05-01T00:00:00Z