The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.
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Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family membersBiochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzymeIdentification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distributionBiochemical characterization of human collagenase-3Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interactionStructural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.Articular cartilage and changes in arthritis: matrix degradation.Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunitiesMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesThe 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 theThe enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPsSpecific, 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-2The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene familyInactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activationHuman progelatinase A can be activated by matrilysinIntermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranesMembrane type 1 matrix metalloproteinase and gelatinase A synergistically degrade type 1 collagen in a cell model.Direct expression of active human tissue inhibitors of metalloproteinases by periplasmic secretion in Escherichia coli.A second independent Tyr168Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophyBiochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2.Proteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.Matrix metalloproteinases in arthritic diseaseEngineering of tissue inhibitor of metalloproteinases mutants as potential therapeuticsAdvances in animal cell recombinant protein production: GS-NS0 expression system.Requirement for matrix metalloproteinase-9 (gelatinase B) expression in metastasis by murine prostate carcinomaCloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation.Bone sialoprotein binding to matrix metalloproteinase-2 alters enzyme inhibition kinetics.TIMPs of parasitic helminths - a large-scale analysis of high-throughput sequence datasets.Matrix metalloproteinases and their tissue inhibitors in preterm perinatal complications.Binding of gelatinases A and B to type-I collagen and other matrix components.Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).Timp-2 binding with cellular MT1-MMP stimulates invasion-promoting MEK/ERK signaling in cancer cells.A biochemical model of matrix metalloproteinase 9 activation and inhibition.Individual Timp deficiencies differentially impact pro-MMP-2 activation.Effects of oxygen tension and dextran-shelled/2H,3H-decafluoropentane-cored oxygen-loaded nanodroplets on secretion of gelatinases and their inhibitors in term human placenta.Cellular cholesterol regulates MT1 MMP dependent activation of MMP 2 via MEK-1 in HT1080 fibrosarcoma cells.
P2860
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P2860
The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
The activity of the tissue inh ...... he inhibition of gelatinase A.
@en
type
label
The activity of the tissue inh ...... he inhibition of gelatinase A.
@en
prefLabel
The activity of the tissue inh ...... he inhibition of gelatinase A.
@en
P2093
P356
P1433
P1476
The activity of the tissue inh ...... he inhibition of gelatinase A.
@en
P2093
Brocklehurst K
Cockett MI
Docherty AJ
Phillips IR
Slocombe PM
Willenbrock F
P304
P356
10.1021/BI00067A023
P407
P577
1993-04-01T00:00:00Z