TIMP-2 is required for efficient activation of proMMP-2 in vivo
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LIM kinase1 modulates function of membrane type matrix metalloproteinase 1: implication in invasion of prostate cancer cellsMT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cellsMatrix metalloproteinases in lung biologyMatrix metalloproteinases: old dogs with new tricksTemporal and spatial expression of tissue inhibitors of metalloproteinases 1 and 2 (TIMP-1 and -2) in the bovine corpus luteumMatrix Metalloproteinases in Non-Neoplastic Disorders.The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatasesRadial glial neural progenitors regulate nascent brain vascular network stabilization via inhibition of Wnt signalingDomain 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 activationStructural analysis of the alpha(2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interactionPro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagenRegulatory mechanisms of anthrax toxin receptor 1-dependent vascular and connective tissue homeostasisInactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activationMast cell-dependent activation of pro matrix metalloprotease 2: A role for serglycin proteoglycan-dependent mast cell proteasesMembrane-type matrix metalloproteinase-1 (MT1-MMP) is down-regulated in estrogen-deficient rat osteoblast in vivoMembrane type 1-matrix metalloproteinase (MMP)-associated MMP-2 activation increases in the rat ovary in response to an ovulatory dose of human chorionic gonadotropinTissue inhibitor of metalloproteinase-2 promotes neuronal differentiation by acting as an anti-mitogenic signal.Matrix metalloproteinases and the regulation of tissue remodellingHow matrix metalloproteinases regulate cell behaviorPotential regulatory relationship between the nested gene DDC8 and its host gene tissue inhibitor of metalloproteinase-2Identification of compounds that inhibit IGF-I signaling in hyperglycemia.Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: contrasting, overlapping and compensatory functions.Thoracic aortic dissection: are matrix metalloproteinases involved?The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityTIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains.Tissue inhibitor of metalloproteinase-2(TIMP-2)-deficient mice display motor deficits.Disruption of matrix metalloproteinase 2 binding to integrin alpha vbeta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivoHyperphagia and leptin resistance in tissue inhibitor of metalloproteinase-2 deficient mice.Sexually dimorphic diet-induced insulin resistance in obese tissue inhibitor of metalloproteinase-2 (TIMP-2)-deficient mice.Active matrix metalloproteinase-2 activity discriminates colonic mucosa, adenomas with and without high-grade dysplasia, and cancers.Metzincin proteases and their inhibitors: foes or friends in nervous system physiology?Phosphorylation status of 72 kDa MMP-2 determines its structure and activity in response to peroxynitrite.Molecular mechanisms of glioma invasiveness: the role of proteases.Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis.Reduced NO signaling during pregnancy attenuates outward uterine artery remodeling by altering MMP expression and collagen and elastin depositionImmobilizing reporters for molecular imaging of the extracellular microenvironment in living animals.ECM-Regulator timp Is Required for Stem Cell Niche Organization and Cyst Production in the Drosophila Ovary.Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3).Matrix metalloproteinases in renal development.
P2860
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P2860
TIMP-2 is required for efficient activation of proMMP-2 in vivo
description
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im August 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/08/25)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/08/25)
@nl
наукова стаття, опублікована в серпні 2000
@uk
name
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@ast
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@en
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@nl
type
label
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@ast
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@en
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@nl
prefLabel
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@ast
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@en
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@nl
P2093
P2860
P3181
P356
P1476
TIMP-2 is required for efficient activation of proMMP-2 in vivo
@en
P2093
P. D. Soloway
R. Juttermann
P2860
P304
26411–26415
P3181
P356
10.1074/JBC.M001270200
P407
P577
2000-08-25T00:00:00Z