Structural basis of the adaptive molecular recognition by MMP9
about
Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domainIn vitro reconstitution of complexes between pro-matrix metalloproteinase-9 and the proteoglycans serglycin and versicanThe Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONSStructure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysisBiochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decadeNeutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)/FGFR-2 pathway.Diffusion of MMPs on the surface of collagen fibrils: the mobile cell surface-collagen substratum interface.A novel CD44-binding peptide from the pro-matrix metalloproteinase-9 hemopexin domain impairs adhesion and migration of chronic lymphocytic leukemia (CLL) cells.Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptidesSmall-molecule anticancer compounds selectively target the hemopexin domain of matrix metalloproteinase-9Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.Targeting Matrix Metalloproteinases in Cancer: Bringing New Life to Old IdeasA thermodynamic definition of protein domainsDimerization of matrix metalloproteinase-2 (MMP-2): functional implication in MMP-2 activationA 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds α4β1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells.Breaking symmetry in protein dimers: designs and functions.A Disintegrin and Metalloproteinase with Thrombospondin Motifs-5 (ADAMTS-5) Forms Catalytically Active OligomersPeptide-based selective inhibitors of matrix metalloproteinase-mediated activitiesBiological and pathobiological functions of gelatinase dimers and complexes.The significance of matrix metalloproteinase (MMP)-2 and MMP-9 in the ischemic stroke.Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines.Development of in-cell imaging assay systems for MMP-2 and MMP-9 based on trans-localizing molecular beacon proteins.Alendronate promotes plasmin-mediated MMP-9 inactivation by exposing cryptic plasmin degradation sites within the MMP-9 catalytic domain.The hemopexin domain of MMP-9 inhibits angiogenesis and retards the growth of intracranial glioblastoma xenograft in nude mice.Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25)Role of the hemopexin domain of matrix metalloproteinases in cell migration.Interaction of pro-matrix metalloproteinase-9/proteoglycan heteromer with gelatin and collagen.A biochemical model of matrix metalloproteinase 9 activation and inhibition.Signatures of positive selection at hemopexin (PEX) domain of matrix metalloproteinase-9 (MMP-9) gene.Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion.Expression and complex formation of MMP9, MMP2, NGAL, and TIMP1 in porcine myocardium but not in skeletal muscles in male pigs with tachycardia-induced systolic heart failure.Inhibition of MMP-9-dependent Degradation of Gelatin, but Not Other MMP-9 Substrates, by the MMP-9 Hemopexin Domain Blades 1 and 4.Crystal structure of an active form of human MMP-1.Association of matrix metalloproteinase 9 genotypes and cardiovascular disease risk factors with serum matrix metalloproteinase 9 concentrations in Taiwanese individuals.Targeting the Hemopexin-like Domain of Latent Matrix Metalloproteinase-9 (proMMP-9) with a Small Molecule Inhibitor Prevents the Formation of Focal Adhesion Junctions.Analysis of the HIV-2 protease's adaptation to various ligands: characterization of backbone asymmetry using a structural alphabet.Rapid Mobilization Reveals a Highly Engraftable Hematopoietic Stem Cell.Decreased homodimerization and increased TIMP-1 complexation of uteroplacental and uterine arterial matrix metalloproteinase-9 during hypertension-in-pregnancy.
P2860
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P2860
Structural basis of the adaptive molecular recognition by MMP9
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structural basis of the adaptive molecular recognition by MMP9
@ast
Structural basis of the adaptive molecular recognition by MMP9
@en
Structural basis of the adaptive molecular recognition by MMP9
@nl
type
label
Structural basis of the adaptive molecular recognition by MMP9
@ast
Structural basis of the adaptive molecular recognition by MMP9
@en
Structural basis of the adaptive molecular recognition by MMP9
@nl
prefLabel
Structural basis of the adaptive molecular recognition by MMP9
@ast
Structural basis of the adaptive molecular recognition by MMP9
@en
Structural basis of the adaptive molecular recognition by MMP9
@nl
P2093
P1476
Structural basis of the adaptive molecular recognition by MMP9
@en
P2093
Erhard Kopetzki
Hyunju Cha
Martin Lanzendörfer
P304
P356
10.1016/S0022-2836(02)00558-2
P407
P577
2002-07-26T00:00:00Z