Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
about
Evolutionary divergence and functions of the ADAM and ADAMTS gene familiesCloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familySites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeatsStructure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpuraBinding of ADAMTS13 to von Willebrand factorProprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi networkC-terminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occlusion and cerebral strokeInhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulinADAMTS-12 associates with and degrades cartilage oligomeric matrix proteinCharacterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanismADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and functionSodium and T1rho MRI for molecular and diagnostic imaging of articular cartilageCrystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5VLA-4-dependent and -independent pathways in cell contact-induced proinflammatory cytokine production by synovial nurse-like cells from rheumatoid arthritis patientsDrugs in development: bisphosphonates and metalloproteinase inhibitorsIntra-articular hyaluronan (hyaluronic acid) and hylans for the treatment of osteoarthritis: mechanisms of actionAggrecanases and cartilage matrix degradationFunctional evolution of ADAMTS genes: evidence from analyses of phylogeny and gene organizationArticular cartilage and changes in arthritis: matrix degradation.What can we do about osteoarthritis?ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis.Pathophysiological Function of ADAMTS Enzymes on Molecular Mechanism of Alzheimer's DiseaseAdvances in understanding cartilage remodelingProteolytic processing of von Willebrand factor by adamts13 and leukocyte proteasesExpression and regulation of metalloproteinases and their inhibitors in intervertebral disc aging and degenerationDeterminants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analoguesStructural and Inhibition Analysis Reveals the Mechanism of Selectivity of a Series of Aggrecanase InhibitorsHigh resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)Structure analysis reveals the flexibility of the ADAMTS-5 active siteTransforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sitesMatrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)ADAMTS-1 cleaves a cartilage proteoglycan, aggrecanDifferential gene expression by endothelial cells in distinct angiogenic statesVersican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilageTissue inhibitor of metalloproteinases-4 (TIMP-4) gene expression is increased in human osteoarthritic femoral head cartilage
P2860
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P2860
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@ast
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en-gb
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@nl
type
label
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@ast
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en-gb
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@nl
prefLabel
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@ast
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en-gb
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@nl
P2093
P921
P3181
P1433
P1476
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
@en
P2093
A Rockwell
B H Wiswall
C P Decicco
G F Hollis
P304
P3181
P356
10.1126/SCIENCE.284.5420.1664
P407
P577
1999-06-01T00:00:00Z