ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region
about
Identification and cloning of a connective tissue growth factor-like cDNA from human osteoblasts encoding a novel regulator of osteoblast functionsCloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familyADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS familyProcollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxisStructure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpuraThe syndrome of microcornea, myopic chorioretinal atrophy, and telecanthus (MMCAT) is caused by mutations in ADAMTS18Binding of ADAMTS13 to von Willebrand factorC-terminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occlusion and cerebral strokeCharacterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and functionExpression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumoursA disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanismsADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis.The conserved ADAMTS-like protein lonely heart mediates matrix formation and cardiac tissue integrityCobra CRISP Functions as an Inflammatory Modulator via a Novel Zn2+- and Heparan Sulfate-dependent Transcriptional Regulation of Endothelial Cell Adhesion MoleculesThe metalloproteinase ADAMTS1: a comprehensive review of its role in tumorigenic and metastatic pathways.Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.ADAMTS-1 is an active metalloproteinase associated with the extracellular matrixADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeatsThrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activityADAMTS-1 cleaves a cartilage proteoglycan, aggrecanProcessing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulationADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide regionVersican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4A systems biology approach for the investigation of the heparin/heparan sulfate interactomeTranscriptional regulation by the Wilms tumor protein, Wt1, suggests a role of the metalloproteinase Adamts16 in murine genitourinary developmentADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formationFibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1The ADAMTS metalloproteinasesADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin.ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan.Expression and activity of ADAMTS-5 in synovium.Molecular biology of ADAMTS13 and diagnostic utility of ADAMTS13 proteolytic activity and inhibitor assays.The cleavage of semaphorin 3C induced by ADAMTS1 promotes cell migrationPGF2α-F-prostanoid receptor signalling via ADAMTS1 modulates epithelial cell invasion and endothelial cell function in endometrial cancer.ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells.The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage.The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family.Binding and invasion of liver cells by Plasmodium falciparum sporozoites. Essential involvement of the amino terminus of circumsporozoite protein.
P2860
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P2860
ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@ast
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@en
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@nl
type
label
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@ast
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@en
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@nl
prefLabel
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@ast
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@en
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@nl
P2860
P3181
P356
P1476
ADAMTS-1 protein anchors at th ...... motifs and its spacing region
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.273.22.13912
P407
P577
1998-05-29T00:00:00Z