ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. - Wikidata - wikimedia - TriplyDB

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

http://www.wikidata.org/entity/Q34407615

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C17 prevents inflammatory arthritis and associated joint destruction in mice The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family Decreased metalloproteinase production as a response to mechanical pressure in human cartilage: a mechanism for homeostatic regulation A transcriptional enhancer from the coding region of ADAMTS5 Microvesicles shed by oligodendroglioma cells and rheumatoid synovial fibroblasts contain aggrecanase activity Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein Fibroblast-like synoviocytes: key effector cells in rheumatoid arthritis Sodium and T1rho MRI for molecular and diagnostic imaging of articular cartilage A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis.Evidence for proteolytic cleavage of brevican by the ADAMTSs in the dentate gyrus after excitotoxic lesion of the mouse entorhinal cortex The protective effect of licofelone on experimental osteoarthritis is correlated with the downregulation of gene expression and protein synthesis of several major cartilage catabolic factors: MMP-13, cathepsin K and aggrecanases.Advances in understanding cartilage remodeling Genetically Engineered Mouse Models Reveal the Importance of Proteases as Osteoarthritis Drug Targets Targets, models and challenges in osteoarthritis research Osteoarthritis pathogenesis: a review of molecular mechanisms Expression and regulation of metalloproteinases and their inhibitors in intervertebral disc aging and degeneration High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)Structure analysis reveals the flexibility of the ADAMTS-5 active site Biochemical markers of ongoing joint damage in rheumatoid arthritis--current and future applications, limitations and opportunities.Detecting early stage osteoarthritis by optical coherence tomography?The ADAMTS(L) family and human genetic disorders O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily Combined anti-inflammatory and anti-AGE drug treatments have a protective effect on intervertebral discs in mice with diabetes Molecular specification and patterning of progenitor cells in the lateral and medial ganglionic eminences Pregnane X receptor knockout mice display aging-dependent wearing of articular cartilage ADAMTS5 Is a Critical Regulator of Virus-Specific T Cell Immunity Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1 The secreted metalloprotease ADAMTS20 is required for melanoblast survival Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is necessary for normal endochondral ossification and aggrecan metabolism Biosynthesis and expression of a disintegrin-like and metalloproteinase domain with thrombospondin-1 repeats-15: a novel versican-cleaving proteoglycanase TNF-α and IL-1β promote a disintegrin-like and metalloprotease with thrombospondin type I motif-5-mediated aggrecan degradation through syndecan-4 in intervertebral disc Exome sequencing of senescence-accelerated mice (SAM) reveals deleterious mutations in degenerative disease-causing genes.Disease-modifying osteoarthritis drugs: in vitro and in vivo data on the development of DMOADs under investigation.Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate.The effect of doxycycline on canine hip osteoarthritis: design of a 6-months clinical trial Biglycan and fibromodulin have essential roles in regulating chondrogenesis and extracellular matrix turnover in temporomandibular joint osteoarthritis.Chondrocytes and meniscal fibrochondrocytes differentially process aggrecan during de novo extracellular matrix assembly.Development of a monoclonal anti-ADAMTS-5 antibody that specifically blocks the interaction with LRP1.

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P2860

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

http://www.wikidata.org/entity/Q34407615

description

2005 nî lūn-bûn

@nan

2005 թուականի Մարտին հրատարակուած գիտական յօդուած

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2005 թվականի մարտին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

@zh-hk

2005年論文

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2005年論文

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2005年论文

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name

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@ast

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@en

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@nl

type

label

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@ast

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@en

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@nl

prefLabel

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@ast

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@en

ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

@nl

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ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro.

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Anne M Fourie

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Charlotte J East

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Clare T Meeker

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Fraser M Rogerson

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Ian K Campbell

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Pamela J Farmer

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Suzanne B Golub

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648-652

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scholarly article

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10.1038/NATURE03417

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Christopher B Little

Heather Stanton

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2005-03-01T00:00:00Z

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7934732

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15800625

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