Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein - Wikidata - awgldk - TriplyDB

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

http://www.wikidata.org/entity/Q24528169

about

Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry.The use of cleavage site specific antibodies to delineate protein processing and breakdown pathways.Matrix metalloproteinases: from biology to therapeutic strategies in cardiovascular disease.Aggrecanolysis and in vitro matrix degradation in the immature bovine meniscus: mechanisms and functional implications.Advances in animal cell recombinant protein production: GS-NS0 expression system.Myocardial matrix metalloproteinase-2: inside out and upside down.Somatic antigens of tropical liver flukes ameliorate collagen-induced arthritis in wistar rats Effects of Articular Cartilage Constituents on Phosphotungstic Acid Enhanced Micro-Computed Tomography.Selective and non-selective metalloproteinase inhibitors reduce IL-1-induced cartilage degradation and loss of mechanical properties.Contribution of host MMP-2 and MMP-9 to promote tumor vascularization and invasion of malignant keratinocytes.The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradation Pathophysiology, diagnosis and prevention of arthropathy in patients with haemophilia.Age-related changes in the composition, the molecular stoichiometry and the stability of proteoglycan aggregates extracted from human articular cartilage.Differential glycosylation of gelatinase B from neutrophils and breast cancer cells.Proteolytic mechanisms of cartilage breakdown: a target for arthritis therapy?Regulation of matrilysin in the rat uterus.Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase.Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase A in human osteoarthritic cartilage.Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate Selection of a histidine-containing inhibitor of gelatinases through deconvolution of combinatorial tetrapeptide libraries.Age-related decrease in susceptibility of human articular cartilage to matrix metalloproteinase-mediated degradation: the role of advanced glycation end products.Substrate hydrolysis by matrix metalloproteinase-9.Link-N: The missing link towards intervertebral disc repair is species-specific.Hyaluronan and proteoglycan link protein 1 (HAPLN1) activates bortezomib-resistant NF-κB activity and increases drug resistance in multiple myeloma.Computational sequence analysis of matrix metalloproteinases.Temporal cardiac remodeling post-myocardial infarction: dynamics and prognostic implications in personalized medicine.Tetraspanin CD151 is expressed in osteoarthritic cartilage and is involved in pericellular activation of pro-matrix metalloproteinase 7 in osteoarthritic chondrocytes.

P2860

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P2860

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

http://www.wikidata.org/entity/Q24528169

description

1993 nî lūn-bûn

@nan

1993 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1993 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

name

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@ast

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en-gb

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@nl

type

label

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@ast

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en-gb

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@nl

prefLabel

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@ast

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en-gb

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@nl

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P1433

Biochemical Journal

P1476

Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein

@en

P2093

C E Hughes

http://www.w3.org/2001/XMLSchema#string

G Murphy

http://www.w3.org/2001/XMLSchema#string

J S Mort

http://www.w3.org/2001/XMLSchema#string

P J Roughley

http://www.w3.org/2001/XMLSchema#string

Q Nguyen

http://www.w3.org/2001/XMLSchema#string

P2860

The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

The primary structure of human cartilage link protein

Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes

Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage.

A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization.

The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.

Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins.

The matrix-degrading metalloproteinases.

Degradation of proteoglycan aggregate by a cartilage metalloproteinase. Evidence for the involvement of stromelysin in the generation of link protein heterogeneity in situ.

P304

595-8

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scholarly article

P356

10.1042/BJ2950595

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P407

P478

295 ( Pt 2)

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P577

1993-10-15T00:00:00Z

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15503734

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7694569

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1134922

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