Structure analysis reveals the flexibility of the ADAMTS-5 active site - Wikidata - awgldk - TriplyDB

Structure analysis reveals the flexibility of the ADAMTS-5 active site

Structure analysis reveals the flexibility of the ADAMTS-5 active site

http://www.wikidata.org/entity/Q27667156

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Genetically Engineered Mouse Models Reveal the Importance of Proteases as Osteoarthritis Drug Targets Metabolic Response of Human Osteoarthritic Cartilage to Biochemically Characterized Collagen Hydrolysates.Inhibition of aggrecanases as a therapeutic strategy in osteoarthritis.Computational Insights into ADAMTS4, ADAMTS5 and MMP13 Inhibitor Selectivity.Molecular basis for the mechanism of action of an anti-TACE antibody.ADAMTS7: a promising new therapeutic target in coronary heart disease.

P2860

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P2860

Structure analysis reveals the flexibility of the ADAMTS-5 active site

http://www.wikidata.org/entity/Q27667156

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@ast

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@en

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@nl

type

label

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@ast

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@en

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@nl

prefLabel

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@ast

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@en

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@nl

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Protein Science

P1476

Structure analysis reveals the flexibility of the ADAMTS-5 active site

@en

P2093

Alfredo G Tomasselli

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

Arthur Wittwer

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

Grace Munie

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

Huey-Sheng Shieh

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

Jennifer M Williams

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

Karl J Mathis

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

Mark E Schnute

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

Micky D Tortorella

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

Nicole Caspers

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

Scott S Woodard

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

P2860

Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5

Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors

Structural and Inhibition Analysis Reveals the Mechanism of Selectivity of a Series of Aggrecanase Inhibitors

Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains

High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)

Extra binding region induced by non-zinc chelating inhibitors into the S1' subsite of matrix metalloproteinase 8 (MMP-8)

Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis.

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

P304

735-744

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P31

scholarly article

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3603984

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10.1002/PRO.606

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4

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P478

20

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Anne-Marie Malfait

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2011-04-01T00:00:00Z

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50269111

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21370305

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3081551

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