Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications
about
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) familyADAMTS proteoglycanases in the physiological and pathological central nervous systemEntropy increases from different sources support the high-affinity binding of the N-terminal inhibitory domains of tissue inhibitors of metalloproteinases to the catalytic domains of matrix metalloproteinases-1 and -3.Proteases involved in cartilage matrix degradation in osteoarthritis.Antibody-based exosite inhibitors of ADAMTS-5 (aggrecanase-2)Pericyte TIMP3 and ADAMTS1 modulate vascular stability after kidney injury.Rearranging exosites in noncatalytic domains can redirect the substrate specificity of ADAMTS proteases.Insights into ectodomain shedding and processing of protein-tyrosine pseudokinase 7 (PTK7)LRP-1-mediated endocytosis regulates extracellular activity of ADAMTS-5 in articular cartilageThermodynamic Basis of Selectivity in the Interactions of Tissue Inhibitors of Metalloproteinases N-domains with Matrix Metalloproteinases-1, -3, and -14.Incorporation of Bulky and Cationic Cyclam-Triazole Moieties into Marimastat Can Generate Potent MMP Inhibitory Activity without Inducing Cytotoxicity.Olive and grape seed extract prevents post-traumatic osteoarthritis damages and exhibits in vitro anti IL-1β activities before and after oral consumption.Engineered Tissue Inhibitor of Metalloproteinases-3 Variants Resistant to Endocytosis Have Prolonged Chondroprotective Activity.Low density lipoprotein receptor-related protein 1 (LRP1)-mediated endocytic clearance of a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4): functional differences of non-catalytic domains of ADAMTS-4 and ADAMTS-5 in LRP1 bCurrent and emerging therapeutic strategies for preventing inflammation and aggrecanase-mediated cartilage destruction in arthritis.Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2).IL-1β promotes ADAMTS enzyme-mediated aggrecan degradation through NF-κB in human intervertebral disc.Suramin Inhibits Osteoarthritic Cartilage Degradation by Increasing Extracellular Levels of Chondroprotective Tissue Inhibitor of Metalloproteinases 3.Anti-Osteoarthritic and Anti-Inflammatory Activities of Diazine: In Vitro and In Vivo Studies.
P2860
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P2860
Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Reactive-site mutants of N-TIM ...... al and structural implications
@ast
Reactive-site mutants of N-TIM ...... al and structural implications
@en
Reactive-site mutants of N-TIM ...... al and structural implications
@nl
type
label
Reactive-site mutants of N-TIM ...... al and structural implications
@ast
Reactive-site mutants of N-TIM ...... al and structural implications
@en
Reactive-site mutants of N-TIM ...... al and structural implications
@nl
prefLabel
Reactive-site mutants of N-TIM ...... al and structural implications
@ast
Reactive-site mutants of N-TIM ...... al and structural implications
@en
Reactive-site mutants of N-TIM ...... al and structural implications
@nl
P2093
P2860
P356
P1433
P1476
Reactive-site mutants of N-TIM ...... al and structural implications
@en
P2093
Hideaki Nagase
Jonathan Jones
Keith Brew
Masahide Kashiwagi
Robert Visse
P2860
P304
P356
10.1042/BJ20100725
P407
P577
2010-10-01T00:00:00Z