Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme
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Matrix Metalloproteinase-10 (MMP-10) Interaction with Tissue Inhibitors of Metalloproteinases TIMP-1 and TIMP-2: BINDING STUDIES AND CRYSTAL STRUCTUREMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesTemporal dynamics of gene expression in the lung in a baboon model of E. coli sepsisThe evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio.Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria.Progress in matrix metalloproteinase research.The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversityTIMP3: a physiological regulator of adult myogenesis.Regulation of myogenic activation of p38 MAPK by TACE-mediated TNFα releaseSelective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).Dynamic interdomain interactions contribute to the inhibition of matrix metalloproteinases by tissue inhibitors of metalloproteinases.Contribution of TIMP3 polymorphisms to the development of preeclampsia in Han Chinese women.What are the roles of metalloproteinases in cartilage and bone damage?Insights into ectodomain shedding and processing of protein-tyrosine pseudokinase 7 (PTK7)ADAMTS13 and 15 are not regulated by the full length and N-terminal domain forms of TIMP-1, -2, -3 and -4.Tissue inhibitor of metalloproteinases-4. The road less traveled.TIMPs: versatile extracellular regulators in cancer.Identification of the extracellular matrix (ECM) binding motifs of tissue inhibitor of metalloproteinases (TIMP)-3 and effective transfer to TIMP-1.Considerations on inhibition approaches for proinflammatory functions of ADAM proteases.Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not tumor necrosis factor-alpha-converting enzyme.
P2860
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P2860
Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@ast
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@en
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@nl
type
label
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@ast
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@en
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@nl
prefLabel
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@ast
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@en
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@nl
P2093
P2860
P356
P1476
Total conversion of tissue inh ...... ctor-{alpha}-converting enzyme
@en
P2093
Gillian Murphy
Magdalini Rapti
Meng-Huee Lee
P2860
P304
P356
10.1074/JBC.M500897200
P407
P577
2005-04-22T00:00:00Z