Source:http://linkedlifedata.com/resource/pubmed/id/17081101
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10-11
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pubmed:dateCreated |
2006-11-3
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pubmed:abstractText |
Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as inflammatory and hypoxic responses. While Nrf2 protein stabilization is known to be redox-sensitive, the transcription factors NF-kappaB and HIF-1alpha for inflammatory and hypoxic responses, respectively, are also influenced by the cellular redox conditions. In this review we present the recently proposed two-site substrate recognition model of the Keap1-Nrf2 system, which regulates the cellular responses against oxidative and xenobiotic stresses. The implications of two destructive motifs in Nrf2, the ETGE and DLG motifs, which appear to function as a hinge and latch attenuating Keap1 activity in different redox states, are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1431-6730
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
387
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1311-20
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pubmed:meshHeading |
pubmed-meshheading:17081101-Animals,
pubmed-meshheading:17081101-Humans,
pubmed-meshheading:17081101-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:17081101-Models, Biological,
pubmed-meshheading:17081101-NF-E2-Related Factor 2,
pubmed-meshheading:17081101-Proteasome Endopeptidase Complex,
pubmed-meshheading:17081101-Protein Binding,
pubmed-meshheading:17081101-Substrate Specificity
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pubmed:articleTitle |
Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism.
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pubmed:affiliation |
Graduate School of Comprehensive Human Sciences, Center for Tsukuba Advanced Research Alliance and JST-ERATO Environmental Response Project, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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