Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2005-11-14
pubmed:abstractText
Reactive oxygen species contribute to the pathogenesis of a number of disparate disorders including tissue inflammation, heart failure, hypertension, and atherosclerosis. In response to oxidative stress, cells activate expression of a number of genes, including those required for the detoxification of reactive molecules as well as for the repair and maintenance of cellular homeostasis. In many cases, these induced genes are regulated by transcription factors whose structure, subcellular localization, or affinity for DNA is directly or indirectly regulated by the level of oxidative stress. This review summarizes the recent progress on how cellular redox status can regulate transcription-factor activity and the implications of this regulation for cardiovascular disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/APEX1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-(Apurinic or Apyrimidinic..., http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Keap1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/NF-E2-Related Factor 2, http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins, http://linkedlifedata.com/resource/pubmed/chemical/SoxR protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/YAP1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/oxyR protein, E coli
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1524-4571
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
967-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16284189-Adaptor Proteins, Signal Transducing, pubmed-meshheading:16284189-Animals, pubmed-meshheading:16284189-Atherosclerosis, pubmed-meshheading:16284189-Bacterial Proteins, pubmed-meshheading:16284189-Cytoskeletal Proteins, pubmed-meshheading:16284189-DNA-(Apurinic or Apyrimidinic Site) Lyase, pubmed-meshheading:16284189-DNA-Binding Proteins, pubmed-meshheading:16284189-Escherichia coli Proteins, pubmed-meshheading:16284189-Histone Deacetylases, pubmed-meshheading:16284189-Humans, pubmed-meshheading:16284189-NAD, pubmed-meshheading:16284189-NF-E2-Related Factor 2, pubmed-meshheading:16284189-Oxidation-Reduction, pubmed-meshheading:16284189-Oxidative Stress, pubmed-meshheading:16284189-Reactive Oxygen Species, pubmed-meshheading:16284189-Repressor Proteins, pubmed-meshheading:16284189-Saccharomyces cerevisiae Proteins, pubmed-meshheading:16284189-Sirtuin 1, pubmed-meshheading:16284189-Sirtuins, pubmed-meshheading:16284189-Transcription, Genetic, pubmed-meshheading:16284189-Transcription Factor AP-1, pubmed-meshheading:16284189-Transcription Factors
pubmed:year
2005
pubmed:articleTitle
Redox-dependent transcriptional regulation.
pubmed:affiliation
National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Intramural