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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0031676,
umls-concept:C0033684,
umls-concept:C0038435,
umls-concept:C0078058,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0225336,
umls-concept:C0441712,
umls-concept:C0443193,
umls-concept:C0679622,
umls-concept:C0851285,
umls-concept:C1256770,
umls-concept:C1412617,
umls-concept:C1552961,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C2911684
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pubmed:issue |
5
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pubmed:dateCreated |
2010-4-15
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pubmed:abstractText |
The ATF4 arm of the unfolded protein response is increasingly recognized for its relevance to pathology, and in particular to angiogenic reactions. Oxidized phospholipids (OxPLs), known to accumulate in atherosclerotic vessels, were shown to upregulate vascular endothelial growth factor (VEGF) and induce angiogenesis via an ATF4-dependent mechanism. In this study, we analyzed the mechanism of ATF4 upregulation by OxPLs and more specifically the involvement of NRF2, the major transcriptional mediator of electrophilic stress response.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATF4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Activating Transcription Factor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/NF-E2-Related Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/NFE2L2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/VEGFA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/oxidized low density lipoprotein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1524-4636
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1007-13
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pubmed:meshHeading |
pubmed-meshheading:20185790-Activating Transcription Factor 4,
pubmed-meshheading:20185790-Binding Sites,
pubmed-meshheading:20185790-Blotting, Western,
pubmed-meshheading:20185790-Cells, Cultured,
pubmed-meshheading:20185790-Chromatin Immunoprecipitation,
pubmed-meshheading:20185790-Endothelial Cells,
pubmed-meshheading:20185790-Humans,
pubmed-meshheading:20185790-Lipoproteins, LDL,
pubmed-meshheading:20185790-NF-E2-Related Factor 2,
pubmed-meshheading:20185790-Neovascularization, Physiologic,
pubmed-meshheading:20185790-Oxidation-Reduction,
pubmed-meshheading:20185790-Phospholipids,
pubmed-meshheading:20185790-Promoter Regions, Genetic,
pubmed-meshheading:20185790-Prostaglandins,
pubmed-meshheading:20185790-RNA, Messenger,
pubmed-meshheading:20185790-RNA Interference,
pubmed-meshheading:20185790-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20185790-Stress, Physiological,
pubmed-meshheading:20185790-Time Factors,
pubmed-meshheading:20185790-Transcriptional Activation,
pubmed-meshheading:20185790-Unfolded Protein Response,
pubmed-meshheading:20185790-Up-Regulation,
pubmed-meshheading:20185790-Vascular Endothelial Growth Factor A
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pubmed:year |
2010
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pubmed:articleTitle |
Oxidized phospholipids regulate expression of ATF4 and VEGF in endothelial cells via NRF2-dependent mechanism: novel point of convergence between electrophilic and unfolded protein stress pathways.
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pubmed:affiliation |
Department of Vascular Biology and Thrombosis Research, Center for Biomolecular Medicine and Pharmacology, Medical University of Vienna, Schwarzspanierstrasse 17, 1090 Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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