15569838

Source:http://linkedlifedata.com/resource/pubmed/id/15569838

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0003762, umls-concept:C0014257, umls-concept:C0040018, umls-concept:C0086418, umls-concept:C0277785, umls-concept:C1704259, umls-concept:C1705987, umls-concept:C2267219
pubmed:issue	24
pubmed:dateCreated	2004-12-14
pubmed:abstractText	Arginase competes with endothelial nitric oxide synthase (eNOS) for the substrate l-arginine and decreases NO production. This study investigated regulatory mechanisms of arginase activity in endothelial cells and its role in atherosclerosis.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0147763
pubmed:citationSubset	AIM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E, http://linkedlifedata.com/resource/pubmed/chemical/Arginase, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/NOS3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type III, http://linkedlifedata.com/resource/pubmed/chemical/Nos3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Thrombin, http://linkedlifedata.com/resource/pubmed/chemical/rho-Associated Kinases, http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1524-4539
pubmed:author	pubmed-author:BarandierChristineC, pubmed-author:HayozDanielD, pubmed-author:KwakBrenda RBR, pubmed-author:MachFrançoisF, pubmed-author:MazzolaiLuciaL, pubmed-author:MingXiu-FenXF, pubmed-author:MontaniJean-PierreJP, pubmed-author:RuffieuxJeanJ, pubmed-author:RusconiSandroS, pubmed-author:ViswambharanHemaH, pubmed-author:YangZhihongZ
pubmed:issnType	Electronic
pubmed:day	14
pubmed:volume	110
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	3708-14
pubmed:dateRevised	2007-11-15
pubmed:meshHeading	pubmed-meshheading:15569838-Animals, pubmed-meshheading:15569838-Aorta, Thoracic, pubmed-meshheading:15569838-Apolipoproteins E, pubmed-meshheading:15569838-Arginase, pubmed-meshheading:15569838-Arteriosclerosis, pubmed-meshheading:15569838-Cells, Cultured, pubmed-meshheading:15569838-Endothelial Cells, pubmed-meshheading:15569838-Endothelium, Vascular, pubmed-meshheading:15569838-Enzyme Activation, pubmed-meshheading:15569838-Humans, pubmed-meshheading:15569838-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:15569838-Isoenzymes, pubmed-meshheading:15569838-Male, pubmed-meshheading:15569838-Mice, pubmed-meshheading:15569838-Mice, Inbred C57BL, pubmed-meshheading:15569838-Mice, Knockout, pubmed-meshheading:15569838-Mutation, pubmed-meshheading:15569838-Nitric Oxide Synthase, pubmed-meshheading:15569838-Nitric Oxide Synthase Type II, pubmed-meshheading:15569838-Nitric Oxide Synthase Type III, pubmed-meshheading:15569838-Protein-Serine-Threonine Kinases, pubmed-meshheading:15569838-Signal Transduction, pubmed-meshheading:15569838-Thrombin, pubmed-meshheading:15569838-Umbilical Veins, pubmed-meshheading:15569838-rho-Associated Kinases, pubmed-meshheading:15569838-rhoA GTP-Binding Protein
pubmed:year	2004
pubmed:articleTitle	Thrombin stimulates human endothelial arginase enzymatic activity via RhoA/ROCK pathway: implications for atherosclerotic endothelial dysfunction.
pubmed:affiliation	Vascular Biology, Department of Medicine, Division of Physiology, University of Fribourg, Fribourg, Switzerland.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't