About: Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases

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About: Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases Goto Sponge NotDistinct Permalink

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scientific article published on 01 February 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 2000 (uk) im Februar 2000 veröffentlichter wissenschaftlicher Artikel (de) wüsseschaftlicher Artikel, wo im Hornig 2000 veröffentlicht worden isch (gsw) artículu científicu espublizáu en febreru de 2000 (ast) artikull shkencor i botuar më 01 shkurt 2000 (sq) scientific article published on 01 February 2000 (en)
publication date	wds:Q73441813-E8111DF9-0122-4FD7-A4C2-CFACD18D2DCE
publication date	2000-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73441813-FAB27001-B171-4EDF-BA13-E8499F034655
language of work or name	English
cites work	wds:Q73441813-A257A1E7-A5EB-4B4A-8600-9460C3A6014F wds:Q73441813-B7E570CD-DCE9-4F09-B8B7-7E3B192CD176
cites work	Regulation of endothelium-derived nitric oxide production by the protein kinase Akt Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
author name string	wds:Q73441813-5958048F-FC14-4404-ADC0-560959DE81F8 wds:Q73441813-8FEACEBC-66A3-4D45-8590-AAB5E84E315E wds:Q73441813-98C62302-BD20-4DD0-8B46-26361D6E605D wds:Q73441813-9EEC2474-E429-4CA8-8CC1-F91CFDF07B4D wds:Q73441813-BB47D5BA-7409-42FD-9428-CCA217FE311E wds:Q73441813-D668E50C-3DF8-4CBE-951A-A0FB412E8F0D
author name string	H E Meyer M Bernhardt H H Schmidt S M Lohmann L G Fröhlich P Kotsonis
rdfs:label	Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (en) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (nl) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (sq)
skos:prefLabel	Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (en) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (nl) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (sq)
name	Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (en) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (nl) Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (sq)
author	wds:Q73441813-650B19F1-1ABA-4D00-9040-DD9C91ED5D03 wds:Q73441813-6BA6357A-8120-4E9A-8DC4-40C24C4AF132 wds:Q73441813-D41C6F25-B89A-4B17-8EBE-AA8F560264D5
author	Albert Sickmann Albert Smolenski Elke Butt
title	wds:Q73441813-4579A9D3-CD08-4958-94D9-8A69B0E11184
title	Endothelial nitric-oxide synthase (type III) is activated and becomes calcium independent upon phosphorylation by cyclic nucleotide-dependent protein kinases (en)
page(s)	wds:Q73441813-2E0DFC5A-9990-404B-9706-AF4E620E96BC
page(s)	5179-5187
instance of	wds:Q73441813-D6B68078-B0F0-43D5-8606-1395F7B78889
instance of	scholarly article
PubMed ID	wds:Q73441813-0A600942-7C21-499D-BB4A-3BF38BFAD2F2
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10671564
PubMed ID	10671564
published in	wds:Q73441813-502BC370-8295-4EF4-9744-C78AA1752238
published in	Journal of Biological Chemistry
issue	wds:Q73441813-C438FD63-13A3-45CA-B1B9-F62CC15279D3
volume	wds:Q73441813-2689C2EE-4E3B-41B0-832B-521545B1D0B4
issue	7
volume	275
DOI	wds:Q73441813-724CCAF4-4FA1-40B2-A5DF-DD19DBC35BA4
DOI	http://dx.doi.org/10.1074/JBC.275.7.5179
DOI	10.1074/JBC.275.7.5179
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73441813
is cites work of	Reactive oxygen species and erectile dysfunction: possible role of NADPH oxidase. Endothelial nitric oxide synthase phosphorylation in treadmill-running mice: role of vascular signalling kinases. Phosphorylated Endothelial Nitric Oxide Synthase Mediates Vascular Endothelial Growth Factor-Induced Penile Erection1 Neural regulation of lacrimal gland secretory processes: relevance in dry eye diseases Role of endothelial nitric oxide in cerebrovascular regulation Reduced cGMP signaling associated with neointimal proliferation and vascular dysfunction in late-stage atherosclerosis Vascular nitric oxide: Beyond eNOS Post-translational mechanisms of endothelial nitric oxide synthase regulation by bradykinin eNOS, metabolic syndrome and cardiovascular disease. The phosphorylation state of eNOS modulates vascular reactivity and outcome of cerebral ischemia in vivo Cyclic GMP signaling in cardiovascular pathophysiology and therapeutics Nitric oxide-dependent beta2-adrenergic dilatation of rat aorta is mediated through activation of both protein kinase A and Akt Phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca(2+) concentrations required for calmodulin to bind and activate the enzyme Dependence of soluble guanylyl cyclase activity on calcium signaling in pituitary cells. A conserved tryptophan 457 modulates the kinetics and extent of N-hydroxy-L-arginine oxidation by inducible nitric-oxide synthase There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling The role of shear stress in the pathogenesis of atherosclerosis Molecular mechanisms underlying the activation of eNOS. Differential regulation of inducible and endothelial nitric oxide synthase by kinin B1 and B2 receptors cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action Regulation of endothelial and myocardial NO synthesis by multi-site eNOS phosphorylation Protein kinase Cdelta regulates endothelial nitric oxide synthase expression via Akt activation and nitric oxide generation AMP-activated protein kinase functionally phosphorylates endothelial nitric oxide synthase Ser633 Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock Pim1 kinase promotes angiogenesis through phosphorylation of endothelial nitric oxide synthase at Ser-633. Endothelial nitric oxide synthase transgenic models of endothelial dysfunction The endothelium and its role in regulating vascular tone Structural basis for endothelial nitric oxide synthase binding to calmodulin Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase Chimeric Enzymes of Cytochrome P450 Oxidoreductase and Neuronal Nitric-oxide Synthase Reductase Domain Reveal Structural and Functional Differences Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain Deficient eNOS phosphorylation is a mechanism for diabetic vascular dysfunction contributing to increased stroke size. Pathophysiology of the diabetic kidney. Regulation of eNOS enzyme activity by posttranslational modification. The cellular mechanisms by which adenosine evokes release of nitric oxide from rat aortic endothelium Endothelial NO synthase phosphorylated at SER635 produces NO without requiring intracellular calcium increase Role of calcitonin gene-related peptide in cerebral vasospasm, and as a therapeutic approach to subarachnoid hemorrhage Rapid increase in endothelial nitric oxide production by bradykinin is mediated by protein kinase A signaling pathway

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