About: Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release

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About: Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) vědecký článek publikovaný v roce 2002 (cs) 2002 թվականի մայիսին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в травні 2002 (uk) 2002 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) article scientifique publié en 2002 (fr) vedecký článok (publikovaný 2002/05/03) (sk) wetenschappelijk artikel (gepubliceerd op 2002/05/03) (nl) مقالة علمية (نشرت في 3-5-2002) (ar) im Mai 2002 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28609861-E9A9DCB0-994E-4E3D-A7C6-A211AC6BA779
publication date	2002-05-03 00:00:00Z (xsd:dateTime)
cites work	wds:Q28609861-AA3A9DC5-BE6F-4B58-9E6E-88E60CA9B33D
cites work	Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
author name string	wds:Q28609861-2E356EAA-3A24-4A34-8CA9-37654F96012B wds:Q28609861-2F82CF07-9CAC-4F93-82EF-0C77EAAA4AED wds:Q28609861-56167944-D464-4351-A113-19652ABD59A2 wds:Q28609861-684AE7AE-C65B-4910-A998-AB9D18A2D39F wds:Q28609861-8B382010-AEB3-4BF0-AC8D-B82ABFE6D0A5 wds:Q28609861-94D354F4-76C0-42CA-BBBD-07300C760FB1
OpenCitations bibliographic resource ID	wds:Q28609861-44AF21E2-A3D0-45DC-9FA5-01EBD76E51CA
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4879885
author name string	Yan Chen Takashi Tsuruo Naoya Fujita Jason Fontana Todd A. Fairchild Timothy J. McCabe
OpenCitations bibliographic resource ID	4879885
rdfs:label	Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (en) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (nl) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (ast)
skos:prefLabel	Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (en) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (nl) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (ast)
name	Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (en) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (nl) Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (ast)
author	wds:Q28609861-C5E41F3C-7F71-44BB-8A86-3BACA844E5FB wds:Q28609861-EC41E599-FC92-4AEE-88AF-C3E94DCB1693
author	William C. Sessa David Fulton
title	wds:Q28609861-9901885F-1A0D-4233-A037-3C85FFBE2A21
title	Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release (en)
page(s)	wds:Q28609861-F45E0311-A148-499B-8820-FB4FF4047984
page(s)	866–873
instance of	wds:Q28609861-709F9E6D-35FC-4F9A-98C6-C85483F81CC1
instance of	scholarly article
main subject	wds:Q28609861-380B9B9E-C4E8-4DCC-B38F-3F173E461076 wds:Q28609861-3FF0D66B-025A-4F69-A0E9-7A3911B4BC73 wds:Q28609861-A9F2A075-4EBE-4783-853F-586E848896CD
main subject	phosphorylation endothelium molecular scaffold
PubMed ID	wds:Q28609861-7672B8D0-A69E-49A9-9714-5D50F0E83718
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11988487
PubMed ID	11988487
published in	wds:Q28609861-FC2F9E7B-FC0F-410D-BEB8-CDC8E276CF4A
published in	Circulation Research
issue	wds:Q28609861-55716C0A-1C67-4733-BD16-DF5968425EBF
volume	wds:Q28609861-42803467-926A-4F9A-86E4-C2734FFFDA0C
issue	8
volume	90
DOI	wds:Q28609861-BE08A5EC-1932-4E8D-A12E-FAB1EAF34CB9
DOI	http://dx.doi.org/10.1161/01.RES.0000016837.26733.BE
DOI	10.1161/01.RES.0000016837.26733.BE
Fatcat ID	wds:Q28609861-00713CDB-EC1B-4CD7-9CBB-40A3759D3151
Fatcat ID	release_hecfdrrtkvezbgcuotgamiwuue
ResearchGate publication ID	wds:Q28609861-F3655D91-6B49-4862-9767-5EC31F42378B
ResearchGate publication ID	11380796
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28609861
is cites work of	Antihypertensive therapy increases tetrahydrobiopterin levels and NO/cGMP signaling in small arteries of angiotensin II-infused hypertensive rats Structural basis for depletion of heat shock protein 90 client proteins by deguelin. Heat-induced increases in endothelial NO synthase expression and activity and endothelial NO release Enhanced eNOS Activation as the Fountain of Youth for Vascular Disease: Is BPIFB4 What Ponce de León Was Looking For? Novel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthase Endothelial function. From vascular biology to clinical applications Calmodulin-dependent and -independent activation of endothelial nitric-oxide synthase by heat shock protein 90. Recent advances in understanding endothelial dysfunction in atherosclerosis Post-translational mechanisms of endothelial nitric oxide synthase regulation by bradykinin Posttranslational modification of constitutive nitric oxide synthase in the penis The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37) Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme Subcellular targeting and trafficking of nitric oxide synthases Molecular targeting therapy of cancer: drug resistance, apoptosis and survival signal Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1 Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone G Protein-coupled Receptor Kinase Interaction with Hsp90 Mediates Kinase Maturation Submaximal PPARγ activation and endothelial dysfunction: new perspectives for the management of cardiovascular disorders Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft Hyperoxia, endothelial progenitor cell mobilization, and diabetic wound healing There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling The critical role of Akt in cardiovascular function S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities Schizosaccharomyces pombe Hsp90/Git10 is required for glucose/cAMP signaling. Immunohistochemical detection of Hsp90 and Ki-67 in pterygium Ligand and protein fishing with heat shock protein 90 coated magnetic beads.

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