Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis.
about
Protein kinase D interacts with neuronal nitric oxide synthase and phosphorylates the activatory residue serine 1412Reconstitution of pterin-free inducible nitric-oxide synthase.Induction of nitric oxide synthase-2 proceeds with the concomitant downregulation of the endogenous caveolin levels.Circulating CD133(+)VEGFR2 (+) and CD34 (+)VEGFR2 (+) cells and arterial function in patients with beta-thalassaemia major.Mutating His29, His125, His133 or His158 abolishes glycosylphosphatidylinositol-specific phospholipase D catalytic activity.Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis.Covalent attachment of heme to the protein moiety in an insect E75 nitric oxide sensor.Distinct influence of N-terminal elements on neuronal nitric-oxide synthase structure and catalysis.Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor.Effect of deferasirox (ICL670) on arterial function in patients with beta-thalassaemia major.Protein kinase D activity controls endothelial nitric oxide synthesis.Role of bound zinc in dimer stabilization but not enzyme activity of neuronal nitric-oxide synthase.
P2860
Q28537962-CA90C839-B4FA-4A68-8211-8F44E236F166Q31448893-FAA0B77F-4584-4C20-BDC9-91A510DFE719Q33201335-AB93F656-E891-4B6A-9514-099299DD9B1EQ35742909-C2D0355F-5C7F-4506-BAA9-1456B3D3157BQ39498057-BE2D5BDC-E462-4CD6-A7CA-026986B7FFE8Q40727257-EB1AF54F-8342-4CAA-9794-EE923AA0FFB4Q42011741-0DD8669D-6EB7-4AA4-9894-A6F573AF4666Q44504070-3C5EBCEB-EA4F-4F24-B1E2-21A4C2E74FA6Q46515576-DF6C86D3-8F2A-4548-9BE3-1AE88A5601D2Q46719555-D297914C-61F9-4F24-96B4-3A1E991A0FF4Q50468755-18DB0C18-628C-4B10-83D1-5B4EDB0509C1Q54039650-E4A0CA5B-D1B1-4BEF-AA8A-A0AD68B518CF
P2860
Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mutation of the five conserved ...... tal requirement for catalysis.
@ast
Mutation of the five conserved ...... tal requirement for catalysis.
@en
type
label
Mutation of the five conserved ...... tal requirement for catalysis.
@ast
Mutation of the five conserved ...... tal requirement for catalysis.
@en
prefLabel
Mutation of the five conserved ...... tal requirement for catalysis.
@ast
Mutation of the five conserved ...... tal requirement for catalysis.
@en
P2093
P2860
P356
P1476
Mutation of the five conserved ...... tal requirement for catalysis.
@en
P2093
Nishida CR
Rodríguez-Crespo I
de Montellano PR
P2860
P304
21617-21624
P356
10.1074/JBC.274.31.21617
P407
P577
1999-07-01T00:00:00Z