A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism
about
Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS)NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domainElectron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulinMechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Lobe-specific calcium binding in calmodulin regulates endothelial nitric oxide synthase activation.A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.Intra- and inter-molecular effects of a conserved arginine residue of neuronal and inducible nitric oxide synthases on FMN and calmodulin binding.Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.Energy landscapes and catalysis in nitric-oxide synthase.Binding kinetics of calmodulin with target peptides of three nitric oxide synthase isozymes.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.Tetrahydrobiopterin redox cycling in nitric oxide synthase: evidence supports a through-heme electron delivery.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.G protein-coupled estrogen receptor is involved in modulating colonic motor function via nitric oxide release in C57BL/6 female mice.Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.
P2860
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P2860
A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism
description
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2010
@ast
im August 2010 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/08/20)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/08/20)
@nl
наукова стаття, опублікована в серпні 2010
@uk
name
A bridging interaction allows ...... e through a bi-modal mechanism
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A bridging interaction allows ...... e through a bi-modal mechanism
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A bridging interaction allows ...... e through a bi-modal mechanism
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type
label
A bridging interaction allows ...... e through a bi-modal mechanism
@ast
A bridging interaction allows ...... e through a bi-modal mechanism
@en
A bridging interaction allows ...... e through a bi-modal mechanism
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prefLabel
A bridging interaction allows ...... e through a bi-modal mechanism
@ast
A bridging interaction allows ...... e through a bi-modal mechanism
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A bridging interaction allows ...... e through a bi-modal mechanism
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P2093
P2860
P356
P1476
A bridging interaction allows ...... e through a bi-modal mechanism
@en
P2093
Deborah Durra
Dennis J Stuehr
Mohammad Mahfuzul Haque
P2860
P304
25941-25949
P356
10.1074/JBC.M110.126797
P407
P50
P577
2010-06-07T00:00:00Z