Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. - Wikidata - awgldk - TriplyDB

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

http://www.wikidata.org/entity/Q33883723

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Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1 NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum Nitric oxide synthases: structure, function and inhibition Nitric oxide synthases: regulation and function A conserved aspartate (Asp-1393) regulates NADPH reduction of neuronal nitric-oxide synthase: implications for catalysis Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme Regulation of interdomain electron transfer in the NOS output state for NO production Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer.Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme.Development of nitric oxide synthase inhibitors for neurodegeneration and neuropathic pain.Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Comparing the temperature dependence of FMN to heme electron transfer in full length and truncated inducible nitric oxide synthase proteins Oxygen reduction by nitric-oxide synthases.Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Bacillus megaterium has both a functional BluB protein required for DMB synthesis and a related flavoprotein that forms a stable radical species Pulsed ENDOR determination of relative orientation of g-frame and molecular frame of imidazole-coordinated heme center of iNOS Therapeutic effect of enhancing endothelial nitric oxide synthase (eNOS) expression and preventing eNOS uncoupling.Solving Kinetic Equations for the Laser Flash Photolysis Experiment on Nitric Oxide Synthases: Effect of Conformational Dynamics on the Interdomain Electron Transfer.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.Janus-faced role of endothelial NO synthase in vascular disease: uncoupling of oxygen reduction from NO synthesis and its pharmacological reversal.Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.Two synthetic peptides corresponding to the proximal heme-binding domain and CD1 domain of human endothelial nitric-oxide synthase inhibit the oxygenase activity by interacting with CaM Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Dynamic control of electron transfers in diflavin reductases.The yin and yang of nitric oxide in cancer progression.Nitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity.Compartmentalized nitric oxide signaling in the resistance vasculature Nitric-oxide synthase output state. Design and properties of nitric-oxide synthase oxygenase/FMN domain constructs.Redox properties of human endothelial nitric-oxide synthase oxygenase and reductase domains purified from yeast expression system.Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis.Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase.Dissecting the kinetics of the NADP(+)-FADH2 charge transfer complex and flavin semiquinones in neuronal nitric oxide synthase.

P2860

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P2860

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

http://www.wikidata.org/entity/Q33883723

description

1999 nî lūn-bûn

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1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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type

label

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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prefLabel

Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase.

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Chapman SK

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