Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes. - Wikidata - awgldk - TriplyDB

Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes.

Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes.

http://www.wikidata.org/entity/Q37608175

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Kinetics of CO binding to the haem domain of murine inducible nitric oxide synthase: differential effects of haem domain ligands Subunit interactions of endothelial nitric-oxide synthase. Comparisons to the neuronal and inducible nitric-oxide synthase isoforms Mutational analysis of the tetrahydrobiopterin-binding site in inducible nitric-oxide synthase.Precise spatiotemporal control of optogenetic activation using an acousto-optic device.Subcellular targeting and differential S-nitrosylation of endothelial nitric-oxide synthase.Regulation of inducible nitric oxide synthase by rapid cellular turnover and cotranslational down-regulation by dimerization inhibitors.Characterization of key residues in the subdomain encoded by exons 8 and 9 of human inducible nitric oxide synthase: a critical role for Asp-280 in substrate binding and subunit interactions.Cloning and characterization of human inducible nitric oxide synthase splice variants: a domain, encoded by exons 8 and 9, is critical for dimerization Life history of eNOS: partners and pathways.Immunobiology of Nitric Oxide and Regulation of Inducible Nitric Oxide Synthase.Physiological and hypoxic O2 tensions rapidly regulate NO production by stimulated macrophages.Identification of residues critical for enzymatic activity in the domain encoded by exons 8 and 9 of the human inducible nitric oxide synthase.Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway.Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer.Distinct dimer interaction and regulation in nitric-oxide synthase types I, II, and III.Bone marrow-derived alternatively activated macrophages reduce colitis without promoting fibrosis: participation of IL-10.Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer.Regulation of voltage-dependent K+ channels by methionine oxidation: effect of nitric oxide and vitamin C.Targeting the superoxide/nitric oxide ratio by L-arginine and SOD mimic in diabetic rat skin.

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Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes.

http://www.wikidata.org/entity/Q37608175

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 1996

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Complementation analysis of mu ...... ctive site requires two hemes.

@en

Complementation analysis of mu ...... ctive site requires two hemes.

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type

label

Complementation analysis of mu ...... ctive site requires two hemes.

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Complementation analysis of mu ...... ctive site requires two hemes.

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prefLabel

Complementation analysis of mu ...... ctive site requires two hemes.

@en

Complementation analysis of mu ...... ctive site requires two hemes.

@nl

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PNAS.93.10.4891

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Proceedings of the National Academy of Sciences of the United States of America

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Complementation analysis of mu ...... ctive site requires two hemes.

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C Nathan

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M Leung

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical

Inducible nitric oxide synthase: identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin

Molecular and biochemical characterization of dNOS: a Drosophila Ca2+/calmodulin-dependent nitric oxide synthase.

Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide.

Purification of a soluble isoform of guanylyl cyclase-activating-factor synthase

Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: an FAD- and FMN-containing flavoprotein.

Prokaryotic expression of the heme- and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: identification of the heme-binding proximal thiolate ligand as cysteine-415.

Cloning and characterization of inducible nitric oxide synthase from mouse macrophages.

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4891-4896

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scholarly article

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10.1073/PNAS.93.10.4891

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