Thiol/Disulfide redox switches in the regulation of heme binding to proteins. - Wikidata - awgldk - TriplyDB

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

http://www.wikidata.org/entity/Q34589250

about

Mitochondrial Cytochrome c Oxidase Biogenesis Is Regulated by the Redox State of a Heme-Binding Translational Activator Cysteine-independent activation/inhibition of heme oxygenase-2 A review on hemeoxygenase-2: focus on cellular protection and oxygen response Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase.Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA from Anabaena sp. PCC 7120.Regulation of sGC via hsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives.Heme Oxygenases in Cardiovascular Health and Disease.Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS).Tailoring nanoarchitectonics to control the release profile of payloads.Glutathione deficiency of the Arabidopsis mutant pad2-1 affects oxidative stress-related events, defense gene expression, and the hypersensitive response.Heme Oxygenase-2 Localizes to Mitochondria and Regulates Hypoxic Responses in Hepatocytes.

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P2860

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

http://www.wikidata.org/entity/Q34589250

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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type

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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prefLabel

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

@ast

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

@en

Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

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Antioxidants & Redox Signaling

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Thiol/Disulfide redox switches in the regulation of heme binding to proteins.

@en

P2093

Li Yi

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Stephen W Ragsdale

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P2860

Hemoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel

Neural roles for heme oxygenase: contrasts to nitric oxide synthase

Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2

The RCK1 high-affinity Ca2+ sensor confers carbon monoxide sensitivity to Slo1 BK channels

The RCK2 domain of the human BKCa channel is a calcium sensor

Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

Quantitative analysis of complex protein mixtures using isotope-coded affinity tags

New disguises for an old channel: MaxiK channel beta-subunits

Hemeoxygenase-2 as an O2 sensor in K+ channel-dependent chemotransduction

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1039-1047

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scholarly article

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10.1089/ARS.2010.3436

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6

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14

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2010-12-27T00:00:00Z

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46123273

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20812781

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3042308

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