About: Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status

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About: Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status Goto Sponge NotDistinct Permalink

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scientific article published on May 1999

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1999 (ast) 1999年學術文章 (zh) наукова стаття, опублікована в травні 1999 (uk) مقالة علمية نشرت في مايو 1999 (ar) scientific article published on May 1999 (en)
publication date	wds:Q37199804-841B9F2F-99B3-4223-97B6-18DF2FB64954
publication date	1999-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37199804-9A315ECA-BDDE-4C18-A182-EE6880F91BB7
language of work or name	English
cites work	wds:Q37199804-0DA1E5A0-FF62-4849-9C7E-A481FF79EEC3 wds:Q37199804-136165E3-5BF9-41D0-8DF1-436C1104A68D wds:Q37199804-202C3C19-EE9A-4178-A64A-A5192CBE33BD wds:Q37199804-2A6286F1-7487-40C1-8A0A-A7315B29D54B wds:Q37199804-3E31ED6D-D33B-41AF-8419-90EF7E01F925 wds:Q37199804-49B49960-014F-4EE7-9697-0B1653149E54 wds:Q37199804-4F505E93-DF9D-4B92-AC2E-B0F1D27AF16A wds:Q37199804-6E15A273-2187-4AB6-B7CF-AFDDA27318E5 wds:Q37199804-7F651D01-827F-4617-9A45-791772F850D8 wds:Q37199804-80475502-6600-4C48-AABA-9003E2326EA5 wds:Q37199804-9FAB5EDD-0A21-4D85-A30B-C9B1A45E7225 wds:Q37199804-A8BB61F5-5D44-417E-857B-09FF3A1C07F2 wds:Q37199804-AAB243A3-2C68-482B-A59C-3CCE84457D0D wds:Q37199804-ACF6DFEB-2A44-43E3-8B81-1C4E6F8DF338 wds:Q37199804-AE2476BA-3F8A-4325-93DD-D4500271EFCB wds:Q37199804-B1E977A4-A1A4-429A-A586-ACB4DFAC5748 wds:Q37199804-BA8779A3-1952-4D0B-A1CF-260604B4F9EE wds:Q37199804-E33B15AC-C62E-4907-9641-21DF8BA16C03 wds:Q37199804-E6DC8C77-B257-4E25-864A-9D44D380E3A1 wds:Q37199804-ECDB401E-E111-4A5A-A1F6-B8C2CA0E7551 wds:Q37199804-EF7682C9-9F6E-4880-9D93-5F64CFC49C33 wds:Q37199804-FEAD15AA-CB89-46B6-A810-B93CA96B96DA
cites work	Chaperone activity with a redox switch Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation A small, stable RNA induced by oxidative stress: role as a pleiotropic regulator and antimutator. Oxidized redox state of glutathione in the endoplasmic reticulum Activation of the OxyR transcription factor by reversible disulfide bond formation Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon OxyR regulon. Determination of glutathione and glutathione disulfide in biological samples The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid Molecular and cellular aspects of thiol-disulfide exchange. Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli. The Levels of Ribonucleotide Reductase, Thioredoxin, Glutaredoxin 1, and GSH Are Balanced inEscherichia coliK12 Effects of peroxides on susceptibilities of Escherichia coli and Mycobacterium smegmatis to isoniazid Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. In vivo transcription of nrdAB operon and of grxA and fpg genes is triggered in Escherichia coli lacking both thioredoxin and glutaredoxin 1 or thioredoxin and glutathione, respectively The in vivo distribution of oxidized and reduced thioredoxin in Escherichia coli
author name string	wds:Q37199804-D3874426-37EE-4449-95BA-7684FB242C92 wds:Q37199804-DA9DF62F-6E8C-4AFA-9B5C-0C248ACAFD57 wds:Q37199804-E966A205-24D0-4462-B60F-04546D21EA5C wds:Q37199804-F4592CAD-B30F-40D9-A8FC-1EC5EE1DE3F9
author name string	J Beckwith M Zheng F Aslund G Storz
rdfs:label	Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (en) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (nl) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (ast)
skos:prefLabel	Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (en) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (nl) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (ast)
name	Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (en) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (nl) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (ast)
title	wds:Q37199804-8FA1C0B7-8E08-49E4-BB84-42D5511D6893
title	Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status (en)
page(s)	wds:Q37199804-5C259A47-37A9-4084-8708-9146E28D301B
page(s)	6161-6165
instance of	wds:Q37199804-C9A57807-661E-4120-8677-541BF9171F9A
instance of	scholarly article
PubMed ID	wds:Q37199804-DDC792BA-487B-4460-BA5D-3F611D76D40A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10339558
PubMed ID	10339558
published in	wds:Q37199804-BCD7EC23-7384-4AD3-B3CC-C6AAF94A7769
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37199804-2D3953D1-188F-4FD7-9338-8C5D072801C3
volume	wds:Q37199804-09C2C76E-E6CD-4C04-BBE8-BC8F412747BA
issue	11
volume	96
DOI	wds:Q37199804-6197482D-D7B4-4B43-92DF-9DC67786F1DD
DOI	http://dx.doi.org/10.1073/PNAS.96.11.6161

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