RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
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Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidansDevelopment of the bacterial photosynthetic apparatusStimulus perception in bacterial signal-transducing histidine kinasesCys303 in the histidine kinase PhoR is crucial for the phosphotransfer reaction in the PhoPR two-component system in Bacillus subtilisCbbR, the Master Regulator for Microbial Carbon Dioxide FixationWhy chloroplasts and mitochondria retain their own genomes and genetic systems: Colocation for redox regulation of gene expressionThe Hidden World within Plants: Ecological and Evolutionary Considerations for Defining Functioning of Microbial EndophytesThe complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environmentsRegulation of ciaXRH operon expression and identification of the CiaR regulon in Streptococcus mutans.Novel regulatory cascades controlling expression of nitrogen-fixation genes in Geobacter sulfurreducens.Role of the Irr protein in the regulation of iron metabolism in Rhodobacter sphaeroidesBioinformatic Approaches Including Predictive Metagenomic Profiling Reveal Characteristics of Bacterial Response to Petroleum Hydrocarbon Contamination in Diverse Environments.RegA Plays a Key Role in Oxygen-Dependent Establishment of Persistence and in Isocitrate Lyase Activity, a Critical Determinant of In vivo Brucella suis Pathogenicity.The tetrapyrrole biosynthetic pathway and its regulation in Rhodobacter capsulatus.Carbon dioxide fixation as a central redox cofactor recycling mechanism in bacteriaRegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone poolA novel three-protein two-component system provides a regulatory twist on an established circuit to modulate expression of the cbbI region of Rhodopseudomonas palustris CGA010A LexA-related protein regulates redox-sensitive expression of the cyanobacterial RNA helicase, crhRThiol-based redox switches and gene regulationWhole-genome transcriptional analysis of chemolithoautotrophic thiosulfate oxidation by Thiobacillus denitrificans under aerobic versus denitrifying conditionsThe poor growth of Rhodospirillum rubrum mutants lacking RubisCO is due to the accumulation of ribulose-1,5-bisphosphateDifferent roles of the two high-oxygen-affinity terminal oxidases of Brucella suis: Cytochrome c oxidase, but not ubiquinol oxidase, is required for persistence in miceAnalysis of the FnrL regulon in Rhodobacter capsulatus reveals limited regulon overlap with orthologues from Rhodobacter sphaeroides and Escherichia coli.The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidasesEvolution of a bacteriophytochrome from light to redox sensorQuinol oxidase encoded by cyoABCD in Rhizobium etli CFN42 is regulated by ActSR and is crucial for growth at low pH or low iron conditions.New target genes controlled by the Bradyrhizobium japonicum two-component regulatory system RegSRRegA control of bacteriochlorophyll and carotenoid synthesis in Rhodobacter capsulatus.RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid.Role of the global transcriptional regulator PrrA in Rhodobacter sphaeroides 2.4.1: combined transcriptome and proteome analysis.Nitrogen metabolism in haloarchaeaActivation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides.Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions.RegA, the regulator of the two-component system RegB/RegA of Brucella suis, is a controller of both oxidative respiration and denitrification required for chronic infection in miceControlling the delicate balance of tetrapyrrole biosynthesis.Regulation of gene expression by PrrA in Rhodobacter sphaeroides 2.4.1: role of polyamines and DNA topology.Half-Site DNA sequence and spacing length contributions to PrrA binding to PrrA site 2 of RSP3361 in Rhodobacter sphaeroides 2.4.1.Purification and assays of Rhodobacter capsulatus RegB-RegA two-component signal transduction system.Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegBCarbon catabolite repression in Pseudomonas : optimizing metabolic versatility and interactions with the environment.
P2860
Q21283753-04191966-4614-4641-BFAB-59C6CED0C081Q24649927-F4F86696-F582-4B0D-B9E5-F8898C7267C2Q24672531-1324CE0D-3D62-4E04-AD3D-2E63C6D706A2Q24675933-2D7A2875-12DA-4530-BD2F-19B55442A464Q26795663-51E597C4-7BB6-433D-BB80-16614FAA0444Q26796678-D8A2ACDA-4691-4D00-9780-AB6CEEDE3E46Q27008650-1D049F8B-3156-4D94-A371-D3900A69F835Q28752350-287DEF6F-4066-459B-BF6E-15D21111A8C5Q29346575-33B7AA15-CA7C-4548-B5AE-664C7ED0AF59Q29346628-D33628C7-0BFE-44BD-B758-29AFBE6F30D3Q31081784-8BFDECAF-E6EE-46FF-A0C1-002DFD85974DQ33682296-560701A9-3FEE-4086-A853-A95761E22841Q33700813-5DD037FC-D38E-4A61-B293-38AC3AF8972FQ33906420-3573D060-C239-4BBD-A8FA-D2FBB34640D0Q33977889-A8859664-ED54-47AC-ABA5-73D50B78995EQ34398742-72233851-4CAE-4E91-A116-37AAD194FE0FQ34563278-EC296BD2-CFE0-47B9-85ED-50BA9ADCC6DEQ34882546-B3244151-CE6D-4028-93A2-F6124C49269CQ35040525-4AF39EB3-BB21-45B1-AD69-BC8BDD263F8DQ35075731-1D1CC8DB-1D38-40D2-9ED8-15CB417F5FC0Q35096333-8F97768B-7A71-4808-B10D-5600A1902706Q35688983-4CF994D8-A807-4177-AEE7-937BD1283667Q35832790-426A95D9-D08B-4CCB-A0DE-184F54A9760FQ35911449-95C7386D-8095-43CD-A320-AF804F9C27E7Q35914611-7A51A921-F1F0-4A7A-8F7F-1D1A58F8A0C5Q36255028-982815C9-35A1-4E18-A931-9C40D630026BQ36314715-14DC105A-2D38-4BF4-A4A3-C19DF6F1083BQ36314887-8DBEFBF5-7771-4546-8DF2-F18AC6074087Q36620755-CD27E74F-C961-4BEB-AEB4-FA09C7878442Q36747822-A78D5997-ECDC-47A0-94A0-19E1AD32EF6AQ36789906-D3A58792-DDD8-4F6B-B955-26CAD870B711Q36839157-817A8A7D-2B08-444E-B7C8-977BBD98B2D2Q36845082-2A68273B-B9C8-44BD-AB0F-50BDA98D08C1Q36911365-FB379842-3B6B-4280-9CC3-3ECDE4B77CB7Q36937107-764000BA-E48E-4107-AEC1-897CA293C199Q37232699-E192582D-7012-4B47-AF56-4815EE999617Q37232718-7F7BE5C1-D508-4828-A9EE-9D1C33449D09Q37415112-6859A10D-A753-40B1-B22B-FA7564A39328Q37418585-A22ACAA6-CEA1-4009-9B13-1EF2AF2FC28CQ37735901-DA71B057-4EC7-498B-9981-57B0C247867D
P2860
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@ast
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@en
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@nl
type
label
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@ast
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@en
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@nl
prefLabel
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@ast
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@en
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@nl
P2093
P2860
P1476
RegB/RegA, a highly conserved redox-responding global two-component regulatory system.
@en
P2093
Carl E Bauer
Danielle L Swem
Lee R Swem
Sylvie Elsen
P2860
P304
P356
10.1128/MMBR.68.2.263-279.2004
P577
2004-06-01T00:00:00Z