PhoP can activate its target genes in a PhoQ-independent manner. - Wikidata - awgldk - TriplyDB

PhoP can activate its target genes in a PhoQ-independent manner.

PhoP can activate its target genes in a PhoQ-independent manner.

http://www.wikidata.org/entity/Q34001462

about

Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride The Atypical Response Regulator Protein ChxR Has Structural Characteristics and Dimer Interface Interactions That Are Unique within the OmpR/PhoB Subfamily Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis Mycobacterium tuberculosis DevR/DosR Dormancy Regulator Activation Mechanism: Dispensability of Phosphorylation, Cooperativity and Essentiality of α10 Helix Stimulus-dependent differential regulation in the Escherichia coli PhoQ PhoP system Coordinated regulation of virulence during systemic infection of Salmonella enterica serovar Typhimurium.Positive autoregulation shapes response timing and intensity in two-component signal transduction systems.Appropriate DevR (DosR)-mediated signaling determines transcriptional response, hypoxic viability and virulence of Mycobacterium tuberculosis Visualization of vacuolar acidification-induced transcription of genes of pathogens inside macrophages.Discovery of novel secreted virulence factors from Salmonella enterica serovar Typhimurium by proteomic analysis of culture supernatants.A novel two-component signaling system facilitates uropathogenic Escherichia coli's ability to exploit abundant host metabolites.PhoP-induced genes within Salmonella pathogenicity island 1.SrfJ, a Salmonella type III secretion system effector regulated by PhoP, RcsB, and IolR.Induction of RpoS degradation by the two-component system regulator RstA in Salmonella enterica Regulation of multidrug efflux systems involved in multidrug and metal resistance of Salmonella enterica serovar Typhimurium PhoP-PhoP interaction at adjacent PhoP binding sites is influenced by protein phosphorylation Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.Bacterial response regulators: versatile regulatory strategies from common domains.RstA-promoted expression of the ferrous iron transporter FeoB under iron-replete conditions enhances Fur activity in Salmonella enterica.Mg2+ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide.Molecular mechanism for establishment of signal-dependent regulation in the PhoP/PhoQ system.mgtA Expression is induced by rob overexpression and mediates a Salmonella enterica resistance phenotype Characterization of phagosome trafficking and identification of PhoP-regulated genes important for survival of Yersinia pestis in macrophages.Unique N-terminal arm of Mycobacterium tuberculosis PhoP protein plays an unusual role in its regulatory function.Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: role of the linker region in regulator-promoter interaction(s).CtrA, a global response regulator, uses a distinct second category of weak DNA binding sites for cell cycle transcription control in Caulobacter crescentus.Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo.Activation of the AtoSC two-component system in the absence of the AtoC N-terminal receiver domain in E. coli.HilD and PhoP independently regulate the expression of grhD1, a novel gene required for Salmonella Typhimurium invasion of host cells.

P2860

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P2860

PhoP can activate its target genes in a PhoQ-independent manner.

http://www.wikidata.org/entity/Q34001462

description

2004 nî lūn-bûn

@nan

2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին 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

PhoP can activate its target genes in a PhoQ-independent manner.

@ast

PhoP can activate its target genes in a PhoQ-independent manner.

@en

PhoP can activate its target genes in a PhoQ-independent manner.

@nl

type

label

PhoP can activate its target genes in a PhoQ-independent manner.

@ast

PhoP can activate its target genes in a PhoQ-independent manner.

@en

PhoP can activate its target genes in a PhoQ-independent manner.

@nl

prefLabel

PhoP can activate its target genes in a PhoQ-independent manner.

@ast

PhoP can activate its target genes in a PhoQ-independent manner.

@en

PhoP can activate its target genes in a PhoQ-independent manner.

@nl

P1433

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P1476

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P2860

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P433

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P577

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P5875

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P932

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P356

JB.186.8.2476-2480.2004

P1433

Journal of Bacteriology

P1476

PhoP can activate its target genes in a PhoQ-independent manner.

@en

P2093

Eleonora García Véscovi

http://www.w3.org/2001/XMLSchema#string

Fernando C Soncini

http://www.w3.org/2001/XMLSchema#string

Linda J Kenney

http://www.w3.org/2001/XMLSchema#string

María Eugenia Castelli

http://www.w3.org/2001/XMLSchema#string

María Laura Cabeza

http://www.w3.org/2001/XMLSchema#string

Sergio Lejona

http://www.w3.org/2001/XMLSchema#string

P2860

The pleiotropic two-component regulatory system PhoP-PhoQ

Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator

Phosphorylation-induced dimerization of the FixJ receiver domain.

Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter.

The unphosphorylated receiver domain of PhoB silences the activity of its output domain

Phosphorylated PmrA interacts with the promoter region of ugd in Salmonella enterica serovar typhimurium.

Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress

Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure

Intramolecular signal transduction within the FixJ transcriptional activator: in vitro evidence for the inhibitory effect of the phosphorylatable regulatory domain.

Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon.

P304

2476-2480

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P31

scholarly article

P356

10.1128/JB.186.8.2476-2480.2004

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P407

P433

8

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P478

186

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P577

2004-04-01T00:00:00Z

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P5875

8641450

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P698

15060051

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P932

412160

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