(Q34490818)

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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

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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 (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

crystal structure

1 reference

based on heuristic

inferred from title

author name string

Yinghua Chen

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Catherine Birck

2

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Jean-Pierre Samama

3

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

F Marion Hulett

4

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

language of work or name

0 references

publication date

1 January 2003

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Journal of Bacteriology

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

185

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

262-273

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

describes a project that uses

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC141829/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface

1 reference

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

1 reference

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Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems.

1 reference

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Crystal structure of activated CheY. Comparison with other activated receiver domains

1 reference

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Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.

1 reference

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Expression of a new operon from Bacillus subtilis, ykzB-ykoL, under the control of the TnrA and PhoP-phoR global regulators

1 reference

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Structural comparison of the PhoB and OmpR DNA-binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box

1 reference

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Conformational changes induced by phosphorylation of the FixJ receiver domain

1 reference

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Structure of a transiently phosphorylated switch in bacterial signal transduction

1 reference

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Mutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promoters

1 reference

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Three-dimensional crystal structure of the transcription factor PhoB receiver domain

1 reference

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Role of Pho-P in transcriptional regulation of genes involved in cell wall anionic polymer biosynthesis in Bacillus subtilis.

1 reference

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Analysis of Bacillus subtilis tagAB and tagDEF expression during phosphate starvation identifies a repressor role for PhoP-P.

1 reference

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Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter

1 reference

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The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the pho regulon

1 reference

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The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor

1 reference

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Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR.

1 reference

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Three two-component signal-transduction systems interact for Pho regulation in Bacillus subtilis

1 reference

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The signal-transduction network for Pho regulation in Bacillus subtilis

1 reference

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Sequential action of two-component genetic switches regulates the PHO regulon in Bacillus subtilis

1 reference

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Tandem Binding of Six OmpR Proteins to the ompF Upstream Regulatory Sequence of Escherichia coli

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12486063

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based on heuristic

inferred from PubMed ID database lookup

Orientation of OmpR monomers within an OmpR:DNA complex determined by DNA affinity cleaving 1 1Edited by K. Yamamoto

1 reference

https://pubmed.ncbi.nlm.nih.gov/12486063

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12486063

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/12486063

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based on heuristic

inferred from PubMed ID database lookup

Signal transduction and osmoregulation in Escherichia coli. A novel type of mutation in the phosphorylation domain of the activator protein, OmpR, results in a defect in its phosphorylation-dependent DNA binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/12486063

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JB.185.1.262-273.2003

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

ResearchGate publication ID

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