Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism - Wikidata - wikimedia - TriplyDB

Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism

Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism

http://www.wikidata.org/entity/Q27644734

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Prokaryotic 2-component systems and the OmpR/PhoB superfamily The aspartate-less receiver (ALR) domains: distribution, structure and function Phosphorylation-Independent Regulation of the Diguanylate Cyclase WspR Intermolecular Interactions in a 44 kDa Interferon−Receptor Complex Detected by Asymmetric Reverse-Protonation and Two-Dimensional NOESY Regulation of Response Regulator Autophosphorylation through Interdomain Contacts The Atypical Response Regulator Protein ChxR Has Structural Characteristics and Dimer Interface Interactions That Are Unique within the OmpR/PhoB Subfamily Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding Atypical OmpR/PhoB Subfamily Response Regulator GlnR of Actinomycetes Functions as a Homodimer, Stabilized by the Unphosphorylated Conserved Asp-focused Charge Interactions The atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis forms homodimers in vivo and binds a direct repeat of nucleotide sequences Response regulator heterodimer formation controls a key stage in Streptomyces development SO2426 is a positive regulator of siderophore expression in Shewanella oneidensis MR-1.Response to metronidazole and oxidative stress is mediated through homeostatic regulator HsrA (HP1043) in Helicobacter pylori.Mutations to essential orphan response regulator HP1043 of Helicobacter pylori result in growth-stage regulatory defects.Transcriptional and post-transcriptional regulation of the GmaR antirepressor governs temperature-dependent control of flagellar motility in Listeria monocytogenes.Receiver domain structure and function in response regulator proteins.Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes VirS, an OmpR/PhoB subfamily response regulator, is required for activation of vapA gene expression in Rhodococcus equi.NMR Study Reveals the Receiver Domain of Arabidopsis ETHYLENE RESPONSE1 Ethylene Receptor as an Atypical Type Response Regulator.Amino acids important for DNA recognition by the response regulator OmpR.Dual Repression of the Multidrug Eﬄux Pump CmeABC by CosR and CmeR in Campylobacter jejuni.Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR.Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of a Chlamydia trachomatis OmpR/PhoB-subfamily response regulator homolog, ChxR.Backbone dynamics of an atypical orphan response regulator protein, Helicobacter pylori 1043.To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Novel Helicobacter pylori therapeutic targets: the unusual suspects.Insight into the essential role of the Helicobacter pylori HP1043 orphan response regulator: genome-wide identification and characterization of the DNA-binding sites.Molecular strategies for phosphorylation-mediated regulation of response regulator activity.NMR study on small proteins from Helicobacter pylori for antibiotic target discovery: a review.Solution NMR studies on Helicobacter pylori proteins for antibiotic target discovery.Molecular Mechanisms of Two-Component Signal Transduction.The CrdRS two-component system in Helicobacter pylori responds to nitrosative stress.Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.Mechanistic insight into how multidrug resistant Acinetobacter baumannii response regulator AdeR recognizes an intercistronic region.Role of CovR phosphorylation in gene transcription in Streptococcus mutans.

P2860

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P2860

Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism

http://www.wikidata.org/entity/Q27644734

description

2007 nî lūn-bûn

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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2007 թվականի հուլիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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Structure of an atypical orpha ...... dependent regulatory mechanism

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P1433

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P1433

Journal of Biological Chemistry

P1476

Structure of an atypical orpha ...... dependent regulatory mechanism

@en

P2093

Byoung-Young Jeon

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

Dong-Uk Kim

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

Eunmi Hong

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Hyang Mi Lee

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

Hyun-Soo Cho

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

Hyunsook Ko

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

Jinwon Jung

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

Joon Shin

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

Sung-Ah Lee

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

Weontae Lee

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

P2860

The complete genome sequence of the gastric pathogen Helicobacter pylori

Molecular characterization of two-component systems of Helicobacter pylori.

Electrostatics of nanosystems: application to microtubules and the ribosome

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Solution structure of the DNA-binding domain of NtrC with three alanine substitutions

Phosphorylated aspartate in the structure of a response regulator protein

Conformational changes induced by phosphorylation of the FixJ receiver domain

P304

20667-75

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P31

scholarly article

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4328776

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P356

10.1074/JBC.M609104200

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P407

P433

28

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P478

282

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P50

Chaejoon Cheong

P577

2007-07-13T00:00:00Z

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17491010

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P921

phosphorylation

protein structure