Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing. - sprookjes - yvandenbroek - TriplyDB

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

http://www.wikidata.org/entity/Q36310730

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A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component system A small-RNA-mediated negative feedback loop controls quorum-sensing dynamics in Vibrio harveyi The arsenal of pathogens and antivirulence therapeutic strategies for disarming them Exploiting Quorum Sensing Interfering Strategies in Gram-Negative Bacteria for the Enhancement of Environmental Applications Bacterial quorum sensing: its role in virulence and possibilities for its control Quorum sensing: how bacteria can coordinate activity and synchronize their response to external signals?Cell fate regulation governed by a repurposed bacterial histidine kinase Polar localization of a tripartite complex of the two-component system DcuS/DcuR and the transporter DctA in Escherichia coli depends on the sensor kinase DcuS Crystal structure of a histidine kinase sensor domain with similarity to periplasmic binding proteins Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS Regulation of the xylan-degrading apparatus of Cellvibrio japonicus by a novel two-component system Changes in Quaternary Structure in the Signaling Mechanisms of PAS Domains † , ‡Ligand-induced conformational changes in a thermophilic ribose-binding protein The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF Structural plasticity and catalysis regulation of a thermosensor histidine kinase Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction Proteins Structural Characterization of the Predominant Family of Histidine Kinase Sensor Domains Structural Basis for Two-component System Inhibition and Pilus Sensing by the Auxiliary CpxP Protein Insight into the sporulation phosphorelay: Crystal structure of the sensor domain ofBacillus subtilishistidine kinase, KinD Solution Structure of the PAS Domain of a Thermophilic YybT Protein Homolog Reveals a Potential Ligand-binding Site An Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAO Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation Crystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiont Quorum sensing in the squid-Vibrio symbiosis.Visualizing autophosphorylation in histidine kinases Specificity and complexity in bacterial quorum-sensing systems The Bacillus subtilis chemoreceptor McpC senses multiple ligands using two discrete mechanisms Cache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in Prokaryotes Blue-light reception through quaternary transitions Sensor domain of histidine kinase KinB of Pseudomonas: a helix-swapped dimer.Regulatory small RNAs circumvent the conventional quorum sensing pathway in pandemic Vibrio cholerae.Distinct sensory pathways in Vibrio cholerae El Tor and classical biotypes modulate cyclic dimeric GMP levels to control biofilm formation.The accommodation index measures the perturbation associated with insertions and deletions in coiled-coils: Application to understand signaling in histidine kinases.Coincidence detection and bi-directional transmembrane signaling control a bacterial second messenger receptor.Metastasis Research Society-American Association For Cancer Research Joint Conference on Metastasis.Quantifying the integration of quorum-sensing signals with single-cell resolution.

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P2860

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

http://www.wikidata.org/entity/Q36310730

description

2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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2006年學術文章

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name

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

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Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

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type

label

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

@ast

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

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prefLabel

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

@ast

Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

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Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.

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Audra J Pompeani

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Bonnie L Bassler

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Danielle L Swem

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Frederick M Hughson

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Matthew B Neiditch

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Michael J Federle

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Philip D Jeffrey

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Robert C Kelly

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P2860

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein

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

Structural identification of a bacterial quorum-sensing signal containing boron

High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor

Multiple open forms of ribose-binding protein trace the path of its conformational change

Likelihood-enhanced fast rotation functions

Protein structure comparison by alignment of distance matrices

Refinement of macromolecular structures by the maximum-likelihood method

Use of non-crystallographic symmetry in protein structure refinement

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