Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo.
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The role of membrane-mediated interactions in the assembly and architecture of chemoreceptor latticesFour-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptorTransmembrane signaling in bacterial chemoreceptorsSiderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains.The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.Mapping out regions on the surface of the aspartate receptor that are essential for kinase activationRole of predicted transmembrane domains for type III translocation, pore formation, and signaling by the Yersinia pseudotuberculosis YopB proteinSide chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning.The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesStructure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors.Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies.Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.Transmembrane helix dynamics of bacterial chemoreceptors supports a piston model of signalling.Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coliDiversity in chemotaxis mechanisms among the bacteria and archaea.Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer.Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.Discovery of novel chemoeffectors and rational design of Escherichia coli chemoreceptor specificityCys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ.Both piston-like and rotational motions are present in bacterial chemoreceptor signaling.Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.Transmembrane signaling in the sensor kinase DcuS of Escherichia coli: A long-range piston-type displacement of transmembrane helix 2Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.Modeling the transmembrane domain of bacterial chemoreceptorsIn vivo protein complex topologies: sights through a cross-linking lensAttractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole.Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor AerThe Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide bindingMutational analysis of ligand recognition by tcp, the citrate chemoreceptor of Salmonella enterica serovar typhimurium.Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanineHAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor KinaseAttractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.Structure, function, and on-off switching of a core unit contact between CheA kinase and CheW adaptor protein in the bacterial chemosensory array: A disulfide mapping and mutagenesis studyDiagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identityThe core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complexIn vivo studies suggest that induction of VanS-dependent vancomycin resistance requires binding of the drug to D-Ala-D-Ala termini in the peptidoglycan cell wall.Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.
P2860
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P2860
Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Detecting the conformational c ...... sulfide cross-linking in vivo.
@en
Detecting the conformational c ...... sulfide cross-linking in vivo.
@nl
type
label
Detecting the conformational c ...... sulfide cross-linking in vivo.
@en
Detecting the conformational c ...... sulfide cross-linking in vivo.
@nl
prefLabel
Detecting the conformational c ...... sulfide cross-linking in vivo.
@en
Detecting the conformational c ...... sulfide cross-linking in vivo.
@nl
P2860
P356
P1476
Detecting the conformational c ...... sulfide cross-linking in vivo.
@en
P2093
A G Hughson
G L Hazelbauer
P2860
P304
11546-11551
P356
10.1073/PNAS.93.21.11546
P407
P577
1996-10-01T00:00:00Z