Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
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Use of 19F NMR to probe protein structure and conformational changesA scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component systemCrystallographic analysis of CD40 recognition and signaling by human TRAF2Lessons in Fundamental Mechanisms and Diverse Adaptations from the 2015 Bacterial Locomotion and Signal Transduction MeetingTwo distinct states of the HAMP domain from sensory rhodopsin transducer observed in unbiased molecular dynamics simulationsThe role of membrane-mediated interactions in the assembly and architecture of chemoreceptor latticesFour-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptorCrystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferiStructural Analysis of Ligand Stimulation of the Histidine Kinase NarXStructural Characterization of the Predominant Family of Histidine Kinase Sensor DomainsAn Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAOStructure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpBCrystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiontStructural basis for amino-acid recognition and transmembrane signalling by tandem Per-Arnt-Sim (tandem PAS) chemoreceptor sensory domainsTransmembrane signaling in bacterial chemoreceptorsIdentification of the histidine protein kinase KinB in Pseudomonas aeruginosa and its phosphorylation of the alginate regulator algBConformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold proteinCache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in ProkaryotesDefining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study.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.The accommodation index measures the perturbation associated with insertions and deletions in coiled-coils: Application to understand signaling in histidine kinases.Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.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 activationMutations that affect ligand binding to the Escherichia coli aspartate receptor: implications for transmembrane signaling.Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.A PAS domain binds asparagine in the chemotaxis receptor McpB in Bacillus subtilisE. coli-based cell-free expression, purification and characterization of the membrane-bound ligand-binding CHASE-TM domain of the cytokinin receptor CRE1/AHK4 of Arabidopsis thaliana.Molecular interactions between extracellular components of the T-cell receptor signaling complex.Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis.Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1.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.Changes in temporal and spatial patterns of outer surface lipoprotein expression generate population heterogeneity and antigenic diversity in the Lyme disease spirochete, Borrelia burgdorferi
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P2860
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@en
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@nl
type
label
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@en
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@nl
prefLabel
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@en
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@nl
P2860
P356
P1476
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
@en
P2093
S A Chervitz
P2860
P304
P356
10.1073/PNAS.93.6.2545
P407
P577
1996-03-01T00:00:00Z