Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor.
about
Use of 19F NMR to probe protein structure and conformational changesTransmembrane signaling in bacterial chemoreceptorsIdentification of the histidine protein kinase KinB in Pseudomonas aeruginosa and its phosphorylation of the alginate regulator algBSiderophore 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.Analysis of protein structure in intact cells: crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor.Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells.New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography.Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.The specificity of interaction of archaeal transducers with their cognate sensory rhodopsins is determined by their transmembrane helices.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Role 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.Substitutions in the periplasmic domain of low-abundance chemoreceptor trg that induce or reduce transmembrane signaling: kinase activation and context effects.Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.Identifying functionally important conformational changes in proteins: activation of the yeast α-factor receptor Ste2pDiscovery 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.Mutational analysis of a transmembrane segment in a bacterial chemoreceptor.Deletion mapping of the sites on the HtrI transducer for sensory rhodopsin I interactionTransduction of envelope stress in Escherichia coli by the Cpx two-component system.Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexStructure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.Converting a transmembrane receptor to a soluble receptor: recognition domain to effector domain signaling after excision of the transmembrane domainModeling the transmembrane domain of bacterial chemoreceptorsProtonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I.Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole.Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo.Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer.Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms.Site-directed spin labeling of a bacterial chemoreceptor reveals a dynamic, loosely packed transmembrane domainThe Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis.Mutational analysis of ligand recognition by tcp, the citrate chemoreceptor of Salmonella enterica serovar typhimurium.
P2860
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P2860
Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor.
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@ast
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@en
type
label
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@ast
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@en
prefLabel
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@ast
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@en
P2860
P356
P1476
Lock on/off disulfides identif ...... lix of the aspartate receptor.
@en
P2093
S A Chervitz
P2860
P304
24043-24053
P356
10.1074/JBC.270.41.24043
P407
P577
1995-10-01T00:00:00Z