Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli.
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The CorA Mg2+ transporter is a homotetramerAssembly of the transmembrane domain of E. coli PhoQ histidine kinase: implications for signal transduction from molecular simulationsDetermination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.A pH- and ionic strength-dependent conformational change in the neck region regulates DNGR-1 function in dendritic cells.Analysis of protein structure in intact cells: crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor.Mutations that affect ligand binding to the Escherichia coli aspartate receptor: implications for transmembrane signaling.Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor.Oxidation of an engineered pore cysteine locks a voltage-gated K+ channel in a nonconducting stateStrategies for differential sensory responses mediated through the same transmembrane receptor.Residues in the pathway through a membrane transporter.Identifying functionally important conformational changes in proteins: activation of the yeast α-factor receptor Ste2pIdentification of functionally important helical faces in transmembrane segments by scanning mutagenesis.The TonB dimeric crystal structures do not exist in vivo.Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo.Flexibility of the N-terminal mVDAC1 segment controls the channel's gating behavior.Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tarCys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ.Self-assembly of receptor/signaling complexes in bacterial chemotaxisSequences determining the cytoplasmic localization of a chemoreceptor domain.Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysisEnergy sensors for aerotaxis in Escherichia coli: something old, something new."Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain.Determination of the multimerization state of the hepatitis delta virus antigens in vivoA functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivityDeducing the transmembrane domain organization of presenilin-1 in gamma-secretase by cysteine disulfide cross-linking.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.Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.The Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis.Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli.Mutational analysis of ligand recognition by tcp, the citrate chemoreceptor of Salmonella enterica serovar typhimurium.Specificity and promiscuity in membrane helix interactions.Site-directed disulfide mapping of helices M4 and M6 in the Ca2+ binding domain of SERCA1a, the Ca2+ ATPase of fast twitch skeletal muscle sarcoplasmic reticulum.Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering.The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli. Implications for transmembrane signaling.Metal-ion sites as structural and functional probes of helix-helix interactions in 7TM receptors.Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.The structure and organization of synthetic putative membranous segments of ROMK1 channel in phospholipid membranes.
P2860
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P2860
Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@en
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@nl
type
label
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@en
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@nl
prefLabel
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@en
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@nl
P2860
P356
P1476
Disulfide cross-linking studie ...... receptor of Escherichia coli.
@en
P2093
D E Koshland
P2860
P304
10402-10406
P356
10.1073/PNAS.88.23.10402
P407
P577
1991-12-01T00:00:00Z