Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.
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Site-specific and synergistic stimulation of methylation on the bacterial chemotaxis receptor Tsr by serine and CheWThe 3.2 Å Resolution Structure of a Receptor:CheA:CheW Signaling Complex Defines Overlapping Binding Sites and Key Residue Interactions within Bacterial Chemosensory ArraysTransmembrane signaling in bacterial chemoreceptorsInformation processing in bacteria: memory, computation, and statistical physics: a key issues reviewDefining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study.New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography.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.The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinitiesReceptor sensitivity in bacterial chemotaxis.Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.Structure 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.Effects of receptor modification and temperature on dynamics of sensory complexes in Escherichia coli chemotaxis.Cooperativity between bacterial chemotaxis receptors.Collaborative signaling by mixed chemoreceptor teams in Escherichia coli.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.Polarity in action: asymmetric protein localization in bacteria.Chemoreceptors in signalling complexes: shifted conformation and asymmetric coupling.Amplification of signaling events in bacteria.Chemotaxis kinase CheA is activated by three neighbouring chemoreceptor dimers as effectively as by receptor clustersAdapt locally and act globally: strategy to maintain high chemoreceptor sensitivity in complex environments.Electron microscopic analysis of membrane assemblies formed by the bacterial chemotaxis receptor Tsr.Core unit of chemotaxis signaling complexes.Importance of Multiple Methylation Sites in Escherichia coli ChemotaxisEvidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexLigand affinity and kinase activity are independent of bacterial chemotaxis receptor concentration: insight into signaling mechanisms.Precision sensing by two opposing gradient sensors: how does Escherichia coli find its preferred pH level?Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole.Chemotaxis in Campylobacter jejuni.Architecture and signal transduction mechanism of the bacterial chemosensory array: progress, controversies, and challengesCooperativity in signal transfer through the Uhp system of Escherichia coli.Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli.Increasing and decreasing the ultrastability of bacterial chemotaxis core signaling complexes by modifying protein-protein contactsConserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching.The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complexQuantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model.Adaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity.Bright lights, abundant operons--fluorescence and genomic technologies advance studies of bacterial locomotion and signal transduction: review of the BLAST meeting, Cuernavaca, Mexico, 14 to 19 January 2001.
P2860
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P2860
Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Attractant regulation of the a ...... e receptor modification state.
@en
type
label
Attractant regulation of the a ...... e receptor modification state.
@en
prefLabel
Attractant regulation of the a ...... e receptor modification state.
@en
P2860
P356
P1433
P1476
Attractant regulation of the a ...... e receptor modification state.
@en
P2093
J A Bornhorst
P2860
P304
P356
10.1021/BI0002737
P407
P577
2000-08-01T00:00:00Z