The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.
about
Stimulus perception in bacterial signal-transducing histidine kinasesTransmembrane signaling in bacterial chemoreceptorsProbabilistic cross-link analysis and experiment planning for high-throughput elucidation of protein structure.Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.Signaling components in bacterial locomotion and sensory reception.Mapping out regions on the surface of the aspartate receptor that are essential for kinase activationThermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylationSide 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.Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding siteCooperativity between bacterial chemotaxis receptors.Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structuresBiophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants.Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer.A phenylalanine rotameric switch for signal-state control in bacterial chemoreceptors.Ancient chemoreceptors retain their flexibilityOrganization of the aerotaxis receptor aer in the membrane of Escherichia coliEvidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexExcitation and adaptation in bacteria-a model signal transduction system that controls taxis and spatial pattern formationBacterial chemoreceptors: high-performance signaling in networked arraysAttractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole.Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors.Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms.The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis.Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.Mass spectrometric analysis reveals O-methylation of pyruvate kinase from pancreatic cancer cells.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 identityEngineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor.Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study.Conserved 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 complexAdaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity.Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers.Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal-modulating helices.Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase.Subunit organization in a soluble complex of tar, CheW, and CheA by electron microscopy.
P2860
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P2860
The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@ast
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@en
type
label
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@ast
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@en
prefLabel
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@ast
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@en
P2860
P1433
P1476
The aspartate receptor cytopla ...... cture, mechanism and dynamics.
@en
P2093
P2860
P304
P356
10.1016/S0969-2126(99)80106-3
P577
1999-07-01T00:00:00Z