Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.
about
Stimulus perception in bacterial signal-transducing histidine kinasesTransmembrane signaling in bacterial chemoreceptorsDefining 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.Membrane association of a protein increases the rate, extent, and specificity of chemical cross-linking.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.Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.Mapping out regions on the surface of the aspartate receptor that are essential for kinase activationCheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites.Flexibility of the cytoplasmic domain of the phototaxis transducer II from Natronomonas pharaonis.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.Substitutions in the periplasmic domain of low-abundance chemoreceptor trg that induce or reduce transmembrane signaling: kinase activation and context effects.Cooperativity between bacterial chemotaxis receptors.Binding and diffusion of CheR molecules within a cluster of membrane receptors.A phenylalanine rotameric switch for signal-state control in bacterial chemoreceptors.Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexAccessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residuesLocations of the beta1 transmembrane helices in the BK potassium channelBacterial chemoreceptors: high-performance signaling in networked arraysSite-directed spin labeling of a bacterial chemoreceptor reveals a dynamic, loosely packed transmembrane domainThe PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis.Isolated bacterial chemosensory array possesses quasi- and ultrastable components: functional links between array stability, cooperativity, and order.Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.Bacterial Chemoreceptor Dynamics: Helical Stability in the Cytoplasmic Domain Varies with Functional Segment and Adaptational Modification.Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor.Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching.Differential backbone dynamics of companion helices in the extended helical coiled-coil domain of a bacterial chemoreceptor.Quantitative 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.Signalling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain.Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.Aqueous access channels in subunit a of rotary ATP synthase.
P2860
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P2860
Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.
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
Signaling domain of the aspart ...... nd disulfide scanning studies.
@ast
Signaling domain of the aspart ...... nd disulfide scanning studies.
@en
type
label
Signaling domain of the aspart ...... nd disulfide scanning studies.
@ast
Signaling domain of the aspart ...... nd disulfide scanning studies.
@en
prefLabel
Signaling domain of the aspart ...... nd disulfide scanning studies.
@ast
Signaling domain of the aspart ...... nd disulfide scanning studies.
@en
P2093
P2860
P356
P1433
P1476
Signaling domain of the aspart ...... nd disulfide scanning studies.
@en
P2093
P2860
P304
P356
10.1021/BI9908179
P407
P577
1999-07-01T00:00:00Z