High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor
about
Propagating conformational changes over long (and short) distances in proteinsCrystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferiCrystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi.Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complexCrystal Structure of a Functional Dimer of the PhoQ Sensor DomainCrystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctBThe Structure of a Soluble Chemoreceptor Suggests a Mechanism for Propagating Conformational Signals † ‡Structural Analysis of Ligand Stimulation of the Histidine Kinase NarXStructural Characterization of the Predominant Family of Histidine Kinase Sensor DomainsLigand Specificity Determined by Differentially Arranged Common Ligand-binding Residues in Bacterial Amino Acid Chemoreceptors Tsr and TarAn Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAOMaking sense of it all: bacterial chemotaxisDefining 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.Coincidence detection and bi-directional transmembrane signaling control a bacterial second messenger receptor.Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.Mutations that affect ligand binding to the Escherichia coli aspartate receptor: implications for transmembrane signaling.A PAS domain binds asparagine in the chemotaxis receptor McpB in Bacillus subtilisNormal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Probing bacterial transmembrane histidine kinase receptor-ligand interactions with natural and synthetic moleculesThe 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.Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.Identification of residues within ligand-binding domain 1 (LBD1) of the Borrelia burgdorferi OspC protein required for function in the mammalian environment.Transmembrane helix dynamics of bacterial chemoreceptors supports a piston model of signalling.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity.Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.Diversity in chemotaxis mechanisms among the bacteria and archaea.Amplification of signaling events in bacteria.Delineating the requirement for the Borrelia burgdorferi virulence factor OspC in the mammalian host.Discovery of novel chemoeffectors and rational design of Escherichia coli chemoreceptor specificityElectron microscopic analysis of membrane assemblies formed by the bacterial chemotaxis receptor Tsr.Transmembrane signaling of chemotaxis receptor tar: insights from molecular dynamics simulation studiesBoth piston-like and rotational motions are present in bacterial chemoreceptor signaling.Two-tiered histidine kinase pathway involved in heat shock and salt sensing in the general stress response of Sphingomonas melonis Fr1.Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxis.Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing.Modeling the transmembrane domain of bacterial chemoreceptorsStructures from anomalous diffraction of native biological macromolecules.
P2860
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P2860
High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
High-resolution structures of ...... e bacterial aspartate receptor
@ast
High-resolution structures of ...... e bacterial aspartate receptor
@en
High-resolution structures of ...... e bacterial aspartate receptor
@nl
type
label
High-resolution structures of ...... e bacterial aspartate receptor
@ast
High-resolution structures of ...... e bacterial aspartate receptor
@en
High-resolution structures of ...... e bacterial aspartate receptor
@nl
prefLabel
High-resolution structures of ...... e bacterial aspartate receptor
@ast
High-resolution structures of ...... e bacterial aspartate receptor
@en
High-resolution structures of ...... e bacterial aspartate receptor
@nl
P2093
P356
P1476
High-resolution structures of ...... e bacterial aspartate receptor
@en
P2093
D E Koshland
H P Biemann
P304
P356
10.1006/JMBI.1996.0507
P407
P577
1996-09-20T00:00:00Z