Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor.
about
Structure of the entire cytoplasmic portion of a sensor histidine-kinase proteinSite-specific and synergistic stimulation of methylation on the bacterial chemotaxis receptor Tsr by serine and CheWTwo distinct states of the HAMP domain from sensory rhodopsin transducer observed in unbiased molecular dynamics simulationsStructure of Concatenated HAMP Domains Provides a Mechanism for Signal TransductionStructural characterization of AS1–membrane interactions from a subset of HAMP domainsTransmembrane signaling in bacterial chemoreceptorsThe aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.Coincidence detection and bi-directional transmembrane signaling control a bacterial second messenger receptor.Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea.Reactions of cysteines substituted in the amphipathic N-terminal tail of a bacterial potassium channel with hydrophilic and hydrophobic maleimides.Organization of FliN subunits in the flagellar motor of Escherichia coliSignaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.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.Conserved residues in the HAMP domain define a new family of proposed bipartite energy taxis receptorsGenetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Bacterial chemoreceptors: providing enhanced features to two-component signaling.Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1.Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning.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.HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptorTopology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coliMutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tarMutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarXMinimal requirements for oxygen sensing by the aerotaxis receptor Aer.Biphasic control logic of HAMP domain signalling in the Escherichia coli serine chemoreceptorElectron microscopic analysis of membrane assemblies formed by the bacterial chemotaxis receptor Tsr.Different conformations of the kinase-on and kinase-off signaling states in the Aer HAMP domain.Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases.Mutational analysis of the control cable that mediates transmembrane signaling in the Escherichia coli serine chemoreceptorA Trigger Residue for Transmembrane Signaling in the Escherichia coli Serine Chemoreceptor.HAMP domain signal relay mechanism in a sensory rhodopsin-transducer complexGating-induced conformational rearrangement of the γ-aminobutyric acid type A receptor β-α subunit interface in the membrane-spanning domainEvidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexStructure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.
P2860
Q24540113-EF703556-A688-4757-A39F-0DC707F3857BQ24793956-37980DF7-0966-4EBA-AADE-30B83594AFCCQ27313495-747E2709-C4BA-4F5B-BE69-FC51F6001806Q27660575-E2669945-FE84-49EE-9F70-BD1C48D8C286Q27670813-AE873734-8E70-48E0-A22E-E3880B9D189EQ28362211-A85C1D31-D156-4A5E-AE26-F50DFCE3AFC0Q30322321-8D494DBD-EFFB-484F-A5EA-E3D79560A379Q30362743-7A810F05-272E-4675-BA78-500B9BB04C02Q30396694-9CF202F9-4758-4F42-87F9-C9F84DABA824Q30401069-17543E3A-5553-4C61-B2C7-81F30D4CF660Q30453183-12885E99-2782-420F-94D9-EF84E912D509Q30477115-C2DC5293-38D2-459B-9E74-B97F97A706CBQ30738971-EA0E1335-6C7E-437C-B220-83910831AD91Q30894653-D250118B-835E-42AF-81A0-D39B218400A5Q33250403-7C2A07F6-A39C-46CD-9377-47C7B37AA389Q33379529-F8C759CC-544D-481A-93D6-9112A8EA8517Q33553390-AD010C62-C80E-4419-917A-9D8FB9642908Q33614907-779972DF-2851-4AEC-9FB8-EF944D6554EDQ33824193-4F72E289-2005-4FB9-94DC-988A9EB58280Q33932303-C0146A67-296D-41D6-A8E0-3AD7F890BAABQ33941413-EF6E1C2E-D2FB-4843-BB4D-A70B161CF096Q33962309-5416EB31-EF3A-4C3F-A5DE-A3A55E2A1FE3Q33988248-0AC61AE8-6EA9-4AEA-91E7-80DB23D871D4Q33988261-54A8D279-52B5-4099-BFB5-B5D56DCD5D0BQ33995361-94464613-062B-4B7D-833D-DFB768525476Q34131237-A8BB1CA2-6B06-4DCD-989A-5AE95190E290Q34303463-E42A77E5-C7DA-4F72-9E1B-70A39367E2A0Q34484908-BDD88BAC-5AD0-453E-AAA6-AE2665DD6809Q34491912-36B51AEA-9E4E-4D68-B16A-E22FBB4273C4Q34536431-BD1AAA2C-A961-4D32-B560-42251F03A7AFQ34982948-AD930598-B2FF-4C05-85D4-34F51C0E7ABEQ35021206-E97CF023-8C73-48C9-8590-707831E66DC9Q35139646-56402945-3625-49D3-AF19-59D63630E97BQ35172217-05F0ADB7-8DF7-48EF-9060-308E8431054CQ35274473-0DB3A9FB-26B0-4C20-988D-B4B4E75E56DDQ35899789-1A347D7E-B5D3-4CAC-8D79-A627FE44C0DAQ36033252-8FFE0DBF-EE35-4709-A9C1-DA2C17E55F66Q36201884-7ED5A845-EF37-4B13-BB2F-D99C693C97C4Q36436405-E2094ED4-398D-4FBD-B704-6041A0B766FBQ36483763-3EF8209D-658D-4A0F-99D4-63913A18A533
P2860
Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@en
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@nl
type
label
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@en
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@nl
prefLabel
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@en
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@nl
P2860
P356
P1433
P1476
Cysteine and disulfide scannin ...... f the aspartate chemoreceptor.
@en
P2093
P2860
P304
10746-10756
P356
10.1021/BI980607G
P407
P577
1998-07-01T00:00:00Z