Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
about
Functional interactions between A' helices in the C-linker of open CNG channels.Block of sodium channels by divalent mercury: role of specific cysteinyl residues in the P-loop region.The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.Analysis of protein structure in intact cells: crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor.Cooperative assembly of CYK-4/MgcRacGAP and ZEN-4/MKLP1 to form the centralspindlin complex.Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.19F nuclear magnetic resonance studies of aqueous and transmembrane receptors. Examples from the Escherichia coli chemosensory pathway.Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylationStructure of the sodium channel pore revealed by serial cysteine mutagenesis.Analysis of F factor TraD membrane topology by use of gene fusions and trypsin-sensitive insertions.The chemoreceptor dimer is the unit of conformational coupling and transmembrane signalingTransmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesisDetection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning.Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor.Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trappingStructure 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.An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding.Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structuresOpen-state disulfide crosslinking between Mycobacterium tuberculosis mechanosensitive channel subunits.Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coliTransmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo.Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.Demonstration of physical proximity between the N terminus and the S4-S5 linker of the human ether-a-go-go-related gene (hERG) potassium channelLarge collective motions regulate the functional properties of glutamate transporter trimers.Reaction of diphtheria toxin channels with sulfhydryl-specific reagents: observation of chemical reactions at the single molecule level.Sequences determining the cytoplasmic localization of a chemoreceptor domain.Disulfide trapping the mechanosensitive channel MscL into a gating-transition state.Analysis of the region between amino acids 30 and 42 of intact UmuD by a monocysteine approach.A cysteine residue in the third membrane-spanning segment of the human D2 dopamine receptor is exposed in the binding-site crevice.A monocysteine approach for probing the structure and interactions of the UmuD proteinAnalysis of protein localization by use of gene fusions with complementary properties."Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.Independent versus coupled inactivation in sodium channels. Role of the domain 2 S4 segment.A cysteine scan of the inner vestibule of cyclic nucleotide-gated channels reveals architecture and rearrangement of the pore.Kinetics of tethering quaternary ammonium compounds to K(+) channelsGenetic identification of the site of DNA contact in the yeast heat shock transcription factorStructure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops
P2860
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P2860
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
description
1988 nî lūn-bûn
@nan
1988 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@ast
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@en
type
label
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@ast
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@en
prefLabel
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@ast
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.
@en
P2093
P1476
Structure of a bacterial sensory receptor. A site-directed sulfhydryl study
@en
P2093
Dernburg AF
Koshland DE Jr
Milligan DL
Sternberg DA
P304
14850-14858
P407
P577
1988-10-01T00:00:00Z