Global flexibility in a sensory receptor: a site-directed cross-linking approach.
about
The CorA Mg2+ transporter is a homotetramerUse of 19F NMR to probe protein structure and conformational changesFunctional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionTransmembrane signaling in bacterial chemoreceptorsCysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interfaceThe 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.Analysis of protein structure in intact cells: crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor.Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylationLigand effects on cross-linking support a conformational mechanism for serotonin transport.Structure of the sodium channel pore revealed by serial cysteine mutagenesis.Pore architecture of the ORAI1 store-operated calcium channel.Molecular motions within the pore of voltage-dependent sodium channelsDetection 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.The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesThermal 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.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.Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.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.The ethylene-receptor family from Arabidopsis: structure and function.An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding.Chemotactic responses of Escherichia coli to small jumps of photoreleased L-aspartateIdentifying functionally important conformational changes in proteins: activation of the yeast α-factor receptor Ste2pThe closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants.Transmembrane segment packing of the Na(+)/Ca(2+) exchanger investigated with chemical cross-linkersStabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds.Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo.Mutational analysis of the transmembrane helix 2-HAMP domain connection in the Escherichia coli aspartate chemoreceptor tarVpu binds directly to tetherin and displaces it from nascent virions.Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.Formation of high-order oligomers by a hyperthemostable Fe-superoxide dismutase (tcSOD).The ToxR protein of Vibrio cholerae forms homodimers and heterodimers.Analysis of the region between amino acids 30 and 42 of intact UmuD by a monocysteine approach.Gating transitions in the selectivity filter region of a sodium channel are coupled to the domain IV voltage sensor.Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.
P2860
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P2860
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
1987年學術文章
@zh-hant
name
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@en
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@nl
type
label
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@en
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@nl
prefLabel
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@en
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@nl
P356
P1433
P1476
Global flexibility in a sensory receptor: a site-directed cross-linking approach.
@en
P2093
Koshland DE Jr
P304
P356
10.1126/SCIENCE.2820061
P407
P577
1987-09-01T00:00:00Z