Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer.
about
End-plate acetylcholine receptor: structure, mechanism, pharmacology, and diseaseInward rectifiers and their regulation by endogenous polyaminesStructure of a potentially open state of a proton-activated pentameric ligand-gated ion channelGating Movement of Acetylcholine Receptor Caught by Plunge-FreezingSubtypes of nicotinic acetylcholine receptors in nicotine reward, dependence, and withdrawal: evidence from genetically modified mice.Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels.Conformational changes in the nicotinic acetylcholine receptor during gating and desensitizationAn iris-like mechanism of pore dilation in the CorA magnesium transport systemNormal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranesTunable pKa values and the basis of opposite charge selectivities in nicotinic-type receptorsCorrelating structural and energetic changes in glycine receptor activation.Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating.Functional Chimeras of GLIC Obtained by Adding the Intracellular Domain of Anion- and Cation-Conducting Cys-Loop Receptors.Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.Experimental determination of the vertical alignment between the second and third transmembrane segments of muscle nicotinic acetylcholine receptorsKirBac1.1: it's an inward rectifying potassium channel.Single-channel current through nicotinic receptor produced by closure of binding site C-loop.Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor.Gating transition of pentameric ligand-gated ion channels.Engineering differential charge selectivity from a single structural template.The structural basis of function in Cys-loop receptors.Emerging approaches to probing ion channel structure and function.The structural mechanism of the Cys-loop receptor desensitization.Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.Estimating the pKa values of basic and acidic side chains in ion channels using electrophysiological recordings: a robust approach to an elusive problem.Probing pore constriction in a ligand-gated ion channel by trapping a metal ion in the pore upon agonist dissociation.A distinct mechanism for activating uncoupled nicotinic acetylcholine receptors.Chasing the open-state structure of pentameric ligand-gated ion channels.
P2860
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P2860
Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Pore-opening mechanism of the ...... or evinced by proton transfer.
@en
type
label
Pore-opening mechanism of the ...... or evinced by proton transfer.
@en
prefLabel
Pore-opening mechanism of the ...... or evinced by proton transfer.
@en
P2860
P356
P1476
Pore-opening mechanism of the ...... or evinced by proton transfer.
@en
P2093
Claudio Grosman
Gisela D Cymes
P2860
P2888
P304
P356
10.1038/NSMB.1407
P577
2008-03-30T00:00:00Z
P5875
P6179
1007541655