Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).
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Common Internal Allosteric Network Links Anesthetic Binding Sites in a Pentameric Ligand-Gated Ion ChannelSignal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion ChannelsX-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.Identification of a pre-active conformation of a pentameric channel receptorConformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.A chimeric prokaryotic pentameric ligand-gated channel reveals distinct pathways of activation.Role of the Fourth Transmembrane α Helix in the Allosteric Modulation of Pentameric Ligand-Gated Ion Channels.Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion ChannelsCrystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel.EPR Studies of Gating Mechanisms in Ion Channels.A chimeric prokaryotic-eukaryotic pentameric ligand gated ion channel reveals interactions between the extracellular and transmembrane domains shape neurosteroid modulation.Genuine open form of the pentameric ligand-gated ion channel GLIC.The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels.
P2860
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P2860
Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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name
Structural basis for allosteri ...... gand-gated ion channel (GLIC).
@en
type
label
Structural basis for allosteri ...... gand-gated ion channel (GLIC).
@en
prefLabel
Structural basis for allosteri ...... gand-gated ion channel (GLIC).
@en
P2860
P356
P1476
Structural basis for allosteri ...... igand-gated ion channel (GLIC)
@en
P2093
Phanindra Velisetty
Sreevatsa V Chalamalasetti
P2860
P304
P356
10.1074/JBC.M113.523050
P407
P577
2013-12-13T00:00:00Z