Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker. - Wikidata - awgldk - TriplyDB

Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker.

Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker.

http://www.wikidata.org/entity/Q36296102

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End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease Size matters in activation/inhibition of ligand-gated ion channels Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation Signal Transduction Pathways in the Pentameric Ligand-Gated Ion Channels Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels Energy and structure of the M2 helix in acetylcholine receptor-channel gating.Propofol binding to the resting state of the gloeobacter violaceus ligand-gated ion channel (GLIC) induces structural changes in the inter- and intrasubunit transmembrane domain (TMD) cavities Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap The role of intracellular linkers in gating and desensitization of human pentameric ligand-gated ion channels Chemical scale studies of the Phe-Pro conserved motif in the cys loop of Cys loop receptors.Energetics of gating at the apo-acetylcholine receptor transmitter binding site.Acetylcholine receptor channels activated by a single agonist molecule.Disruption of an intersubunit electrostatic bond is a critical step in glycine receptor activation.Unresponsive correlated motion in alpha7 nAChR to halothane binding explains its functional insensitivity to volatile anesthetics.Linking the acetylcholine receptor-channel agonist-binding sites with the gate Anesthetic binding in a pentameric ligand-gated ion channel: GLIC Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes Subunit symmetry at the extracellular domain-transmembrane domain interface in acetylcholine receptor channel gating.Mapping heat exchange in an allosteric protein Design and control of acetylcholine receptor conformational change Correlating structural and energetic changes in glycine receptor activation.Contributions of conserved residues at the gating interface of glycine receptors.Functional anatomy of an allosteric protein.The intrinsic energy of the gating isomerization of a neuromuscular acetylcholine receptor channel.Subunit stoichiometry and arrangement in a heteromeric glutamate-gated chloride channel.Loop C and the mechanism of acetylcholine receptor-channel gating.Perturbation of Critical Prolines in Gloeobacter violaceus Ligand-gated Ion Channel (GLIC) Supports Conserved Gating Motions among Cys-loop Receptors.Role of the Fourth Transmembrane α Helix in the Allosteric Modulation of Pentameric Ligand-Gated Ion Channels.Nicotinic receptor interloop proline anchors beta1-beta2 and Cys loops in coupling agonist binding to channel gating.Function of interfacial prolines at the transmitter-binding sites of the neuromuscular acetylcholine receptor.Unliganded gating of acetylcholine receptor channels The interface between extracellular and transmembrane domains of homomeric Cys-loop receptors governs open-channel lifetime and rate of desensitization.The gating isomerization of neuromuscular acetylcholine receptors.In pursuit of the high-resolution structure of nicotinic acetylcholine receptors.The energy and work of a ligand-gated ion channel.The energetic consequences of loop 9 gating motions in acetylcholine receptor-channels.Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions Aromatic Residues {epsilon}Trp-55 and {delta}Trp-57 and the Activation of Acetylcholine Receptor Channels.

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Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker.

http://www.wikidata.org/entity/Q36296102

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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type

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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The Journal of General Physiology

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Acetylcholine receptor gating ...... the cys-loop and M2-M3 linker.

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P2093

Anthony Auerbach

http://www.w3.org/2001/XMLSchema#string

Archana Jha

http://www.w3.org/2001/XMLSchema#string

David J Cadugan

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Prasad Purohit

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P2860

Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia

Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis

The Croonian Lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission

Structure and gating mechanism of the acetylcholine receptor pore

Mutations in different functional domains of the human muscle acetylcholine receptor alpha subunit in patients with the slow-channel congenital myasthenic syndrome

Molecular dynamics and protein function.

Mutational analysis of familial and sporadic hyperekplexia

Recent advances in Cys-loop receptor structure and function

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel

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10.1085/JGP.200709856

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6

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130

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2007-12-01T00:00:00Z

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5807891

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18040057

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transmembrane protein

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2151658

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