Energy and structure of the M2 helix in acetylcholine receptor-channel gating. - Wikidata - wikimedia - TriplyDB

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

http://www.wikidata.org/entity/Q30377179

about

Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue Structural basis for ion permeation mechanism in pentameric ligand-gated ion channels Energetics of gating at the apo-acetylcholine receptor transmitter binding site.Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors Linking the acetylcholine receptor-channel agonist-binding sites with the gate Pore opening and closing of a pentameric ligand-gated ion channel Subunit symmetry at the extracellular domain-transmembrane domain interface in acetylcholine receptor channel gating.Temperature dependence of acetylcholine receptor channels activated by different agonists Mapping heat exchange in an allosteric protein Glycine hinges with opposing actions at the acetylcholine receptor-channel transmitter binding site.Energetic contributions to channel gating of residues in the muscle nicotinic receptor β1 subunit.Linear rate-equilibrium relations arising from ion channel-bilayer energetic coupling.Functional anatomy of an allosteric protein.An integrated catch-and-hold mechanism activates nicotinic acetylcholine receptors.Drying transition in the hydrophobic gate of the GLIC channel blocks ion conduction Action of nicotine and analogs on acetylcholine receptors having mutations of transmitter-binding site residue αG153 Energy for wild-type acetylcholine receptor channel gating from different choline derivatives Loop C and the mechanism of acetylcholine receptor-channel gating.Gating transition of pentameric ligand-gated ion channels.A mechanism for acetylcholine receptor gating based on structure, coupling, phi, and flip.The gating isomerization of neuromuscular acetylcholine receptors.The energy and work of a ligand-gated ion channel.Molecular interactions between mecamylamine enantiomers and the transmembrane domain of the human α4β2 nicotinic receptor.The energetic consequences of loop 9 gating motions in acetylcholine receptor-channels.Function of the M1 π-helix in endplate receptor activation and desensitization.Mutations Causing Slow-Channel Myasthenia Reveal That a Valine Ring in the Channel Pore of Muscle AChR is Optimized for Stabilizing Channel Gating.Heterologous expression and nonsense suppression provide insights into agonist behavior at α6β2 nicotinic acetylcholine receptors.

P2860

Q27334133-427AE403-5096-4252-896F-2799444CA992 Q27660303-19A57488-8EDC-4DD5-BE7B-736CC0518D71 Q27676348-CDA27BBD-2AC7-48A6-9AAB-38633985BC05 Q33763151-DE0C4067-FB02-4FEC-8A9F-CEB04F0CA1CF Q33858349-79CC04C2-7197-4F1C-B004-30A1A4046E79 Q34032739-303A79BB-8328-4C5C-9339-237E0D3886AA Q34359229-5B09DC18-5092-444C-B846-1C7E7607E27F Q34385979-718F6CB0-5B81-483D-9EC8-1FACCC716DB8 Q34568158-E26BC72B-2CA1-443B-BF6D-84C4AA07CA47 Q34568707-73D37963-AB35-4116-8A27-F4409D59BCA1 Q34701070-093C5742-C834-409A-B920-D7DB415E02BE Q35032615-B2BA2226-0D76-4ED9-A1AC-82433C28C228 Q35149448-39F5948E-851B-4DE2-A888-D8ED3A442B7A Q35531523-0FB9CE8F-709C-4166-B550-BB8AFC5D6E9E Q36057107-D43515EA-0DF7-4694-89E5-3CB50C9E32B0 Q36105334-E6C21157-45CF-4D24-B945-B3B7A9B856E2 Q36507213-C28B9A53-8540-44A6-ADDA-7EFAE1357321 Q36592870-9D6A3AED-7B8D-457B-8BDE-251A9B4D8F52 Q36715289-39C005C7-3EEF-4F0F-BBB6-F717405BB522 Q37405994-3185F6AD-F065-4582-949C-81EDCF2A5C11 Q37565659-E29C73D1-97AE-4E2B-A8ED-B058E666868A Q37637585-03FAD5EF-6FC5-4ABA-A896-0431C47AF0CC Q38077337-0E7652C2-6F46-4439-9891-7F42981A70FF Q38582617-1E5D7C1C-34FE-4CB0-9578-826C12812AE2 Q39453131-D05DF313-9748-4DE5-A268-26FD56F64E71 Q40992011-C6C0060B-43F7-4C0D-99B7-89BC6C1CB32E Q41643507-ECCB7CAE-0495-446B-8D64-2EE4A65F1059 Q41815493-8DD96FBC-E4CA-4B51-8147-435189CBE35C

P2860

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

http://www.wikidata.org/entity/Q30377179

description

2009 nî lūn-bûn

@nan

2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@ast

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@en

type

label

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@ast

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@en

prefLabel

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@ast

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@en

P1433

Q30377179-EE716882-2568-456E-BB3F-BCED7C80BBBD

P1476

Q30377179-54C42055-3BED-4C6C-92C8-9D39D285B51B

P2093

Q30377179-090CB9C5-5438-4EB6-9971-67DA56D24B9E

Q30377179-268EA99D-7618-4401-BD61-0E779815FD39

Q30377179-E71D9FC6-7118-4538-9CF2-578188B63FA5

P2860

Q30377179-00D6506F-A134-4BBD-9C64-7A71FB135BD3

Q30377179-0416F6E9-E9E6-4993-9CA1-2529CFA6EFE8

Q30377179-06C4850F-4BD4-403B-AB64-56E4FD439AB1

Q30377179-0FACAFE8-DC41-4F07-A26F-FB0ADEBD2557

Q30377179-144F8DAD-89EC-4D34-A6D4-66B47DC713FA

Q30377179-165D4C77-79DB-4AD0-A517-0F2C6DB1870A

Q30377179-1A3A9B7A-6E06-43EA-A6D6-4A989E072E78

Q30377179-2159186D-1E41-4A5E-97C5-83CE9707A9C2

Q30377179-252A4420-FF44-4EBA-81FF-A9DB3EB2891D

Q30377179-26F971AE-8008-4ABD-AB34-C84D9A457B81

P304

Q30377179-6E46A67E-8175-4516-BAD6-330C621C4E63

P31

Q30377179-A3726D7F-5A80-4244-96E4-1407D5FF8DBF

P356

Q30377179-6D4DA631-6DDB-479A-9E9E-4BC6DB14FF5F

P407

Q30377179-923BBBC4-C892-4C1C-BB38-7445CB845085

P433

Q30377179-C4651C08-9922-4CE2-89BF-CCE842F2021B

P478

Q30377179-05B41691-E5A9-47C2-8CD2-D494860E90B1

P577

Q30377179-198F02E6-D75E-4702-982C-F1A9E73853B1

P5875

Q30377179-A0E216E8-25D3-4863-B9EA-F1A756715FF0

P698

Q30377179-40C94F22-6255-4285-A0B3-CAF7142E69AA

P921

Q30377179-3B0337DB-8949-4CAD-8EE6-89AF0CAFF533

P932

Q30377179-E20B7256-30EE-44FE-ABC0-5140E4836532

P356

J.BPJ.2009.02.030

P1433

Biophysical Journal

P1476

Energy and structure of the M2 helix in acetylcholine receptor-channel gating.

@en

P2093

Anthony Auerbach

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

Archana Jha

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

Prasad Purohit

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

P2860

X-ray structure of a prokaryotic pentameric ligand-gated ion channel

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

Recent advances in Cys-loop receptor structure and function

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

Dynamics of the acetylcholine receptor pore at the gating transition state.

Gating of acetylcholine receptor channels: brownian motion across a broad transition state.

Control of cation permeation through the nicotinic receptor channel

Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap

A speed limit for conformational change of an allosteric membrane protein.

P304

4075-4084

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

P31

scholarly article

P356

10.1016/J.BPJ.2009.02.030

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

P407

P433

10

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

P478

96

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

P577

2009-05-01T00:00:00Z

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

P5875

24435318

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

P698

19450479

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

P921

P932

2712209

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