A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore. - Wikidata - awgldk - TriplyDB

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

http://www.wikidata.org/entity/Q34186730

about

Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants.A gating mechanism proposed from a simulation of a human alpha7 nicotinic acetylcholine receptor Theoretical studies of the M2 transmembrane segment of the glycine receptor: models of the open pore structure and current-voltage characteristics.Probing ion-channel pores one proton at a time.Structural answers and persistent questions about how nicotinic receptors work.Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: structure and collective motions.Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state.The alpha7 nicotinic acetylcholine receptor: molecular modelling, electrostatics, and energetics.Fluorescence and molecular dynamics studies of the acetylcholine receptor gammaM4 transmembrane peptide in reconstituted systems.

P2860

Q33317424-25ADC2FF-9F83-4367-AF9A-2B2C91D53568 Q33784234-18361FAD-4788-42F7-A0CF-6B54BC73A4D9 Q34351064-50BCB360-914F-4FA2-B8A4-F21A0AA73464 Q34412072-F8769D89-30E5-4E26-B1E0-DC402972CAA6 Q34782188-BBC604A7-605F-4CC6-B6C3-4AF61D792E1A Q40329021-2BC4CB19-E28A-47D6-B9B8-6CB84B66D3DB Q45182918-536826A3-D808-4D9D-9246-ADD0DA35478D Q46646720-9DB0CBEB-975B-4850-8D29-01B266F131B1 Q46864497-D05E5928-51E3-43F4-AEA4-5F8653431A59

P2860

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

http://www.wikidata.org/entity/Q34186730

description

2004 nî lūn-bûn

@nan

2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@ast

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@en

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@nl

type

label

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@ast

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@en

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@nl

prefLabel

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@ast

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@en

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@nl

P1433

Q34186730-998DFF8E-30BD-4BE0-9DDE-01DC73280ABE

P1476

Q34186730-DD202235-7118-413F-8217-E2ADB8D4337D

P2093

Q34186730-3F22D1B7-8C78-446B-923C-D3D12B678458

Q34186730-DB2C4EED-C941-4B50-B04B-5A4970366ACB

Q34186730-FF866866-B6F4-430A-8C65-C3D0A662D53C

P2860

Q34186730-025988BA-92FD-4D13-B37F-1A84DE1935DF

Q34186730-053154FE-4508-49A9-B727-4DF2F117432E

Q34186730-099FD77A-B1EC-4E7B-A76D-F0789ADE8D7A

Q34186730-1A1DC6D4-1C3A-40B8-8718-B97B2D50D699

Q34186730-299E8E0B-C11B-4C54-8176-6EF1C9E60459

Q34186730-40018EDF-7EAA-407C-98CC-E572B320B0E2

Q34186730-48AF0010-7625-4774-822E-ED412D3309B6

Q34186730-52BD7FF9-FC5D-43A4-B2A3-35BD8C9B3716

Q34186730-559EC6CC-A311-4384-BF2F-C5F5E0F12212

Q34186730-59C056D0-2A07-4523-BF25-C35CBDF61005

P304

Q34186730-D0315ACA-2EB3-40A2-836A-643D5CF830C7

P31

Q34186730-C40A9660-17DF-44E5-8A0C-CEF1C637261F

P356

Q34186730-D4333249-9341-4600-A09D-FCC5F6635642

P407

Q34186730-D35D7520-E7D7-4A3C-8977-81E5C866A8D9

P433

Q34186730-19F1D092-3FBC-4D18-BE18-A223674E4C1B

P478

Q34186730-8E6CEA22-49C6-40FE-8C6E-EA6C22834ED0

P577

Q34186730-B77A7157-AE0F-45C7-B900-5EA2CE8AD14C

P5875

Q34186730-9A8BC59A-0FEF-4395-97F8-D68F997D0B64

P698

Q34186730-386F26BA-41FC-4271-96B7-52C030183500

P932

Q34186730-1FE91DE3-9B58-4EC1-8677-665C3EEB36D0

P356

BIOPHYSJ.103.039396

P1433

Biophysical Journal

P1476

A model of the closed form of the nicotinic acetylcholine receptor m2 channel pore.

@en

P2093

Aaron K Chamberlain

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

James U Bowie

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

Sanguk Kim

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

P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

Structure of the transmembrane region of the M2 protein H+ channel

Structure and gating mechanism of the acetylcholine receptor pore

A solid-state NMR index of helical membrane protein structure and topology.

Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: a new homology modeling tool.

Uniformity, ideality, and hydrogen bonds in transmembrane alpha-helices.

M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.

Nicotinic receptors at the amino acid level.

Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism.

P304

792-799

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

P31

scholarly article

P356

10.1529/BIOPHYSJ.103.039396

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

P407

P433

2

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

P478

87

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

P577

2004-08-01T00:00:00Z

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

P5875

8412011

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

P698

15298888

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

P932

1304489

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