Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism - Wikidata - awgldk - TriplyDB

Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism

Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism

http://www.wikidata.org/entity/Q34190634

about

End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease The concept of allosteric interaction and its consequences for the chemistry of the brain The nicotinic acetylcholine receptor: the founding father of the pentameric ligand-gated ion channel superfamily Size matters in activation/inhibition of ligand-gated ion channels Motion and flexibility in human cytochrome p450 aromatase Inherent dynamics of the acid-sensing ion channel 1 correlates with the gating mechanism Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue NMR structure of the transmembrane domain of the n-acetylcholine receptor β2 subunit Gating Movement of Acetylcholine Receptor Caught by Plunge-Freezing Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation Structural basis for cooperative interactions of substituted 2-aminopyrimidines with the acetylcholine binding protein Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics Recent advances in Cys-loop receptor structure and function A Structural Model of the Human α7 Nicotinic Receptor in an Open Conformation Subtypes of nicotinic acetylcholine receptors in nicotine reward, dependence, and withdrawal: evidence from genetically modified mice.In silico models for the human alpha4beta2 nicotinic acetylcholine receptor.Tightening of the ATP-binding sites induces the opening of P2X receptor channels Real time ligand-induced motion mappings of AChBP and nAChR using X-ray single molecule tracking Targeted molecular dynamics study of C-loop closure and channel gating in nicotinic receptors.Mechanics of channel gating of the nicotinic acetylcholine receptor.Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors Linking the acetylcholine receptor-channel agonist-binding sites with the gate Pore conformations and gating mechanism of a Cys-loop receptor.Molecular tuning of fast gating in pentameric ligand-gated ion channels.Pore opening and closing of a pentameric ligand-gated ion channel Ligand- and subunit-specific conformational changes in the ligand-binding domain and the TM2-TM3 linker of {alpha}1 {beta}2 {gamma}2 GABAA receptors A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors.Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel.Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.Design and control of acetylcholine receptor conformational change Coarse-grained normal mode analysis in structural biology.Structural answers and persistent questions about how nicotinic receptors work.Potentiation of alpha7 nicotinic acetylcholine receptors via an allosteric transmembrane site.Conformational changes in acetylcholine binding protein investigated by temperature accelerated molecular dynamics.Implications of the quaternary twist allosteric model for the physiology and pathology of nicotinic acetylcholine receptors.Structural basis for alcohol modulation of a pentameric ligand-gated ion channel Allosteric regulation of pentameric ligand-gated ion channels: an emerging mechanistic perspective

P2860

Q24618824-940CCB79-A795-4572-8490-71DA43835735 Q26827321-86B26CE0-FD56-49E4-BC52-6F3B935342EB Q26830810-CAC10A4C-7EB6-4739-AC58-539D84B9602B Q27008299-DF0872B4-3BCA-4B5E-98C6-37B6C713E1EF Q27308070-F0ADCC7B-D8DA-404C-8CD1-279754AC8DCB Q27329883-4C029216-DE81-442B-A94F-406550CD81E2 Q27334133-FA379626-3A19-44C1-897A-0AA3F47574B6 Q27652789-674D0E85-FA66-47EA-B71B-344E58CF3D79 Q27660303-00E3DD8E-3844-48F6-BF42-CB59474A2F42 Q27661310-67F721E6-D707-4478-97A1-AF904100B860 Q27670932-CE12DBFB-6200-4E61-979C-B65F56303D78 Q27681074-6234967D-2958-4751-9216-8967D15BDED5 Q27684621-663AF883-323A-4DB7-A710-173AB4A981A8 Q28271977-DBCB902E-5DE9-4A1F-B3CE-C57F52887DAD Q28303306-4540AEF5-C2B9-43E6-B268-05A7B762EABC Q28546747-E697C897-745C-4962-BDD3-22E60004C5F8 Q30487079-8CE4715C-A757-41B1-B96E-E15CF33C8B1A Q30491595-8F5C89B2-FFF3-42EC-8140-FFA603D4DC72 Q30513952-6F47B530-12B0-4DA4-A3E7-F69333207787 Q30587060-8233E0EA-4E90-4378-87D8-7F52C8614702 Q33258812-8B512457-B0B7-4E5F-9B92-E62D445B4DED Q33316816-5E1DE082-9BC2-45DC-8CFA-B506F5661E8E Q33718901-C5A22797-953F-4739-A174-452A06B04F58 Q33858349-2CB4BEA3-2339-4E5E-9CC7-4E25DC1CFB99 Q34032739-292181CB-3F32-46CA-94F6-E4618360DF2B Q34116031-CDA9E1D4-5768-42C4-A6B6-6FCA4BB93E2F Q34212824-24479ED1-0A66-405C-8907-12CFFA74901C Q34359229-45C907E1-DEB1-4A52-82EF-9E25D2BD9C61 Q34401189-94BDA864-291C-4E17-87C2-D5A681248379 Q34458574-8E841AA3-D49A-4B30-8A12-4A95B51324FD Q34466626-9270922E-CEA1-4980-8AEE-66641DEE220A Q34572493-E659937C-6645-44E5-8432-B166C7FFB63D Q34693795-DF5EAC18-E137-48BF-9B36-4BAE14E18A72 Q34694568-09D7F720-390E-4E85-B44E-166D6CB66D8A Q34782188-AD0FD255-9E7D-40A5-A3DF-C8D3F3882845 Q34827173-A86708F1-CC88-4C9C-999E-A9B66C24C3C0 Q35097431-725F91E5-EA92-4840-AB8E-40FB0269793C Q35119081-99912C9A-0895-4876-9E4A-955BAFD2A2A9 Q35122953-9398D714-E827-45C6-81D7-57BEC6ED2FB3 Q35493550-8492786C-8C03-49B1-962A-A2FCDC3F4840

P2860

Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism

http://www.wikidata.org/entity/Q34190634

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

name

Normal mode analysis suggests ...... inic receptor gating mechanism

@ast

Normal mode analysis suggests ...... inic receptor gating mechanism

@en

Normal mode analysis suggests ...... inic receptor gating mechanism

@nl

type

label

Normal mode analysis suggests ...... inic receptor gating mechanism

@ast

Normal mode analysis suggests ...... inic receptor gating mechanism

@en

Normal mode analysis suggests ...... inic receptor gating mechanism

@nl

prefLabel

Normal mode analysis suggests ...... inic receptor gating mechanism

@ast

Normal mode analysis suggests ...... inic receptor gating mechanism

@en

Normal mode analysis suggests ...... inic receptor gating mechanism

@nl

P1433

Q34190634-36844679-CF4A-4E0F-B401-945376A81816

P1476

Q34190634-97346CA6-F59E-4204-9C9A-CCE1ED9EE6C1

P2093

Q34190634-ADD72E28-5B69-437C-B753-219FFF2710D0

Q34190634-B3B3F89A-D674-400C-983A-4841CAB20B95

Q34190634-BA151701-4DC3-4A66-A4C6-68A6F6B39809

Q34190634-C3C513C1-2DD6-480F-9A0C-AEF78CAC79DF

P2860

Q34190634-00E13547-C20E-4717-BA41-F7822AA0BC34

Q34190634-09771B58-FE90-4548-AC61-1699EE9529D4

Q34190634-0BA63065-7A44-4751-910D-4825874B21C5

Q34190634-0E4EBE34-505B-463E-8B38-B19A7B8E9544

Q34190634-10616BE9-F7D4-450E-B47A-D81BD1800D49

Q34190634-19A80DBA-6808-490D-8643-11EAC0E3EEBF

Q34190634-22E04473-A2D5-4C57-9DA0-6AADC9716531

Q34190634-2356BB69-A432-4460-8DC7-3ECC872F2CAD

Q34190634-2B0AC87C-F0C1-4B11-8BA5-4143B36578E0

Q34190634-31A138B9-65F0-438A-B04B-0B6EB596F871

P304

Q34190634-D68DF836-0373-4496-B37A-A947F46059C7

P31

Q34190634-D1922468-0F22-449F-847B-9400A849D302

P356

Q34190634-1055DCD2-EF84-43D8-8628-70846FF4855E

P407

Q34190634-2FFA1CEB-8C77-4440-BD1A-C4156068D645

P433

Q34190634-7AD58E0D-57FE-4A76-9E32-9B58F2C0E016

P478

Q34190634-D0D48052-3958-4D66-A7B6-09AA2FA0449A

P50

Q34190634-39649B96-9C3A-4A84-BDF7-BC88C0C44D1F

Q34190634-62F82956-E9DA-4DDD-BF04-0A6D1C9DEE83

Q34190634-AA1639AD-DEBB-457E-9A95-46CC11A76965

P577

Q34190634-CCE41CC1-1995-43B8-BFD4-CDA6DB0E1C3B

P5875

Q34190634-7D804BA4-8EC4-4AC1-BF80-FC90D09DD969

P698

Q34190634-BD220070-9D0F-463E-8D7F-BCFD512A178D

P932

Q34190634-421E0685-A9CF-444A-9CC4-A3870661D6A3

P356

BIOPHYSJ.104.050229

P1433

Biophysical Journal

P1476

Normal mode analysis suggests ...... inic receptor gating mechanism

@en

P2093

Antoine Taly

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

Marc Delarue

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

Pierre-Jean Corringer

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

Thomas Grutter

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

P2860

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

Structural model of nicotinic acetylcholine receptor isotypes bound to acetylcholine and nicotine

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors

Structure and gating mechanism of the acetylcholine receptor pore

Comparative protein modelling by satisfaction of spatial restraints

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic

Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures

Allosteric changes in protein structure computed by a simple mechanical model: hemoglobin T<-->R2 transition.

Improved secondary structure predictions for a nicotinic receptor subunit: incorporation of solvent accessibility and experimental data into a two-dimensional representation.

P304

3954-3965

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

P31

scholarly article

P356

10.1529/BIOPHYSJ.104.050229

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

P407

P433

6

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

P478

88

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

P50

Nicolas Le Novère

Jean-Pierre Changeux

P577

2005-04-01T00:00:00Z

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

P5875

7931247

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

P698

15805177

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

P932

1305627

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