Functional Validation of Heteromeric Kainate Receptor Models.

about

Biophysics of the Brain: From Molecules to Networks.Competition between Li+ and Na+ in sodium transporters and receptors: Which Na+-Binding sites are "therapeutic" Li+ targets?A structurally derived model of subunit-dependent NMDA receptor function

P2860

Q47997406-88DEBFA3-4834-43F7-9754-146B1CAB3A00 Q55333423-57692922-F819-4962-B35D-FA708A588D82 Q58805055-E6327082-28A0-4ACD-8865-0E44D804A0D1

P2860

Functional Validation of Heteromeric Kainate Receptor Models.

Item

http://www.wikidata.org/entity/Q47765932

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Functional Validation of Heteromeric Kainate Receptor Models.

@en

Functional Validation of Heteromeric Kainate Receptor Models.

@nl

type

Item

label

Functional Validation of Heteromeric Kainate Receptor Models.

@en

Functional Validation of Heteromeric Kainate Receptor Models.

@nl

prefLabel

Functional Validation of Heteromeric Kainate Receptor Models.

@en

Functional Validation of Heteromeric Kainate Receptor Models.

@nl

P1476

Functional Validation of Heteromeric Kainate Receptor Models.

@en

P2093

Derek Bowie

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

Patricia M G E Brown

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

Teresa Paramo

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

P2860

Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

Structural basis for partial agonist action at ionotropic glutamate receptors

Molecular Basis of Kainate Receptor Modulation by Sodium

Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

Structure and Assembly Mechanism for Heteromeric Kainate Receptors

Correlating efficacy and desensitization with GluK2 ligand-binding domain movements

Crystal structure of a heterotetrameric NMDA receptor ion channel

NMDA receptor structures reveal subunit arrangement and pore architecture.

L-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domain

P304

2173-2177

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

P31

scholarly article

P356

10.1016/J.BPJ.2017.08.047

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

P407

English

P433

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

P478

113

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

P50

Maria Musgaard

Philip C Biggin

P577

2017-09-19T00:00:00Z

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

P698

28935133

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

P932

5700254

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

Functional Validation of Heteromeric Kainate Receptor Models.

about

P2860

P2860

Functional Validation of Heteromeric Kainate Receptor Models.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932