Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.

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Assessment of the functionality and stability of detergent purified nAChR from Torpedo using lipidic matrixes and macroscopic electrophysiology.The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels.

P2860

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P2860

Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.

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http://www.wikidata.org/entity/Q42236580

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2012 nî lūn-bûn

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2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

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2012年论文

@zh-cn

name

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@en

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@nl

type

Item

label

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@en

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@nl

prefLabel

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@en

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@nl

P1476

Tryptophan scanning mutagenesi ...... otinic acetylcholine receptor.

@en

P2093

Daniel Caballero-Rivera

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

David A Torres-Nunez

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

Jessica Oyola-Cintrón

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

Jose D Otero-Cruz

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

José A Lasalde-Dominicci

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

Omar A Cruz-Nieves

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

P2860

Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel

Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy

Structure of bacteriorhodopsin at 1.55 A resolution

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

Structure and gating mechanism of the acetylcholine receptor pore

The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors

Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution

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

P304

111-123

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P31

scholarly article

P356

10.4161/CHAN.19540

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

P433

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

P478

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

P577

2012-03-01T00:00:00Z

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P5875

225058332

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P698

22622285

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P921

transmembrane protein

P932

3396688

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

Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.

about

P2860

P2860

Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932