Tryptophan scanning of the acetylcholine receptor's betaM4 transmembrane domain: decoding allosteric linkage at the lipid-protein interface with ion-channel gating.
about
Tryptophan scanning mutagenesis of the first transmembrane domain of the innexin Shaking-B(Lethal).Fourier transform coupled tryptophan scanning mutagenesis identifies a bending point on the lipid-exposed δM3 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels.Tryptophan scanning mutagenesis reveals distortions in the helical structure of the δM4 transmembrane domain of the Torpedo californica nicotinic acetylcholine receptor.
P2860
Tryptophan scanning of the acetylcholine receptor's betaM4 transmembrane domain: decoding allosteric linkage at the lipid-protein interface with ion-channel gating.
description
2008 nî lūn-bûn
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2008年の論文
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2008年論文
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2008年論文
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2008年論文
@zh-hk
2008年論文
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2008年論文
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2008年论文
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2008年论文
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2008年论文
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name
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@ast
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@en
type
label
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@ast
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@en
prefLabel
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@ast
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@en
P2093
P2860
P1433
P1476
Tryptophan scanning of the ace ...... rface with ion-channel gating.
@en
P2093
Anette Casiano
David Abner Torres-Nuñez
José Antonio Lasalde-Dominicci
José David Otero-Cruz
Rosedelma Díaz-De León
P2860
P304
P577
2008-11-06T00:00:00Z