Influence of C-terminal protein domains and protein-lipid interactions on tetramerization and stability of the potassium channel KcsA.
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Crystal structure of full-length KcsA in its closed conformationSynchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly.Molecular and electrophysiological characterization of a novel cation channel of Trypanosoma cruzi.GCN4 enhances the stability of the pore domain of potassium channel KcsA.Identification of the self-incompatibility locus F-box protein-containing complex in Petunia inflata.NMR study of the tetrameric KcsA potassium channel in detergent micelles.Functional role and affinity of inorganic cations in stabilizing the tetrameric structure of the KcsA K+ channelThe Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) ReceptorsConformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.Kv10.1 K(+) channel: from physiology to cancer.Cellular cholesterol controls TRPC3 function: evidence from a novel dominant-negative knockdown strategy.The role of extramembranous cytoplasmic termini in assembly and stability of the tetrameric K(+)-channel KcsAMolecular determinants of tetramerization in the KcsA cytoplasmic domain.Do small headgroups of phosphatidylethanolamine and phosphatidic acid lead to a similar folding pattern of the K(+) channel?N-type inactivation of the potassium channel KcsA by the Shaker B "ball" peptide: mapping the inactivating peptide-binding epitope.Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA).Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.Phosphatidic acid plays a special role in stabilizing and folding of the tetrameric potassium channel KcsA.Characterization of the C-terminal domain of a potassium channel from Streptomyces lividans (KcsA).Effects of conducting and blocking ions on the structure and stability of the potassium channel KcsA.An engineered right-handed coiled coil domain imparts extreme thermostability to the KcsA channelThe influence of a membrane environment on the structure and stability of a prokaryotic potassium channel, KcsA
P2860
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P2860
Influence of C-terminal protein domains and protein-lipid interactions on tetramerization and stability of the potassium channel KcsA.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Influence of C-terminal protei ...... of the potassium channel KcsA.
@en
Influence of C-terminal protei ...... of the potassium channel KcsA.
@nl
type
label
Influence of C-terminal protei ...... of the potassium channel KcsA.
@en
Influence of C-terminal protei ...... of the potassium channel KcsA.
@nl
prefLabel
Influence of C-terminal protei ...... of the potassium channel KcsA.
@en
Influence of C-terminal protei ...... of the potassium channel KcsA.
@nl
P2093
P356
P1433
P1476
Influence of C-terminal protei ...... of the potassium channel KcsA
@en
P2093
Fernández-Ballester G
González-Ros JM
Riquelme G
P304
14924-14931
P356
10.1021/BI048889+
P407
P577
2004-11-01T00:00:00Z