The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.
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NS1643 interacts around L529 of hERG to alter voltage sensor movement on the path to activation.Gating mechanism of Kv11.1 (hERG) K+ channels without covalent connection between voltage sensor and pore domains.The Fast Component of hERG Gating Charge: An Interaction between D411 in the S1 and S4 Residues.Functional characterization of Kv11.1 (hERG) potassium channels split in the voltage-sensing domain.
P2860
The neutral, hydrophobic isoleucine at position I521 in the extracellular S4 domain of hERG contributes to channel gating equilibrium.
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2013年の論文
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The neutral, hydrophobic isole ...... to channel gating equilibrium.
@en
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@nl
type
label
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@en
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@nl
prefLabel
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@en
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@nl
P2093
P2860
P1476
The neutral, hydrophobic isole ...... to channel gating equilibrium.
@en
P2093
David Fedida
Robert Vander Velde
Samuel J Goodchild
P2860
P304
P356
10.1152/AJPCELL.00147.2013
P577
2013-06-12T00:00:00Z