Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.
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The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel TraffickingTuning of EAG K(+) channel inactivation: molecular determinants of amplification by mutations and a small moleculeRegions of KCNQ K(+) channels controlling functional expression
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Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.
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2012年の論文
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Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
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Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
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type
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Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
@ast
Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
@en
prefLabel
Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
@ast
Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
@en
P2093
P2860
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Pore helix-S6 interactions are ...... plitudes of KCNQ3 K+ channels.
@en
P2093
Frank S Choveau
Mark S Shapiro
Sonya M Bierbower
P2860
P304
P356
10.1016/J.BPJ.2012.04.019
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P577
2012-06-05T00:00:00Z