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1 KTx specificity for calcium-activated versus voltage-dependent potassium channels.
2 Shaker (Kv1) and Shal (Kv4), both expressing voltage-dependent potassium channels.
3 Application of indole slows activation of voltage-dependent potassium channels and reduces steady-
4 elopmental transcriptional regulation of Kv1 voltage-dependent potassium channels and the resulting p
5 Kv3.3 proteins are pore-forming subunits of voltage-dependent potassium channels, and mutations in t
6 lices, consisting of S1-S6, conserved in all voltage-dependent potassium channels, and the unique S0
11 ods were used to determine the expression of voltage-dependent potassium channel currents and mRNAs i
13 CA, is a rapidly activating and inactivating voltage-dependent potassium channel expressed in chemose
16 rized the properties and functional roles of voltage-dependent potassium channels in the dendrites of
17 that METH exposure affected the activity of voltage-dependent potassium channels in these neurons.
19 ood flow responses, and identify upregulated voltage-dependent potassium channel (KV) number in cereb
25 se in IGABA was assessed by coexpressing the voltage-dependent potassium channel Kv1.4 along with the
27 e beta subunit (Kvbeta) of the Shaker family voltage-dependent potassium channels (Kv1) is a cytosoli
29 ion of ERK results in phosphorylation of the voltage-dependent potassium channel Kv4.2 and the nuclea
30 that oxidation of a methionine residue in a voltage-dependent potassium channel modulates its inacti
31 ved lncRNA, named Kcna2 antisense RNA, for a voltage-dependent potassium channel mRNA, Kcna2, in firs
32 key and rat optic nerves, immunolabeling for voltage-dependent potassium channels of the Shaker famil
34 s inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adip
36 nd that reduced functional expression of the voltage-dependent potassium channel subunit Kv1.1 substa
40 pret the recent atomic structures of the Kv (voltage-dependent potassium) channel T1 domain in a func
41 pioid receptors are coupled to a Shaker-type voltage-dependent potassium channel that is sensitive to
43 s study, we analyze KvAP, an archaebacterial voltage-dependent potassium channel, to study the mobili
44 to membrane potential, indicating few active voltage-dependent potassium channels, whereas sympatheti
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