Calcicludine binding to the outer pore of L-type calcium channels is allosterically coupled to dihydropyridine binding
about
A genetic screen for dihydropyridine (DHP)-resistant worms reveals new residues required for DHP-blockage of mammalian calcium channelsUse of venom peptides to probe ion channel structure and function.A single amino acid change in Ca(v)1.2 channels eliminates the permeation and gating differences between Ca(2+) and Ba(2+).The ionic mechanism of membrane potential oscillations and membrane resonance in striatal LTS interneurons.Fasxiator, a novel factor XIa inhibitor from snake venom, and its site-specific mutagenesis to improve potency and selectivity.
P2860
Calcicludine binding to the outer pore of L-type calcium channels is allosterically coupled to dihydropyridine binding
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Calcicludine binding to the ou ...... led to dihydropyridine binding
@en
type
label
Calcicludine binding to the ou ...... led to dihydropyridine binding
@en
prefLabel
Calcicludine binding to the ou ...... led to dihydropyridine binding
@en
P2093
P2860
P356
P1433
P1476
Calcicludine binding to the ou ...... led to dihydropyridine binding
@en
P2093
Blaise Z Peterson
Xianming Wang
P2860
P304
P356
10.1021/BI7001696
P407
P577
2007-05-31T00:00:00Z