The binding of kappa-Conotoxin PVIIA and fast C-type inactivation of Shaker K+ channels are mutually exclusive.

The binding of kappa-Conotoxin PVIIA and fast C-type inactivation of Shaker K+ channels are mutually exclusive.

Item
http://www.wikidata.org/entity/Q40267541
A β-amyloid oligomer directly modulates P/Q-type calcium currents in Xenopus oocytes.Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel blocker: evaluation of cardioprotective effects of kappaM-conotoxins.Slow inactivation in voltage gated potassium channels is insensitive to the binding of pore occluding peptide toxins.Stabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanismNeuroprotective and cardioprotective conopeptides: an emerging class of drug leads.Hunting the chameleon: structural conformations of the intrinsically disordered protein alpha-synuclein.P/Q-type calcium channel modulators.Small Packages, Big Returns: Uncovering the Venom Diversity of Small Invertebrate Conoidean Snails.Nanofiber-based paramagnetic probes for rapid, real-time biomedical oximetry.Dysregulation of Intracellular Calcium Signaling in Alzheimer's Disease
P2860

The binding of kappa-Conotoxin PVIIA and fast C-type inactivation of Shaker K+ channels are mutually exclusive.

Item
http://www.wikidata.org/entity/Q40267541
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The binding of kappa-Conotoxin ...... annels are mutually exclusive.
@en
type
label
The binding of kappa-Conotoxin ...... annels are mutually exclusive.
@en
prefLabel
The binding of kappa-Conotoxin ...... annels are mutually exclusive.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932
P356
P1433
P1476
The binding of kappa-Conotoxin ...... annels are mutually exclusive.
@en
P2093
P2860
P304
P31
P356
10.1016/S0006-3495(04)74096-5
P407
P433
P478
P577
P698
P932