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1 ion, markedly different in activity from (-)-batrachotoxin.
2 of site 2 neurotoxins, such as aconitine and batrachotoxin.
3 overlaps receptors for local anesthetics and batrachotoxin.
5 in-A and an isomer (3 and 3a, respectively), batrachotoxin (4), batrachotoxinin-A 3'-hydroxypentanoat
6 two other classes of sodium channel toxins, batrachotoxin (a site 2 toxin) and Lqhalpha-IT (a site 3
8 rthermore, both hNav1.5-CW/F1760K mutant and batrachotoxin-activated hNav1.5 Na(+) channels became co
9 effects of such sodium channel activators as batrachotoxin and a pumiliotoxin B/scorpion venom combin
10 g of the anticonvulsant drug Lamotrigine and batrachotoxin are also seen in the modified channels.
12 natural (-) and non-natural (+) antipodes of batrachotoxin, as well both enantiomers of a C-20 benzoa
13 uced a strong synergistic stimulation of [3H]batrachotoxin binding in combination with brevetoxin, wh
14 he ATX-induced allosteric enhancement of [3H]batrachotoxin binding to neurotoxin site 2 of the alpha
15 id RU51049, positive allosteric enhancers of batrachotoxin binding, a protein with an apparent molecu
18 ctural model of the rNav1.4 Na+ channel with batrachotoxin (BTX) bound within the inner cavity sugges
20 quester lethal amounts of steroidal alkaloid batrachotoxin (BTX) in their skin as a defense mechanism
24 ted Na+ channels in excitable cells, whereas batrachotoxin (BTX) keeps these channels open persistent
27 double mutant channel remained sensitive to batrachotoxin (BTX), even though nearby residues S1276 a
29 localized using a photoreactive radiolabeled batrachotoxin derivative to covalently label purified an
30 ecifically photolabeled by the photoreactive batrachotoxin derivative was identified by antibody mapp
31 of South America could be the source of the batrachotoxins found in the highly toxic Phyllobates fro
33 e we describe the presence of high levels of batrachotoxins in a little-studied group of beetles, gen
35 th trypsin or V8 protease indicated that the batrachotoxin receptor site is formed in part by a porti
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