about
High yield production and refolding of the double-knot toxin, an activator of TRPV1 channels.Tarantula toxins use common surfaces for interacting with Kv and ASIC ion channels.An external sodium ion binding site controls allosteric gating in TRPV1 channelsStructural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxinTRPM channels come into focus.Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Chanhyung Bae
@ast
Chanhyung Bae
@en
Chanhyung Bae
@es
Chanhyung Bae
@nl
type
label
Chanhyung Bae
@ast
Chanhyung Bae
@en
Chanhyung Bae
@es
Chanhyung Bae
@nl
prefLabel
Chanhyung Bae
@ast
Chanhyung Bae
@en
Chanhyung Bae
@es
Chanhyung Bae
@nl
P106
P31
P496
0000-0003-3407-2857