The voltage-gated proton channel H v 1 is a member of voltage-gated ion channels
containing voltage-sensing domains (VSDs). The VSDs are made of four membrane …

In voltage-gated Na+ and K+ channels, the hydrophobicity of non-charged residues in the
S4 helix has been shown to regulate the S4 movement underlying the process of voltage …

Voltage-gated sodium, potassium, and calcium channels are made of a pore domain (PD)
controlled by four voltage-sensing domains (VSDs). The PD contains the ion permeation …

The voltage sensor domain (VSD) is the key module for voltage sensing in voltage-gated ion
channels and voltage-sensing phosphatases. Structurally, both the VSD and the recently …

The voltage-gated proton channel Hv1 (or VSOP) has a voltage-sensor domain (VSD) with
dual roles of voltage sensing and proton permeation. Its gating is sensitive to pH and Zn2+ …

Ever since Hodgkin and Huxley's work in 1952 first described the permeation changes for
sodium and potassium in the squid giant axon (1), scientists in the membrane biophysics …

Voltage-dependent gating of the voltage-gated proton channels (HV 1) remains poorly
understood, partly because of the difficulty of obtaining direct measurements of voltage …

Voltage-gated proton (Hv1) channels play important roles in the respiratory burst, in pH
regulation, in spermatozoa, in apoptosis, and in cancer metastasis. Unlike other voltage …

The majority of voltage-gated ion channels contain a defined voltage-sensing domain and a
pore domain composed of highly conserved amino acid residues that confer electrical …

Voltage‐gated proton channels have been described in different cells and organisms since
the early'80s, but the first member of the family, Hv1, was cloned only recently. The Hv1 …