Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insights into the structure and function of HV1 from a meta-analysis of mutation studies.

The Journal of general physiology - 1 Aug 2016

DeCoursey Thomas E, Morgan Deri, Musset Boris, Cherny Vladimir V

Abstract excerpt

The voltage-gated proton channel (HV1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for HV1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Ion Channel Gating
Share to Ion Channels
Share to Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 27481712
DOI: 10.1085/jgp.201611619
PMCID: PMC4969798

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into the structure and function of HV1 from a meta-analysis of mutation studies.PMID 27481712Read ↗

Biophysical Properties of Somatic Cancer Mutations in the S4 Transmembrane Segment of the Human Voltage-Gated Proton Channel hHV1.Semantic proximity Read ↗

Modulators of the human voltage-gated proton channel Hv1Semantic proximity Read ↗

Tryptophan 207 is crucial to the unique properties of the human voltage-gated proton channel, hHV1.Semantic proximity Read ↗

The pore of the voltage-gated proton channel.Semantic proximity Read ↗

Quantitative insights into the mechanism of proton conduction and selectivity for the human voltage-gated proton channel Hv1.Semantic proximity Read ↗

A voltage-gated proton-selective channel lacking the pore domain.Semantic proximity Read ↗

Computational Approaches for Investigating Disease-causing Mutations in Membrane Proteins: Database Development, Analysis and Prediction.Semantic proximity Read ↗

Mapping Structural Distribution and Gating-Property Impacts of Disease-Associated Missense Mutations in Voltage-Gated Sodium ChannelsSemantic proximity Read ↗

Mutations in transmembrane proteins: diseases, evolutionary insights, prediction and comparison with globular proteinsSemantic proximity Read ↗

Mapping the gating and permeation pathways in the voltage-gated proton channel Hv1.Semantic proximity Read ↗

An aqueous H+ permeation pathway in the voltage-gated proton channel Hv1.Semantic proximity Read ↗

Selectivity Mechanism of the Voltage-gated Proton Channel, HV1.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.