title: Insights into the structure and function of HV1 from a meta-analysis of mutation studies.
abstract: 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 information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of HV1 await future revelation.
authors.affiliation: Department of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612 tdecours@rush.edu.
authors.forename: Thomas E
authors.identifier: 0000-0002-4263-180X
authors.initials: TE
authors.lastname: DeCoursey
authors.affiliation: Department of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612.
authors.forename: Deri
authors.initials: D
authors.lastname: Morgan
authors.affiliation: Institut für Physiologie, PMU Klinikum Nürnberg, 90419 Nürnberg, Germany.
authors.forename: Boris
authors.initials: B
authors.lastname: Musset
authors.affiliation: Department of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612.
authors.forename: Vladimir V
authors.initials: VV
authors.lastname: Cherny
mesh_terms: D000818:Animals; D006801:Humans; D015640:Ion Channel Gating; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D011487:Protein Conformation
chemical_list: C510235:HVCN1 protein, human; D007473:Ion Channels