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Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies

The voltage-gated proton channel (H(V)1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for H(V)1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by...

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Autores principales: DeCoursey, Thomas E., Morgan, Deri, Musset, Boris, Cherny, Vladimir V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969798/
https://www.ncbi.nlm.nih.gov/pubmed/27481712
http://dx.doi.org/10.1085/jgp.201611619
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author DeCoursey, Thomas E.
Morgan, Deri
Musset, Boris
Cherny, Vladimir V.
author_facet DeCoursey, Thomas E.
Morgan, Deri
Musset, Boris
Cherny, Vladimir V.
author_sort DeCoursey, Thomas E.
collection PubMed
description The voltage-gated proton channel (H(V)1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for H(V)1 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 H(V)1 await future revelation.
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spelling pubmed-49697982017-02-01 Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies DeCoursey, Thomas E. Morgan, Deri Musset, Boris Cherny, Vladimir V. J Gen Physiol Reviews The voltage-gated proton channel (H(V)1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for H(V)1 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 H(V)1 await future revelation. The Rockefeller University Press 2016-08 /pmc/articles/PMC4969798/ /pubmed/27481712 http://dx.doi.org/10.1085/jgp.201611619 Text en © 2016 DeCoursey et al. https://creativecommons.org/licenses/by-nc-sa/3.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ (https://creativecommons.org/licenses/by-nc-sa/3.0/) ).
spellingShingle Reviews
DeCoursey, Thomas E.
Morgan, Deri
Musset, Boris
Cherny, Vladimir V.
Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title_full Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title_fullStr Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title_full_unstemmed Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title_short Insights into the structure and function of H(V)1 from a meta-analysis of mutation studies
title_sort insights into the structure and function of h(v)1 from a meta-analysis of mutation studies
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969798/
https://www.ncbi.nlm.nih.gov/pubmed/27481712
http://dx.doi.org/10.1085/jgp.201611619
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