| pubmed-article:21354396 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21354396 | lifeskim:mentions | umls-concept:C0003075 | lld:lifeskim |
| pubmed-article:21354396 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
| pubmed-article:21354396 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:21354396 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:21354396 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:21354396 | pubmed:dateCreated | 2011-2-28 | lld:pubmed |
| pubmed-article:21354396 | pubmed:abstractText | ClC-4 is a secondary active transporter that exchanges Cl(-) ions and H(+) with a 2:1 stoichiometry. In external SCN(-), ClC-4 becomes uncoupled and transports anions with high unitary transport rate. Upon voltage steps, the number of active transporters varies in a time-dependent manner, resembling voltage-dependent gating of ion channels. We here investigated modification of the voltage dependence of uncoupled ClC-4 by protons and anions to quantify association of substrates with the transporter. External acidification shifts voltage dependence of ClC-4 transport to more positive potentials and leads to reduced transport currents. Internal pH changes had less pronounced effects. Uncoupled ClC-4 transport is facilitated by elevated external [SCN(-)] but impaired by internal Cl(-) and I(-). Block by internal anions indicates the existence of an internal anion-binding site with high affinity that is not present in ClC channels. The voltage dependence of ClC-4 coupled transport is modulated by external protons and internal Cl(-) in a manner similar to what is observed under uncoupling conditions. Our data illustrate functional differences but also similarities between ClC channels and transporters. | lld:pubmed |
| pubmed-article:21354396 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21354396 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21354396 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21354396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21354396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21354396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21354396 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21354396 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21354396 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21354396 | pubmed:issn | 1542-0086 | lld:pubmed |
| pubmed-article:21354396 | pubmed:author | pubmed-author:FahlkeChristo... | lld:pubmed |
| pubmed-article:21354396 | pubmed:author | pubmed-author:AlekovAlexi... | lld:pubmed |
| pubmed-article:21354396 | pubmed:author | pubmed-author:OrhanGökceG | lld:pubmed |
| pubmed-article:21354396 | pubmed:copyrightInfo | Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21354396 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21354396 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:21354396 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:21354396 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21354396 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21354396 | pubmed:pagination | 1233-41 | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:meshHeading | pubmed-meshheading:21354396... | lld:pubmed |
| pubmed-article:21354396 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21354396 | pubmed:articleTitle | Anion- and proton-dependent gating of ClC-4 anion/proton transporter under uncoupling conditions. | lld:pubmed |
| pubmed-article:21354396 | pubmed:affiliation | Institut für Neurophysiologie, Medizinische Hochschule, Hannover, Germany. | lld:pubmed |
| pubmed-article:21354396 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21354396 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1183 | entrezgene:pubmed | pubmed-article:21354396 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21354396 | lld:entrezgene |
