CLC chloride channels and transporters. Export

@article{citeulike:997084, abstract = {CLC proteins are found in cells from prokaryotes to mammals and perform functions in plasma membranes and intracellular vesicles. Several genetic human diseases and mouse models underscore their broad physiological functions in mammals. These functions range from the control of excitability to transepithelial transport, endocytotic trafficking and acidification of synaptic vesicles. The recent crystallization of bacterial CLC proteins gave surprising insights into CLC Cl(-)-channel permeation and gating and provides an excellent basis for structure-function studies. Surprisingly, the CLC from Escherichia coli functions as a Cl-/H+ exchanger, thus demonstrating the thin line separating transporters and channels.}, address = {Zentrum f\"{u}r Molekulare Neurobiologie, ZMNH, Universit\"{a}t Hamburg, Falkenried 94, D-20246 Hamburg. Jentsch@zmnh.uni-hamburg.de}, author = {Jentsch, T. J. and Neagoe, I. and Scheel, O.}, citeulike-article-id = {997084}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.conb.2005.05.002}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15913981}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15913981}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6VS3-4G7G4FW-1/2/fc99a2311672c728d4383e710e2bb795}, doi = {10.1016/j.conb.2005.05.002}, issn = {0959-4388}, journal = {Curr Opin Neurobiol}, keywords = {channel, clc}, month = {June}, number = {3}, pages = {319--325}, posted-at = {2009-07-01 21:01:03}, priority = {2}, title = {CLC chloride channels and transporters.}, url = {http://dx.doi.org/10.1016/j.conb.2005.05.002}, volume = {15}, year = {2005} }

TY - JOUR ID - citeulike:997084 L3 - citeulike-article-id:997084 N2 - CLC proteins are found in cells from prokaryotes to mammals and perform functions in plasma membranes and intracellular vesicles. Several genetic human diseases and mouse models underscore their broad physiological functions in mammals. These functions range from the control of excitability to transepithelial transport, endocytotic trafficking and acidification of synaptic vesicles. The recent crystallization of bacterial CLC proteins gave surprising insights into CLC Cl(-)-channel permeation and gating and provides an excellent basis for structure-function studies. Surprisingly, the CLC from Escherichia coli functions as a Cl-/H+ exchanger, thus demonstrating the thin line separating transporters and channels. IS - 3 JF - Curr Opin Neurobiol SN - 0959-4388 AD - Zentrum für Molekulare Neurobiologie, ZMNH, Universität Hamburg, Falkenried 94, D-20246 Hamburg. Jentsch@zmnh.uni-hamburg.de EP - 325 TI - CLC chloride channels and transporters. VL - 15 SP - 319 KW - channel KW - clc AU - Jentsch, TJ AU - Neagoe, I AU - Scheel, O PY - 2005/06// UR - http://dx.doi.org/10.1016/j.conb.2005.05.002 ER -