<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Preston, G M</style></author><author><style face="normal" font="default" size="100%">Carroll, T P</style></author><author><style face="normal" font="default" size="100%">Guggino, W B</style></author><author><style face="normal" font="default" size="100%">Agre, P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Science</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Aquaporin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Aquaporins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane Permeability</style></keyword><keyword><style  face="normal" font="default" size="100%">Electric Conductivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Erythrocyte Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoblotting</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Mercuric Chloride</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Oocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Osmolar Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermodynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">Transfection</style></keyword><keyword><style  face="normal" font="default" size="100%">Water</style></keyword><keyword><style  face="normal" font="default" size="100%">Xenopus laevis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1992</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1992 Apr 17</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">256</style></volume><pages><style face="normal" font="default" size="100%">385-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5055</style></issue><custom1><style face="normal" font="default" size="100%">&lt;p&gt;http://www.ncbi.nlm.nih.gov/pubmed/1373524?dopt=Abstract&lt;/p&gt;
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