The Human Sodium-Glucose Cotransporter (hSGLT1) Is a Disulfide-Bridged Homodimer with a Re-Entrant C-Terminal Loop

Author:

Sasseville Louis J.,Morin Michael,Coady Michael J.,Blunck Rikard,Lapointe Jean-Yves

Funder

Natural Sciences and Engineering Research Council of Canada

CIHR

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference46 articles.

1. The structural basis of secondary active transport mechanisms;LR Forrest;Biochimica et Biophysica Acta (BBA)-Bioenergetics,2010

2. Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy;S Eskandari;Proceedings of the National Academy of Sciences,1998

3. Identification of a disulfide bridge linking the fourth and the seventh extracellular loops of the Na+/glucose cotransporter;DG Gagnon;The Journal of general physiology,2006

4. Voltage-Clamp Fluorometry in the Local Environment of the C255-C511 Disulfide Bridge of the Na+/Glucose Cotransporter;DG Gagnon;Biophysical journal,2007

5. Membrane topology of loop 13–14 of the Na+/glucose cotransporter (SGLT1): A SCAM and fluorescent labelling study;DG Gagnon;Biochimica et Biophysica Acta (BBA)-Biomembranes,2005

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