3-D structural and functional characterization of the purified KATPchannel complex Kir6.2-SUR1
Author:
Affiliation:
1. Laboratory of Physiology, University of Oxford; Oxford UK
2. Department of Biochemistry, University of Oxford; Oxford UK
3. Faculty of Life Sciences, University of Manchester; Manchester UK
Publisher
Wiley
Subject
General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience
Reference57 articles.
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3. New windows on the mechanism of action of KATP channel openers;Ashcroft;Trends Pharmacol Sci,2000
4. SUR-dependent modulation of KATP channels by an N-terminal KIR6.2 peptide. Defining intersubunit gating interactions;Babenko;J Biol Chem,2002
5. Three-dimensional structure of Wza, the protein required for translocation of group 1 capsular polysaccharide across the outer membrane of Escherichia coli;Beis;J Biol Chem,2004
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