JBC M9:031724, Revised ISOLATION AND CHARACTERIZATION OF A HIGH AFFINITY PEPTIDE INHIBITOR OF CLC-2 CHLORIDE CHANNELS
نویسندگان
چکیده
1 School of Biology, Georgia Institute of Technology, 310 Ferst Drive, Atlanta, GA, 30332. Program in Molecular and Systems Pharmacology, Emory University, 1510 Clifton Road, Atlanta, GA, 30322. 3 Peptide Synthesis Core Facility, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, Canada, T2N 4N1. Dept. of Physiology & Biophysics, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, Canada, T2N 4N1. Microchemical and Proteomics Facility, Emory University, 1365 Clifton Road, Atlanta, GA, 30322. School of Chemistry & Biochemistry, Georgia Institute of Technology, 310 Ferst Drive, Atlanta, GA, 30332. Children’s Healthcare of Atlanta and Department of Pediatrics, Emory University, 2015 Uppergate Drive, Atlanta, GA 30322.
منابع مشابه
Isolation and characterization of a high affinity peptide inhibitor of ClC-2 chloride channels.
The ClC protein family includes voltage-gated chloride channels and chloride/proton exchangers. In eukaryotes, ClC proteins regulate membrane potential of excitable cells, contribute to epithelial transport, and aid in lysosomal acidification. Although structure/function studies of ClC proteins have been aided greatly by the available crystal structures of a bacterial ClC chloride/proton exchan...
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