Structure/function analysis of the Ca2+ binding and translocation domain of SERCA1 and the role in Brody disease of the ATP2A1 gene encoding SERCA1.
MacLennan
D H
DH
Banting and Best Department of Medical Research, University of Toronto, Charles H. Best Institute, Ontario, Canada. david.maclennan@utoronto.ca
Rice
W J
WJ
Odermatt
A
A
D000244:Adenosine Diphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018656:Muscle Fibers, Fast-Twitch / Q000201:enzymology; D018482:Muscle, Skeletal / Q000201:enzymology; D009135:Muscular Diseases / Q000201:enzymology* / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000201:enzymology
D011994:Recombinant Proteins; D000244:Adenosine Diphosphate; D000252:Calcium-Transporting ATPases; D002118:Calcium