David H. MacLennan
Banting and Best Department of Medical Research
University of Toronto
C. H. Best Institute
Ontario
Canada
Name/email consistency: high
- Store overload-induced Ca2+ release as a triggering mechanism for CPVT and MH episodes caused by mutations in RYR and CASQ genes. MacLennan, D.H., Chen, S.R. J. Physiol. (Lond.) (2009)
- The regulation of SERCA-type pumps by phospholamban and sarcolipin. MacLennan, D.H., Asahi, M., Tupling, A.R. Ann. N. Y. Acad. Sci. (2003)
- Phospholamban: a crucial regulator of cardiac contractility. MacLennan, D.H., Kranias, E.G. Nat. Rev. Mol. Cell Biol. (2003)
- Structure-function relationships in Ca(2+) cycling proteins. MacLennan, D.H., Abu-Abed, M., Kang, C. J. Mol. Cell. Cardiol. (2002)
- Ca2+ signalling and muscle disease. MacLennan, D.H. Eur. J. Biochem. (2000)
- The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. MacLennan, D.H., Rice, W.J., Green, N.M. J. Biol. Chem. (1997)
- 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., Rice, W.J., Odermatt, A. Ann. N. Y. Acad. Sci. (1997)
- Scanning mutagenesis reveals a similar pattern of mutation sensitivity in transmembrane sequences M4, M5, and M6, but not in M8, of the Ca2+-ATPase of sarcoplasmic reticulum (SERCA1a). Rice, W.J., MacLennan, D.H. J. Biol. Chem. (1996)
