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David H. MacLennan, Ph.D.

Affiliations: 
University of Toronto, Toronto, ON, Canada 
Area:
Calcium handling
Website:
http://www.utoronto.ca/maclennan/director.htm
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"David MacLennan"
Bio:

David MacLennan Born July 3, 1937 Swan River, Manitoba, Canada Died June 24, 2020 (aged 82) Toronto, Ontario, Canada Nationality Canadian Education University of Manitoba (B.S.A.) Purdue University (M.S., Ph.D.) Scientific career Fields Biochemistry, Genetics Institutions University of Toronto Thesis Compartmentation of organic acids in plant tissues (1963) Doctoral advisor Harry Beevers David Herman MacLennan OC OOnt FRS FRSC (July 3, 1937 - June 24, 2020) was a Canadian biochemist and geneticist known for his basic work on proteins that regulate calcium flux through the sarcoplasmic reticulum (SR), thereby regulating muscle contraction and relaxation, and for his discoveries in the field of muscle diseases caused by genetic defects in calcium regulatory proteins.[1]

http://www.nasonline.org/member-directory/members/3012729.html

https://sce.library.utoronto.ca/index.php?title=MacLennan,_David

Mean distance: 18.13 (cluster 46)
 
SNBCP
Cross-listing: Neurotree

Parents

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Harry Beevers grad student 1963 Purdue
 (Compartmentation of organic acids in plant tissues)
David E. Green post-doc 1963-1964 UW Madison
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Publications

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Chen W, Koop A, Liu Y, et al. (2017) Reduced Threshold for Store-Overload-Induced-Ca(2+)-Release is a Common Defect of RyR1 Mutations Associated with Malignant Hyperthermia and Central Core Disease. The Biochemical Journal
Teng AC, Miyake T, Yokoe S, et al. (2015) Metformin increases degradation of phospholamban via autophagy in cardiomyocytes. Proceedings of the National Academy of Sciences of the United States of America. 112: 7165-70
Zvaritch E, MacLennan DH. (2015) Muscle spindles exhibit core lesions and extensive degeneration of intrafusal fibers in the Ryr1(I4895T/wt) mouse model of core myopathy. Biochemical and Biophysical Research Communications. 460: 34-9
Sambuughin N, Zvaritch E, Kraeva N, et al. (2014) Exome analysis identifies Brody myopathy in a family diagnosed with malignant hyperthermia susceptibility. Molecular Genetics & Genomic Medicine. 2: 472-83
Amador FJ, Kimlicka L, Stathopulos PB, et al. (2013) Type 2 ryanodine receptor domain A contains a unique and dynamic α-helix that transitions to a β-strand in a mutant linked with a heritable cardiomyopathy. Journal of Molecular Biology. 425: 4034-46
Kraeva N, Zvaritch E, Frodis W, et al. (2013) CASQ1 gene is an unlikely candidate for malignant hyperthermia susceptibility in the North American population. Anesthesiology. 118: 344-9
Kraeva N, Zvaritch E, Rossi AE, et al. (2013) Novel excitation-contraction uncoupled RYR1 mutations in patients with central core disease. Neuromuscular Disorders : Nmd. 23: 120-32
Sharma P, Ishiyama N, Nair U, et al. (2012) Structural determination of the phosphorylation domain of the ryanodine receptor. The Febs Journal. 279: 3952-64
De Crescenzo V, Fogarty KE, Lefkowitz JJ, et al. (2012) Type 1 ryanodine receptor knock-in mutation causing central core disease of skeletal muscle also displays a neuronal phenotype. Proceedings of the National Academy of Sciences of the United States of America. 109: 610-5
Tupling AR, Bombardier E, Gupta SC, et al. (2011) Enhanced Ca2+ transport and muscle relaxation in skeletal muscle from sarcolipin-null mice. American Journal of Physiology. Cell Physiology. 301: C841-9
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