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Vijay K. Khanna

Researcher at University of Toronto

Publications -  21
Citations -  4423

Vijay K. Khanna is an academic researcher from University of Toronto. The author has contributed to research in topics: RYR1 & Ryanodine receptor. The author has an hindex of 20, co-authored 21 publications receiving 4286 citations.

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Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia

TL;DR: Haplotyping suggests that the mutation in all five breeds of lean, heavily muscled swine has a common origin, and the development of a noninvasive diagnostic test will provide the basis for elimination of the MH gene or its controlled inclusion in swine breeding programs.
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Molecular cloning of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum.

TL;DR: Analysis of predicted secondary structures and hydropathy plots suggests that the two isoforms exhibit the same topology in both transmembrane and cytoplasmic domains, and suggests that a modulator binding domain in the protein lies between residues 2619 and 3016.
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A mutation in the human ryanodine receptor gene associated with central core disease.

TL;DR: A causal relationship between malignant hyperthermia (MH) and central core disease (CCD) has been found in this paper, with a lod score of 48 at a recombinant fraction of 00 in 16 informative meioses in a 130 member family.
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A substitution of cysteine for arginine 614 in the ryanodine receptor is potentially causative of human malignant hyperthermia.

TL;DR: Analysis of 35 human families predisposed to malignant hyperthermia has revealed the presence, and cosegregation with phenotype, of the corresponding substitution in a single family, which may be causal for predisposition to MH in this family.
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Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase.

TL;DR: Mutational analysis of the transmembrane helix, together with the additive regulatory effects of coexpression of both SLN and phospholamban (PLN) with SERCA1, provided evidence for different mechanisms of interaction of SLN