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Arvind Chopra

Researcher at McMaster University

Publications -  7
Citations -  237

Arvind Chopra is an academic researcher from McMaster University. The author has contributed to research in topics: Digitoxigenin & Hamster. The author has an hindex of 6, co-authored 7 publications receiving 225 citations.

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Cellular basis for the species differences in sensitivity to cardiac glycosides (digitalis)

TL;DR: Failure to see any significant differences in cellular toxicity for a larger number of other compounds which either bear limited structural resemblance to cardiac glycosides or interact with the Na+/K+ ATPase in a different manner provides strong evidence that the observed species‐related differences are highly specific for cardiotonic steroids.
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Implications of the noncoding RNAs in rheumatoid arthritis pathogenesis.

TL;DR: This review article attempted to gain a comprehensive understanding of the role of ncRNAs, long nc RNAs, miRN as well as other subtypes in pathogenesis, diagnosis, and treatment of rheumatoid arthritis (RA).
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Genetic and biochemical studies with mutants of mammalian cells affected in microtubule-related proteins other than tubulin: mitochondrial localization of a microtubule-related protein.

TL;DR: In Chinese hamster ovary cells, stable mutants exhibiting specific resistance or collateral sensitivity towards the various microtubule inhibitors podophyllotoxin, colchicine, griseofulvin, taxol, nocodazole, vinblastine, and maytansine have been isolated, mitochondrial localization of the microtubules-related protein P1 provides strong suggestive evidence regarding the existence of a chemical and functional linkage between these two structures.
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Cross-resistance and biochemical studies with two classes of HeLa cell mutants resistant to cardiac glycosides. The unusual behavior of cardenolide SC4453.

TL;DR: The lack of cross-resistance of the group A mutants to SC4453 and normal sensitivity of their Na+/K+-ATPase to this compound provides strong evidence that the mechanism of interaction ofSC4453 with Na+ or K+- ATPase differs from that of other cardiac glycosides.
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Human cell mutants affected in the interaction of the 12β-OH group of cardiac glycosides with the digitalis receptor

TL;DR: It is suggested that the genetic lesion in the group D mutant leads to the creation of a new binding site in the digitalis receptor, which specifically interacts with the 12 beta-OH group and either prevents or distorts the binding of the compounds to the drug binding site on the receptor.