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Govindasamy Mugesh

Researcher at Indian Institute of Science

Publications -  181
Citations -  9826

Govindasamy Mugesh is an academic researcher from Indian Institute of Science. The author has contributed to research in topics: Glutathione peroxidase & Iodothyronine deiodinase. The author has an hindex of 46, co-authored 173 publications receiving 8278 citations. Previous affiliations of Govindasamy Mugesh include Indian Institutes of Technology & University of Washington.

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Remarkable Effect of Chalcogen Substitution on an Enzyme Mimetic for Deiodination of Thyroid Hormones

TL;DR: The tellurium compounds reported in this paper represent the first examples of deiodinase mimetics which mediate sequential deiodination of T4 to produce all the hormone derivatives including T0 under physiologically relevant conditions.
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Protein Folding in the Presence of Water‐Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities

TL;DR: It is reported that water‐soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfides bonds in misfolded proteins.
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Regioselective Deiodination of Iodothyronamines, Endogenous Thyroid Hormone Derivatives, by Deiodinase Mimics

TL;DR: Kinetic studies and single-crystal X-ray structures of T3 and T3 AM reveal that intermolecular I⋅ⓂⓁ⓽I interactions may play an important role in deiodination, and detailed experimental and theoretical investigations suggest that T3 AM forms a weaker halogen bond with selenium donors than T3.
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Modeling Thioredoxin Reductase-Like Activity with Cyclic Selenenyl Sulfides: Participation of an NH⋅⋅⋅Se Hydrogen Bond through Stabilization of the Mixed Se-S Intermediate.

TL;DR: The selenenyl sulfides exhibited a defensive ability against H2 O2 -induced oxidative stress in cultured cells, which suggests the possibility for medicinal applications to control the redox balance in cells.
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Antioxidant activity of peptide-based angiotensin converting enzyme inhibitors

TL;DR: The presence of an L-Pro moiety in captopril analogues appears to be important for ACE inhibition as the replacement of L- pro by L-piperidine 2-carboxylic acid decreases the ACE inhibition.