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Sheril Daniel

Researcher at Rhodes University

Publications -  6
Citations -  372

Sheril Daniel is an academic researcher from Rhodes University. The author has contributed to research in topics: Heat shock protein & Lipid peroxidation. The author has an hindex of 5, co-authored 6 publications receiving 344 citations.

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Through metal binding, curcumin protects against lead- and cadmium-induced lipid peroxidation in rat brain homogenates and against lead-induced tissue damage in rat brain.

TL;DR: The results of the study show that there is an interaction between curcumin and both cadmium and lead, with the possible formation of a complex between the metal and this ligand, implying that curcuming could be used therapeutically to chelate these toxic metals, thus potentially reducing their neurotoxicity and tissue damage.
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Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding

TL;DR: Results showed for the first time that the subcellular localization of Hop was stress regulated and that the major arm of the putative NLS was not directly important for nuclear translocation but was critical for Hop-Hsp90 association in vitro.
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Acetylcholine reduces cyanide-induced superoxide anion generation and lipid peroxidation in rat brain homogenates.

TL;DR: The ability of Ach to scavenge free radicals using the nitroblue tetrazolium (NBT) assay and its ability to inhibit KCN-induced lipid peroxidation in rat brain homogenates are determined and show that Ach appears to have neuroprotective properties.
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Stress Protein Responses in South African Freshwater Invertebrates Exposed to Detergent Surfactant Linear Alkylbenzene Sulfonate (LAS)

TL;DR: Investigation of stress protein induction as a sub-organism level stress response in two South African freshwater aquatic macroinvertebrates exposed to detergent linear alkylbenzene sulfonate found no protein induction was observed in exposed B. stenochorias and C. nilotica.
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The TPR2B domain of the Hsp70/Hsp90 organizing protein (Hop) may contribute towards its dimerization.

TL;DR: It is shown for the first time that the TPR1 and TPR2B domains of Hop independently dimerized, and that the dimerization of T PR2B was not dependent on its predicted two-carboxylate clamp residues.