B
Bhupesh Goyal
Researcher at Thapar University
Publications - 38
Citations - 929
Bhupesh Goyal is an academic researcher from Thapar University. The author has contributed to research in topics: Protein folding & Protein structure. The author has an hindex of 14, co-authored 38 publications receiving 623 citations. Previous affiliations of Bhupesh Goyal include Sri Guru Granth Sahib World University & Indian Institute of Technology Bombay.
Papers
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Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy.
Bhupesh Goyal,Deepti Goyal +1 more
TL;DR: The literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV Mpro on its dimerization and, thus, catalytic activity are compiled to stimulate research in this less explored yet quite significant area.
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Rationally Designed Peptides and Peptidomimetics as Inhibitors of Amyloid-β (Aβ) Aggregation: Potential Therapeutics of Alzheimer’s Disease
TL;DR: Peptide-based aggregation inhibitors hold significant promise for future AD therapy owing to their high selectivity, effectiveness, low toxicity, good tolerance, low accumulation in tissues, high chemical and biological diversity, possibility of rational design, and highly developed methods for analyzing their mode of action.
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Benzofuran and Indole: Promising Scaffolds for Drug Development in Alzheimer's Disease.
TL;DR: The history and recent advances of benzofuran‐ and indole‐based compounds as inhibitors of butyrylcholinesterase, acetylcholinerase, γ‐secretase, β‐ secretase, tau misfolding, and β‐amyloid aggregation are focused on.
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Multi-target-directed triazole derivatives as promising agents for the treatment of Alzheimer’s disease
Anupamjeet Kaur,Sukhmani Mann,Amandeep Kaur,Nitesh Priyadarshi,Bhupesh Goyal,Nitin Kumar Singhal,Deepti Goyal +6 more
TL;DR: A novel triazole-based compound, 6n, does not display cytotoxicity and was able to inhibit toxicity induced by Aβ42 aggregates in SH-SY5Y cells and is highlighted as a promising MTDL against AD.
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Scrutiny of the mechanism of small molecule inhibitor preventing conformational transition of amyloid-β42 monomer: insights from molecular dynamics simulations.
Suniba Shuaib,Bhupesh Goyal +1 more
TL;DR: Comp comparable molecular dynamics simulations were performed to elucidate the inhibitory mechanism of a sulfonamide inhibitor C1, revealing that C1 inhibits Aβ42 aggregation by stabilizing native helical conformation and inhibiting the formation of aggregation-prone β-sheet conformation.