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Bhupendra P. Doctor
Researcher at Walter Reed Army Institute of Research
Publications - 218
Citations - 6765
Bhupendra P. Doctor is an academic researcher from Walter Reed Army Institute of Research. The author has contributed to research in topics: Acetylcholinesterase & Butyrylcholinesterase. The author has an hindex of 45, co-authored 218 publications receiving 6574 citations. Previous affiliations of Bhupendra P. Doctor include Israel Institute for Biological Research & United States Department of the Army.
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Journal ArticleDOI
Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
Miroslaw Cygler,Joseph D. Schrag,Joel L. Sussman,Michal Harel,Israel Silman,Mary K. Gentry,Bhupendra P. Doctor +6 more
TL;DR: An improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained, and 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved.
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Stable Complexes Involving Acetylcholinesterase and Amyloid-β Peptide Change the Biochemical Properties of the Enzyme and Increase the Neurotoxicity of Alzheimer’s Fibrils
Alejandra R. Alvarez,Rodrigo Alarcón,Carlos Opazo,Eliseo O. Campos,Francisco J. Muñoz,Frances Calderon,Federico Dajas,Mary K. Gentry,Bhupendra P. Doctor,Fernando G. de Mello,Nibaldo C. Inestrosa +10 more
TL;DR: Brain acetylcholinesterase, by forming stable complexes with amyloid-β peptide during its assembly into filaments, may increase the neurotoxicity of Aβ fibrils and thus determine the selective neuronal loss observed in Alzheimer’s brain.
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Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase
TL;DR: Volume calculations for the active site gorge showed that the poor inhibitory activity of ethopropazine toward acetylcholinesterase was due to the smaller dimension of the active sites gorge which was unable to accommodate the bulky inhibitor molecule.
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Bioscavengers for the protection of humans against organophosphate toxicity.
TL;DR: Plasma derived HuBChE is judged to be the most suitable bioscavenger for its advancement for human use and is being developed at the present time for conducting a safety clinical trial in human volunteers.
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Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon.
TL;DR: The increased rate obtained with the double mutant displaying characteristics of the B cholinesterase active center provides a rationale for higher efficacy of CPO scavenging by BChE, compared with AChE.