D
Deepak Sharma
Researcher at Jawaharlal Nehru University
Publications - 234
Citations - 8472
Deepak Sharma is an academic researcher from Jawaharlal Nehru University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 46, co-authored 148 publications receiving 7484 citations. Previous affiliations of Deepak Sharma include Dr. Shakuntala Misra National Rehabilitation University & Mayo Clinic.
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Age-related decline in multiple unit action potentials of ca3 region of rat hippocampus: Correlation with lipid peroxidation and lipofuscin concentration and the effect of centrophenoxine
TL;DR: Changes in lipid peroxidation, lipofuscin concentration, and multiple unit activity in the CA3 region were studied in the hippocampus of male Wistar rats aged 4, 8, 16, and 24 months to suggest that age-related increase in lipidperoxidation may contribute to an age-associated decline in neuronal electrical activity.
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Antiepileptic effect of fisetin in iron-induced experimental model of traumatic epilepsy in rats in the light of electrophysiological, biochemical, and behavioral observations.
TL;DR: This study demonstrated the antiepileptic action of fisetin in iron-induced model of epileptic rats by inhibiting oxidative stress.
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Configurational entropy modulates the mechanical stability of protein GB1.
TL;DR: In this paper, the role of configurational entropy in the mechanical unfolding kinetics and mechanical stability of proteins was examined. But the authors focused on the structural deformation of the loop regions in mechanical unfolding transition state.
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Stabilization Provided by Neighboring Strands Is Critical for the Mechanical Stability of Proteins
TL;DR: It is shown that Top7 and barstar, which have similar topology in their force-bearing region, exhibit vastly different mechanical-stability characteristics, and this previously overlooked stabilization effect from neighboring beta-strands is likely to be a general mechanism in protein mechanics.
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Cytoplasmic Domain of Human Myelin Protein Zero Likely Folded as β-Structure in Compact Myelin
XiaoYang Luo,Deepak Sharma,Hideyo Inouye,Daniel Lee,Robin L. Avila,Mario Salmona,Daniel A. Kirschner +6 more
TL;DR: It is proposed that when hP0-cyt is bound at sufficient concentration to lamellar lipid bilayers such as myelin, it folds into a beta-conformation; before this threshold lipid/protein ratio is reached, the domain is alpha-helical.