Prof. Dr. Timir Tripathi
North Eastern Hill University, Shillong, Meghālaya, International
Understanding the nature of proteins at the molecular, struc...
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Academic Career Length
20Years (2007-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications1 February 2021 in Acta Tropica
Journal Article
SMSanjay Kumar Mishra
Sanjay Kumar Mishra
Timir Tripathi1 August 2020 in Microbial Pathogenesis
Journal Article
PKParismita Kalita
Parismita KalitaAPAditya Padhi
Aditya PadhiKZKam Y. J. Zhang
Kam Y. J. ZhangTimir Tripathi1 May 2018 in International Journal of Biological Macromolecules
Journal Article
VRVijayakumar Rajendran
Vijayakumar RajendranPKParismita Kalita
Parismita KalitaHSHarish Shukla
Harish Shukla
Awanish KumarTimir Tripathi10 April 2016 in Advances in Bioinformatics
Journal Article
CNChaluveelaveedu Murleedharan Nisha
Chaluveelaveedu Murleedharan Nisha
Ashwini KumarPNPrateek Nair
Prateek Nair
NGNityasha Gupta
Nityasha Gupta
CSChitrangda Silakari
Chitrangda Silakari
Awanish Kumar +1
Amyloidogenic pathway in Alzheimer’s disease (AD) involves breakdown of APP by β-secretase followed by γ-secretase and results in formation of amyloid beta plaque. β-secretase has been a promising target for developing novel anti-Alzheimer drugs. To test different molecules for this purpose, test ligands like acylguanidine 7a, rosiglitazone, pioglitazone, and tartaric acid were docked against our target protein β-secretase enzyme retrieved from Protein Data Bank, considering MK-8931 (phase III trial, Merck) as the positive control. Docking revealed that, with respect to their free binding energy, acylguanidine 7a has the lowest binding energy followed by MK-8931 and pioglitazone and binds significantly to β-secretase. In silico ADMET predictions revealed that except tartaric acid all other compounds had minimal toxic effects and had good absorption as well as solubility characteristics. These compounds may serve as potential lead compound for developing new anti-Alzheimer drug.
1 January 2016 in Journal of the Formosan Medical Association
Journal Article
Ashwini KumarCNChaluveelaveedu Murleedharan Nisha
Chaluveelaveedu Murleedharan Nisha
CSChitrangda Silakari
Chitrangda Silakari
ISIsha Sharma
Isha Sharma
KAKanukanti Anusha
Kanukanti Anusha
Awanish Kumar +3
Alzheimer's disease (AD) is a neurodegenerative disorder in which the death of brain cells causes memory loss and cognitive decline, i.e., dementia. The disease starts with mild symptoms and gradually becomes severe. AD is one of the leading causes of mortality worldwide. Several different hallmarks of the disease have been reported such as deposits of β-amyloid around neurons, hyperphosphorylated tau protein, oxidative stress, dyshomeostasis of bio-metals, low levels of acetylcholine, etc. AD is not simple to diagnose since there is no single diagnostic test for it. Pharmacotherapy for AD currently provides only symptomatic relief and mostly targets cognitive revival. Computational biology approaches have proved to be reliable tools for the selection of novel targets and therapeutic ligands. Molecular docking is a key tool in computer-assisted drug design and development. Docking has been utilized to perform virtual screening on large libraries of compounds, and propose structural hypotheses of how the ligands bind with the target with lead optimization. Another potential application of docking is optimization stages of the drug-discovery cycle. This review summarizes the known drug targets of AD, in vivo active agents against AD, state-of-the-art docking studies done in AD, and future prospects of the docking with particular emphasis on AD.
Journal Article
SSSushma Subedi
Sushma Subedi
Santanu Sasidharan
Niharika Nag
Prakash SaudagarTimir TripathiMost neurodegenerative diseases such as Alzheimer’s disease, type 2 diabetes, Parkinson’s disease, etc. are caused by inclusions and plaques containing misfolded protein aggregates. These protein aggregates are essentially formed by the interactions of either the same (homologous) or different (heterologous) sequences. Several experimental pieces of evidence have revealed the presence of cross-seeding in amyloid proteins, which results in a multicomponent assembly; however, the molecular and structural details remain less explored. Here, we discuss the amyloid proteins and the cross-seeding phenomena in detail. Data suggest that targeting the common epitope of the interacting amyloid proteins may be a better therapeutic option than targeting only one species. We also examine the dual inhibitors that target the amyloid proteins participating in the cross-seeding events. The future scopes and major challenges in understanding the mechanism and developing therapeutics are also considered. Detailed knowledge of the amyloid cross-seeding will stimulate further research in the practical aspects and better designing anti-amyloid therapeutics.
About Me
Timir Tripathi is a professor of Molecular Biology in the Department of Zoology, North-Eastern Hill University, Shillong, India. He holds a Ph.D. from Jawaharlal Nehru University, New Delhi. His research focuses on protein–substrate interactions, conformational dynamics, and understanding the roles of non-catalytic domains in regulating the catalytic activity of proteins. His primary focus is studying the structural and functional characteristics of drug target proteins from Fasciola gigantica to develop novel therapeutic strategies. He has received several awards, such as the NASI-Prof. B.K. Bachhawat Memorial Young Scientist Lecture Award (2020), the ISCB-Young Scientist Award (2019), and the ICMR-Shakuntala Amir Chand Prize (2018). He is an Associate Fellow of the Indian National Science Academy and a member of the National Academy of Sciences India, the Royal Society of Chemistry, and the Royal Society of Biology (UK). He has secured several research grants from national and international funding agencies. He has authored over 150 publications, including research papers, reviews, and editorial articles in leading international journals. He has edited six books and authored two textbooks. Currently, he is the Senior Editor for Critical Insights in Biophysics (T&F), Editor of the International Journal of Biological Macromolecules (Elsevier), Associate Editor of PLOS Neglected Tropical Diseases, and is a member of editorial boards of several esteemed international journals.
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