Dr. Nitu Radheshyam Singh, Ph.D.

Senior Scientist
Pharmacology & Drug Discovery Division
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Research Focus

Our lab aims to decode and rewire early molecular dysfunctions in neurodegenerative diseases, with a particular focus on the selective vulnerability of neurons. We study how disruptions in intracellular organization, axonal trafficking, and protein homeostasis contribute to disease initiation and progression. Our goal is to identify targetable signaling nodes and develop pharmacological strategies for both therapeutic intervention and early-stage diagnostics. We adopt a chemical biology-driven approach, integrating activity-based probes, quantitative mass spectrometry, high-resolution imaging, and preclinical evaluations to dissect and modulate disease-relevant protein networks.

Research Interest

  • Investigating how axonal transport defects contribute to neurodegeneration in Parkinson’s and Alzheimer’s disease, and evaluating pharmacological strategies to restore neuronal function
  • Evaluating the mechanism of drug action and treatment response in preclinical models 
  • Exploring the role of biomolecular condensates at synapses and how their composition and organization are altered under disease conditions
  • Applying proximity labeling and mass spectrometry to map dynamic protein interaction networks and post-translational modifications
  • Using quantitative proteomics to identify early molecular signatures and develop diagnostic biomarkers

Credentials

  • Senior Scientist (2025-present) CSIR-Indian Institute of Chemical Biology, Kolkata 
  • DST INSPIRE Faculty (2024-2025) Regional Centre for Biotechnology, Faridabad
  • MK Bhan Young Research Fellow (2021-2024) Regional Centre for Biotechnology, Faridabad
  • DBT-Research Associate (2020-2021) Regional Centre for Biotechnology, Faridabad
  • National Postdoctoral Fellow (2017-2019) Indian Institute of Technology Bombay, Mumbai
  • PhD (2015) Advanced Centre for Treatment, Research and Education in Cancer, Navi-Mumbai

Patents & Publications

Research Articles:

  1. Srivastava M, Kumari D, Majumder S, Singh N, Mathur R, Maiti TK, Kumar A, Asthana S. Rational Computational Workflow for Structure-Guided Discovery of a Novel USP7 Inhibitor. J Chem Inf Model. 2025 May 12; 65(9):4468-4487. doi: 10.1021/acs.jcim.4c01400. 
  2. Gaur KK*, Asuru TR*, Srivastava M, Singh N, Purushotham N, Poojary B, Das B, Bhattacharyya S, Asthana S, Guchhait P. 7D, a small molecule inhibits dengue infection by increasing interferons and neutralizing-antibodies via CXCL4: CXCR3: p38: IRF3 and Sirt1: STAT3 axes respectively. EMBO Mol Med. 2024 Oct; 16(10):2376-2401. doi: 10.1038/s44321-024-00137-8. 
  3. Mehra S, Ahlawat S, Kumar H, Datta D, Navalkar A, Singh N, Patel K, Gadhe L, Kadu P, Kumar R, Jha NN, Sakunthala A, Sawner AS, Padinhateeri R, Udgaonkar JB, Agarwal V, Maji SK. α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties. J Mol Biol. 2022 Oct 15; 434(19):167761. doi: 10.1016/j.jmb.2022.167761. 
  4. Parui AL*, Singh N*, Dutta S, Bose K. Role of conserved regulatory loop residues in allosteric propagation of serine protease HtrA2. Biochem Biophys Res Commun. 2022 Feb 26;594:63-68. doi: 10.1016/j.bbrc.2022.01.042. (*Co-first author)
  5. Ray S*, Singh N*, Kumar R, Patel K, Pandey S, Datta D, Mahato J, Panigrahi R, Navalkar A, Mehra S, Gadhe L, Chatterjee D, Sawner AS, Maiti S, Bhatia S, Gerez JA, Chowdhury A, Kumar A, Padinhateeri R, Riek R, Krishnamoorthy G, Maji SK. α-Synuclein aggregation nucleates through liquid-liquid phase separation. Nat Chem. 2020 Aug; 12(8):705-716. doi: 10.1038/s41557-020-0465-9. (*Co-first author) 
  6. Mehra S, Ghosh D, Kumar R, Mondal M, Gadhe LG, Das S, Anoop A, Jha NN, Jacob RS, Chatterjee D, Ray S, Singh N, Kumar A, Maji SK. Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils. J Biol Chem. 2018 Aug 24; 293(34):12975-12991. doi: 10.1074/jbc.RA118.004267. 
  7. Mohite GM, Kumar R, Panigrahi R, Navalkar A, Singh N, Datta D, Mehra S, Ray S, Gadhe LG, Das S, Singh N, Chatterjee D, Kumar A, Maji SK. Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation. Biochemistry. 2018 Sep 4; 57(35):5183-5187. doi: 10.1021/acs.biochem.8b00314. 
  8. Singh N, Senapati S, Bose K. Insights into the mechanism of human papillomavirus E2-induced procaspase-8 activation and cell death. Sci Rep. 2016 Feb 24; 6:21408. doi: 10.1038/srep21408. 
  9. Singh N, Hassan A, Bose K. Molecular basis of death effector domain chain assembly and its role in caspase-8 activation. FASEB J. 2016 Jan;30(1):186-200. doi: 10.1096/fj.15-272997. Epub 2015 Sep 14. 
  10. Singh N, Kanthaje S, Bose K. Equilibrium dissociation and unfolding of human papillomavirus E2 transactivation domain. Biochem Biophys Res Commun. 2015 Aug 7; 463(4):496-503. doi: 10.1016/j.bbrc.2015.05.057. 
  11. Singh N, D'Souza A, Cholleti A, Sastry GM, Bose K. Dual regulatory switch confers tighter control on HtrA2 proteolytic activity. FEBS J. 2014 May; 281(10):2456-70. doi: 10.1111/febs.12799. 
  12. Bejugam PR, Kuppili RR, Singh N, Gadewal N, Chaganti LK, Sastry GM, Bose K. Allosteric regulation of serine protease HtrA2 through novel non-canonical substrate binding pocket. PLoS One. 2013; 8(2):e55416. doi: 10.1371/journal.pone.0055416. 

 

Review:

  1. Singh N, Malik S, Gupta A, Srivastava KR. Revolutionizing enzyme engineering through artificial intelligence and machine learning. Emerg Top Life Sci. 2021 May 14;5(1):113-125. doi: 10.1042/ETLS20200257.
  2. Singh N, Kuppili RR, Bose K. The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases. Arch Biochem Biophys. 2011 Dec 15; 516(2):85-96. doi: 10.1016/j.abb.2011.10.007. 

 

Book Chapters:

  1. Ray S, Singh N, Patel K, G. Krishnamoorthy, and Maji SK. (2023) FRAP & FRET investigation of α-synuclein fibrillization via liquid-liquid phase separation in vitro and in HeLa cells. Methods Molecular Biology, Protein Aggregation, Springer Nature Switzerland. ISBN 978-1-0716-2596-5, 490785_1_En, (Chapter 26)
  2. Singh N and Bose K. (2022) Introduction to Recombinant Protein Purification. Springer Nature Singapore. 115-140. doi.10.1007/978-981-16-4987-5 
  3. Singh N and Bose K. (2015) Apoptosis: Pathways, Molecules and Beyond. Springer International Publishing, Switzerland. 1-30. ISBN978-3-319-19496-7
  4. Chaganti L, Singh N and Bose K. (2015) Cathepsins and HtrAs - multitasking proteases in programmed cell death. Springer International Publishing, Switzerland, 95-141 ISBN978-3- 319-19496-7 
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