Biography

Dr. Jithesh Kottur

Institute of Advanced Virology, India


Email: [email protected]


Qualifications

2017 Ph.D., Biotechnology, Regional Centre for Biotechnology of Faridabad

2011 M.Sc., Biochemistry, Medical Biochemistry Kannur University

2007 B.Sc., Biochemistry, Botany and Microbiology, University of Mysore


Publications (Selected)

  1. Chen, H., Dutta, R. P., & Li, Z., et al. (2026). Discovery of a potent, selective, and in vivo efficacious covalent inhibitor for lysine methyltransferase SETD8. Journal of Medicinal Chemistry, 69(4), 4255–4269.
  2. Rechkoblit, O., Sciaky, D., & Ni, M., et al. (2025). Mechanism of DNA degradation by CBASS Cap5 endonuclease immune effector. Nature Communications, 16(1), Article 5243.
  3. Quintana-Feliciano, R., Kottur, J., & Ni, M., et al. (2024). Burkholderia cenocepacia epigenetic regulator M.BceJIV simultaneously engages two DNA recognition sequences for methylation. Nature Communications, 15(1), Article 7839.
  4. Karakus, U., Mena, I., & Kottur, J., et al. (2024). H19 influenza A virus exhibits species-specific MHC class II receptor usage. Cell Host & Microbe, 32(7), 1089–1102.
  5. Kottur, J., Malik, R., & Aggarwal, A. K. (2024). Nucleic acid mediated activation of a short prokaryotic Argonaute immune system. Nature Communications, 15(1), Article 4852.
  6. Rechkoblit, O., Sciaky, D., & Kreitler, D. F., et al. (2024). Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides. Nature Structural & Molecular Biology, 31(5), 767–776.
  7. Yu, X., Li, D., & Kottur, J., et al. (2023). Discovery of potent and selective WDR5 proteolysis targeting chimeras as potential therapeutics for pancreatic cancer. Journal of Medicinal Chemistry, 66(23), 16168–16182.
  8. Kottur, J., White, K. M., & Rodriguez, M. L., et al. (2023). Structures of SARS-CoV-2 N7-methyltransferase with DOT1L and PRMT7 inhibitors provide a platform for new antivirals. PLoS Pathogens, 19(7), Article e1011546.
  9. Kottur, J., Rechkoblit, O., & Quintana-Feliciano, R., et al. (2022). High-resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic development. Nature Structural & Molecular Biology, 29(9), 850–853.
  10. Li, D., Yu, X., & Kottur, J., et al. (2022). Discovery of a dual WDR5 and Ikaros PROTAC degrader as an anti-cancer therapeutic. Oncogene, 41(24), 3328–3340.
  11. Yu, X., Li, D., & Kottur, J., et al. (2021). A selective WDR5 degrader inhibits acute myeloid leukemia in patient-derived mouse models. Science Translational Medicine, 13(613), Article eabj1578.
  12. Johnson, M. K., Kottur, J., & Nair, D. T. (2019). A polar filter in DNA polymerases prevents ribonucleotide incorporation. Nucleic Acids Research, 47(20), 10693–10705.
  13. Kottur, J., & Nair, D. T. (2018). Pyrophosphate hydrolysis is an intrinsic and critical step of the DNA synthesis reaction. Nucleic Acids Research, 46(12), 5875–5885.
  14. Kottur, J., & Nair, D. T. (2016). Reactive oxygen species play an important role in the bactericidal activity of quinolone antibiotics. Angewandte Chemie International Edition, 55(7), 2397–2400.
  15. Ghodke, P. P., Gore, K. R., & Harikrishna, S., et al. (2016). The N2-furfuryl-deoxyguanosine adduct does not alter the structure of B-DNA. The Journal of Organic Chemistry, 81(2), 502–511.
  16. Nair, D. T., Kottur, J., & Sharma, R. (2015). A rescue act: Translesion DNA synthesis past N2-deoxyguanosine adducts. IUBMB Life, 67(7), 564–574.
  17. Kottur, J., Sharma, A., & Gore, K. R., et al. (2015). Unique structural features in DNA polymerase IV enable efficient bypass of the N2 adduct induced by the nitrofurazone antibiotic. Structure, 23(1), 56–67.
  18. Sharma, A., Kottur, J., & Narayanan, N., et al. (2013). A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli. Nucleic Acids Research, 41(9), 5104–5114.


Profile Details:

https://iav.res.in/people/dr-jithesh-kottur/
https://scholar.google.com/citations?user=ICHHFD0AAAAJ&hl=en
https://www.researchgate.net/profile/Jithesh-Kottur-2

WOS ResearchID: AAT-4092-2021

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