| 1. |
Subedi, S.; Shukla, H.; Uversky, V. N.; Tripathi, T. Physical Principles and Molecular Interactions Underlying Protein Phase Separation. The Three Functional States of Proteins, 2025, 197–212 |
2025 |
| 2. |
Nag, N.; Shukla, H.; Uversky, V. N.; Tripathi, T. Targeting Phase-Separated Protein States for Drug Discovery. The Three Functional States of Proteins, 2025, 255–273. |
2025 |
| 3. |
Nag, N., Shukla, H., Padhi, A. K., & Tripathi, T. (2023). Comprehensive analysis of liquid-liquid phase separation propensities of HSV‐1 proteins and their interaction with host factors. Journal of Cellular Biochemistry. |
2023 |
| 4. |
Shukla, R., Shukla, H., & Tripathi, T. (2021). Structure-based discovery of phenyl-diketo acids derivatives as Mycobacterium tuberculosis malate synthase inhibitors. Journal of Biomolecular Structure and Dynamics, 39(8), 2945-2958. |
2021 |
| 5. |
Tripathi, T., Ghosh, A., Todur, V. N., Kalita, P., Rajendran, V., Kalita, J., Shukla, R., Chetri, P. B., Shukla, H., Sonkar, A., Lyngdoh, D. L., Singh, R., Chikara, S. K., & Tripathi, T. (2020). Draft genome of the liver fluke Fasciola gigantica. ACS Omega, 5(19), 11084-11091. |
2020 |
| 6. |
Yadav, S., Prakash, J., Shukla, H., Das, K. C., Tripathi, T., & Dubey, V. K. (2020). Design of a multi-epitope subunit vaccine for immune protection against the Leishmania parasite. Pathogens and Global Health, 114(8), 471-481. |
2020 |
| 7. |
Kalita, P., Das, K. C., Shukla, H., & Tripathi, T. (2019). Conserved Arg451 residue is critical for maintaining the stability and activity of thioredoxin glutathione reductase. Archives of Biochemistry and Biophysics. https://doi.org/10.1016/j.abb.2019.108098 |
2019 |
| 8. |
Gupta, S., Shukla, H., Kumar, A., Shukla, R., Kumari, R., Tripathi, T., Singh, R. K., & Anupurba, S. (2019). Mycobacterium tuberculosis nucleoside diphosphate kinase shows interaction with putative ATP binding cassette (ABC) transporter, Rv1273c. Journal of Biomolecular Structure and Dynamics, 1-11. https://doi.org/10.1080/07391102.2019.1595150 |
2019 |
| 9. |
Lyngdoh, D. L., Shukla, H., Sonkar, A., Anupam, R., & Tripathi, T. (2019). Portrait of the Intrinsically Disordered Side of the HTLV-1 Proteome. ACS Omega, 4(6), 10003-10018. |
2019 |
| 10. |
Kalita, P., Lyngdoh, D. L., Padhi, A. K., Shukla, H., & Tripathi, T. (2019). Development of multi-epitope driven subunit vaccine against Fasciola gigantica using immunoinformatics approach. International Journal of Biological Macromolecules. https://doi.org/10.1016/j.ijbiomac.2019.07.024 |
2019 |
| 11. |
Sonkar, A., Shukla, H., Shukla, R., Kalita, J., & Tripathi, T. (2019). Unfolding of Acinetobacter baumannii MurA proceeds through a metastable intermediate: A combined spectroscopic and structure computational investigation. International Journal of Biological Macromolecules, 126, 941-951. |
2019 |
| 12. |
Vijayakumar, R., Shukla, R., Shukla, H., & Tripathi, T. (2018). Structure-function studies of the asparaginyl tRNA synthetase from Fasciola gigantica: Understanding the role of catalytic and non-catalytic domains. Biochemical Journal, 475(21), 3377-3391. |
2018 |
| 13. |
Sonkar, A., Lyngdoh, D., Shukla, R., Shukla, H., Tripathi, T., & Ahmed, S. (2018). Point mutation A394E in the central intrinsic disordered region of Rna14 leads to chromosomal instability in fission yeast. International Journal of Biological Macromolecules, 119, 785-791. |
2018 |
| 14. |
Kalita, P., Shukla, H., Shukla, R., & Tripathi, T. (2018). Biochemical and thermodynamic comparison of the selenocysteine containing and non-containing thioredoxin glutathione reductase of Fasciola gigantica. Biochimica et Biophysica Acta (BBA) - General Subjects, 1862(6), 1306-1316. |
2018 |
| 15. |
Rajendran, V., Kalita, P., Shukla, H., Kumar, A., & Tripathi, T. (2018). Aminoacyl-tRNA synthetases: Structure, function, and drug discovery. International Journal of Biological Macromolecules, 111, 400-414. |
2018 |
| 16. |
Tripathi, T., Ghosh, A., Todur, V. N., Kalita, P., Rajendran, V., Kalita, J., Shukla, R., Chetri, P. B., Shukla, H., Sonkar, A., Lyngdoh, D. L., Singh, R., Chikara, S. K., & Tripathi, T. (2018). Draft genome of the liver fluke Fasciola gigantica. bioRxiv. https://doi.org/10.1101/451476 |
2018 |
| 17. |
Shukla, H., Khan, S. R., Shukla, R., Krishnan, M. Y., Akhtar, M. S., & Tripathi, T. (2018). Alternate pathway to ascorbate induced inhibition of Mycobacterium tuberculosis. Tuberculosis, 111, 161-169. |
2018 |
| 18. |
Shukla, H., Khan, S. R., Shukla, R., Krishnan, M. Y., Akhtar, M. S., & Tripathi, T. (2018). Alternate pathway to ascorbate induced inhibition of Mycobacterium tuberculosis. Tuberculosis, 111, 161-169. |
2018 |
| 19. |
19. Shukla, R., Shukla, H., & Tripathi, T. (2018). Activity loss by H46 mutation in Mycobacterium tuberculosis isocitrate lyase is due to decrease in structural plasticity and collective motions of the active site. Tuberculosis, 108, 143-150. |
2018 |
| 20. |
20. Shukla, R., Shukla, H., Sonkar, A., Pandey, T., & Tripathi, T. (2018). Structure-based screening and molecular dynamics simulations offer novel natural compounds as potential inhibitors of Mycobacterium tuberculosis isocitrate lyase. Journal of Biomolecular Structure and Dynamics, 36(8), 2045-2057. |
2018 |
| 21. |
Shukla, R., Shukla, H., Kalita, P., & Tripathi, T. (2018). Structural insights into natural compounds as inhibitors of Fasciola gigantica thioredoxin glutathione reductase. Journal of Cellular Biochemistry, 119, 3067-3080. |
2018 |
| 22. |
Shukla, R., Shukla, H., Kalita, P., Sonkar, A., Pandey, T., Singh, D. B., Kumar, A., & Tripathi, T. (2018). Identification of potential inhibitors of Fasciola gigantica thioredoxin1: Computational screening, molecular dynamics simulation and binding free energy studies. Journal of Biomolecular Structure and Dynamics, 36(8), 2147-2162. |
2018 |
| 23. |
Shukla, R., Shukla, H., & Tripathi, T. (2018). Structural and energetic understanding of novel natural inhibitors of Mycobacterium tuberculosis malate synthase. Journal of Cellular Biochemistry, 120(2), 2469-2482. |
2018 |
| 24. |
Shukla, H., & Tripathi, T. (2018). Studying parasite gene function and interaction through ribozymes and riboswitches design mechanism. In S. Singh (Ed.), Synthetic Biology: Omics tools and their applications (pp. 51-74). Springer Singapore. |
2018 |
| 25. |
Kalita, J., Shukla, R., Shukla, H., Gadhave, K., Giri, R., & Tripathi, T. (2017). Comprehensive analysis of the catalytic and structural properties of a mu-class glutathione s-transferase from Fasciola gigantica. Scientific Reports, 7, 17547. |
2017 |
| 26. |
Pandey, T., Shukla, R., Shukla, H., Sonkar, A., Tripathi, T., & Singh, A. K. (2017). A combined biochemical and computational studies of the rho-class glutathione s-transferase sll1545 of Synechocystis PCC 6803. International Journal of Biological Macromolecules, 94, 378-385. |
2017 |
| 27. |
Singh, A. K., Rastogi, S., Shukla, H., Asalam, M., Rath, S. K., & Akhtar, M. S. (2017). Cdc15 Phosphorylates the C-terminal Domain of RNA Polymerase II for Transcription during Mitosis. Journal of Biological Chemistry, 292(13), 5507-5518. |
2017 |
| 28. |
Shukla, H., Shukla, R., Sonkar, A., & Tripathi, T. (2017). Alterations in conformational topology and interaction dynamics caused by L418A mutation leads to activity loss of Mycobacterium tuberculosis isocitrate lyase. Biochemical and Biophysical Research Communications, 490(2), 276-282. |
2017 |
| 29. |
Shukla, H., Kumar, R., Sonkar, A., Mitra, K., Akhtar, M. S., & Tripathi, T. (2017). Salt-regulated reversible fibrillation of Mycobacterium tuberculosis isocitrate lyase: Concurrent restoration of structure and activity. International Journal of Biological Macromolecules, 104, 89-96. |
2017 |
| 30. |
Shukla, H., Shukla, R., Sonkar, A., Pandey, T., & Tripathi, T. (2017). Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility. Scientific Reports, 7, 1058. https://doi.org/10.1038/s41598-017-01235-z |
2017 |
| 31. |
Sonkar, A., Shukla, H., Shukla, R., Kalita, J., Pandey, T., & Tripathi, T. (2017). UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) of Acinetobacter baumannii (AbMurA): Structural and functional properties. International Journal of Biological Macromolecules, 97, 106-114. |
2017 |
| 32. |
Shukla, H., Kumar, V., Singh, A. K., Rastogi, S., Khan, S. R., Siddiqi, M. I., Krishnan, M. Y., & Akhtar, M. S. (2015). Isocitrate lyase of Mycobacterium tuberculosis is inhibited by quercetin through binding at N-terminus. International Journal of Biological Macromolecules, 78, 137-141. |
2015 |
| 33. |
33. Shukla, H., Kumar, V., Singh, A. K., Singh, N., Kashif, M., Siddiqi, M. I., Krishnan, M. Y., & Akhtar, M. S. (2015). Insight into the structural flexibility and function of Mycobacterium tuberculosis Isocitrate Lyase. Biochimie, 110, 73-80. |
2015 |
| 34. |
Shukla, H., Singh, S. K., Singh, A. K., Mitra, K., & Akhtar, M. S. (2015). The C-terminus hot spot region helps in the fibril formation of bacteriophage-associated Hyaluronate Lyase (HylP2). Scientific Reports, 5, 1442. |
2015 |
| 35. |
Kalita, P., Shukla, H., Gadhave, K., Giri, R., & Tripathi, T. (2018). Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase. Archives of Biochemistry and Biophysics, 656, 38-45. |
2013 |
| 36. |
Gautam, A., Shukla, H., Khan, S., Rishi, P., & Bhakuni, V. (2010). Structural and functional features of UDP-N-acetylenolpyruvylglucosamine reductase of Mycobacterium tuberculosis H37Rv. International Journal of Integrative Biology. |
2010 |