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* Chakraborty, S., Deshmukh, A., Kesari, P., & Bhaumik, P. (2024). Toxoplasma gondii aspartic protease 5: structural basis of substrate binding and inhibition mechanism. J. Biomol. Struct. Dyn. (In Press)
* Mishra, V., Deshmukh, A., Rathore, I., Chakraborty, S., Patankar, S., Gustchina, A., Wlodawer, A., Yada, R. Y., & Bhaumik, P. (2024). Inhibition of Plasmodium falciparum plasmepsins by drugs targeting HIV-1 protease: A way forward for antimalarial drug discovery. Curr. Res. Struct. Biol., 7, 100128.
* Kesari, P., Deshmukh, A., Pahelkar, N., Suryawanshi, A. B., Rathore, I., Mishra, V., Dupuis, J. H., Xiao, H., Gustchina, A., Abendroth, J., Labaied, M., Yada, R. Y., Wlodawer, A., Edwards, T. E., Lorimer, D. D. & Bhaumik, P. (2022). Structures of plasmepsin X from P. falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme. Protein Sci. 31(4):882-899..
* Parui, A. L., Mishra, V., Dutta, S., Bhaumik, P., & Bose, K. (2022). Inter-subunit crosstalk via PDZ synergistically governs allosteric activation of proapoptotic HtrA2. Structure, 30(9):1307-1320.
* Godsora, B. K. J., Punekar, N. S., & Bhaumik, P. (2021). Molecular insights into the inhibition of glutamate dehydrogenase by the dicarboxylic acid metabolites. Proteins. 90(3):810-823.
* Rathore, I., Mishra, V., & Bhaumik, P. (2021). Advancements in macromolecular crystallography: from past to present. Emerg. Top. Life Sci. 5(1):127-149.
* Rathore, I., Mishra, V., Patel, C., Xiao, H., Gustchina, A., Wlodawer, A., Yada, R.Y., & Bhaumik, P. (2021). Activation mechanism of plasmepsins, pepsin-like aspartic proteases from Plasmodium, follows a unique trans-activation pathway, FEBS J. 288(2):678-698.
* Badgujar, D. C., Anil, A., Green, A. E., Surve, M. V., Madhavan, S., Beckett, A., Prior, I. A., Godsora, B. K., Patil, S. B., More, P. K., Sarkar, S. G., Mitchell, A., Banerjee, R., Phale, P. S., Mitchell, T. J., Neill, D. R., Bhaumik, P., & Banerjee, A. (2020). Structural insights into loss of function of a pore forming toxin and its role in pneumococcal adaptation to an intracellular lifestyle. PLOS Pathogens. 16(11):e1009016
* Yarramala, D. S., Prakash, P., Ranade, D. S., Doshi, S, Kulkarni, P. P., Bhaumik P., & Rao, C. P. (2019). Cytotoxicity of apo bovine α-lactalbumin complexed with La3+ on cancer cells supported by its high resolution crystal structure. Sci Rep. 9, 1780.
* Pandey, S.; Phale, P. S. & Bhaumik, P. (2018). Structural modulation of a periplasmic sugar-binding protein probes into its evolutionary ancestry. J. Struct. Biol. 204(3):498-506
* Mishra, V., Rathore, I., Arekar, A., Sthanam, L. K., Xiao, H., Kiso, Y., Sen, S., Patankar, S., Gustchina, A., Hidaka. K., Wlodawer, A., Yada, R. Y., & Bhaumik, P. (2018). Deciphering the mechanism of potent peptidomimetic inhibitors targeting Plasmepsins - Biochemical and structural insights. FEBS J. 285, 3077-3096.
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* Wangchuk, J., Prakash, P., Bhaumik, P. & Kondabagil, K. (2018). Bacteriophage N4 large terminase: expression, purification and X-ray crystallographic analysis. Acta Cryst. F74, 198-204.
* Rane, J. S., Bhaumik, P. & Panda, D. (2017). Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro. J Alzheimers Dis. 60(3), 999-1014.
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* Jaafar, A. H., Xiao, H,, Dee, D. R., Bryksa, B. C., Bhaumik, P., Yada, R. Y. (2016). The prosegment catalyzes native folding of Plasmodium falciparum plasmepsin II. Biochim. Biophys. Acta. 1864, 1356-1362.
* Pandey, S., Modak, A., Phale, P. S. & Bhaumik, P. (2016). High Resolution Structures of Periplasmic Glucose-binding Protein of Pseudomonas putida CSV86 Reveal Structural Basis of Its Substrate Specificity. J. Biol. Chem. 291, 7844-7857.
* Prakash, P., Walvekar, A. S., Punekar, N. S. & Bhaumik, P. (2014). Purification, crystallization and preliminary X-ray diffraction analysis of NADP-dependent glutamate dehydrogenase from Aspergillus niger. Acta Crystallogr. F 70, 1508-1512.
* Modak, A., Bhaumik, P. & Phale, P. S. (2014). Periplasmic glucose-binding protein from Pseudomonas putida CSV86--identification of the glucose-binding pocket by homology-model-guided site-specific mutagenesis. FEBS J. 281(1), 365-375.
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