[1] Nandi, S. K., Panda, A. K., Chakraborty, A., Rathee, S., Roy, I., Barik, S., Mohapatra, S. S., and Biswas, A. (2022) Role of ATP-Small Heat Shock Protein Interaction in Human Diseases, Front Mol Biosci 9, 844826.

[2] Nandi, S. K., Singh, D., Upadhay, J., Gupta, N., Dhiman, N., Mittal, S. K., and Mahindroo, N. (2021) Identification of tear-based protein and non-protein biomarkers: Its application in diagnosis of human diseases using biosensors, Int J Biol Macromol 193, 838-846.

[3] Nandi, S. K., Rankenberg, J., Rakete, S., Nahomi, R. B., Glomb, M. A., Linetsky, M. D., and Nagaraj, R. H. (2021) Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro, Glycoconj J 38, 347-359.

[4] Panda, A. K., Chakraborty, A., Nandi, S. K., and Biswas, A. (2020) The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3, Proteins 88, 759-774.

[5] Nandi, S. K., Rankenberg, J., Glomb, M. A., and Nagaraj, R. H. (2020) Transient elevation of temperature promotes cross-linking of alpha-crystallin-client proteins through formation of advanced glycation endproducts: A potential role in presbyopia and cataracts, Biochem Biophys Res Commun 533, 1352-1358.

[6] Nandi, S. K., Nahomi, R. B., Rankenberg, J., Glomb, M. A., and Nagaraj, R. H. (2020) Glycation-mediated inter-protein cross-linking is promoted by chaperone-client complexes of alpha-crystallin: Implications for lens aging and presbyopia, J Biol Chem 295, 5701-5716.

[7] Nandi, S. K., Chakraborty, A., Panda, A. K., and Biswas, A. (2020) M. leprae HSP18 suppresses copper (II) mediated ROS generation: Effect of redox stress on its structure and function, Int J Biol Macromol 146, 648-660.

[8] Nahomi, R. B.^#, Nandi, S. K.^#, Rakete, S., Michel, C., Fritz, K. S., and Nagaraj, R. H. (2020) Lysine malonylation and propionylation are prevalent in human lens proteins, Exp Eye Res 190, 107864. ^#Contributed equally

[9] Stankowska, D. L., Nam, M. H., Nahomi, R. B., Chaphalkar, R. M., Nandi, S. K., Fudala, R., Krishnamoorthy, R. R., and Nagaraj, R. H. (2019) Systemically administered peptain-1 inhibits retinal ganglion cell death in animal models: implications for neuroprotection in glaucoma, Cell Death Discov 5, 112.

[10] Nandi, S. K., Rakete, S., Nahomi, R. B., Michel, C., Dunbar, A., Fritz, K. S., and Nagaraj, R. H. (2019) Succinylation Is a Gain-of-Function Modification in Human Lens alphaB-Crystallin, Biochemistry 58, 1260-1274.

[11] Nandi, S. K., Nahomi, R. B., Harris, P. S., Michel, C. R., Fritz, K. S., and Nagaraj, R. H. (2019) The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of alpha-crystallin in mouse lenses, Exp Eye Res 182, 1-9.

[12] Nahomi, R. B., Nandi, S. K., and Nagaraj, R. H. (2019) A monoclonal antibody targeted to the functional peptide of alphaB-crystallin inhibits the chaperone and anti-apoptotic activities, J Immunol Methods 467, 37-47.

[13] Nandi, S. K., Chakraborty, A., Panda, A. K., Kar, R. K., Bhunia, A., and Biswas, A. (2018) Evidences for zinc (II) and copper (II) ion interactions with Mycobacterium leprae HSP18: Effect on its structure and chaperone function, J Inorg Biochem 188, 62-75.

[14] Chakraborty, A., Nandi, S. K., Panda, A. K., Mahapatra, P. P., Giri, S., and Biswas, A. (2018) Probing the structure-function relationship of Mycobacterium leprae HSP18 under different UV radiations, Int J Biol Macromol 119, 604-616.

[15] Panda, A. K., Chakraborty, A., Nandi, S. K., Kaushik, A., and Biswas, A. (2017) The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function, FEBS J 284, 277-300.

[16] Panda, A. K.^#, Nandi, S. K.^#, Chakraborty, A., Nagaraj, R. H., and Biswas, A. (2016) Differential role of arginine mutations on the structure and functions of alpha-crystallin, Biochim Biophys Acta 1860, 199-210. ^#Contributed equally

[17] Nandi, S. K., Chakraborty, A., Panda, A. K., and Biswas, A. (2016) Conformational perturbation, hydrophobic interactions and oligomeric association are responsible for the enhanced chaperone function of Mycobacterium leprae HSP18 under pre-thermal condition, RSC Advances 6, 62146-62156.

[18] Nandi, S. K., Panda, A. K., Chakraborty, A., Sinha Ray, S., and Biswas, A. (2015) Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18, PLoS One 10, e0129734.

[19] Nandi, S. K., Chakraborty, A., Panda, A. K., Ray, S. S., Kar, R. K., Bhunia, A., and Biswas, A. (2015) Interaction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and function, PLoS Negl Trop Dis 9, e0003661.

[20] DiMauro, M. A.^#, Nandi, S. K.^#, Raghavan, C. T., Kar, R. K., Wang, B., Bhunia, A., Nagaraj, R. H., and Biswas, A. (2014) Acetylation of Gly1 and Lys2 promotes aggregation of human gammaD-crystallin, Biochemistry 53, 7269-7282. ^#Contributed equally

[21] Nandi, S. K., Rehna, E. A., Panda, A. K., Shiburaj, S., Dharmalingam, K., and Biswas, A. (2013) A S52P mutation in the 'alpha-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function, FEBS J 280, 5994-6009.

[22] Nahomi, R. B., Huang, R., Nandi, S. K., Wang, B., Padmanabha, S., Santhoshkumar, P., Filipek, S., Biswas, A., and Nagaraj, R. H. (2013) Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human alphaB-crystallin, , 8126-8138.Biochemistry 52