Wong, C.F., Saw, W., Basak, S., Sano, M., Ueno, H., Kerk, H. W., Litty, D., Ragunathan, P., Dick, T., Müller, V., Noji, H. and Grüber, G. (2022) Structural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for Inhibitors. Antimicrobial Agents  chemotherapy. 66(12):e0105622.

Kumar, A., Kindig, K., Rao, S., Zaki, A., Basak, S., Sansom, M.S.P., Biggin, P. and Chakrapani, S. (2022) Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs. Nature communications. 13, 1528.

Qiao, Z., Yokoyama, T., Yan, X., Beh, I., Shi, J., Basak, S., Akiyama, Y. and Gao, Y. (2022) Cryo-EM structure of the entire FtsH-HflKC AAA protease complex. Cell Reports. 39, 110890.


Jobichen, Chacko., Chong, T. Y., Rattinam, R., Basak, S., Srinivasan, M., Pandey, K. P.,  Ngoc,T. B., Shi, J., Angayarkanni, J. and Sivaraman, J. (2021) Cryo-EM Structure of Bacterioferritin Nanocages Provides Insight into the Bio-mineralization of Ferritins. bioRxiv

Kumar, A., Basak, S. and Chakrapani, S*. (2021) Recombinant expression and purification of pentameric ligand-gated ion channels for Cryo-EM structural studies. Methods in Enzymology. 652, 81.

Basak, S., Kumar, A., Ramsey, S., Gibbs, E., Kapoor, A., Filizola, M. and Chakrapani, S*. (2020) High-resolution Structures of multiple 5-HT3AR-setron complexes reveal a novel mechanism of competitive inhibition. eLife. 9:e57870.

Kumar, A., Basak, S., Rao, S., Gicheru, Y., Mayer, M. L., Sansom, M., and Chakrapani, S*. (2020) Mechanism of activation and inhibition of full-length Glycine receptor in membranes. Nature communications. 11, 3752.

Basak, S., Gicheru, Y., Kapoor, Abhijeet., Mayer, M. L., Filizola, M. and Chakrapani, S*. (2019) Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor. Nature communications. 10 (1), 3225.

Basak, S., Gicheru, Y., Rao, S., Sansom, M. and Chakrapnai, S*. (2018) Cryo-EM reveals two distinct states along serotonin-mediated activation pathway of the full-length 5-HT3A receptor. Nature. 563, 270.

Basak, S., Gicheru, Y., Samanta, A., Molugu, S., Huang, W., Fuente, M. D. L., Hughes, T., Taylor, D., Nieman, M., Moiseenkova-Bell, V.Y. and Chakrapani, S*. (2018) Cryo-EM structure of 5-HT3A receptor in its resting conformation. Nature communications. 9, 514.

Taylor, E.T., Lodowski, D.T, Huynh, K.W., Yazici, A., Rosario, J. D., Kapoor, A., Basak, S., Samanta, A., Han, X., Chakrapani, S., Zhou, Z.H., Filizola, M., Rohacs, T., Han, S., and Moiseenkova-Bell, V.Y*. (2018) Structural basis of the TRPV5 channel inhibition revealed by cryoEM. Nature Structural & Molecular Biology. 25, 53060.

Basak, S., Schmandt, N., Gicheru, Y. and Chakrapani, S*. (2017) Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel. eLife. 6:e23886.


Basak, S., Chatterjee, S. and Chakrapani, S*. (2015) Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels. Journal Visualized Experiments. 113, e54127.

Nartey, W., Basak, S., Kamariah, N., Manimekalai, M. S., Robson, S., Wagner, G., Eisenhaber, B., Eisenhaber, F. and Grüber, G*. (2015) NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery. FEBS Journal. 282, 4620-4638. 

Balakrishna, A. M., Basak, S., Manimekalai, M. S. S. and Grüber, G*. (2015) Crystal structure of subunits D and F in complex give insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae. Journal of Biological Chemistry. 290, 3183-3196.

Basak, S., Lim, J., Manimekalai, M. S. S., Balakrishna, A. M. and Grüber, G*. (2013) Crystal- and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae. Journal of Biological Chemistry. 288, 11930-11939.

Biuković, G., Basak, S., Manimekalai, M. S. S., Rishikesan, S., Roessle, M., Dick, T., Rao, S., Hunke, C. and Grüber, G*. (2013) Variations of subunit ɛ of the Mycobacterium tuberculosis F1FO ATP synthase and a novel model for mechanism of action of the TB drug TMC207. Antimicrobial Agents Chemotherapy. 57, 168-176.

Basak, S., Balakrishna, A. M., Manimekalai, M. S. S. and Grüber, G*. (2012) Crystallization and preliminary X-ray crystallographic analysis of subunit F, F1-94, an essential coupling subunit of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae. Acta Crystallographica. F68, 1055-1059.

Pattnaik, G., Sinha, B., Mukherjee, B.*, Ghosh, S., Basak, S., Mondal, S. and Bera, T. (2012) Submicron-size biodegradable polymer-based didanosine particles for treating HIV at early stage: an in vitro study. Journal of Microencapsulation. 29, 666-676.

Basak, S., Gayen, S., Ramalingam, J., Grüber, A., Preiser, R. P. and Grüber, G*. (2011) NMR solution structure of NBD94483-502 of the nucleotide binding domain of the Plasmodium yoelii reticulocyte binding protein Py235. FEMS Microbiology Letters. 318, 152-158.

Basak, S., Gayen, S., Thaker, Y. R., Manimekalai, M. S. S., Roessle, M., Hunke, C. and Grüber, G*. (2011) Solution structure of subunit F (Vma7p) of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae derived from SAXS and NMR spectroscopy. Biochimica Biophysica Acta-Biomembranes.1808, 360-368.