35. Felt K, Stauffer M, Salas-Estrada L, Guzzo PR, Xie D, Huang J, Filizola M, Chakrapani S. Structural basis for partial agonism in 5-HT3A receptors. Nat Struct Mol Biol. 2024 Jan 4. https://doi.org/10.1038/s41594-023-01140-2
34. Gibbs E, Klemm E, Seiferth D, Kumar A, Ilca SL, Biggin PC, Chakrapani S. Conformational transitions and allosteric modulation in a heteromeric glycine receptor. Nat Commun. 2023 https://doi.org/10.1038/s41467-023-37106-7
33. Kumar A, Kindig K, Rao S, Zaki AM, Basak S, Sansom MSP, Biggin PC, Chakrapani S. Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs. Nat Commun. 2022 Aug 18;13(1):4862. https://doi.org/10.1038/s41467-022-32594-5. PMID: 35982060; PMCID: PMC9388682.
32. Kumar, A., Basak, S., & Chakrapani, S. (2021). Recombinant expression and purification of pentameric ligand-gated ion channels for Cryo-EM structural studies. In Ion Channels Part A (1st ed.). Elsevier Inc. https://doi.org/10.1016/bs.mie.2021.01.022
30. Eric Gibbs and Sudha Chakrapani. Structure, Function and Physiology of 5-Hydroxytryptamine ReceptorsSubtype 3 in Subcellular Biochemistry: Macromolecular Protein Complexes III. Editors:Dr. J. Robin Harris and Dr. Jon Marles-Wright (10.1007/978-3-030-58971-4)
29. Kumar, A., Basak, S., Rao, S., Gicheru, Y., Mayer, M.L., M S.P Sansom., and Chakrapani,S . Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs. Nature communication. 2020 (Preprint link on bioRxiv 788695; doi: https://doi.org/10.1101/788695)
28. Basak, S*., Gicheru, Y*., Kapoor, A., Mayer, M.L, Filizola, M., and Chakrapani,S. Molecular mechanism of setron-mediated inhibition of full-length 5-HT3A receptor. Nature communication. 2019
27. Basak, S., Gicheru, Y., Rao, S., M S.P Sansom., and Chakrapani,S . Cryo-EM reveals two distinct serotonin-bound conformations of full-length 5-HT 3A receptor. Nature volume 563, pages270–274 (2018)
25. Chatterjee, S., Vyas, R., Chalamalasetti, S., Sahu, I., Clatot, J., Lorigan, GA., Deschêne I., and Chakrapani, S . The Voltage-Gated Sodium Channel Pore exhibits Conformational Flexibility during Slow Inactivation. J. Gen. Physiol. 2018 **
** JGP featured a commentary to highlight this work. [ link ]
24. Basak, S., Gicheru, Y., Samanta, A., Molugu, S., Huang, W., Fuente, M. D. L., Hughes, T., Taylor, D., Nieman, M., Moiseenkova-Bell, V.Y. & Chakrapani,S . Cryo-EM structure of 5-HT3A receptor in its resting conformation. Nature communication. 2018;9,514.
23. Hughes TET, Lodowski DT, Huynh KW, Yazici A, Del Rosario J, Kapoor A, Basak S, Samanta A, Han X, Chakrapani S , Zhou ZH, Filizola M, Rohacs T, Han S, Moiseenkova-Bell VY. Structural basis of TRPV5 channel inhibition by econazole revealed by cryo-EM. Nature structural & molecular biology. 2018; 25(1):53-60.
22. Basak S, Schmandt N, Gicheru Y, Chakrapani S . Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel. eLife. 2017; 6.
21. Maiti B, Manna AK, McCleese C, Doane TL, Chakrapani S , Burda C, Dunietz BD. Photoinduced Homolytic Bond Cleavage of the Central Si-C Bond in Porphyrin Macrocycles Is a Charge Polarization Driven Process. The journal of physical chemistry. A. 2016; 120(39):7634-7640.
20. Guo X, Sun X, Hu D, Wang YJ, Fujioka H, Vyas R, Chakrapani S , Joshi AU, Luo Y, Mochly-Rosen D, Qi X. VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington's disease. Nature communications. 2016; 7:12646.
15. Velisetty P, Chalamalasetti SV, Chakrapani S . Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC). The Journal of biological chemistry. 2014; 289(5):3013-25
14. Ostmeyer J, Chakrapani S , Pan AC, Perozo E, Roux B. Recovery from slow inactivation in K+ channels is controlled by water molecules. Nature. 2013;501(7465):121-4.
13. Velisetty P, Chalamalasetti SV, Chakrapani S . Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC). The Journal of biological chemistry.2012; 287(44):36864-72.
9. Cuello LG, Jogini V, Cortes DM, Pan AC, Gagnon DG, Dalmas O, Cordero-Morales JF, Chakrapani S , Roux B, Perozo E. Structural basis for the coupling between activation and inactivation gates in K(+) channels. Nature. 2010; 466(7303):272-5.