Ahuja Lab

Publications

*Co-authors with equal contributions
#Reed undergraduate students

  1. Shi, H#; Fu Yu#; Kodyte, V#, *; Andreas, M#, *; Sachla, A; Miller, K#; Shrestha, R; Helmann, J. D; Glasfeld, A; and Ahuja, S (2024). Structural basis for transcription activation through cooperative recruitment of MntR. Submitted to BioRxiv and Nat. Comm.

  2. Ahuja, S; Cahill, J; Hartfield, K and Whorton, M. R. (2021). Inhibition of CMP-sialic acid transport by endogenous 5-methyl CMP. PLoS One, 16(6):e0249905.

  3. Cahill, J*; Ahuja, S* and Whorton, M. R. (2020). In vitro Measurement of CMP-Sialic Acid Transporter Activity in Reconstituted Proteoliposomes. Bio Protocols 10, Iss 6. 10.21769/BioProtoc.3551

  4. Ahujas, S and Whorton, M. R. (2019). Structural basis for mammalian nucleotide sugar transport. eLife 8:e45221

  5. Ahuja, S*., Mukund, S*., Deng, L., Khakh, K., Chang, E., Ho, H., Shriver, S., Young, C., Lin, S., Johnson Jr. J. P., Wu, P., Li, Jun., Coons, M., Tam, C., Brillantes, B., Sampang, H., Mortara, K., Bowman, K., Clark, K. R., Estevez, A., Xie, Z., Verschoof, H., Grimwood, M., Christoph, D., Andrez, J.C., Focken, T., Sutherlin, D., Safina, B.S., Starovasnik, M., Ortwine, D. F., Franke, Y., Cohen, C. J., Hackos, D., Koth, C. M., and Payandeh, J. (2015). Structural basis of a mammalian voltage gated sodium channel inhibition by an isoform-selective small molecule antagonist. Science 350 no. 6267, aac5454.

  6. Ahuja, S*., Rouge, L*., Swem, D. L., Sudhamsu, J., Wu, P., Russell, S., Alexander, M. K., Tam, C., Nishiyama, M., Starovasnik, M., Koth, C. M. (2015). Structural analysis of bacterial ABC transporter inhibition by an antibody fragment. Structure 23, 713-23.

  7. Zhang, M., Le Claire, S., Huang, R., Ahuja, S., Im, S. C., Waskell, L., Ramamoorthy, A. (2015). Insights into the Role of Substrates on the Interaction between Cytochrome b5 and Cytochrome P450 2B4 by NMR. Sci Rep 5, 8392, doi:10.1038/srep08392.

  8. Vivekanandan, S., Ahuja, S., Im, S. C., Waskell, L. and Ramamoorthy, A. (2014). 1H, 13C and 15N resonance assignments for the full-length mammalian cytochrome b in a membrane environment. Biomol NMR Assign 8, 409-413.

  9. Pandey, M. K., Vivekanandan, S., Ahuja, S., Huang, R., Im, S. C., Waskell, L., Ramamoorthy, A. (2013) Cytochrome-P450-cytochrome-b5 interaction in a membrane environment changes 15N chemical shift anisotropy tensors. J Phys Chem B 117, 13851-13860.

  10. Yamamoto, K., Gildenberg, M., Ahuja, S., Im, S. C., Pearcy, P., Waskell, L., Ramamoorthy, A. (2013). Probing the transmembrane structure and topology of microsomal cytochrome-p450 by solid-state NMR on temperature-resistant bicelles. Sci Rep 3, 2556, doi:10.1038/srep02556.

  11. Ahuja, S., Jahr, N., Im. S.C., Vivekanandan, S., Popovych, N., Le Claire, S., Huang, R., Soong, R., Xu, J., Yamamoto, K., Nanga, R. P. R., Bridges, A., Waskell, L. and Ramamoorthy, A. (2013). A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data. J. Biol. Chem. 288, 22080-22095

  12. Pandey, M. K., Vivekanandan, S., Ahuja, S., Pichumani, K., Im, S. C., Waskell, L., Ramamoorthy, A. (2012). Determination of 15N chemical shift anisotropy from a membrane-bound protein by NMR spectroscopy. J. Phys. Chem. B. 116, 7181-7189.

  13. Eilers, M., Goncalves, J. A., Ahuja, S., Kirkup, C., Hirshfeld, A., Simmerling, C., Reeves, P. J., Sheves, M., Smith, S. O. (2012). Structural Transitions of Transmembrane Helix 6 in the Formation of Metarhodopsin I. J. Phys. Chem. B. 116, 10477-10489.

  14. Goncalves, J., South, K., Ahuja, S., Zaitseva, E., Opefi, C., Eilers, M., Vogel, R., Reeves, P. and Smith, S. O. (2010). Highly conserved tyrosine stabilizes the active state of rhodopsin, Proc. Natl. Acad. Sci. USA, 107, 19861-19866.

  15. Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E. and Smith, S. O. (2010). Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils, Nat. Struct. Mol. Biol., 17, 561-567.

  16. Goncalves, J. A., Ahuja, S., Erfani, S., Eilers M. and Smith, S. O. (2010). Structure and function of G protein-coupled receptors using NMR spectroscopy, Prog. Nucl. Magn. Reson. Spectrosc., 57, 159-180.

  17. Hornak, V., Ahuja, S., Eilers, M., Reeves, P. J., Sheves, M. and Smith, S. O. (2010). A view of the activated state of rhodopsin from guided molecular dynamics simulations, J. Mol. Biol., 396, 510-527.

  18. Ahuja, S., Eilers, M., Hirshfeld, A., Yan, E. C., Ziliox, M., Sakmar, T. P., Sheves, M. and Smith, S. O. (2009). 6-s-cis conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin, J. Am. Chem. Soc., 131, 15160-15169.

  19. Ahuja, S. and Smith, S. O. (2009). Multiple switches in G protein-coupled receptor activation, Trends Pharmacol. Sci. 30, 494-502.

  20. Ahuja, S., Crocker, E., Eilers, M., Hornak, V., Hirshfeld, A., Ziliox, M., Syrett, N., Reeves, P. J., Khorana, H. G., Sheves, M. and Smith, S. O. (2009). Location of the retinal chromophore in the activated state of rhodopsin, J. Biol. Chem., 284, 10190-10201.

  21. Ahuja, S., Hornak, V., Yan, E. C., Syrett, N., Goncalves, J. A., Hirshfeld, A., Ziliox, M., Sakmar, T. P., Sheves, M., Reeves, P. J., Smith, S. O. and Eilers, M. (2009). Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation, Nat. Struct. Mol. Biol., 16, 168-175.

  22. Crocker, E., Eilers, M., Ahuja, S., Hornak, V., Hirshfeld, A., Sheves, M. and S. O. Smith (2006). Location of Trp265 in metarhodopsin II: Implications for the activation mechanism of the visual receptor rhodopsin. J. Mol. Biol., 357, 163-172.