Publications

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Journal Article
Geng, Y., Deng, Z., Zhang, G., Budelli, G., Butler, A., Yuan, P., Cui, J., Salkoff, L., and Magleby, K. L. (2020) Coupling of Ca and voltage activation in BK channels through the αB helix/voltage sensor interface.. Proc Natl Acad Sci U S A. 117, 14512-14521
Prucha, G. R., Henry, S., Hollander, K., Carter, Z. J., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2023) Covalent and noncovalent strategies for targeting Lys102 in HIV-1 reverse transcriptase. Eur J Med Chem. 262, 115894
Ippolito, J. A., Niu, H., Bertoletti, N., Carter, Z. J., Jin, S., Spasov, K. A., Cisneros, J. A., Valhondo, M., Cutrona, K. J., Anderson, K. S., and Jorgensen, W. L. (2021) Covalent Inhibition of Wild-Type HIV-1 Reverse Transcriptase Using a Fluorosulfate Warhead. ACS Med Chem Lett. 12, 249-255
Chan, A. H., Lee, W. - G., Spasov, K. A., Cisneros, J. A., Kudalkar, S. N., Petrova, Z. O., Buckingham, A. B., Anderson, K. S., and Jorgensen, W. L. (2017) Covalent inhibitors for eradication of drug-resistant HIV-1 reverse transcriptase: From design to protein crystallography. Proc Natl Acad Sci U S A. 10.1073/pnas.1711463114
Kim, S., Grant, R. A., and Sauer, R. T. (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell. 145, 67-78
Campbell, A. C., Becker, D. F., Gates, K. S., and Tanner, J. J. (2020) Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. ACS Chem Biol. 10.1021/acschembio.9b00935
Cavalier, M. C., Pierce, A. D., Wilder, P. T., Alasady, M. J., Hartman, K. G., Neau, D. B., Foley, T. L., Jadhav, A., Maloney, D. J., Simeonov, A., Toth, E. A., and Weber, D. J. (2014) Covalent small molecule inhibitors of Ca(2+)-bound S100B. Biochemistry. 53, 6628-40
Baytshtok, V., Chen, J., Glynn, S. E., Nager, A. R., Grant, R. A., Baker, T. A., and Sauer, R. T. (2017) Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 292, 5695-5704
Baca, C. F., Yu, Y., Rostøl, J. T., Majumder, P., Patel, D. J., and Marraffini, L. A. (2024) The CRISPR effector Cam1 mediates membrane depolarization for phage defence. Nature. 10.1038/s41586-023-06902-y
Jia, N., Jones, R., Yang, G., Ouerfelli, O., and Patel, D. J. (2019) CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA Cleavage with ApA>p Formation Terminating RNase Activity. Mol Cell. 75, 944-956.e6
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Sethi, D. K., Gordo, S., Schubert, D. A., and Wucherpfennig, K. W. (2013) Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop. Nat Commun. 4, 2623
Teplova, M., Falschlunger, C., Krasheninina, O., Egger, M., Ren, A., Patel, D. J., and Micura, R. (2019) Crucial Roles of Two Hydrated Mg Ions in Reaction Catalysis of the Pistol Ribozyme. Angew Chem Int Ed Engl. 10.1002/anie.201912522
Deng, Z., Paknejad, N., Maksaev, G., Sala-Rabanal, M., Nichols, C. G., Hite, R. K., and Yuan, P. (2018) Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms. Nat Struct Mol Biol. 25, 252-260
Wu, X., and Rapoport, T. A. (2021) Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies). Proc Natl Acad Sci U S A. 10.1073/pnas.2115001118
Liu, Y., Pan, J., Jenni, S., Raymond, D. D., Caradonna, T., Do, K. T., Schmidt, A. G., Harrison, S. C., and Grigorieff, N. (2017) CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. J Mol Biol. 429, 1829-1839
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Lu, J., Cao, Q., Hughes, M. P., Sawaya, M. R., Boyer, D. R., Cascio, D., and Eisenberg, D. S. (2020) CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nat Commun. 11, 4090
Guo, T. Wei, Bartesaghi, A., Yang, H., Falconieri, V., Rao, P., Merk, A., Eng, E. T., Raczkowski, A. M., Fox, T., Earl, L. A., Patel, D. J., and Subramaniam, S. (2017) Cryo-EM Structures Reveal Mechanism and Inhibition of DNA Targeting by a CRISPR-Cas Surveillance Complex. Cell. 171, 414-426.e12
M Joyce, G., Sankhala, R. S., Chen, W. - H., Choe, M., Bai, H., Hajduczki, A., Yan, L., Sterling, S. L., Peterson, C. E., Green, E. C., Smith, C., de Val, N., Amare, M., Scott, P., Laing, E. D., Broder, C. C., Rolland, M., Michael, N. L., and Modjarrad, K. (2020) A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein. bioRxiv. 10.1101/2020.03.15.992883
Mao, Y., Xu, X., Xu, W., Ishida, Y., Leal, W. S., Ames, J. B., and Clardy, J. (2010) Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone. Proc Natl Acad Sci U S A. 107, 19102-7
Jin, R., Singh, S. K., Gu, S., Furukawa, H., Sobolevsky, A. I., Zhou, J., Jin, Y., and Gouaux, E. (2009) Crystal structure and association behaviour of the GluR2 amino-terminal domain. EMBO J. 28, 1812-23
Unciuleac, M. - C., Smith, P. C., and Shuman, S. (2016) Crystal Structure and Biochemical Characterization of a Mycobacterium smegmatis AAA-Type Nucleoside Triphosphatase Phosphohydrolase (Msm0858). J Bacteriol. 198, 1521-33
Bozzi, A. T., Bane, L. B., Weihofen, W. A., Singharoy, A., Guillen, E. R., Ploegh, H. L., Schulten, K., and Gaudet, R. (2016) Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter. Structure. 24, 2102-2114
Ellis-Guardiola, K., Rui, H., Beckner, R. L., Srivastava, P., Sukumar, N., Roux, B., and Lewis, J. C. (2019) Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase. Biochemistry. 10.1021/acs.biochem.9b00031

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