Publications

Found 131 results
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2022
Hwang, T., Parker, S. S., Hill, S. M., Grant, R. A., Ilunga, M. W., Sivaraman, V., Mouneimne, G., and Keating, A. E. (2022) Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH. Elife. 10.7554/eLife.70680
Lam, K. - H., Tremblay, J. M., Perry, K., Ichtchenko, K., Shoemaker, C. B., and Jin, R. (2022) Probing the structure and function of the protease domain of botulinum neurotoxins using single-domain antibodies. PLoS Pathog. 18, e1010169
Johnson, C. W., Seo, H. - S., Terrell, E. M., Yang, M. - H., KleinJan, F., Gebregiworgis, T., Gasmi-Seabrook, G. M. C., Geffken, E. A., Lakhani, J., Song, K., Bashyal, P., Popow, O., Paulo, J. A., Liu, A., Mattos, C., Marshall, C. B., Ikura, M., Morrison, D. K., Dhe-Paganon, S., and Haigis, K. M. (2022) Regulation of GTPase function by autophosphorylation. Mol Cell. 82, 950-968.e14
Liu, Y., Iqbal, A., Li, W., Ni, Z., Wang, Y., Ramprasad, J., Abraham, K. Joshua, Zhang, M., Zhao, D. Yanling, Qin, S., Loppnau, P., Jiang, H., Guo, X., Brown, P. J., Zhen, X., Xu, G., Mekhail, K., Ji, X., Bedford, M. T., Greenblatt, J. F., and Min, J. (2022) A small molecule antagonist of SMN disrupts the interaction between SMN and RNAP II. Nat Commun. 13, 5453
Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Frey, K. M., Bertoletti, N., Chan, A. H., Ippolito, J. A., Bollini, M., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2022) Structural Studies and Structure Activity Relationships for Novel Computationally Designed Non-nucleoside Inhibitors and Their Interactions With HIV-1 Reverse Transcriptase. Front Mol Biosci. 9, 805187
Gorelik, A., Illes, K., Bui, K. Huy, and Nagar, B. (2022) Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase. Proc Natl Acad Sci U S A. 119, e2203518119
Nakaya, T., Yabe, M., Mashalidis, E. H., Sato, T., Yamamoto, K., Hikiji, Y., Katsuyama, A., Shinohara, M., Minato, Y., Takahashi, S., Horiuchi, M., Yokota, S. - I., Lee, S. - Y., and Ichikawa, S. (2022) Synthesis of macrocyclic nucleoside antibacterials and their interactions with MraY. Nat Commun. 13, 7575
2021
Slavik, K. M., Morehouse, B. R., Ragucci, A. E., Zhou, W., Ai, X., Chen, Y., Li, L., Wei, Z., Bähre, H., König, M., Seifert, R., S Y Lee, A., Cai, H., Imler, J. - L., and Kranzusch, P. J. (2021) cGAS-like receptors sense RNA and control 3'2'-cGAMP signaling in Drosophila. Nature. 10.1038/s41586-021-03743-5
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
Khan, N., Pelletier, D., McAlear, T. S., Croteau, N., Veyron, S., Bayne, A. N., Black, C., Ichikawa, M., Khalifa, A. Abdelzaher, Chaaban, S., Kurinov, I., Brouhard, G., Bechstedt, S., Bui, K. Huy, and Trempe, J. - F. (2021) Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding. Structure. 29, 572-586.e6
Hwang, T., Parker, S. S., Hill, S. M., Ilunga, M. W., Grant, R. A., Mouneimne, G., and Keating, A. E. (2021) A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers. Elife. 10.7554/eLife.70601
Ren, X., Gelinas, A. D., Linehan, M., Iwasaki, A., Wang, W., Janjic, N., and Pyle, A. Marie (2021) Evolving A RIG-I Antagonist: A Modified DNA Aptamer Mimics Viral RNA. J Mol Biol. 433, 167227
Tsai, W. - C., Gilbert, N. C., Ohler, A., Armstrong, M., Perry, S., Kalyanaraman, C., Yasgar, A., Rai, G., Simeonov, A., Jadhav, A., Standley, M., Lee, H. - W., Crews, P., Iavarone, A. T., Jacobson, M. P., Neau, D. B., Offenbacher, A. R., Newcomer, M., and Holman, T. R. (2021) Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2. Bioorg Med Chem. 46, 116349
Iketani, S., Forouhar, F., Liu, H., Hong, S. Jung, Lin, F. - Y., Nair, M. S., Zask, A., Huang, Y., Xing, L., Stockwell, B. R., Chavez, A., and Ho, D. D. (2021) Lead compounds for the development of SARS-CoV-2 3CL protease inhibitors. Nat Commun. 12, 2016
Mulvaney, K. M., Blomquist, C., Acharya, N., Li, R., Ranaghan, M. J., O'Keefe, M., Rodriguez, D. J., Young, M. J., Kesar, D., Pal, D., Stokes, M., Nelson, A. J., Jain, S. S., Yang, A., Mullin-Bernstein, Z., Columbus, J., Bozal, F. K., Skepner, A., Raymond, D., LaRussa, S., McKinney, D. C., Freyzon, Y., Baidi, Y., Porter, D., Aguirre, A. J., Ianari, A., McMillan, B., and Sellers, W. R. (2021) Molecular basis for substrate recruitment to the PRMT5 methylosome. Mol Cell. 81, 3481-3495.e7
Dawson, C. D., Irwin, S. M., Backman, L. R. F., Le, C., Wang, J. X., Vennelakanti, V., Yang, Z., Kulik, H. J., Drennan, C. L., and Balskus, E. P. (2021) Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Cell Chem Biol. 10.1016/j.chembiol.2021.03.001
Yu, C. H., Bhattacharya, A., Persaud, M., Taylor, A. B., Wang, Z., Bulnes-Ramos, A., Xu, J., Selyutina, A., Martinez-Lopez, A., Cano, K., Demeler, B., Kim, B., Hardies, S. C., Diaz-Griffero, F., and Ivanov, D. N. (2021) Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification. Nat Commun. 12, 731
Zhang, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332
Zhang, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332
Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475
Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475
Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170
Dempsey, D. R., Viennet, T., Iwase, R., Park, E., Henriquez, S., Chen, Z., Jeliazkov, J. R., Palanski, B. A., Phan, K. L., Coote, P., Gray, J. J., Eck, M. J., Gabelli, S. B., Arthanari, H., and Cole, P. A. (2021) The structural basis of PTEN regulation by multi-site phosphorylation. Nat Struct Mol Biol. 28, 858-868
Deshmukh, M. G., Ippolito, J. A., Zhang, C. - H., Stone, E. A., Reilly, R. A., Miller, S. J., Jorgensen, W. L., and Anderson, K. S. (2021) Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease. Structure. 10.1016/j.str.2021.06.002

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