Publications

Found 1231 results
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2020
Niu, Y., Suzuki, H., Hosford, C. J., Walz, T., and Chappie, J. S. (2020) Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes. Nat Commun. 11, 5907
Heppner, D. E., Günther, M., Wittlinger, F., Laufer, S. A., and Eck, M. J. (2020) Structural Basis for EGFR Mutant Inhibition by Trisubstituted Imidazole Inhibitors. J Med Chem. 10.1021/acs.jmedchem.0c00200
Chitrakar, I., Iuliano, J. N., He, Y. L., Woroniecka, H. A., Collado, J. Tolentino, Wint, J. M., Walker, S. G., Tonge, P. J., and French, J. B. (2020) Structural Basis for the Regulation of Biofilm Formation and Iron Uptake in by the Blue-Light-Using Photoreceptor, BlsA. ACS Infect Dis. 6, 2592-2603
Herbst-Gervasoni, C. J., Steimbach, R. R., Morgen, M., Miller, A. K., and Christianson, D. W. (2020) Structural Basis for the Selective Inhibition of HDAC10, the Cytosolic Polyamine Deacetylase. ACS Chem Biol. 10.1021/acschembio.0c00362
Viswanathan, T., Arya, S., Chan, S. - H., Qi, S., Dai, N., Misra, A., Park, J. - G., Oladunni, F., Kovalskyy, D., Hromas, R. A., Martinez-Sobrido, L., and Gupta, Y. K. (2020) Structural basis of RNA cap modification by SARS-CoV-2. Nat Commun. 11, 3718
Cho, J., Lee, M., C Cochrane, S., Webster, C. G., Fenton, B. A., Zhao, J., Hong, J., and Zhou, P. (2020) Structural basis of the UDP-diacylglucosamine pyrophosphohydrolase LpxH inhibition by sulfonyl piperazine antibiotics. Proc Natl Acad Sci U S A. 117, 4109-4116
He, F., DuPrez, K., Hilario, E., Chen, Z., and Fan, L. (2020) Structural basis of the XPB helicase-Bax1 nuclease complex interacting with the repair bubble DNA. Nucleic Acids Res. 48, 11695-11705
He, F., DuPrez, K., Hilario, E., Chen, Z., and Fan, L. (2020) Structural basis of the XPB helicase-Bax1 nuclease complex interacting with the repair bubble DNA. Nucleic Acids Res. 48, 11695-11705
Devlin, J. R., Alonso, J. A., Ayres, C. M., Keller, G. L. J., Bobisse, S., Kooi, C. W. Vander, Coukos, G., Gfeller, D., Harari, A., and Baker, B. M. (2020) Structural dissimilarity from self drives neoepitope escape from immune tolerance. Nat Chem Biol. 10.1038/s41589-020-0610-1
Edani, B. H., Grabińska, K. A., Zhang, R., Park, E. Joo, Siciliano, B., Surmacz, L., Ha, Y., and Sessa, W. C. (2020) Structural elucidation of the -prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proc Natl Acad Sci U S A. 10.1073/pnas.2008381117
Slater, B. T., Han, X., Chen, L., and Xiong, Y. (2020) Structural insight into T cell coinhibition by PD-1H (VISTA). Proc Natl Acad Sci U S A. 10.1073/pnas.1908711117
Hoffer, E., Hong, S., Sunita, S., Maehigashi, T., Gonzalez, R. L., Whitford, P., and Dunham, C. M. (2020) Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing. Elife. 10.7554/eLife.51898
Hoffer, E., Hong, S., Sunita, S., Maehigashi, T., Gonzalez, R. L., Whitford, P., and Dunham, C. M. (2020) Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing. Elife. 10.7554/eLife.51898
Smith, N. A., Clarke, O. B., Lee, M., Hodder, A. N., and Smith, B. J. (2020) Structure of the Plasmodium falciparum PfSERA5 pseudo-zymogen. Protein Sci. 29, 2245-2258
Zimanyi, C. M., Guo, M., Mahmood, A., Hendrickson, W. A., Hirsh, D., and Cheung, J. (2020) Structure of the Regulatory Cytosolic Domain of a Eukaryotic Potassium-Chloride Cotransporter. Structure. 10.1016/j.str.2020.06.009
Zimanyi, C. M., Guo, M., Mahmood, A., Hendrickson, W. A., Hirsh, D., and Cheung, J. (2020) Structure of the Regulatory Cytosolic Domain of a Eukaryotic Potassium-Chloride Cotransporter. Structure. 10.1016/j.str.2020.06.009
Manz, T. D., Sivakumaren, S. C., Yasgar, A., Hall, M. D., Davis, M. I., Seo, H. - S., Card, J. D., Ficarro, S. B., Shim, H., Marto, J. A., Dhe-Paganon, S., Sasaki, A. T., Boxer, M. B., Simeonov, A., Cantley, L. C., Shen, M., Zhang, T., Ferguson, F. M., and Gray, N. S. (2020) Structure-Activity Relationship Study of Covalent Pan-phosphatidylinositol 5-Phosphate 4-Kinase Inhibitors. ACS Med Chem Lett. 11, 346-352
Xie, W., Sowemimo, I., Hayashi, R., Wang, J., Burkard, T. R., Brennecke, J., Ameres, S. L., and Patel, D. J. (2020) Structure-function analysis of microRNA 3'-end trimming by Nibbler. Proc Natl Acad Sci U S A. 10.1073/pnas.2018156117
Xie, W., Sowemimo, I., Hayashi, R., Wang, J., Burkard, T. R., Brennecke, J., Ameres, S. L., and Patel, D. J. (2020) Structure-function analysis of microRNA 3'-end trimming by Nibbler. Proc Natl Acad Sci U S A. 10.1073/pnas.2018156117
Kwak, S. - H., C Cochrane, S., Ennis, A. F., Lim, W. Young, Webster, C. G., Cho, J., Fenton, B. A., Zhou, P., and Hong, J. (2020) Synthesis and evaluation of sulfonyl piperazine LpxH inhibitors. Bioorg Chem. 102, 104055
Mukherjee, S., Erramilli, S. K., Ammirati, M., Alvarez, F. J. D., Fennell, K. F., Purdy, M. D., Skrobek, B. M., Radziwon, K., Coukos, J., Kang, Y., Dutka, P., Gao, X., Qiu, X., Yeager, M., H Xu, E., Han, S., and Kossiakoff, A. A. (2020) Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins. Nat Commun. 11, 1598
Sivakumaren, S. Carmen, Shim, H., Zhang, T., Ferguson, F. M., Lundquist, M. R., Browne, C. M., Seo, H. - S., Paddock, M. N., Manz, T. D., Jiang, B., Hao, M. - F., Krishnan, P., Wang, D. G., T Yang, J., Kwiatkowski, N. P., Ficarro, S. B., Cunningham, J. M., Marto, J. A., Dhe-Paganon, S., Cantley, L. C., and Gray, N. S. (2020) Targeting the PI5P4K Lipid Kinase Family in Cancer Using Covalent Inhibitors. Cell Chem Biol. 10.1016/j.chembiol.2020.02.003
Zhang, H., Pan, Y., Hu, L., M Hudson, A., Hofstetter, K. S., Xu, Z., Rong, M., Wang, Z., Prasad, B. V. Venkatar, Lockless, S. W., Chiu, W., and Zhou, M. (2020) TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat Commun. 11, 547
Zhang, H., Pan, Y., Hu, L., M Hudson, A., Hofstetter, K. S., Xu, Z., Rong, M., Wang, Z., Prasad, B. V. Venkatar, Lockless, S. W., Chiu, W., and Zhou, M. (2020) TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat Commun. 11, 547
Zhang, H., Pan, Y., Hu, L., M Hudson, A., Hofstetter, K. S., Xu, Z., Rong, M., Wang, Z., Prasad, B. V. Venkatar, Lockless, S. W., Chiu, W., and Zhou, M. (2020) TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat Commun. 11, 547

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