Publications

Found 2704 results
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Zhou, T., Ren, X., Adams, R. L., and Pyle, A. Marie (2017) NS3 from HCV strain JFH-1 is an unusually robust helicase that is primed to bind and unwind viral RNA. J Virol. 10.1128/JVI.01253-17
Zhou, Q., Zhou, P., Wang, A. L., Wu, D., Zhao, M., Südhof, T. C., and Brunger, A. T. (2017) The primed SNARE-complexin-synaptotagmin complex for neuronal exocytosis. Nature. 10.1038/nature23484
Zhou, W., Yin, Y., Smith, E., Chou, J., Shumate, J., Scampavia, L., Spicer, T. P., Carpino, N., and French, J. B. (2019) Discovery and Characterization of Two Classes of Selective Inhibitors of the Suppressor of the TCR Signaling Family of Proteins. ACS Infect Dis. 5, 250-259
Zhou, M., Ehsan, F., Gan, L., Dong, A., Li, Y., Liu, K., and Min, J. (2021) Structural basis for the recognition of the S2, S5-phosphorylated RNA polymerase II CTD by the mRNA anti-terminator protein hSCAF4. FEBS Lett. 10.1002/1873-3468.14256
Zhou, W., Ercan, D., Chen, L., Yun, C. -hong, Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., Engen, J. R., Wong, K. - K., Eck, M. J., Gray, N. S., and Jänne, P. A. (2009) Novel mutant-selective EGFR kinase inhibitors against EGFR T790M. Nature. 462, 1070-4
Zhou, L., Hinerman, J. M., Blaszczyk, M., Miller, J. L. C., Conrady, D. G., Barrow, A. D., Chirgadze, D. Y., Bihan, D., Farndale, R. W., and Herr, A. B. (2016) Structural basis for collagen recognition by the immune receptor OSCAR. Blood. 127, 529-37
Zhou, W., Whiteley, A. T., Mann, C. C. de Olive, Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., and Kranzusch, P. J. (2018) Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance. Cell. 174, 300-311.e11
Zhou, D., Tanzawa, T., Lin, J., and Gagnon, M. G. (2020) Structural basis for ribosome recycling by RRF and tRNA. Nat Struct Mol Biol. 27, 25-32
Zhou, W., Yin, Y., Weinheimer, A. S., Kaur, N., Carpino, N., and French, J. B. (2017) Structural and Functional Characterization of the Histidine Phosphatase Domains of Human Sts-1 and Sts-2. Biochemistry. 10.1021/acs.biochem.7b00638
Zhou, W., Tsai, A., Dattmore, D. A., Stives, D. P., Chitrakar, I., D'alessandro, A. M., Patil, iv, S., Hicks, K. A., and French, J. B. (2019) Crystal structure of E. coli PRPP synthetase. BMC Struct Biol. 19, 1
Zhou, X., Levin, E. J., Pan, Y., McCoy, J. G., Sharma, R., Kloss, B., Bruni, R., Quick, M., and Zhou, M. (2014) Structural basis of the alternating-access mechanism in a bile acid transporter. Nature. 505, 569-73
Zhou, J. O., Zaidi, H. A., Ton, T., and Fera, D. (2020) The Effects of Framework Mutations at the Variable Domain Interface on Antibody Affinity Maturation in an HIV-1 Broadly Neutralizing Antibody Lineage. Front Immunol. 11, 1529
Zhou, K., Gao, Y., Hoy, J. A., Mann, F. M., Honzatko, R. B., and Peters, R. J. (2012) Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis. J Biol Chem. 287, 6840-50
Zhou, W., Richmond-Buccola, D., Wang, Q., and Kranzusch, P. J. (2022) Structural basis of human TREX1 DNA degradation and autoimmune disease. Nat Commun. 13, 4277
Zhou, L., Bosscher, M., Zhang, C., Ozçubukçu, S., Zhang, L., Zhang, W., Li, C. J., Liu, J., Jensen, M. P., Lai, L., and He, C. (2014) A protein engineered to bind uranyl selectively and with femtomolar affinity. Nat Chem. 6, 236-41
Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Brewster, A. S., Sauter, N. K., Cohen, A. E., S Soltis, M., Alonso-Mori, R., Chollet, M., Lemke, H. T., Pfuetzner, R. A., Choi, U. B., Weis, W. I., Diao, J., Südhof, T. C., and Brunger, A. T. (2015) Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Nature. 525, 62-7
Zhong, X., Du, J., Hale, C. J., Gallego-Bartolome, J., Feng, S., Vashisht, A. A., Chory, J., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Molecular mechanism of action of plant DRM de novo DNA methyltransferases. Cell. 157, 1050-60
Zhong, M., Lynch, A., Muellers, S. N., Jehle, S., Luo, L., Hall, D. R., Iwase, R., Carolan, J. P., Egbert, M., Wakefield, A., Streu, K., Harvey, C. M., Ortet, P. C., Kozakov, D., Vajda, S., Allen, K. N., and Whitty, A. (2020) Interaction Energetics and Druggability of the Protein-Protein Interaction between Kelch-like ECH-Associated Protein 1 (KEAP1) and Nuclear Factor Erythroid 2 Like 2 (Nrf2). Biochemistry. 10.1021/acs.biochem.9b00943
Zheng, J., Sagar, V., Smolinsky, A., Bourke, C., LaRonde-LeBlanc, N., and T Cropp, A. (2009) Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin. J Mol Biol. 387, 1250-60
Zheng, C., Page, R. C., Das, V., Nix, J. C., Wigren, E., Misra, S., and Zhang, B. (2013) Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII). J Biol Chem. 288, 20499-509
Zheng, Y., Qiu, Y., Grace, C. R. R., Liu, X., Klionsky, D. J., and Schulman, B. A. (2019) A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade. Nat Commun. 10, 3600
Zheng, L., Falschlunger, C., Huang, K., Mairhofer, E., Yuan, S., Wang, J., Patel, D. J., Micura, R., and Ren, A. (2019) Hatchet ribozyme structure and implications for cleavage mechanism. Proc Natl Acad Sci U S A. 10.1073/pnas.1902413116
Zhao, J., An, J., Hwang, D., Wu, Q., Wang, S., Gillespie, R. A., Yang, E. Gyeong, Guan, Z., Zhou, P., and Chung, H. Suk (2019) The Lipid A 1-Phosphatase, LpxE, Functionally Connects Multiple Layers of Bacterial Envelope Biogenesis. MBio. 10.1128/mBio.00886-19
Zhao, Z., Zhou, M., Zemerov, S. D., Marmorstein, R., and Dmochowski, I. J. (2023) Rational design of a genetically encoded NMR zinc sensor. Chem Sci. 14, 3809-3815
Zhao, S., Lu, J., Pan, B., Fan, H., Byrum, S. D., Xu, C., Kim, A., Guo, Y., Kanchi, K. L., Gong, W., Sun, T., Storey, A. J., Burkholder, N. T., Mackintosh, S. G., Kuhlers, P. C., Edmondson, R. D., Strahl, B. D., Diao, Y., Tackett, A. J., Raab, J. R., Cai, L., Song, J., and Wang, G. Greg (2023) TNRC18 engages H3K9me3 to mediate silencing of endogenous retrotransposons. Nature. 623, 633-642

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