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Zuo, H., Glaaser, I., Zhao, Y., Kurinov, I., Mosyak, L., Wang, H., Liu, J., Park, J., Frangaj, A., Sturchler, E., Zhou, M., McDonald, P., Geng, Y., Slesinger, P. A., and Fan, Q. R. (2019) Structural basis for auxiliary subunit KCTD16 regulation of the GABA receptor. Proc Natl Acad Sci U S A. 116, 8370-8379
Zuo, Y., Vincent, H. A., Zhang, J., Wang, Y., Deutscher, M. P., and Malhotra, A. (2006) Structural basis for processivity and single-strand specificity of RNase II. Mol Cell. 24, 149-56
Zuo, Y., and Steitz, T. A. (2017) A structure-based kinetic model of transcription. Transcription. 8, 1-8
Zubcevic, L., Le, S., Yang, H., and Lee, S. - Y. (2018) Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol. 25, 405-415
Zong, Y., Zhang, B., Gu, S., Lee, K., Zhou, J., Yao, G., Figueiredo, D., Perry, K., Mei, L., and Jin, R. (2012) Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 26, 247-58
Zoltowski, B. D., Chelliah, Y., Wickramaratne, A., Jarocha, L., Karki, N., Xu, W., Mouritsen, H., Hore, P. J., Hibbs, R. E., Green, C. B., and Takahashi, J. S. (2019) Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon. Proc Natl Acad Sci U S A. 116, 19449-19457
Zoltowski, B. D., Vaidya, A. T., Top, D., Widom, J., Young, M. W., and Crane, B. R. (2011) Structure of full-length Drosophila cryptochrome. Nature. 480, 396-9
Zinder, J. C., Wasmuth, E. V., and Lima, C. D. (2016) Nuclear RNA Exosome at 3.1 Å Reveals Substrate Specificities, RNA Paths, and Allosteric Inhibition of Rrp44/Dis3.. Mol Cell. 64, 734-745
Zimmer, J., Nam, Y., and Rapoport, T. A. (2008) Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature. 455, 936-43
Zimmer, J., Li, W., and Rapoport, T. A. (2006) A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA. J Mol Biol. 364, 259-65
Zimanyi, C. M., Ando, N., Brignole, E. J., Asturias, F. J., Stubbe, J. A., and Drennan, C. L. (2012) Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure. 20, 1374-83
Zimanyi, C. M., Chen, P. Yang- Ting, Kang, G., Funk, M. A., and Drennan, C. L. (2016) Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Elife. 5, e07141
Ziervogel, B. K., and Roux, B. (2013) The binding of antibiotics in OmpF porin. Structure. 21, 76-87
Ziegler, S. J., Liu, C., Landau, M., Buzovetsky, O., Desimmie, B. A., Zhao, Q., Sasaki, T., Burdick, R. C., Pathak, V. K., Anderson, K. S., and Xiong, Y. (2018) Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies. PLoS One. 13, e0195048
Zhuang, M., Calabrese, M. F., Liu, J., M Waddell, B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., Hoggard, T., J Harper, W., White, K. P., and Schulman, B. A. (2009) Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Mol Cell. 36, 39-50
Zhu, Y., Luo, S., Sabo, Y., Wang, C., Tong, L., and Goff, S. P. (2017) Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling. Cell Host Microbe. 21, 220-230
Zhu, W., Haile, A. M., Singh, R. K., Larson, J. D., Smithen, D., Chan, J. Y., Tanner, J. J., and Becker, D. F. (2013) Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A.. Biochemistry. 52, 4482-91
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, C., Pourmal, S., and Pavletich, N. P. (2015) Dna2 nuclease-helicase structure, mechanism and regulation by Rpa. Elife. 10.7554/eLife.09832
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, 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, 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, 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, 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, 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

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