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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., Mohr, L., Maciejowski, J., and Kranzusch, P. J. (2021) cGAS phase separation inhibits TREX1-mediated DNA degradation and enhances cytosolic DNA sensing. Mol Cell. 81, 739-755.e7
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., 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., 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, 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
Zhu, N., Mealka, M., Mitchel, S., Milani, C., Acuña, L. M., Rogers, E., Lahana, A. N., and Huxford, T. (2023) X-ray Crystallographic Study of Preferred Spacing by the NF-κB p50 Homodimer on κB DNA.. Biomolecules. 10.3390/biom13091310
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
Zhu, S. - J., Zhao, P., Yang, J., Ma, R., Yan, X. - E., Yang, S. - Y., Yang, J. - W., and Yun, C. -hong (2018) Structural insights into drug development strategy targeting EGFR T790M/C797S. Oncotarget. 9, 13652-13665
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
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
Ziervogel, B. K., and Roux, B. (2013) The binding of antibiotics in OmpF porin. Structure. 21, 76-87
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., 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
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
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
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
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
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
Zuk, A., Si, Z., Loi, S., Bommegowda, S., Hoivik, D., Danthi, S., Molnar, G., Csizmadia, V., and Rabinowitz, M. (2022) Preclinical characterization of vadadustat (AKB-6548), an oral small molecule hypoxia inducible factor prolyl-4-hydroxylase inhibitor, for the potential treatment of renal anemia. J Pharmacol Exp Ther. 10.1124/jpet.122.001126

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