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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., 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
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
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., 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
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
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
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
Zuo, Y., De, S., Feng, Y., and Steitz, T. A. (2020) Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation. iScience. 23, 101445
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
Zwe, Y. Htut, Yadav, M., Ten, M. Mei Zhen, Srinivasan, M., Jobichen, C., Sivaraman, J., and Li, D. (2021) Bacterial Antagonism of Chromobacterium haemolyticum and Characterization of its Putative Type VI Secretion System. Res Microbiol. 10.1016/j.resmic.2021.103918

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