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Zahid, H., Buchholz, C. R., Singh, M., Ciccone, M. F., Chan, A., Nithianantham, S., Shi, K., Aihara, H., Fischer, M., Schönbrunn, E., Santos, C. O. Dos, Landry, J. W., and Pomerantz, W. C. K. (2021) New Design Rules for Developing Potent Cell-Active Inhibitors of the Nucleosome Remodeling Factor (NURF) via BPTF Bromodomain Inhibition. J Med Chem. 64, 13902-13917
Zahm, J. A., Jenni, S., and Harrison, S. C. (2023) Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface. Open Biol. 13, 220378
Zahm, J. A., Stewart, M. G., Carrier, J. S., Harrison, S. C., and Miller, M. P. (2021) Structural basis of Stu2 recruitment to yeast kinetochores. Elife. 10.7554/eLife.65389
Zang, Y., Wang, W. - H., Wu, S. - W., Ealick, S. E., and Wang, C. C. (2005) Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex. J Biol Chem. 280, 22318-25
Zangerl-Plessl, E. - M., Lee, S. - J., Maksaev, G., Bernsteiner, H., Ren, F., Yuan, P., Stary-Weinzinger, A., and Nichols, C. G. (2020) Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels. J Gen Physiol. 10.1085/jgp.201912422
Zee, C. - T., Glynn, C., Gallagher-Jones, M., Miao, J., Santiago, C. G., Cascio, D., Gonen, T., Sawaya, M. R., and Rodriguez, J. A. (2019) Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ. IUCrJ. 6, 197-205
Zein, F., Zhang, Y., Kang, Y. - N., Burns, K., Begley, T. P., and Ealick, S. E. (2006) Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry. 45, 14609-20
Zeiske, T., Baburajendran, N., Kaczynska, A., Brasch, J., Palmer, A. G., Shapiro, L., Honig, B., and Mann, R. S. (2018) Intrinsic DNA Shape Accounts for Affinity Differences between Hox-Cofactor Binding Sites. Cell Rep. 24, 2221-2230
Zeller, M. J., Favorov, O., Li, K., Nuthanakanti, A., Hussein, D., Michaud, A., Lafontaine, D. A., Busan, S., Serganov, A., Aubé, J., and Weeks, K. M. (2022) SHAPE-enabled fragment-based ligand discovery for RNA. Proc Natl Acad Sci U S A. 119, e2122660119
Zeller, M. J., Nuthanakanti, A., Li, K., Aubé, J., Serganov, A., and Weeks, K. M. (2022) Subsite Ligand Recognition and Cooperativity in the TPP Riboswitch: Implications for Fragment-Linking in RNA Ligand Discovery. ACS Chem Biol. 17, 438-448
Zeng, F., and Jin, H. (2018) Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Sci Rep. 8, 2349
Zeqiraj, E., Tang, X., Hunter, R. W., García-Rocha, M., Judd, A., Deak, M., von Wilamowitz-Moellendorff, A., Kurinov, I., Guinovart, J. J., Tyers, M., Sakamoto, K., and Sicheri, F. (2014) Structural basis for the recruitment of glycogen synthase by glycogenin. Proc Natl Acad Sci U S A. 111, E2831-40
Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F., Keszei, A. F. A., Lorenzen, K., Kurinov, I., Orlicky, S., Gish, G. D., Heck, A. J. R., Guarné, A., Greenberg, R. A., and Sicheri, F. (2015) Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Mol Cell. 59, 970-83
Zeyen, P., Zeyn, Y., Herp, D., Mahmoudi, F., Yesiloglu, T. Z., Erdmann, F., Schmidt, M., Robaa, D., Romier, C., Ridinger, J., Herbst-Gervasoni, C. J., Christianson, D. W., Oehme, I., Jung, M., Krämer, O. H., and Sippl, W. (2022) Identification of histone deacetylase 10 (HDAC10) inhibitors that modulate autophagy in transformed cells. Eur J Med Chem. 234, 114272
Zhan, C., Patskovsky, Y., Yan, Q., Li, Z., Ramagopal, U., Cheng, H., Brenowitz, M., Hui, X., Nathenson, S. G., and Almo, S. C. (2011) Decoy strategies: the structure of TL1A:DcR3 complex. Structure. 19, 162-71
Zhan, X., Gimenez, L. E., Gurevich, V. V., and Spiller, B. W. (2011) Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol. 406, 467-78
Zhang, Y., Kittredge, A., Ward, N., Ji, C., Chen, S., and Yang, T. (2018) ATP activates bestrophin ion channels through direct interaction. Nat Commun. 9, 3126
Zhang, E. Y., Ha, B. Hak, and Boggon, T. J. (2017) PAK4 crystal structures suggest unusual kinase conformational movements. Biochim Biophys Acta. 10.1016/j.bbapap.2017.10.004
Zhang, J., Kiser, P. D., Badiee, M., Palczewska, G., Dong, Z., Golczak, M., Tochtrop, G. P., and Palczewski, K. (2015) Molecular pharmacodynamics of emixustat in protection against retinal degeneration. J Clin Invest. 125, 2781-94
Zhang, J., and Ferré-D'Amaré, A. R. (2014) Dramatic improvement of crystals of large RNAs by cation replacement and dehydration. Structure. 22, 1363-71
Zhang, L., Lu, X., Lu, J., Liang, H., Dai, Q., Xu, G. - L., Luo, C., Jiang, H., and He, C. (2012) Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA. Nat Chem Biol. 8, 328-30
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, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332

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