Publications

Found 2775 results
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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, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475
Zhang, W., Shi, K., Hsueh, F. - C., Mendoza, A., Ye, G., Huang, L., Perlman, S., Aihara, H., and Li, F. (2024) Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses. Proc Natl Acad Sci U S A. 121, e2322600121
Zhang, H., Astrof, N. S., Liu, J. -huan, Wang, J. -huai, and Shimaoka, M. (2009) Crystal structure of isoflurane bound to integrin LFA-1 supports a unified mechanism of volatile anesthetic action in the immune and central nervous systems. FASEB J. 23, 2735-40
Zhang, Z., Liu, Q., and Hendrickson, W. A. (2014) Crystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiont. FEBS J. 281, 4263-79
Zhang, Y., Shan, C. - M., Wang, J., Bao, K., Tong, L., and Jia, S. (2017) Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation. Sci Rep. 7, 43906
Zhang, W., Shi, K., Geng, Q., Herbst, M., Wang, M., Huang, L., Bu, F., Liu, B., Aihara, H., and Li, F. (2023) Structural evolution of SARS-CoV-2 omicron in human receptor recognition. J Virol. 97, e0082223
Zhang, J., Huang, J., Xu, K., Xing, P., Huang, Y., Liu, Z., Tong, L., and Manley, J. L. (2022) DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer. Proc Natl Acad Sci U S A. 119, e2216712119
Zhang, R., Li, X., and Boggon, T. J. (2015) Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface. J Struct Biol. 192, 449-56
Zhang, J., and Ferré-D'Amaré, A. R. (2013) Co-crystal structure of a T-box riboswitch stem I domain in complex with its cognate tRNA. Nature. 500, 363-6
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, 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, 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, Y., Secrist, J. A., and Ealick, S. E. (2006) The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activation. Acta Crystallogr D Biol Crystallogr. 62, 133-9
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, 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
Zhang, Y., Dougherty, M., Downs, D. M., and Ealick, S. E. (2004) Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily. Structure. 12, 1809-21
Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36
Zhang, Y., Colabroy, K. L., Begley, T. P., and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry. 44, 7632-43
Zhang, Y., Porcelli, M., Cacciapuoti, G., and Ealick, S. E. (2006) The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds. J Mol Biol. 357, 252-62

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