Publications

Found 858 results
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2018
Lv, Z., Yuan, L., Atkison, J. H., Williams, K. M., Vega, R., E Sessions, H., Divlianska, D. B., Davies, C., Chen, Y., and Olsen, S. K. (2018) Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme. Nat Commun. 9, 5145
Cosmanescu, F., Katsamba, P. S., Sergeeva, A. P., Ahlsen, G., Patel, S. D., Brewer, J. J., Tan, L., Xu, S., Xiao, Q., Nagarkar-Jaiswal, S., Nern, A., Bellen, H. J., S Zipursky, L., Honig, B., and Shapiro, L. (2018) Neuron-Subtype-Specific Expression, Interaction Affinities, and Specificity Determinants of DIP/Dpr Cell Recognition Proteins. Neuron. 100, 1385-1400.e6
Ragwan, E. R., Arai, E., and Kung, Y. (2018) New Crystallographic Snapshots of Large Domain Movements in Bacterial 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase. Biochemistry. 57, 5715-5725
Ribeiro, C. J. A., Kankanala, J., Shi, K., Kurahashi, K., Kiselev, E., Ravji, A., Pommier, Y., Aihara, H., and Wang, Z. (2018) New fluorescence-based high-throughput screening assay for small molecule inhibitors of tyrosyl-DNA phosphodiesterase 2 (TDP2). Eur J Pharm Sci. 118, 67-79
Pantel, L., Florin, T., Dobosz-Bartoszek, M., Racine, E., Sarciaux, M., Serri, M., Houard, J., Campagne, J. - M., de Figueiredo, R. Marcia, Midrier, C., Gaudriault, S., Givaudan, A., Lanois, A., Forst, S., Aumelas, A., Cotteaux-Lautard, C., Bolla, J. - M., Lundberg, C. Vingsbo, Huseby, D. L., Hughes, D., Villain-Guillot, P., Mankin, A. S., Polikanov, Y. S., and Gualtieri, M. (2018) Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site. Mol Cell. 70, 83-94.e7
Alex, J. M., Rennie, M. L., Volpi, S., Sansone, F., Casnati, A., and Crowley, P. B. (2018) Phosphonated Calixarene as a "€œMolecular Glue"€ for Protein Crystallization. Crystal Growth & DesignCryst. Growth Des. 18, 2467-2473
Nowak, R. P., DeAngelo, S. L., Buckley, D., He, Z., Donovan, K. A., An, J., Safaee, N., Jedrychowski, M. P., Ponthier, C. M., Ishoey, M., Zhang, T., Mancias, J. D., Gray, N. S., Bradner, J. E., and Fischer, E. S. (2018) Plasticity in binding confers selectivity in ligand-induced protein degradation. Nat Chem Biol. 10.1038/s41589-018-0055-y
Brown, K. L., Banerjee, S., Feigley, A., Abe, H., Blackwell, T. S., Pozzi, A., Hudson, B. G., and Zent, R. (2018) Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains.. Sci Rep. 8, 2916
Buzovetsky, O., Tang, C., Knecht, K. M., Antonucci, J. M., Wu, L., Ji, X., and Xiong, Y. (2018) The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Nat Commun. 9, 411
Wang, J., Erazo, T., Ferguson, F. M., Buckley, D. L., Gomez, N., Muñoz-Guardiola, P., Diéguez-Martínez, N., Deng, X., Hao, M., Massefski, W., Fedorov, O., Offei-Addo, N. Kwaku, Park, P. M., Dai, L., DiBona, A., Becht, K., Kim, N. Doo, McKeown, M. R., Roberts, J. M., Zhang, J., Sim, T., Alessi, D. R., Bradner, J. E., Lizcano, J. M., Blacklow, S. C., Qi, J., Xu, X., and Gray, N. S. (2018) Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 10.1021/acschembio.7b00638
Shelke, S. A., Shao, Y., Laski, A., Koirala, D., Weissman, B. P., Fuller, J. R., Tan, X., Constantin, T. P., Waggoner, A. S., Bruchez, M. P., Armitage, B. A., and Piccirilli, J. A. (2018) Structural basis for activation of fluorogenic dyes by an RNA aptamer lacking a G-quadruplex motif. Nat Commun. 9, 4542
Nithianantham, S., McNally, F. J., and Al-Bassam, J. (2018) Structural Basis for Disassembly of Katanin Heterododecamers. J Biol Chem. 10.1074/jbc.RA117.001215
Rechkoblit, O., Choudhury, J. Roy, Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2018) Structural basis for polymerase η-promoted resistance to the anticancer nucleoside analog cytarabine.. Sci Rep. 8, 12702
Omattage, N. S., Deng, Z., Pinkner, J. S., Dodson, K. W., Almqvist, F., Yuan, P., and Hultgren, S. J. (2018) Structural basis for usher activation and intramolecular subunit transfer in P pilus biogenesis in Escherichia coli. Nat Microbiol. 10.1038/s41564-018-0255-y
Ji, T., Zhang, C., Zheng, L., Dunaway-Mariano, D., and Allen, K. N. (2018) Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions. Biochemistry. 57, 3480-3492
Nithianantham, S., Cook, B. D., Beans, M., Guo, F., Chang, F., and Al-Bassam, J. (2018) Structural basis of tubulin recruitment and assembly by microtubule polymerases with Tumor Overexpressed Gene (TOG) domain arrays. Elife. 10.7554/eLife.38922
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410
Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Varlakhanova, N. V., Alvarez, F. J. D., Brady, T. M., Tornabene, B. A., Hosford, C. J., Chappie, J. S., Zhang, P., and Ford, M. G. J. (2018) Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. J Cell Biol. 10.1083/jcb.201712021
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
Mondal, S., Jacoby, G., Sawaya, M. R., Arnon, Z. A., Adler-Abramovich, L., Rehak, P., Vuković, L., Shimon, L. J. W., Král, P., Beck, R., and Gazit, E. (2018) Transition of metastable cross-α crystals into cross-β fibrils by β-turn flipping.. J Am Chem Soc. 10.1021/jacs.8b10289
Mondal, S., Jacoby, G., Sawaya, M. R., Arnon, Z. A., Adler-Abramovich, L., Rehak, P., Vuković, L., Shimon, L. J. W., Král, P., Beck, R., and Gazit, E. (2018) Transition of metastable cross-α crystals into cross-β fibrils by β-turn flipping.. J Am Chem Soc. 10.1021/jacs.8b10289

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