Publications

Found 1675 results
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2018
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
Coleman, J. A., and Gouaux, E. (2018) Structural basis for recognition of diverse antidepressants by the human serotonin transporter. Nat Struct Mol Biol. 10.1038/s41594-018-0026-8
Chen, P., Tao, L., Wang, T., Zhang, J., He, A., Lam, K. - H., Liu, Z., He, X., Perry, K., Dong, M., and Jin, R. (2018) Structural basis for recognition of frizzled proteins by toxin B. Science. 360, 664-669
Chan, R. T., Peters, J. K., Robart, A. R., Wiryaman, T., Rajashankar, K. R., and Toor, N. (2018) Structural basis for the second step of group II intron splicing. Nat Commun. 9, 4676
Wang, W., Chen, X., Wolin, S. L., and Xiong, Y. (2018) Structural Basis for tRNA Mimicry by a Bacterial Y RNA. Structure. 10.1016/j.str.2018.09.001
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
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
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
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
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Jobichen, C., Chong, T. Ying, Prabhakar, M. Tirumuru, Nayak, D., Biswas, D., Pannu, N. Singh, Hanski, E., and Sivaraman, J. (2018) Structure of ScpC, a virulence protease from , reveal the functional domains and maturation mechanism. Biochem J. 10.1042/BCJ20180145
Cheung, J., Mahmood, A., Kalathur, R., Liu, L., and Carlier, P. R. (2018) Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance. Structure. 26, 130-136.e2
Cheung, J., Mahmood, A., Kalathur, R., Liu, L., and Carlier, P. R. (2018) Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance. Structure. 26, 130-136.e2
Sanghai, Z. Assur, Liu, Q., Clarke, O. B., Belcher-Dufrisne, M., Wiriyasermkul, P., M Giese, H., Leal-Pinto, E., Kloss, B., Tabuso, S., Love, J., Punta, M., Banerjee, S., Rajashankar, K. R., Rost, B., Logothetis, D., Quick, M., Hendrickson, W. A., and Mancia, F. (2018) Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife. 10.7554/eLife.27829
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
Lee, S., Choi, J., Mohanty, J., Sousa, L. P., Tome, F., Pardon, E., Steyaert, J., Lemmon, M. A., Lax, I., and Schlessinger, J. (2018) Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.. Nature. 10.1038/nature25010
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0
Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J., and Palczewski, K. (2018) Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 9, 1996
Chen, Y., Bensing, B. A., Seepersaud, R., Mi, W., Liao, M., Jeffrey, P. D., Shajahan, A., Sonon, R. N., Azadi, P., Sullam, P. M., and Rapoport, T. A. (2018) Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from. J Biol Chem. 10.1074/jbc.RA117.000963
Clark, L. E., Mahmutovic, S., Raymond, D. D., Dilanyan, T., Koma, T., Manning, J. T., Shankar, S., Levis, S. C., Briggiler, A. M., Enria, D. A., Wucherpfennig, K. W., Paessler, S., and Abraham, J. (2018) Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses. Nat Commun. 9, 1884
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Jaiganesh, A., De-la-Torre, P., Patel, A. A., Termine, D. J., Velez-Cortes, F., Chen, C., and Sotomayor, M. (2018) Zooming in on Cadherin-23: Structural Diversity and Potential Mechanisms of Inherited Deafness. Structure. 10.1016/j.str.2018.06.003
Chen, G., Liu, Y., Goetz, R., Fu, L., Jayaraman, S., Hu, M. - C., Moe, O. W., Liang, G., Li, X., and Mohammadi, M. (2018) α-Klotho is a non-enzymatic molecular scaffold for FGF23 hormone signalling.. Nature. 10.1038/nature25451
2017
Ye, Q., Kim, D. Hyun, Dereli, I., Rosenberg, S. C., Hagemann, G., Herzog, F., Tóth, A., Cleveland, D. W., and Corbett, K. D. (2017) The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding. EMBO J. 10.15252/embj.201797291

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