Publications

Found 2720 results
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2018
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Zhang, Z. - M., Lu, R., Wang, P., Yu, Y., Chen, D., Gao, L., Liu, S., Ji, D., Rothbart, S. B., Wang, Y., Wang, G. Greg, and Song, J. (2018) Structural basis for DNMT3A-mediated de novo DNA methylation. Nature. 554, 387-391
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
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
Reimer, J. M., Harb, I., Ovchinnikova, O. G., Jiang, J., Whitfield, C., and T Schmeing, M. (2018) Structural Insight into a Novel Formyltransferase and Evolution to a Nonribosomal Peptide Synthetase Tailoring Domain. ACS Chem Biol. 10.1021/acschembio.8b00739
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
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
Banerjee, A., Ghosh, S., Goldgur, Y., and Shuman, S. (2018) Structure and two-metal mechanism of fungal tRNA ligase. Nucleic Acids Res. 10.1093/nar/gky1275
Nayak, D., and Sivaraman, J. (2018) Structure of LNX1:Ubc13~Ubiquitin complex reveals the role of additional motifs for the E3 ligase activity of LNX1. J Mol Biol. 10.1016/j.jmb.2018.02.016
Ge, J., Elferich, J., Goehring, A., Zhao, H., Schuck, P., and Gouaux, E. (2018) Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. Elife. 10.7554/eLife.38770
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
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Brown, B. L., Kardon, J. R., Sauer, R. T., and Baker, T. A. (2018) Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure. 10.1016/j.str.2018.02.012
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017
Mompeán, M., Li, W., Li, J., Laage, S., Siemer, A. B., Bozkurt, G., Wu, H., and McDermott, A. E. (2018) The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. Cell. 173, 1244-1253.e10
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
Gorelik, M., Manczyk, N., Pavlenco, A., Kurinov, I., Sidhu, S. S., and Sicheri, F. (2018) A Structure-Based Strategy for Engineering Selective Ubiquitin Variant Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases. Structure. 10.1016/j.str.2018.06.004
Gorelik, M., Manczyk, N., Pavlenco, A., Kurinov, I., Sidhu, S. S., and Sicheri, F. (2018) A Structure-Based Strategy for Engineering Selective Ubiquitin Variant Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases. Structure. 10.1016/j.str.2018.06.004
Xing, Q., Shi, K., Portaliou, A., Rossi, P., Economou, A., and Kalodimos, C. G. (2018) Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. Nat Commun. 9, 1773
Knappenberger, A. John, Reiss, C. Wetheringt, and Strobel, S. A. (2018) Structures of two aptamers with differing ligand specificity reveal ruggedness in the functional landscape of RNA. Elife. 10.7554/eLife.36381
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
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

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