Publications

Found 1619 results
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2018
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
Emptage, R. P., Lemmon, M. A., Ferguson, K. M., and Marmorstein, R. (2018) Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Structure. 26, 1137-1143.e3
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
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
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
Miller, B. R., and Kung, Y. (2018) Structural insight into substrate and product binding in an archaeal mevalonate kinase. PLoS One. 13, e0208419
Zhu, S. - J., Zhao, P., Yang, J., Ma, R., Yan, X. - E., Yang, S. - Y., Yang, J. - W., and Yun, C. -hong (2018) Structural insights into drug development strategy targeting EGFR T790M/C797S. Oncotarget. 9, 13652-13665
Rivera, S., Young, P. G., Hoffer, E. D., Vansuch, G. E., Metzler, C. L., Dunham, C. M., and Weinert, E. E. (2018) Structural Insights into Oxygen-Dependent Signal Transduction within Globin Coupled Sensors. Inorg Chem. 57, 14386-14395
Ren, Z., Lee, J., Moosa, M. Muhammad, Nian, Y., Hu, L., Xu, Z., McCoy, J. G., Ferreon, A. Chris M., Im, W., and Zhou, M. (2018) Structure of an EIIC sugar transporter trapped in an inward-facing conformation. Proc Natl Acad Sci U S A. 10.1073/pnas.1800647115
Ren, Z., Lee, J., Moosa, M. Muhammad, Nian, Y., Hu, L., Xu, Z., McCoy, J. G., Ferreon, A. Chris M., Im, W., and Zhou, M. (2018) Structure of an EIIC sugar transporter trapped in an inward-facing conformation. Proc Natl Acad Sci U S A. 10.1073/pnas.1800647115
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
Gottlieb, L., and Marmorstein, R. (2018) Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. Structure. 10.1016/j.str.2018.04.003
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
Zhou, W., Whiteley, A. T., Mann, C. C. de Olive, Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., and Kranzusch, P. J. (2018) Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance. Cell. 174, 300-311.e11
Zhou, W., Whiteley, A. T., Mann, C. C. de Olive, Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., and Kranzusch, P. J. (2018) Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance. Cell. 174, 300-311.e11
Zhou, W., Whiteley, A. T., Mann, C. C. de Olive, Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., and Kranzusch, P. J. (2018) Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance. Cell. 174, 300-311.e11
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
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
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
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
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
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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