Publications

Found 575 results
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2018
Chen, W., Mandali, S., Hancock, S. P., Kumar, P., Collazo, M., Cascio, D., and Johnson, R. C. (2018) Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS-family transposition. Elife. 10.7554/eLife.39611
Jenson, J. M., Xue, V., Stretz, L., Mandal, T., Reich, L. Luther, and Keating, A. E. (2018) Peptide design by optimization on a data-parameterized protein interaction landscape. Proc Natl Acad Sci U S A. 115, E10342-E10351
Hand, T. H., Das, A., Roth, M. O., Smith, C. L., Jean-Baptiste, U. L., and Li, H. (2018) Phosphate Lock Residues of Acidothermus cellulolyticus Cas9 Are Critical to Its Substrate Specificity. ACS Synth Biol. 7, 2908-2917
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
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
Papp-Wallace, K. M., Nguyen, N. Q., Jacobs, M. R., Bethel, C. R., Barnes, M. D., Kumar, V., Bajaksouzian, S., Rudin, S. D., Rather, P. N., Bhavsar, S., Ravikumar, T., Deshpande, P. K., Patil, V., Yeole, R., Bhagwat, S. S., Patel, M. V., van den Akker, F., and Bonomo, R. A. (2018) Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.. J Med Chem. 61, 4067-4086
Lam, K. - H., Sikorra, S., Weisemann, J., Maatsch, H., Perry, K., Rummel, A., Binz, T., and Jin, R. (2018) Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA. Pathog Dis. 10.1093/femspd/fty044
Xiong, S., Lorenzen, K., Couzens, A. L., Templeton, C. M., Rajendran, D., Mao, D. Y. L., Juang, Y. - C., Chiovitti, D., Kurinov, I., Guettler, S., Gingras, A. - C., and Sicheri, F. (2018) Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment. Structure. 26, 1101-1115.e6
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
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
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
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
Huang, J., Dey, R., Wang, Y., Jakoncic, J., Kurinov, I., and Huang, X. - Y. (2018) Structural Insights into the Induced-fit Inhibition of Fascin by a Small-Molecule Inhibitor. J Mol Biol. 10.1016/j.jmb.2018.03.009
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
Jenni, S., and Harrison, S. C. (2018) Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface. Science. 360, 552-558
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
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
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
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
Lam, K. - H., Guo, Z., Krez, N., Matsui, T., Perry, K., Weisemann, J., Rummel, A., Bowen, M. E., and Jin, R. (2018) A viral-fusion-peptide-like molecular switch drives membrane insertion of botulinum neurotoxin A1. Nat Commun. 9, 5367
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

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