Publications

Found 138 results
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2018
Rothé, B., Leettola, C. N., Leal-Esteban, L., Cascio, D., Fortier, S., Isenschmid, M., Bowie, J. U., and Constam, D. B. (2018) Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6. Structure. 10.1016/j.str.2017.12.002
Ivanochko, D., Halabelian, L., Henderson, E., Savitsky, P., Jain, H., Marcon, E., Duan, S., Hutchinson, A., Seitova, A., Barsyte-Lovejoy, D., Filippakopoulos, P., Greenblatt, J., Lima-Fernandes, E., and Arrowsmith, C. H. (2018) Direct interaction between the PRDM3 and PRDM16 tumor suppressors and the NuRD chromatin remodeling complex. Nucleic Acids Res. 10.1093/nar/gky1192
Kono, M., Ochida, A., Oda, T., Imada, T., Banno, Y., Taya, N., Masada, S., Kawamoto, T., Yonemori, K., Nara, Y., Fukase, Y., Yukawa, T., Tokuhara, H., Skene, R., Sang, B. - C., Hoffman, I. D., Snell, G. P., Uga, K., Shibata, A., Igaki, K., Nakamura, Y., Nakagawa, H., Tsuchimori, N., Yamasaki, M., Shirai, J., and Yamamoto, S. (2018) Discovery of [cis-3-({(5 R)-5-[(7-Fluoro-1,1-dimethyl-2,3-dihydro-1H-inden-5-yl)carbamoyl]-2-methoxy-7,8-dihydro-1,6-naphthyridin-6(5H)-yl}carbonyl)cyclobutyl]acetic Acid (TAK-828F) as a Potent Selective and Orally Available Novel Retinoic Acid Receptor-R. J Med Chem. 10.1021/acs.jmedchem.8b00061
Kono, M., Ochida, A., Oda, T., Imada, T., Banno, Y., Taya, N., Masada, S., Kawamoto, T., Yonemori, K., Nara, Y., Fukase, Y., Yukawa, T., Tokuhara, H., Skene, R., Sang, B. - C., Hoffman, I. D., Snell, G. P., Uga, K., Shibata, A., Igaki, K., Nakamura, Y., Nakagawa, H., Tsuchimori, N., Yamasaki, M., Shirai, J., and Yamamoto, S. (2018) Discovery of [cis-3-({(5 R)-5-[(7-Fluoro-1,1-dimethyl-2,3-dihydro-1H-inden-5-yl)carbamoyl]-2-methoxy-7,8-dihydro-1,6-naphthyridin-6(5H)-yl}carbonyl)cyclobutyl]acetic Acid (TAK-828F) as a Potent Selective and Orally Available Novel Retinoic Acid Receptor-R. J Med Chem. 10.1021/acs.jmedchem.8b00061
Do, T. D., Sangwan, S., de Almeida, N. E. C., Ilitchev, A. I., Giammona, M., Sawaya, M. R., Buratto, S. K., Eisenberg, D. S., and Bowers, M. T. (2018) Distal Amyloid β-Protein Fragments Template Amyloid Assembly.. Protein Sci. 10.1002/pro.3375
Yoo, J., Mashalidis, E. H., C Y Kuk, A., Yamamoto, K., Kaeser, B., Ichikawa, S., and Lee, S. - Y. (2018) GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation. Nat Struct Mol Biol. 10.1038/s41594-018-0031-y
Ray, L. C., Das, D., Entova, S., Lukose, V., Lynch, A. J., Imperiali, B., and Allen, K. N. (2018) Membrane association of monotopic phosphoglycosyl transferase underpins function. Nat Chem Biol. 10.1038/s41589-018-0054-z
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
Fontán, L., Qiao, Q., Hatcher, J. M., Casalena, G., Us, I., Teater, M., Durant, M., Du, G., Xia, M., Bilchuk, N., Chennamadhavuni, S., Palladino, G., Inghirami, G., Philippar, U., Wu, H., Scott, D. A., Gray, N. S., and Melnick, A. (2018) Specific covalent inhibition of MALT1 paracaspase suppresses B cell lymphoma growth. J Clin Invest. 128, 4397-4412
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
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
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
2017
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Kim, S. Kyung, Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., Richter, B., Kodali, R., Taylor, A. B., Du, S., Barnes, C. O., Sulea, T., Calero, G., P Hart, J., Hart, M. J., Demeler, B., and Hinck, A. P. (2017) An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.. J Biol Chem. 292, 7173-7188
Orlova, N., Gerding, M., Ivashkiv, O., Olinares, P. Dominic B., Chait, B. T., Waldor, M. K., and Jeruzalmi, D. (2017) The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators. Nucleic Acids Res. 45, 3724-3737
Buzovetsky, O., Kwon, Y., Pham, N. Tuyet, Kim, C., Ira, G., Sung, P., and Xiong, Y. (2017) Role of the Pif1-PCNA Complex in Pol δ-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication.. Cell Rep. 21, 1707-1714
Vincent, J., Adura, C., Gao, P., Luz, A., Lama, L., Asano, Y., Okamoto, R., Imaeda, T., Aida, J., Rothamel, K., Gogakos, T., Steinberg, J., Reasoner, S., Aso, K., Tuschl, T., Patel, D. J., J Glickman, F., and Ascano, M. (2017) Small molecule inhibition of cGAS reduces interferon expression in primary macrophages from autoimmune mice. Nat Commun. 8, 750
Lanier, M., Pickens, J., Bigi, S. V., Bradshaw-Pierce, E. L., Chambers, A., Cheruvallath, Z. S., Cole, D., Dougan, D. R., Ermolieff, J., Gibson, T., Halkowycz, P., Hirokawa, A., Ivetac, A., Miura, J., Nunez, E., Sabat, M., Tyhonas, J., Wang, H., Wang, X., and Swann, S. (2017) Structure-Based Design of ASK1 Inhibitors as Potential Agents for Heart Failure. ACS Med Chem Lett. 8, 316-320
Lamberto, I., Liu, X., Seo, H. - S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., Anderson, K. C., Chauhan, D., Dhe-Paganon, S., and Buhrlage, S. J. (2017) Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7. Cell Chem Biol. 10.1016/j.chembiol.2017.09.003
De Schutter, J. W., Morrison, J. P., Morrison, M. J., Ciulli, A., and Imperiali, B. (2017) Targeting Bacillosamine Biosynthesis in Bacterial Pathogens: Development of Inhibitors to a Bacterial Amino-Sugar Acetyltransferase from Campylobacter jejuni. J Med Chem. 60, 2099-2118
2016
Valverde, R., Ingram, J., and Harrison, S. C. (2016) Conserved Tetramer Junction in the Kinetochore Ndc80 Complex. Cell Rep. 17, 1915-1922
Li, L., Park, E., Ling, J. J., Ingram, J., Ploegh, H., and Rapoport, T. A. (2016) Crystal structure of a substrate-engaged SecY protein-translocation channel. Nature. 531, 395-399
Taylor, N. D., Garruss, A. S., Moretti, R., Chan, S., Arbing, M. A., Cascio, D., Rogers, J. K., Isaacs, F. J., Kosuri, S., Baker, D., Fields, S., Church, G. M., and Raman, S. (2016) Engineering an allosteric transcription factor to respond to new ligands. Nat Methods. 13, 177-83
Saredi, G., Huang, H., Hammond, C. M., Alabert, C., Bekker-Jensen, S., Forne, I., Reverón-Gómez, N., Foster, B. M., Mlejnkova, L., Bartke, T., Cejka, P., Mailand, N., Imhof, A., Patel, D. J., and Groth, A. (2016) H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex.. Nature. 534, 714-718
Raymond, D. D., Stewart, S. M., Lee, J., Ferdman, J., Bajic, G., Do, K. T., Ernandes, M. J., Suphaphiphat, P., Settembre, E. C., Dormitzer, P. R., Del Giudice, G., Finco, O., Kang, T. Hyun, Ippolito, G. C., Georgiou, G., Kepler, T. B., Haynes, B. F., M Moody, A., Liao, H. - X., Schmidt, A. G., and Harrison, S. C. (2016) Influenza immunization elicits antibodies specific for an egg-adapted vaccine strain. Nat Med. 22, 1465-1469

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