Publications

Found 125 results
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2020
Chitrakar, I., Iuliano, J. N., He, Y. L., Woroniecka, H. A., Collado, J. Tolentino, Wint, J. M., Walker, S. G., Tonge, P. J., and French, J. B. (2020) Structural Basis for the Regulation of Biofilm Formation and Iron Uptake in by the Blue-Light-Using Photoreceptor, BlsA. ACS Infect Dis. 6, 2592-2603
Duong, V. N., Ippolito, J. A., Chan, A. H., Lee, W. - G., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2020) Structural investigation of 2-naphthyl phenyl ether inhibitors bound to WT and Y181C reverse transcriptase highlights key features of the NNRTI binding site. Protein Sci. 10.1002/pro.3910
Indurthi, V. S. K., Jensen, J. L., Leclerc, E., Sinha, S., Colbert, C. L., and Vetter, S. W. (2020) The Trp triad within the V-domain of the receptor for advanced glycation end products modulates folding, stability and ligand binding. Biosci Rep. 10.1042/BSR20193360
2019
Mashalidis, E. H., Kaeser, B., Terasawa, Y., Katsuyama, A., Kwon, D. - Y., Lee, K., Hong, J., Ichikawa, S., and Lee, S. - Y. (2019) Chemical logic of MraY inhibition by antibacterial nucleoside natural products. Nat Commun. 10, 2917
Cai, X. - C., Zhang, T., Kim, E. - J., Jiang, M., Wang, K., Wang, J., Chen, S., Zhang, N., Wu, H., Li, F., Seña, C. C. Dela, Zeng, H., Vivcharuk, V., Niu, X., Zheng, W., Lee, J. P., Chen, Y., Barsyte, D., Szewczyk, M., Hajian, T., Ibáñez, G., Dong, A., Dombrovski, L., Zhang, Z., Deng, H., Min, J., Arrowsmith, C. H., Mazutis, L., Shi, L., Vedadi, M., Brown, P. J., Xiang, J., Qin, L. - X., Xu, W., and Luo, M. (2019) A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion. Elife. 10.7554/eLife.47110
Geldenhuys, W. J., Long, T. E., Saralkar, P., Iwasaki, T., Nuñez, R. A. A., Nair, R. R., Konkle, M. E., Menze, M. A., Pinti, M. V., Hollander, J. M., Hazlehurst, L. A., and Robart, A. R. (2019) Crystal structure of the mitochondrial protein mitoNEET bound to a benze-sulfonide ligand. Communications Chemistry. 2, 77
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749
Lama, L., Adura, C., Xie, W., Tomita, D., Kamei, T., Kuryavyi, V., Gogakos, T., Steinberg, J. I., Miller, M., Ramos-Espiritu, L., Asano, Y., Hashizume, S., Aida, J., Imaeda, T., Okamoto, R., Jennings, A. J., Michino, M., Kuroita, T., Stamford, A., Gao, P., Meinke, P., J Glickman, F., Patel, D. J., and Tuschl, T. (2019) Development of human cGAS-specific small-molecule inhibitors for repression of dsDNA-triggered interferon expression. Nat Commun. 10, 2261
Allali-Hassani, A., Szewczyk, M. M., Ivanochko, D., Organ, S. L., Bok, J., Ho, J. Sook Yuin, Gay, F. P. H., Li, F., Blazer, L., Eram, M. S., Halabelian, L., Dilworth, D., Luciani, G. M., Lima-Fernandes, E., Wu, Q., Loppnau, P., Palmer, N., S Talib, Z. A., Brown, P. J., Schapira, M., Kaldis, P., O'Hagan, R. C., Guccione, E., Barsyte-Lovejoy, D., Arrowsmith, C. H., Sanders, J. M., Kattar, S. D., D Bennett, J., Nicholson, B., and Vedadi, M. (2019) Discovery of a chemical probe for PRDM9. Nat Commun. 10, 5759
Ceccarelli, D. F., Ivantsiv, S., Mullin, A. Anne, Coyaud, E., Manczyk, N., Maisonneuve, P., Kurinov, I., Zhao, L., Go, C., Gingras, A. - C., Raught, B., Cordes, S., and Sicheri, F. (2019) FAM105A/OTULINL Is a Pseudodebuiquitinase of the OTU-Class that Localizes to the ER Membrane. Structure. 10.1016/j.str.2019.03.022
de Araujo, E. D., Erdogan, F., Neubauer, H. A., Meneksedag-Erol, D., Manaswiyoungkul, P., Eram, M. S., Seo, H. - S., Qadree, A. K., Israelian, J., Orlova, A., Suske, T., Pham, H. T. T., Boersma, A., Tangermann, S., Kenner, L., Rülicke, T., Dong, A., Ravichandran, M., Brown, P. J., Audette, G. F., Rauscher, S., Dhe-Paganon, S., Moriggl, R., and Gunning, P. T. (2019) Structural and functional consequences of the STAT5B driver mutation. Nat Commun. 10, 2517
2018
Iglesias, N., Currie, M. A., Jih, G., Paulo, J. A., Siuti, N., Kalocsay, M., Gygi, S. P., and Moazed, D. (2018) Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability. Nature. 560, 504-508
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

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