Publications

Found 1344 results
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2018
Diver, M. M., Pedi, L., Koide, A., Koide, S., and Long, S. B. (2018) Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature. 10.1038/nature25439
Zhang, Y., Kittredge, A., Ward, N., Ji, C., Chen, S., and Yang, T. (2018) ATP activates bestrophin ion channels through direct interaction. Nat Commun. 9, 3126
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
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Gunaratne, R., Kumar, S., Frederiksen, J. W., Stayrook, S., Lohrmann, J. L., Perry, K., Bompiani, K. M., Chabata, C. V., Thalji, N. K., Ho, M. D., Arepally, G., Camire, R. M., Krishnaswamy, S., and Sullenger, B. A. (2018) Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass. Nat Biotechnol. 10.1038/nbt.4153
Gunaratne, R., Kumar, S., Frederiksen, J. W., Stayrook, S., Lohrmann, J. L., Perry, K., Bompiani, K. M., Chabata, C. V., Thalji, N. K., Ho, M. D., Arepally, G., Camire, R. M., Krishnaswamy, S., and Sullenger, B. A. (2018) Combination of aptamer and drug for reversible anticoagulation in cardiopulmonary bypass. Nat Biotechnol. 10.1038/nbt.4153
Rudolph, M. J., Vance, D. J., Kelow, S., Angalakurthi, S. Krishna, Nguyen, S., Davis, S. A., Rong, Y., C Middaugh, R., Weis, D. D., Dunbrack, R., Karanicolas, J., and Mantis, N. J. (2018) Contribution of an unusual CDR2 element of a single domain antibody in ricin toxin binding affinity and neutralizing activity. Protein Eng Des Sel. 10.1093/protein/gzy022
Rudolph, M. J., Vance, D. J., Kelow, S., Angalakurthi, S. Krishna, Nguyen, S., Davis, S. A., Rong, Y., C Middaugh, R., Weis, D. D., Dunbrack, R., Karanicolas, J., and Mantis, N. J. (2018) Contribution of an unusual CDR2 element of a single domain antibody in ricin toxin binding affinity and neutralizing activity. Protein Eng Des Sel. 10.1093/protein/gzy022
Kurniawan, F., Shi, K., Kurahashi, K., Bielinsky, A. - K., and Aihara, H. (2018) Crystal Structure of Cdc45 Suggests a Conformational Switch that May Regulate DNA Replication. iScience. 3, 102-109
Kurniawan, F., Shi, K., Kurahashi, K., Bielinsky, A. - K., and Aihara, H. (2018) Crystal Structure of Cdc45 Suggests a Conformational Switch that May Regulate DNA Replication. iScience. 3, 102-109
Lee, J. K., Bosnakovski, D., Toso, E. A., Dinh, T., Banerjee, S., Bohl, T. E., Shi, K., Orellana, K., Kyba, M., and Aihara, H. (2018) Crystal Structure of the Double Homeodomain of DUX4 in Complex with DNA. Cell Rep. 25, 2955-2962.e3
Trachman, R. J., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2018) Crystal Structures of the Mango-II RNA Aptamer Reveal Heterogeneous Fluorophore Binding and Guide Engineering of Variants with Improved Selectivity and Brightness. Biochemistry. 57, 3544-3548
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Guagnini, F., Antonik, P. M., Rennie, M. L., O'Byrne, P., Khan, A. R., Pinalli, R., Dalcanale, E., and Crowley, P. B. (2018) Cucurbit[7]uril-Dimethyllysine Recognition in a Model Protein. Angew Chem Int Ed Engl. 10.1002/anie.201803232
Rugel, A., Tarpley, R. S., Lopez, A., Menard, T., Guzman, M. A., Taylor, A. B., Cao, X., Kovalskyy, D., Chevalier, F. D., Anderson, T. J. C., P Hart, J., LoVerde, P. T., and McHardy, S. F. (2018) Design, Synthesis, and Characterization of Novel Small Molecules as Broad Range Antischistosomal Agents. ACS Med Chem Lett. 9, 967-973
Jang, J., Son, J., Park, E., Kosaka, T., Saxon, J. A., De Clercq, D. J. H., Choi, H. Geun, Tanizaki, J., Eck, M. J., Jänne, P. A., and Gray, N. S. (2018) Discovery of a Highly Potent and Broadly Effective Epidermal Growth Factor Receptor and HER2 Exon 20 Insertion Mutant Inhibitor. Angew Chem Int Ed Engl. 57, 11629-11633
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
Assadieskandar, A., Yu, C., Maisonneuve, P., Liu, X., Chen, Y. - C., Prakash, G. K. Surya, Kurinov, I., Sicheri, F., and Zhang, C. (2018) Effects of rigidity on the selectivity of protein kinase inhibitors. Eur J Med Chem. 146, 519-528
Mukherjee, S., Griffin, D. H., Horn, J. R., Rizk, S. S., Nocula-Lugowska, M., Malmqvist, M., Kim, S. S., and Kossiakoff, A. A. (2018) Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.. J Biol Chem. 10.1074/jbc.RA117.000656
Mukherjee, S., Griffin, D. H., Horn, J. R., Rizk, S. S., Nocula-Lugowska, M., Malmqvist, M., Kim, S. S., and Kossiakoff, A. A. (2018) Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins.. J Biol Chem. 10.1074/jbc.RA117.000656
Kearney, C., Olenginski, L. T., Hirn, T. D., Fowler, G. D., Tariq, D., Brewer, S. H., and Phillips-Piro, C. M. (2018) Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine. RSC Adv. 8, 13503-13512

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