Publications

Found 1294 results
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A
G Hobbs, A., Baker, N. M., Miermont, A. M., Thurman, R. D., Pierobon, M., Tran, T. H., Anderson, A. O., Waters, A. M., J Diehl, N., Papke, B., Hodge, R. G., Klomp, J. E., Goodwin, C. M., DeLiberty, J. M., Wang, J., Ng, R. W. S., Gautam, P., Bryant, K. L., Esposito, D., Campbell, S. L., Petricoin, E. F., Simanshu, D. K., Aguirre, A. J., Wolpin, B. M., Wennerberg, K., Rudloff, U., Cox, A. D., and Der, C. J. (2019) Atypical KRASG12R Mutant Is Impaired in PI3K Signaling and Macropinocytosis in Pancreatic Cancer. Cancer Discov. 10.1158/2159-8290.CD-19-1006
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
Kasznel, A. J., Harris, T., Porter, N. J., Zhang, Y., and Chenoweth, D. M. (2019) Aza-proline effectively mimics l-proline stereochemistry in triple helical collagen. Chem Sci. 10, 6979-6983
Steimbach, R. R., Herbst-Gervasoni, C. J., Lechner, S., Stewart, T. Murray, Klinke, G., Ridinger, J., Géraldy, M. N. E., Tihanyi, G., Foley, J. R., Uhrig, U., Kuster, B., Poschet, G., Casero, R. A., Médard, G., Oehme, I., Christianson, D. W., Gunkel, N., and Miller, A. K. (2022) Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J Am Chem Soc. 144, 18861-18875
Steimbach, R. R., Herbst-Gervasoni, C. J., Lechner, S., Stewart, T. Murray, Klinke, G., Ridinger, J., Géraldy, M. N. E., Tihanyi, G., Foley, J. R., Uhrig, U., Kuster, B., Poschet, G., Casero, R. A., Médard, G., Oehme, I., Christianson, D. W., Gunkel, N., and Miller, A. K. (2022) Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J Am Chem Soc. 144, 18861-18875
B
Whiteley, A. T., Eaglesham, J. B., Mann, C. C. de Olive, Morehouse, B. R., Lowey, B., Nieminen, E. A., Danilchanka, O., King, D. S., S Y Lee, A., Mekalanos, J. J., and Kranzusch, P. J. (2019) Bacterial cGAS-like enzymes synthesize diverse nucleotide signals. Nature. 10.1038/s41586-019-0953-5
Whiteley, A. T., Eaglesham, J. B., Mann, C. C. de Olive, Morehouse, B. R., Lowey, B., Nieminen, E. A., Danilchanka, O., King, D. S., S Y Lee, A., Mekalanos, J. J., and Kranzusch, P. J. (2019) Bacterial cGAS-like enzymes synthesize diverse nucleotide signals. Nature. 10.1038/s41586-019-0953-5
Johnson, A. G., Wein, T., Mayer, M. L., Duncan-Lowey, B., Yirmiya, E., Oppenheimer-Shaanan, Y., Amitai, G., Sorek, R., and Kranzusch, P. J. (2022) Bacterial gasdermins reveal an ancient mechanism of cell death. Science. 375, 221-225
Brogan, A. P., Habib, C., Hobbs, S. J., Kranzusch, P. J., and Rudner, D. Z. (2023) Bacterial SEAL domains undergo autoproteolysis and function in regulated intramembrane proteolysis. Proc Natl Acad Sci U S A. 120, e2310862120
Kuo, A. J., Song, J., Cheung, P., Ishibe-Murakami, S., Yamazoe, S., Chen, J. K., Patel, D. J., and Gozani, O. (2012) The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome. Nature. 484, 115-9
Rosen, M. D., Venkatesan, H., Peltier, H. M., Bembenek, S. D., Kanelakis, K. C., Zhao, L. X., Leonard, B. E., Hocutt, F. M., Wu, X., Palomino, H. L., Brondstetter, T. I., Haugh, P. V., Cagnon, L., Yan, W., Liotta, L. A., Young, A., Mirzadegan, T., Shankley, N. P., Barrett, T. D., and Rabinowitz, M. H. (2010) Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Med Chem Lett. 1, 526-9
McKeown, M. R., Shaw, D. L., Fu, H., Liu, S., Xu, X., Marineau, J. J., Huang, Y., Zhang, X., Buckley, D. L., Kadam, A., Zhang, Z., Blacklow, S. C., Qi, J., Zhang, W., and Bradner, J. E. (2014) Biased multicomponent reactions to develop novel bromodomain inhibitors. J Med Chem. 57, 9019-27
Xia, S., Eom, S. Hyun, Konigsberg, W. H., and Wang, J. (2012) Bidentate and tridentate metal-ion coordination states within ternary complexes of RB69 DNA polymerase. Protein Sci. 21, 447-51
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
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
An, L., Said, M., Tran, L., Majumder, S., Goreshnik, I., Lee, G. Rie, Juergens, D., Dauparas, J., Anishchenko, I., Coventry, B., Bera, A. K., Kang, A., Levine, P. M., Alvarez, V., Pillai, A., Norn, C., Feldman, D., Zorine, D., Hicks, D. R., Li, X., Sanchez, M. Garcia, Vafeados, D. K., Salveson, P. J., Vorobieva, A. A., and Baker, D. (2024) Binding and sensing diverse small molecules using shape-complementary pseudocycles. Science. 385, 276-282
Jonnalagadda, R., Flores, A. Del Rio, Cai, W., Mehmood, R., Narayanamoorthy, M., Ren, C., Zaragoza, J. Paulo T., Kulik, H. J., Zhang, W., and Drennan, C. L. (2020) Biochemical and crystallographic investigations into isonitrile formation by a non-heme iron-dependent oxidase/decarboxylase. J Biol Chem. 10.1074/jbc.RA120.015932
Korasick, D. A., Singh, H., Pemberton, T. A., Luo, M., Dhatwalia, R., and Tanner, J. J. (2017) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
Kelso, S., Orlicky, S., Beenstock, J., Ceccarelli, D. F., Kurinov, I., Gish, G., and Sicheri, F. (2021) Bipartite binding of the N terminus of Skp2 to cyclin A. Structure. 10.1016/j.str.2021.04.011
Kelso, S., Orlicky, S., Beenstock, J., Ceccarelli, D. F., Kurinov, I., Gish, G., and Sicheri, F. (2021) Bipartite binding of the N terminus of Skp2 to cyclin A. Structure. 10.1016/j.str.2021.04.011
Fischer, P. D., Papadopoulos, E., Dempersmier, J. M., Wang, Z. - F., Nowak, R. P., Donovan, K. A., Kalabathula, J., Gorgulla, C., Junghanns, P. P. M., Kabha, E., Dimitrakakis, N., Petrov, O. I., Mitsiades, C., Ducho, C., Gelev, V., Fischer, E. S., Wagner, G., and Arthanari, H. (2021) A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders. Eur J Med Chem. 219, 113435
Fischer, P. D., Papadopoulos, E., Dempersmier, J. M., Wang, Z. - F., Nowak, R. P., Donovan, K. A., Kalabathula, J., Gorgulla, C., Junghanns, P. P. M., Kabha, E., Dimitrakakis, N., Petrov, O. I., Mitsiades, C., Ducho, C., Gelev, V., Fischer, E. S., Wagner, G., and Arthanari, H. (2021) A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders. Eur J Med Chem. 219, 113435

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