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Cui, H., Carlson, A. S., Schleiff, M. A., Divakaran, A., Johnson, J. A., Buchholz, C. R., Zahid, H., Vail, N. R., Shi, K., Aihara, H., Harki, D. A., Miller, G. P., Topczewski, J. J., and Pomerantz, W. C. K. (2021) 4-Methyl-1,2,3-Triazoles as -Acetyl-Lysine Mimics Afford Potent BET Bromodomain Inhibitors with Improved Selectivity. J Med Chem. 64, 10497-10511
A
Liu, Y., Esyunina, D., Olovnikov, I., Teplova, M., Kulbachinskiy, A., Aravin, A. A., and Patel, D. J. (2018) Accommodation of Helical Imperfections in Rhodobacter sphaeroides Argonaute Ternary Complexes with Guide RNA and Target DNA. Cell Rep. 24, 453-462
Bhardwaj, G., O'Connor, J., Rettie, S., Huang, Y. - H., Ramelot, T. A., Mulligan, V. Khipple, Alpkilic, G. Gokce, Palmer, J., Bera, A. K., Bick, M. J., Di Piazza, M., Li, X., Hosseinzadeh, P., Craven, T. W., Tejero, R., Lauko, A., Choi, R., Glynn, C., Dong, L., Griffin, R., van Voorhis, W. C., Rodriguez, J., Stewart, L., Montelione, G. T., Craik, D., and Baker, D. (2022) Accurate de novo design of membrane-traversing macrocycles. Cell. 10.1016/j.cell.2022.07.019
Lu-Culligan, W. J., Connor, L. J., Xie, Y., Ekundayo, B. E., Rose, B. T., Machyna, M., Pintado-Urbanc, A. P., Zimmer, J. T., Vock, I. W., Bhanu, N. V., King, M. C., Garcia, B. A., Bleichert, F., and Simon, M. D. (2023) Acetyl-methyllysine marks chromatin at active transcription start sites. Nature. 622, 173-179
Polikanov, Y. S., and Moore, P. B. (2015) Acoustic vibrations contribute to the diffuse scatter produced by ribosome crystals. Acta Crystallogr D Biol Crystallogr. 71, 2021-31
Pan, C., Zimmer, A., Shah, M., Huynh, M. Sang, Lai, C. Chieh- Lin, Sit, B., Hooda, Y., Curran, D. M., and Moraes, T. F. (2021) Actinobacillus utilizes a binding-protein dependent ABC transporter to acquire the active form of Vitamin B. J Biol Chem. 10.1016/j.jbc.2021.101046
Baranovskiy, A. G., Duong, V. N., Babayeva, N. D., Zhang, Y., Pavlov, Y. I., Anderson, K. S., and Tahirov, T. H. (2018) Activity and fidelity of human DNA polymerase α depend on primer structure.. J Biol Chem. 10.1074/jbc.RA117.001074
Rut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S. J., Oualid, F. El, Huang, T. T., Békés, M., Drag, M., and Olsen, S. K. (2020) Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design. Sci Adv. 10.1126/sciadv.abd4596
Koirala, D., Shelke, S. A., Dupont, M., Ruiz, S., DasGupta, S., Bailey, L. J., Benner, S. A., and Piccirilli, J. A. (2018) Affinity maturation of a portable Fab-RNA module for chaperone-assisted RNA crystallography. Nucleic Acids Res. 10.1093/nar/gkx1292
Wang, B., Dai, P., Ding, D., Del Rosario, A., Grant, R. A., Pentelute, B. L., and Laub, M. T. (2019) Affinity-based capture and identification of protein effectors of the growth regulator ppGpp. Nat Chem Biol. 15, 141-150
Pinger, J., Nešić, D., Ali, L., Aresta-Branco, F., Lilic, M., Chowdhury, S., Kim, H. - S., Verdi, J., Raper, J., Ferguson, M. A. J., F Papavasiliou, N., and C Stebbins, E. (2018) African trypanosomes evade immune clearance by O-glycosylation of the VSG surface coat. Nat Microbiol. 3, 932-938
Pinger, J., Nešić, D., Ali, L., Aresta-Branco, F., Lilic, M., Chowdhury, S., Kim, H. - S., Verdi, J., Raper, J., Ferguson, M. A. J., F Papavasiliou, N., and C Stebbins, E. (2018) African trypanosomes evade immune clearance by O-glycosylation of the VSG surface coat. Nat Microbiol. 3, 932-938
Ingram, J. R., Knockenhauer, K. E., Markus, B. M., Mandelbaum, J., Ramek, A., Shan, Y., Shaw, D. E., Schwartz, T. U., Ploegh, H. L., and Lourido, S. (2015) Allosteric activation of apicomplexan calcium-dependent protein kinases. Proc Natl Acad Sci U S A. 112, E4975-84
To, C., Beyett, T. S., Jang, J., Feng, W. W., Bahcall, M., Haikala, H. M., Shin, B. H., Heppner, D. E., Rana, J. K., Leeper, B. A., Soroko, K. M., Poitras, M. J., Gokhale, P. C., Kobayashi, Y., Wahid, K., Kurppa, K. J., Gero, T. W., Cameron, M. D., Ogino, A., Mushajiang, M., Xu, C., Zhang, Y., Scott, D. A., Eck, M. J., Gray, N. S., and Jänne, P. A. (2022) An allosteric inhibitor against the therapy-resistant mutant forms of EGFR in non-small cell lung cancer. Nat Cancer. 3, 402-417
Ceccarelli, D. F., Tang, X., Pelletier, B., Orlicky, S., Xie, W., Plantevin, V., Neculai, D., Chou, Y. - C., Ogunjimi, A., Al-Hakim, A., Varelas, X., Koszela, J., Wasney, G. A., Vedadi, M., Dhe-Paganon, S., Cox, S., Xu, S., Lopez-Girona, A., Mercurio, F., Wrana, J., Durocher, D., Meloche, S., Webb, D. R., Tyers, M., and Sicheri, F. (2011) An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme. Cell. 145, 1075-87
Ceccarelli, D. F., Tang, X., Pelletier, B., Orlicky, S., Xie, W., Plantevin, V., Neculai, D., Chou, Y. - C., Ogunjimi, A., Al-Hakim, A., Varelas, X., Koszela, J., Wasney, G. A., Vedadi, M., Dhe-Paganon, S., Cox, S., Xu, S., Lopez-Girona, A., Mercurio, F., Wrana, J., Durocher, D., Meloche, S., Webb, D. R., Tyers, M., and Sicheri, F. (2011) An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme. Cell. 145, 1075-87
Del Pino, G. L. Gonzalez, Li, K., Park, E., Schmoker, A. M., Ha, B. Hak, and Eck, M. J. (2021) Allosteric MEK inhibitors act on BRAF/MEK complexes to block MEK activation. Proc Natl Acad Sci U S A. 10.1073/pnas.2107207118
Gannam, Z. T. K., Min, K., Shillingford, S. R., Zhang, L., Herrington, J., Abriola, L., Gareiss, P. C., Pantouris, G., Tzouvelekis, A., Kaminski, N., Zhang, X., Yu, J., Jamali, H., Ellman, J. A., Lolis, E., Anderson, K. S., and Bennett, A. M. (2020) An allosteric site on MKP5 reveals a strategy for small-molecule inhibition. Sci Signal. 10.1126/scisignal.aba3043
Hobbs, K. F., Propp, J., Vance, N. R., Kalenkiewicz, A., Witkin, K. R., and M Spies, A. (2023) Allosteric Tuning of Caspase-7: Establishing the Nexus of Structure and Catalytic Power. Chemistry. 29, e202300872
Patrick, J. W., Boone, C. D., Liu, W., Conover, G. M., Liu, Y., Cong, X., and Laganowsky, A. (2018) Allostery revealed within lipid binding events to membrane proteins. Proc Natl Acad Sci U S A. 115, 2976-2981
Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., Bulkley, D., Malanicheva, I. A., Efimenko, T. A., Efremenkova, O. V., Konevega, A. L., Shaw, K. J., Bogdanov, A. A., Rodnina, M. V., Dontsova, O. A., Mankin, A. S., Steitz, T. A., and Sergiev, P. V. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Mol Cell. 56, 531-40
Sui, X., Kiser, P. D., Che, T., Carey, P. R., Golczak, M., Shi, W., von Lintig, J., and Palczewski, K. (2014) Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO). J Biol Chem. 289, 12286-99
J Y Wu, K., Tresco, B. I. C., Ramkissoon, A., Aleksandrova, E. V., Syroegin, E. A., N Y See, D., Liow, P., Dittemore, G. A., Yu, M., Testolin, G., Mitcheltree, M. J., Liu, R. Y., Svetlov, M. S., Polikanov, Y. S., and Myers, A. G. (2024) An antibiotic preorganized for ribosomal binding overcomes antimicrobial resistance. Science. 383, 721-726
Bulkley, D., Brandi, L., Polikanov, Y. S., Fabbretti, A., O'Connor, M., Gualerzi, C. O., and Steitz, T. A. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Rep. 6, 357-65
Liu, L., Iketani, S., Guo, Y., Casner, R. G., Reddem, E. R., Nair, M. S., Yu, J., Chan, J. F. - W., Wang, M., Cerutti, G., Li, Z., Morano, N. C., Castagna, C. D., Corredor, L., Chu, H., Yuan, S., Poon, V. Kwok- Man, Chan, C. Chun- Sing, Chen, Z., Luo, Y., Cunningham, M., Chavez, A., Yin, M. T., Perlin, D. S., Tsuji, M., Yuen, K. - Y., Kwong, P. D., Sheng, Z., Huang, Y., Shapiro, L., and Ho, D. D. (2022) An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses. Sci Transl Med. 10.1126/scitranslmed.abn6859

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