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Sinha, S., Cheng, S., Sung, Y. Won, McNamara, D. E., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2014) Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J Mol Biol. 426, 2328-45
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
Sohn, J., Grant, R. A., and Sauer, R. T. (2007) Allosteric activation of DegS, a stress sensor PDZ protease. Cell. 131, 572-83
Wojcik, J., Lamontanara, A. Joaquim, Grabe, G., Koide, A., Akin, L., Gerig, B., Hantschel, O., and Koide, S. (2016) Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface. J Biol Chem. 291, 8836-47
Primi, M. C., Tavares, M. T., Hatcher, J. M., Kang, H., Kresina, T. A. C., Chakraborty, S., Leroy, E., Schmoker, A. M., Jeon, H., Weisberg, E. L., Akatsu, T., Griffin, J. D., Scott, D. A., and Eck, M. J. (2025) Allosteric inhibition of JAK2 with lysine-reactive compounds that bind the pseudokinase domain. Eur J Med Chem. 302, 118274
Yildiz, M., Ghosh, S., Bell, J. A., Sherman, W., and Hardy, J. A. (2013) Allosteric inhibition of the NS2B-NS3 protease from dengue virus. ACS Chem Biol. 8, 2744-52
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
Zhang, Z. - M., Rothbart, S. B., Allison, D. F., Cai, Q., Harrison, J. S., Li, L., Wang, Y., Strahl, B. D., Wang, G. Greg, and Song, J. (2015) An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1. Cell Rep. 12, 1400-6
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
Thompson, M. C., Cascio, D., Leibly, D. J., and Yeates, T. O. (2015) An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein. Protein Sci. 24, 956-75
Yang, M. Hee, Tran, T. H., Hunt, B., Agnor, R., Johnson, C. W., Shui, B., Waybright, T. J., Nowak, J. A., Stephen, A. G., Simanshu, D. K., and Haigis, K. M. (2023) Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity. Cancer Res. 83, 3176-3183
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
Sohn, J., Grant, R. A., and Sauer, R. T. (2010) Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. J Biol Chem. 285, 34039-47
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
Miller, J. E., Agdanowski, M. P., Dolinsky, J. L., Sawaya, M. R., Cascio, D., Rodriguez, J. A., and Yeates, T. O. (2024) AlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallography. Acta Crystallogr D Struct Biol. 80, 270-278
Xia, S., Wood, M., Bradley, M. J., De La Cruz, E. M., and Konigsberg, W. H. (2013) Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Res. 41, 9077-89
Clancy-Thompson, E., Devlin, C. A., Tyler, P. M., Servos, M. M., Ali, L. R., Ventre, K. S., M Bhuiyan, A., Bruck, P. T., Birnbaum, M. E., and Dougan, S. K. (2018) Altered Binding of Tumor Antigenic Peptides to MHC Class I Affects CD8 T Cell-Effector Responses. Cancer Immunol Res. 6, 1524-1536
Oruganti, S., Zhang, Y., Li, H., Robinson, H., Terns, M. P., Terns, R. M., Yang, W., and Li, H. (2007) Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. J Mol Biol. 371, 1141-50
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
Cheng, P. - N., Liu, C., Zhao, M., Eisenberg, D., and Nowick, J. S. (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.. Nat Chem. 4, 927-33
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
Andorfer, M. C., Evans, D., Yang, S., He, C. Qixin, Girlich, A. M., Vergara-Coll, J., Sukumar, N., Houk, K. N., and Lewis, J. C. (2022) Analysis of Laboratory-Evolved Flavin-Dependent Halogenases Affords a Computational Model for Predicting Halogenase Site Selectivity. Chem Catal. 2, 2658-2674
Tsai, Y., Sawaya, M. R., and Yeates, T. O. (2009) Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr D Biol Crystallogr. 65, 980-8

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