Publications

Found 2704 results
Journal Article
Dawson, T. K., Dziedzic, P., Robertson, M. J., Cisneros, J. A., Krimmer, S. G., Newton, A. S., Tirado-Rives, J., and Jorgensen, W. L. (2017) Adding a Hydrogen Bond May Not Help: Naphthyridinone vs Quinoline Inhibitors of Macrophage Migration Inhibitory Factor. ACS Med Chem Lett. 8, 1287-1291
Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Zhou, Q., Zhao, M., Brewster, A. S., Michels-Clark, T., Holton, J. M., Sauter, N. K., Weis, W. I., and Brunger, A. T. (2016) Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex. Elife. 10.7554/eLife.18740
McCarthy, K. R., Raymond, D. D., Do, K. T., Schmidt, A. G., and Harrison, S. C. (2019) Affinity maturation in a human humoral response to influenza hemagglutinin. Proc Natl Acad Sci U S A. 10.1073/pnas.1915620116
Fera, D., Schmidt, A. G., Haynes, B. F., Gao, F., Liao, H. - X., Kepler, T. B., and Harrison, S. C. (2014) Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains. Proc Natl Acad Sci U S A. 111, 10275-80
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
Ivanova, M. I., Sievers, S. A., Guenther, E. L., Johnson, L. M., Winkler, D. D., Galaleldeen, A., Sawaya, M. R., P Hart, J., and Eisenberg, D. S. (2014) Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS. Proc Natl Acad Sci U S A. 111, 197-201
Qiao, Q., Wang, L., Meng, F. - L., Hwang, J. K., Alt, F. W., and Wu, H. (2017) AID Recognizes Structured DNA for Class Switch Recombination. Mol Cell. 67, 361-373.e4
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
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
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

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