Publications

Found 2819 results
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
A
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Sohn, J., Grant, R. A., and Sauer, R. T. (2007) Allosteric activation of DegS, a stress sensor PDZ protease. Cell. 131, 572-83
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
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
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
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
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
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
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
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

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