Publications

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Setser, J. Wayne (2014) Conformational Dynamics Control Catalysis in Disparate Systems: Structural Insights from DNA Repair and Antibiotic Biosynthetic Enzymes. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, MA
Wang, W., Liu, Q., Liu, Q., and Hendrickson, W. A. (2021) Conformational equilibria in allosteric control of Hsp70 chaperones. Mol Cell. 10.1016/j.molcel.2021.07.039
Wang, L., Ferrao, R., Li, Q., Hatcher, J. M., Choi, H. Geun, Buhrlage, S. J., Gray, N. S., and Wu, H. (2019) Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). J Biol Chem. 10.1074/jbc.RA118.005428
Blankenship, E., Vukoti, K., Miyagi, M., and Lodowski, D. T. (2014) Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. Acta Crystallogr D Biol Crystallogr. 70, 833-40
Lin, D. Yin-wei, Kueffer, L. E., Juneja, P., and Wales, T. E. (2024) Conformational heterogeneity of the BTK PHTH domain drives multiple regulatory states. Elife. 10.7554/eLife.89489
Zubcevic, L., Le, S., Yang, H., and Lee, S. - Y. (2018) Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol. 25, 405-415
Shi, K., Demir, Ö., Carpenter, M. A., Wagner, J., Kurahashi, K., Harris, R. S., Amaro, R. E., and Aihara, H. (2017) Conformational Switch Regulates the DNA Cytosine Deaminase Activity of Human APOBEC3B. Sci Rep. 7, 17415
Wiechmann, S., Maisonneuve, P., Grebbin, B. Moyo, Hoffmeister, M., Kaulich, M., Clevers, H., Rajalingam, K., Kurinov, I., Farin, H. F., Sicheri, F., and Ernst, A. (2020) Conformation-specific inhibitors of activated Ras GTPases reveal limited Ras dependency of patient-derived cancer organoids. J Biol Chem. 10.1074/jbc.RA119.011025
Todd, R. C., and Lippard, S. J. (2010) Consequences of cisplatin binding on nucleosome structure and dynamics. Chem Biol. 17, 1334-43
Handa, S., Paul, B. G., Miller, J. F., Valentine, D. L., and Ghosh, P. (2016) Conservation of the C-type lectin fold for accommodating massive sequence variation in archaeal diversity-generating retroelements. BMC Struct Biol. 16, 13
Ostrander, E. L., Larson, J. D., Schuermann, J. P., and Tanner, J. J. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry. 48, 951-9
Raymond, D. D., Bajic, G., Ferdman, J., Suphaphiphat, P., Settembre, E. C., M Moody, A., Schmidt, A. G., and Harrison, S. C. (2018) Conserved epitope on influenza-virus hemagglutinin head defined by a vaccine-induced antibody. Proc Natl Acad Sci U S A. 115, 168-173
West, A. Mv, Rosenberg, S. C., Ur, S. N., Lehmer, M. K., Ye, Q., Hagemann, G., Caballero, I., Usón, I., MacQueen, A. J., Herzog, F., and Corbett, K. D. (2019) A conserved filamentous assembly underlies the structure of the meiotic chromosome axis. Elife. 10.7554/eLife.40372
Dalton, K. M., and Crosson, S. (2010) A conserved mode of protein recognition and binding in a ParD-ParE toxin-antitoxin complex. Biochemistry. 49, 2205-15
Buffalo, C. Z., Bahn-Suh, A. J., Hirakis, S. P., Biswas, T., Amaro, R. E., Nizet, V., and Ghosh, P. (2016) Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein. Nat Microbiol. 1, 16155
Koirala, D., Shao, Y., Koldobskaya, Y., Fuller, J. R., Watkins, A. M., Shelke, S. A., Pilipenko, E. V., Das, R., Rice, P. A., and Piccirilli, J. A. (2019) A conserved RNA structural motif for organizing topology within picornaviral internal ribosome entry sites. Nat Commun. 10, 3629
Lau, R. K., Enustun, E., Gu, Y., Nguyen, J. V., and Corbett, K. D. (2022) A conserved signaling pathway activates bacterial CBASS immune signaling in response to DNA damage. EMBO J. 10.15252/embj.2022111540
Valverde, R., Ingram, J., and Harrison, S. C. (2016) Conserved Tetramer Junction in the Kinetochore Ndc80 Complex. Cell Rep. 17, 1915-1922
Arora, K., and Corbett, K. D. (2018) The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding. Nucleic Acids Res. 10.1093/nar/gky1273
Tabtiang, R. K., Cezairliyan, B. O., Grant, R. A., Cochrane, J. C., and Sauer, R. T. (2005) Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure. Proc Natl Acad Sci U S A. 102, 2305-9
Bryson, D. I., Fan, C., Guo, L. - T., Miller, C., Söll, D., and Liu, D. R. (2017) Continuous directed evolution of aminoacyl-tRNA synthetases. Nat Chem Biol. 13, 1253-1260
Rudolph, M. J., Vance, D. J., Kelow, S., Angalakurthi, S. Krishna, Nguyen, S., Davis, S. A., Rong, Y., C Middaugh, R., Weis, D. D., Dunbrack, R., Karanicolas, J., and Mantis, N. J. (2018) Contribution of an unusual CDR2 element of a single domain antibody in ricin toxin binding affinity and neutralizing activity. Protein Eng Des Sel. 10.1093/protein/gzy022
Xia, S., Vashishtha, A., Bulkley, D., Eom, S. Hyun, Wang, J., and Konigsberg, W. H. (2012) Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA. Biochemistry. 51, 4922-31
Robinson, R., Qureshi, I. A., Klancher, C. A., Rodriguez, P. J., Tanner, J. J., and Sobrado, P. (2015) Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Arch Biochem Biophys. 585, 25-31
Li, X., Lee, H., Wu, J., and Breslow, E. (2007) Contributions of the interdomain loop, amino terminus, and subunit interface to the ligand-facilitated dimerization of neurophysin: crystal structures and mutation studies of bovine neurophysin-I. Protein Sci. 16, 52-68

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