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P
Pemberton, T. A., Still, B. R., Christensen, E. M., Singh, H., Srivastava, D., and Tanner, J. J. (2012) Proline: Mother Nature's cryoprotectant applied to protein crystallography. Acta Crystallogr D Biol Crystallogr. 68, 1010-8
Simmons, H. C., Finney, J., Kotaki, R., Adachi, Y., Moseman, A. Park, Watanabe, A., Song, S., Robinson-McCarthy, L. R., Le Sage, V., Kuraoka, M., E Moseman, A., Kelsoe, G., Takahashi, Y., and McCarthy, K. R. (2025) A protective and broadly binding antibody class engages the influenza virus hemagglutinin head at its stem interface. mBio. 16, e0089225
Torbeev, V. Yu, Raghuraman, H., Hamelberg, D., Tonelli, M., Westler, W. M., Perozo, E., and Kent, S. B. H. (2011) Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc Natl Acad Sci U S A. 108, 20982-7
Torbeev, V. Yu, Raghuraman, H., Hamelberg, D., Tonelli, M., Westler, W. M., Perozo, E., and Kent, S. B. H. (2011) Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc Natl Acad Sci U S A. 108, 20982-7
Goodman, K. M., Rubinstein, R., Dan, H., Bahna, F., Mannepalli, S., Ahlsen, G., Thu, C. Aye, Sampogna, R. V., Maniatis, T., Honig, B., and Shapiro, L. (2017) Protocadherin cis-dimer architecture and recognition unit diversity. Proc Natl Acad Sci U S A. 10.1073/pnas.1713449114
Ameriks, M. K., Axe, F. U., Bembenek, S. D., Edwards, J. P., Gu, Y., Karlsson, L., Randal, M., Sun, S., Thurmond, R. L., and Zhu, J. (2009) Pyrazole-based cathepsin S inhibitors with arylalkynes as P1 binding elements. Bioorg Med Chem Lett. 19, 6131-4
W Tolbert, D., Graham, D. E., White, R. H., and Ealick, S. E. (2003) Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms. Structure. 11, 285-94
Q
Gero, T. W., Heppner, D. E., Beyett, T. S., To, C., Azevedo, S. C., Jang, J., Bunnell, T., Feru, F., Li, Z., Shin, B. Hee, Soroko, K. M., Gokhale, P. C., Gray, N. S., Jänne, P. A., Eck, M. J., and Scott, D. A. (2022) Quinazolinones as allosteric fourth-generation EGFR inhibitors for the treatment of NSCLC. Bioorg Med Chem Lett. 10.1016/j.bmcl.2022.128718
R
Castel, P., Dharmaiah, S., Sale, M. J., Messing, S., Rizzuto, G., Cuevas-Navarro, A., Cheng, A., Trnka, M. J., Urisman, A., Esposito, D., Simanshu, D. K., and McCormick, F. (2021) RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity. Proc Natl Acad Sci U S A. 10.1073/pnas.2103261118
Blum, E., Zhang, J., Zaluski, J., Einstein, D. E., Korshin, E. E., Kubas, A., Gruzman, A., Tochtrop, G. P., Kiser, P. D., and Palczewski, K. (2021) Rational Alteration of Pharmacokinetics of Chiral Fluorinated and Deuterated Derivatives of Emixustat for Retinal Therapy. J Med Chem. 10.1021/acs.jmedchem.1c00279
LoVerde, P. T., Alwan, S. N., Taylor, A. B., Rhodes, J., Chevalier, F. D., Anderson, T. Jc, and McHardy, S. F. (2021) Rational approach to drug discovery for human schistosomiasis. Int J Parasitol Drugs Drug Resist. 16, 140-147
Doherty, E. E., Wilcox, X. E., Fiet, Lvan Sint, Kemmel, C., Turunen, J. J., Klein, B., Tantillo, D. J., Fisher, A. J., and Beal, P. A. (2021) Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position. J Am Chem Soc. 143, 6865-6876
Doherty, E. E., Wilcox, X. E., Fiet, Lvan Sint, Kemmel, C., Turunen, J. J., Klein, B., Tantillo, D. J., Fisher, A. J., and Beal, P. A. (2021) Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position. J Am Chem Soc. 143, 6865-6876
Kiser, P. D., Zhang, J., Badiee, M., Kinoshita, J., Peachey, N. S., Tochtrop, G. P., and Palczewski, K. (2017) Rational Tuning of Visual Cycle Modulator Pharmacodynamics. J Pharmacol Exp Ther. 362, 131-145
Murn, J., Teplova, M., Zarnack, K., Shi, Y., and Patel, D. J. (2016) Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt. Nat Struct Mol Biol. 23, 16-23
Singh, H., Schuermann, J. P., Reilly, T. J., Calcutt, M. J., and Tanner, J. J. (2010) Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase. J Mol Biol. 404, 639-49
Chetty, A. K., Sexton, J. A., Ha, B. Hak, Turk, B. E., and Boggon, T. J. (2020) Recognition of physiological phosphorylation sites by p21-activated kinase 4. J Struct Biol. 211, 107553
Wan, L. C. K., Mao, D. Y. L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R. K., Lissina, E., Nislow, C., Caudy, A. A., Durocher, D., and Sicheri, F. (2013) Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41, 6332-46
Chao, F. - A., Chan, A. H., Dharmaiah, S., Schwieters, C. D., Tran, T. H., Taylor, T., Ramakrishnan, N., Esposito, D., Nissley, D. V., McCormick, F., Simanshu, D. K., and Cornilescu, G. (2023) Reduced dynamic complexity allows structure elucidation of an excited state of KRAS. Commun Biol. 6, 594
Chao, F. - A., Chan, A. H., Dharmaiah, S., Schwieters, C. D., Tran, T. H., Taylor, T., Ramakrishnan, N., Esposito, D., Nissley, D. V., McCormick, F., Simanshu, D. K., and Cornilescu, G. (2023) Reduced dynamic complexity allows structure elucidation of an excited state of KRAS. Commun Biol. 6, 594
Johnson, C. W., Seo, H. - S., Terrell, E. M., Yang, M. - H., KleinJan, F., Gebregiworgis, T., Gasmi-Seabrook, G. M. C., Geffken, E. A., Lakhani, J., Song, K., Bashyal, P., Popow, O., Paulo, J. A., Liu, A., Mattos, C., Marshall, C. B., Ikura, M., Morrison, D. K., Dhe-Paganon, S., and Haigis, K. M. (2022) Regulation of GTPase function by autophosphorylation. Mol Cell. 82, 950-968.e14
Teng, P. K., Anderson, N. J., Goldschmidt, L., Sawaya, M. R., Sambashivan, S., and Eisenberg, D. (2012) Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation. Protein Sci. 21, 26-37
Peek, J., Lilic, M., Montiel, D., Milshteyn, A., Woodworth, I., Biggins, J. B., Ternei, M. A., Calle, P. Y., Danziger, M., Warrier, T., Saito, K., Braffman, N., Fay, A., Glickman, M. S., Darst, S. A., Campbell, E. A., and Brady, S. F. (2018) Rifamycin congeners kanglemycins are active against rifampicin-resistant bacteria via a distinct mechanism. Nat Commun. 9, 4147
Yudina, Z., Roa, A., Johnson, R., Biris, N., Vieira, D. A. de Souza, Tsiperson, V., Reszka, N., Taylor, A. B., P Hart, J., Demeler, B., Diaz-Griffero, F., and Ivanov, D. N. (2015) RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.. Cell Rep. 12, 788-97
Yudina, Z., Roa, A., Johnson, R., Biris, N., Vieira, D. A. de Souza, Tsiperson, V., Reszka, N., Taylor, A. B., P Hart, J., Demeler, B., Diaz-Griffero, F., and Ivanov, D. N. (2015) RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.. Cell Rep. 12, 788-97

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