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Arnett, K. L., Hass, M., McArthur, D. G., Ilagan, M. Xenia G., Aster, J. C., Kopan, R., and Blacklow, S. C. (2010) Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes. Nat Struct Mol Biol. 17, 1312-7
Arndt, J. W., Schwarzenbacher, R., Page, R., Abdubek, P., Ambing, E., Biorac, T., Canaves, J. M., Chiu, H. - J., Dai, X., Deacon, A. M., DiDonato, M., Elsliger, M. - A., Godzik, A., Grittini, C., Grzechnik, S. K., Hale, J., Hampton, E., Han, G. Won, Haugen, J., Hornsby, M., Klock, H. E., Koesema, E., Kreusch, A., Kuhn, P., Jaroszewski, L., Lesley, S. A., Levin, I., McMullan, D., McPhillips, T. M., Miller, M. D., Morse, A., Moy, K., Nigoghossian, E., Ouyang, J., Peti, W. S., Quijano, K., Reyes, R., Sims, E., Spraggon, G., Stevens, R. C., van den Bedem, H., Velasquez, J., Vincent, J., von Delft, F., Wang, X., West, B., White, A., Wolf, G., Xu, Q., Zagnitko, O., Hodgson, K. O., Wooley, J., and Wilson, I. A. (2005) Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution. Proteins. 58, 755-8
Armstrong, A. A., Mohideen, F., and Lima, C. D. (2012) Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2. Nature. 483, 59-63
Armache, K. - J., Garlick, J. D., Canzio, D., Narlikar, G. J., and Kingston, R. E. (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.. Science. 334, 977-82
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Archer, C. R., Enslow, B. T., Taylor, A. B., De la Rosa, V., Bhattacharya, A., and Shapiro, M. S. (2019) A mutually-induced conformational fit underlies Ca-directed interactions between calmodulin and the proximal C terminus of KCNQ4 K channels. J Biol Chem. 10.1074/jbc.RA118.006857
Arbing, M. A., Handelman, S. K., Kuzin, A. P., Verdon, G., Wang, C., Su, M., Rothenbacher, F. P., Abashidze, M., Liu, M., Hurley, J. M., Xiao, R., Acton, T., Inouye, M., Montelione, G. T., Woychik, N. A., and Hunt, J. F. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 18, 996-1010
Arbing, M. A., Chan, S., Shin, A., Phan, T., Ahn, C. J., Rohlin, L., and Gunsalus, R. P. (2012) Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans. Proc Natl Acad Sci U S A. 109, 11812-7
Arbing, M. A., Kaufmann, M., Phan, T., Chan, S., Cascio, D., and Eisenberg, D. (2010) The crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer. Protein Sci. 19, 1692-703
Arbing, M. A., Chan, S., Harris, L., Kuo, E., Zhou, T. T., Ahn, C. J., Nguyen, L., He, Q., Lu, J., Menchavez, P. T., Shin, A., Holton, T., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2013) Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. PLoS One. 8, e81753
Araya-Secchi, R., Neel, B. L., and Sotomayor, M. (2016) An elastic element in the protocadherin-15 tip link of the inner ear. Nat Commun. 7, 13458
Aranda, R., Cai, H., Worley, C. E., Levin, E. J., Li, R., Olson, J. S., Phillips, G. N., and Richards, M. P. (2009) Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins. 75, 217-30
Araghi, R. Rezaei, Bird, G. H., Ryan, J. A., Jenson, J. M., Godes, M., Pritz, J. R., Grant, R. A., Letai, A., Walensky, L. D., and Keating, A. E. (2018) Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells. Proc Natl Acad Sci U S A. 115, E886-E895
Aquino, B., Couñago, R. M., Verza, N., Ferreira, L. M., Massirer, K. B., Gileadi, O., and Arruda, P. (2017) Structural Characterization of Maize SIRK1 Kinase Domain Reveals an Unusual Architecture of the Activation Segment. Front Plant Sci. 8, 852
Apostol, M. I., Perry, K., and Surewicz, W. K. (2013) Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. J Am Chem Soc. 135, 10202-5
Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 285, 29671-5
Aoki, S. T., Settembre, E. C., Trask, S. D., Greenberg, H. B., Harrison, S. C., and Dormitzer, P. R. (2009) Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab. Science. 324, 1444-7
Aoki, M., Vinokur, J., Motoyama, K., Ishikawa, R., Collazo, M., Cascio, D., Sawaya, M. R., Ito, T., Bowie, J. U., and Hemmi, H. (2022) Crystal structure of mevalonate 3,5-bisphosphate decarboxylase reveals insight into the evolution of decarboxylases in the mevalonate metabolic pathways. J Biol Chem. 10.1016/j.jbc.2022.102111
Antipenko, A., Himanen, J. - P., van Leyen, K., Nardi-Dei, V., Lesniak, J., Barton, W. A., Rajashankar, K. R., Lu, M., Hoemme, C., Püschel, A. W., and Nikolov, D. B. (2003) Structure of the semaphorin-3A receptor binding module. Neuron. 39, 589-98
Antine, S. P., Johnson, A. G., Mooney, S. E., Leavitt, A., Mayer, M. L., Yirmiya, E., Amitai, G., Sorek, R., and Kranzusch, P. J. (2023) Structural basis of Gabija anti-phage defence and viral immune evasion. Nature. 10.1038/s41586-023-06855-2
Anmangandla, A., Jana, S., Peng, K., Wallace, S. D., Bagde, S. R., Drown, B. S., Xu, J., Hergenrother, P. J., J Fromme, C., and Lin, H. (2023) A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain. ACS Chem Biol. 18, 1200-1207
Anishchenko, I., Pellock, S. J., Chidyausiku, T. M., Ramelot, T. A., Ovchinnikov, S., Hao, J., Bafna, K., Norn, C., Kang, A., Bera, A. K., DiMaio, F., Carter, L., Chow, C. M., Montelione, G. T., and Baker, D. (2021) De novo protein design by deep network hallucination. Nature. 10.1038/s41586-021-04184-w
Andrews, L. D., Kane, T. R., Dozzo, P., Haglund, C. M., Hilderbrandt, D. J., Linsell, M. S., Machajewski, T., McEnroe, G., Serio, A. W., Wlasichuk, K. B., Neau, D. B., Pakhomova, S., Waldrop, G. L., Sharp, M., Pogliano, J., Cirz, R. T., and Cohen, F. (2019) Optimization and Mechanistic Characterization of Pyridopyrimidine Inhibitors of Bacterial Biotin Carboxylase. J Med Chem. 62, 7489-7505
Andreev, V. I., Yu, C., Wang, J., Schnabl, J., Tirian, L., Gehre, M., Handler, D., Duchek, P., Novatchkova, M., Baumgartner, L., Meixner, K., Sienski, G., Patel, D. J., and Brennecke, J. (2022) Panoramix SUMOylation on chromatin connects the piRNA pathway to the cellular heterochromatin machinery. Nat Struct Mol Biol. 29, 130-142
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

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