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Kozlov, G., Mattijssen, S., Jiang, J., Nyandwi, S., Sprules, T., Iben, J. R., Coon, S. L., Gaidamakov, S., Noronha, A. M., Wilds, C. J., Maraia, R. J., and Gehring, K. (2022) Structural basis of 3'-end poly(A) RNA recognition by LARP1. Nucleic Acids Res. 10.1093/nar/gkac696
Nomura, Y., Montemayor, E. J., Virta, J. M., Hayes, S. M., and Butcher, S. E. (2019) Structural basis for the evolution of cyclic phosphodiesterase activity in the U6 snRNA exoribonuclease Usb1. Nucleic Acids Res. 10.1093/nar/gkz1177
Schmier, B. J., Nelersa, C. M., and Malhotra, A. (2017) Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep. 7, 11085
Westblade, L. F., Campbell, E. A., Pukhrambam, C., Padovan, J. C., Nickels, B. E., Lamour, V., and Darst, S. A. (2010) Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction. Nucleic Acids Res. 38, 8357-69
Seegar, T. C. M., Killingsworth, L. B., Saha, N., Meyer, P. A., Patra, D., Zimmerman, B., Janes, P. W., Rubinstein, E., Nikolov, D. B., Skiniotis, G., Kruse, A. C., and Blacklow, S. C. (2017) Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.. Cell. 171, 1638-1648.e7
Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. J Biol Chem. 299, 104608
Nguyen, H. An, Hoffer, E. D., Fagan, C. E., Maehigashi, T., and Dunham, C. M. (2023) Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches. bioRxiv. 10.1101/2023.01.28.526049
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
Nair, P. A., Nandakumar, J., Smith, P., Odell, M., Lima, C. D., and Shuman, S. (2007) Structural basis for nick recognition by a minimal pluripotent DNA ligase. Nat Struct Mol Biol. 14, 770-8
Nair, P. A., Nandakumar, J., Smith, P., Odell, M., Lima, C. D., and Shuman, S. (2007) Structural basis for nick recognition by a minimal pluripotent DNA ligase. Nat Struct Mol Biol. 14, 770-8
Nithianantham, S., McNally, F. J., and Al-Bassam, J. (2018) Structural Basis for Disassembly of Katanin Heterododecamers. J Biol Chem. 10.1074/jbc.RA117.001215
Nabel, K. G., Clark, S. A., Shankar, S., Pan, J., Clark, L. E., Yang, P., Coscia, A., McKay, L. G. A., Varnum, H. H., Brusic, V., Tolan, N. V., Zhou, G., Desjardins, M., Turbett, S. E., Kanjilal, S., Sherman, A. C., Dighe, A., LaRocque, R. C., Ryan, E. T., Tylek, C., Cohen-Solal, J. F., Darcy, A. T., Tavella, D., Clabbers, A., Fan, Y., Griffiths, A., Correia, I. R., Seagal, J., Baden, L. R., Charles, R. C., and Abraham, J. (2021) Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain. Science
Deaconescu, A. M., Chambers, A. L., Smith, A. J., Nickels, B. E., Hochschild, A., Savery, N. J., and Darst, S. A. (2006) Structural basis for bacterial transcription-coupled DNA repair. Cell. 124, 507-20
Yu, X., Seegar, T. C. M., Dalton, A. C., Tzvetkova-Robev, D., Goldgur, Y., Rajashankar, K. R., Nikolov, D. B., and Barton, W. A. (2013) Structural basis for angiopoietin-1-mediated signaling initiation. Proc Natl Acad Sci U S A. 110, 7205-10
Fairman, J. Wesley, Wijerathna, S. Ranjan, Ahmad, M. Faiz, Xu, H., Nakano, R., Jha, S., Prendergast, J., R Welin, M., Flodin, S., Roos, A., Nordlund, P., Li, Z., Walz, T., and Dealwis, C. Godfrey (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol. 18, 316-22
Fairman, J. Wesley, Wijerathna, S. Ranjan, Ahmad, M. Faiz, Xu, H., Nakano, R., Jha, S., Prendergast, J., R Welin, M., Flodin, S., Roos, A., Nordlund, P., Li, Z., Walz, T., and Dealwis, C. Godfrey (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol. 18, 316-22
Yelshanskaya, M. V., Singh, A. K., Sampson, J. M., Narangoda, C., Kurnikova, M., and Sobolevsky, A. I. (2016) Structural Bases of Noncompetitive Inhibition of AMPA-Subtype Ionotropic Glutamate Receptors by Antiepileptic Drugs. Neuron. 91, 1305-15
Niu, Y., Suzuki, H., Hosford, C. J., Walz, T., and Chappie, J. S. (2020) Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes. Nat Commun. 11, 5907
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Gilbert, N. C., Gerstmeier, J., Schexnaydre, E. E., Börner, F., Garscha, U., Neau, D. B., Werz, O., and Newcomer, M. E. (2020) Structural and mechanistic insights into 5-lipoxygenase inhibition by natural products. Nat Chem Biol. 10.1038/s41589-020-0544-7
Gilbert, N. C., Gerstmeier, J., Schexnaydre, E. E., Börner, F., Garscha, U., Neau, D. B., Werz, O., and Newcomer, M. E. (2020) Structural and mechanistic insights into 5-lipoxygenase inhibition by natural products. Nat Chem Biol. 10.1038/s41589-020-0544-7
Nomura, Y., Roston, D., Montemayor, E. J., Cui, Q., and Butcher, S. E. (2018) Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1. Nucleic Acids Res. 10.1093/nar/gky812
de Araujo, E. D., Erdogan, F., Neubauer, H. A., Meneksedag-Erol, D., Manaswiyoungkul, P., Eram, M. S., Seo, H. - S., Qadree, A. K., Israelian, J., Orlova, A., Suske, T., Pham, H. T. T., Boersma, A., Tangermann, S., Kenner, L., Rülicke, T., Dong, A., Ravichandran, M., Brown, P. J., Audette, G. F., Rauscher, S., Dhe-Paganon, S., Moriggl, R., and Gunning, P. T. (2019) Structural and functional consequences of the STAT5B driver mutation. Nat Commun. 10, 2517
Dayeh, D. M., Kruithoff, B. C., and Nakanishi, K. (2018) Structural and functional analyses reveal the contributions of the C- and N-lobes of Argonaute protein to selectivity of RNA target cleavage. J Biol Chem. 10.1074/jbc.RA117.001051
Laing, E. D., Navaratnarajah, C. K., Da Silva, S. Cheliout, Petzing, S. R., Xu, Y., Sterling, S. L., Marsh, G. A., Wang, L. - F., Amaya, M., Nikolov, D. B., Cattaneo, R., Broder, C. C., and Xu, K. (2019) Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 116, 20707-20715

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