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Yu, A., Xing, Y., Harrison, S. C., and Kirchhausen, T. (2010) Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling. Structure. 18, 1311-20
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
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
Yin, L., Shi, K., and Aihara, H. (2023) Structural basis of sequence-specific cytosine deamination by double-stranded DNA deaminase toxin DddA. Nat Struct Mol Biol. 10.1038/s41594-023-01034-3
Yin, F. Fang, Bailey, S., C Innis, A., Ciubotaru, M., Kamtekar, S., Steitz, T. A., and Schatz, D. G. (2009) Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat Struct Mol Biol. 16, 499-508
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
Yelshanskaya, M. V., Singh, A. K., Narangoda, C., Williams, R. S. B., Kurnikova, M. G., and Sobolevsky, A. I. (2020) Structural basis of AMPA receptor inhibition by 4-BCCA. Br J Pharmacol. 10.1111/bph.15254
Yelshanskaya, M. V., Li, M., and Sobolevsky, A. I. (2014) Structure of an agonist-bound ionotropic glutamate receptor. Science. 345, 1070-4
Ye, Q., Ur, S. N., Su, T. Y., and Corbett, K. D. (2016) Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. EMBO J. 35, 2139-2151
Ye, Q., Lu, S., and Corbett, K. D. (2021) Structural Basis for SARS-CoV-2 Nucleocapsid Protein Recognition by Single-Domain Antibodies. Front Immunol. 12, 719037
Yasuda, H., Park, E., Yun, C. -hong, Sng, N. J., Lucena-Araujo, A. R., Yeo, W. - L., Huberman, M. S., Cohen, D. W., Nakayama, S., Ishioka, K., Yamaguchi, N., Hanna, M., Oxnard, G. R., Lathan, C. S., Moran, T., Sequist, L. V., Chaft, J. E., Riely, G. J., Arcila, M. E., Soo, R. A., Meyerson, M., Eck, M. J., Kobayashi, S. S., and Costa, D. B. (2013) Structural, biochemical, and clinical characterization of epidermal growth factor receptor (EGFR) exon 20 insertion mutations in lung cancer. Sci Transl Med. 5, 216ra177
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
Yang, Y., Liu, C., Zhou, W., Shi, W., Chen, M., Zhang, B., Schatz, D. G., Hu, Y., and Liu, B. (2021) Structural visualization of transcription activated by a multidrug-sensing MerR family regulator. Nat Commun. 12, 2702
Yang, Y., Eichhorn, C. D., Wang, Y., Cascio, D., and Feigon, J. (2019) Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE.. Nat Chem Biol. 15, 132-140
Yang, H., Ji, X., Zhao, G., Ning, J., Zhao, Q., Aiken, C., Gronenborn, A. M., Zhang, P., and Xiong, Y. (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5α.. Proc Natl Acad Sci U S A. 109, 18372-7
Yang, X., Chen, G., Weng, N. - P., and Mariuzza, R. A. (2017) Structural basis for clonal diversity of the human T-cell response to a dominant influenza virus epitope. J Biol Chem. 292, 18618-18627
Yang, H., Wang, J., Jia, X., McNatt, M. W., Zang, T., Pan, B., Meng, W., Wang, H. - W., Bieniasz, P. D., and Xiong, Y. (2010) Structural insight into the mechanisms of enveloped virus tethering by tetherin. Proc Natl Acad Sci U S A. 107, 18428-32
Yang, Y., Harris, K. A., Widner, D. L., and Breaker, R. R. (2021) Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex. Proc Natl Acad Sci U S A. 10.1073/pnas.2020393118
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Yan, W., Markegard, E., Dharmaiah, S., Urisman, A., Drew, M., Esposito, D., Scheffzek, K., Nissley, D. V., McCormick, F., and Simanshu, D. K. (2020) Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Rep. 32, 107909
Yamaguchi, M., Yu, S., Qiao, R., Weissmann, F., Miller, D. J., VanderLinden, R., Brown, N. G., Frye, J. J., Peters, J. - M., and Schulman, B. A. (2015) Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome. J Mol Biol. 427, 1748-64

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