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Xu, Y., Robev, D., Saha, N., Wang, B., Dalva, M. B., Xu, K., Himanen, J. P., and Nikolov, D. B. (2021) The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism. Int J Mol Sci. 10.3390/ijms221910473
Xue, S., Calvin, K., and Li, H. (2006) RNA recognition and cleavage by a splicing endonuclease. Science. 312, 906-10
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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
Yan, X., Wang, X., Li, Y., Zhou, M., Li, Y., Song, L., Mi, W., Min, J., and Dong, C. (2021) Molecular basis for ubiquitin ligase CRL2-mediated recognition of C-degron. Nat Chem Biol. 10.1038/s41589-020-00703-4
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
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
Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., and Pavletich, N. P. (2013) mTOR kinase structure, mechanism and regulation. Nature. 497, 217-23
Yang, Y., Liu, X. Roger, Greenberg, Z. J., Zhou, F., He, P., Fan, L., Liu, S., Shen, G., Egawa, T., Gross, M. L., Schuettpelz, L. G., and Li, W. (2020) Open conformation of tetraspanins shapes interaction partner networks on cell membranes. EMBO J. 39, e105246
Yang, G., Fu, Y., Malakhova, M., Kurinov, I., Zhu, F., Yao, K., Li, H., Chen, H., Li, W., Lim, D. Young, Sheng, Y., Bode, A. M., Dong, Z., and Dong, Z. (2014) Caffeic acid directly targets ERK1/2 to attenuate solar UV-induced skin carcinogenesis. Cancer Prev Res (Phila). 7, 1056-66
Yang, M. Hee, Tran, T. H., Hunt, B., Agnor, R., Johnson, C. W., Shui, B., Waybright, T. J., Nowak, J. A., Stephen, A. G., Simanshu, D. K., and Haigis, K. M. (2023) Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity. Cancer Res. 83, 3176-3183
Yang, Y., Ke, N., Liu, S., and Li, W. (2017) Methods for Structural and Functional Analyses of Intramembrane Prenyltransferases in the UbiA Superfamily. Methods Enzymol. 584, 309-347
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, 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, 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., and Patel, D. J. (2017) Inhibition Mechanism of an Anti-CRISPR Suppressor AcrIIA4 Targeting SpyCas9. Mol Cell. 10.1016/j.molcel.2017.05.024
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., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., and Pavletich, N. P. (2017) Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. Nature. 552, 368-373
Yang, H., Gao, P., Rajashankar, K. R., and Patel, D. J. (2016) PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease. Cell. 167, 1814-1828.e12
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, 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
Yao, G., Zhang, S., Mahrhold, S., Lam, K. - H., Stern, D., Bagramyan, K., Perry, K., Kalkum, M., Rummel, A., Dong, M., and Jin, R. (2016) N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Nat Struct Mol Biol. 23, 656-62
Yao, G., Lam, K. - H., Weisemann, J., Peng, L., Krez, N., Perry, K., Shoemaker, C. B., Dong, M., Rummel, A., and Jin, R. (2017) A camelid single-domain antibody neutralizes botulinum neurotoxin A by blocking host receptor binding. Sci Rep. 7, 7438
Yao, G., Lam, K. - H., Perry, K., Weisemann, J., Rummel, A., and Jin, R. (2017) Crystal Structure of the Receptor-Binding Domain of Botulinum Neurotoxin Type HA, Also Known as Type FA or H. Toxins (Basel). 10.3390/toxins9030093
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

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