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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
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
Yi, C., Chen, B., Qi, B., Zhang, W., Jia, G., Zhang, L., Li, C. J., Dinner, A. R., Yang, C. - G., and He, C. (2012) Duplex interrogation by a direct DNA repair protein in search of base damage. Nat Struct Mol Biol. 19, 671-6
Yildiz, M., Ghosh, S., Bell, J. A., Sherman, W., and Hardy, J. A. (2013) Allosteric inhibition of the NS2B-NS3 protease from dengue virus. ACS Chem Biol. 8, 2744-52
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, Y., Romei, M. G., Sankar, K., Pal, L. R., Hoi, K. Hon, Yang, Y., Leonard, B., Boenig, G. De Leon, Kumar, N., Matsumoto, M., Payandeh, J., Harris, S. F., Moult, J., and Lazar, G. A. (2022) Antibody interfaces revealed through structural mining. Comput Struct Biotechnol J. 20, 4952-4968
Yin, Z., Shi, K., Banerjee, S., Pandey, K. K., Bera, S., Grandgenett, D. P., and Aihara, H. (2016) Crystal structure of the Rous sarcoma virus intasome. Nature. 530, 362-6
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
Yin, Q., Sester, D. P., Tian, Y., Hsiao, Y. - S., Lu, A., Cridland, J. A., Sagulenko, V., Thygesen, S. J., Choubey, D., Hornung, V., Walz, T., Stacey, K. J., and Wu, H. (2013) Molecular mechanism for p202-mediated specific inhibition of AIM2 inflammasome activation. Cell Rep. 4, 327-39
Yirmiya, E., Leavitt, A., Lu, A., Ragucci, A. E., Avraham, C., Osterman, I., Garb, J., Antine, S. P., Mooney, S. E., Hobbs, S. J., Kranzusch, P. J., Amitai, G., and Sorek, R. (2024) Phages overcome bacterial immunity via diverse anti-defence proteins. Nature. 625, 352-359
Yockey, O. P., Jha, V., Ghodke, P. P., Xu, T., Xu, W., Ling, H., Pradeepkumar, P. I., and Zhao, L. (2017) Mechanism of Error-Free DNA Replication Past Lucidin-Derived DNA Damage by Human DNA Polymerase κ.. Chem Res Toxicol. 10.1021/acs.chemrestox.7b00227
Yoder, N., Yoshioka, C., and Gouaux, E. (2018) Gating mechanisms of acid-sensing ion channels. Nature. 10.1038/nature25782
Yoder, N., and Gouaux, E. (2018) Divalent cation and chloride ion sites of chicken acid sensing ion channel 1a elucidated by x-ray crystallography. PLoS One. 13, e0202134
Yoo, J., Mashalidis, E. H., C Y Kuk, A., Yamamoto, K., Kaeser, B., Ichikawa, S., and Lee, S. - Y. (2018) GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation. Nat Struct Mol Biol. 10.1038/s41594-018-0031-y
Yoon, J., Zhang, Y. Meng, Her, C., Grant, R. A., Ponomarenko, A. I., Ackermann, B. E., Hui, T., Lin, Y. - S., Debelouchina, G. T., and Shoulders, M. D. (2024) The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure. Sci Adv. 10, eadl6144
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
Youn, B., Kim, S. - J., Moinuddin, S. G. A., Lee, C., Bedgar, D. L., Harper, A. R., Davin, L. B., Lewis, N. G., and Kang, C. (2006) Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970. J Biol Chem. 281, 40076-88
Young, T., Niks, D., Hakopian, S., Tam, T. K., Yu, X., Hille, R., and Blaha, G. M. (2020) Crystallographic and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase FdsABG from Cupriavidus necator. J Biol Chem. 10.1074/jbc.RA120.013264
Yu, C. H., Bhattacharya, A., Persaud, M., Taylor, A. B., Wang, Z., Bulnes-Ramos, A., Xu, J., Selyutina, A., Martinez-Lopez, A., Cano, K., Demeler, B., Kim, B., Hardies, S. C., Diaz-Griffero, F., and Ivanov, D. N. (2021) Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification. Nat Commun. 12, 731
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, Q., Anderson, D. E., Kaur, R., Fisher, A. J., and Ames, J. B. (2021) The Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues Phe4246-Val4271 Reveals a Fifth Calcium Binding Site. Biochemistry. 10.1021/acs.biochem.1c00152
Yu, Y., Zhu, J., Huang, P. - S., Wang, J. -huai, Pullen, N., and Springer, T. A. (2013) Domain 1 of mucosal addressin cell adhesion molecule has an I1-set fold and a flexible integrin-binding loop. J Biol Chem. 288, 6284-94
Yu, Y., Zheng, Q., Erramilli, S. K., Pan, M., Park, S., Xie, Y., Li, J., Fei, J., Kossiakoff, A. A., Liu, L., and Zhao, M. (2021) K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle. Nat Chem Biol. 17, 896-905
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

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