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Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
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Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36
Carlson, A. S., Cui, H., Divakaran, A., Johnson, J. A., Brunner, R. M., Pomerantz, W. C. K., and Topczewski, J. J. (2019) Systematically Mitigating the p38α Activity of Triazole-based BET Inhibitors.. ACS Med Chem Lett. 10, 1296-1301
Banayan, N. E., Loughlin, B. J., Singh, S., Forouhar, F., Lu, G., Wong, K. - H., Neky, M., Hunt, H. S., Bateman, L. B., Tamez, A., Handelman, S. K., W Price, N., and Hunt, J. F. (2024) Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution. Protein Sci. 33, e4898
Banayan, N. E., Loughlin, B. J., Singh, S., Forouhar, F., Lu, G., Wong, K. - H., Neky, M., Hunt, H. S., Bateman, L. B., Tamez, A., Handelman, S. K., W Price, N., and Hunt, J. F. (2024) Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution. Protein Sci. 33, e4898
G Forse, J., Ram, N., D Banatao, R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A., and Yeates, T. O. (2011) Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-78
Lee, S., Bowman, B. R., Ueno, Y., Wang, S., and Verdine, G. L. (2008) Synthesis and structure of duplex DNA containing the genotoxic nucleobase lesion N7-methylguanine. J Am Chem Soc. 130, 11570-1
Ochoa, J. M., Nguyen, V. N., Nie, M., Sawaya, M. R., Bobik, T. A., and Yeates, T. O. (2020) Symmetry Breaking and Structural Polymorphism in a Bacterial Microcompartment Shell Protein for Choline Utilization. Protein Sci. 10.1002/pro.3941
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7
Windsor, M. A., Hermanson, D. J., Kingsley, P. J., Xu, S., Crews, B. C., Ho, W., Keenan, C. M., Banerjee, S., Sharkey, K. A., and Marnett, L. J. (2012) Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes. ACS Med Chem Lett. 3, 759-763
Rosenberg, O. S., Dovala, D., Li, X., Connolly, L., Bendebury, A., Finer-Moore, J., Holton, J., Cheng, Y., Stroud, R. M., and Cox, J. S. (2015) Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 161, 501-512
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Fang, J., Leichter, S. M., Jiang, J., Biswal, M., Lu, J., Zhang, Z. - M., Ren, W., Zhai, J., Cui, Q., Zhong, X., and Song, J. (2021) Substrate deformation regulates DRM2-mediated DNA methylation in plants. Sci Adv. 10.1126/sciadv.abd9224
Gao, J., Ha, B. Hak, Lou, H. Jane, Morse, E. M., Zhang, R., Calderwood, D. A., Turk, B. E., and Boggon, T. J. (2013) Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PLoS One. 8, e77818
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
Shnitsar, V., Li, J., Li, X., Calmettes, C., Basu, A., Casey, J. R., Moraes, T. F., and Reithmeier, R. A. F. (2013) A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters. J Biol Chem. 288, 33848-60
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0
Rajagopalan, S., Teter, S. J., Zwart, P. H., Brennan, R. G., Phillips, K. J., and Kiley, P. J. (2013) Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat Struct Mol Biol. 20, 740-7
Hou, X., Burstein, S. R., and Long, S. Barstow (2018) Structures reveal opening of the store-operated calcium channel Orai. Elife. 10.7554/eLife.36758
Gürel, G., Blaha, G., Steitz, T. A., and Moore, P. B. (2009) Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui. Antimicrob Agents Chemother. 53, 5010-4
Singh, H., Arentson, B. W., Becker, D. F., and Tanner, J. J. (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A. 111, 3389-94
Gorelik, A., Illes, K., Bui, K. Huy, and Nagar, B. (2022) Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase. Proc Natl Acad Sci U S A. 119, e2203518119
Varlakhanova, N. V., Alvarez, F. J. D., Brady, T. M., Tornabene, B. A., Hosford, C. J., Chappie, J. S., Zhang, P., and Ford, M. G. J. (2018) Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. J Cell Biol. 10.1083/jcb.201712021

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