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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
Liang, B., Xue, S., Terns, R. M., Terns, M. P., and Li, H. (2007) Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex. Nat Struct Mol Biol. 14, 1189-95
Taabazuing, C. Y., Fermann, J., Garman, S., and Knapp, M. J. (2016) Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.. Biochemistry. 55, 277-86
Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus aureus. J Am Chem Soc. 140, 2442-2445
Cao, H., Pauff, J. M., and Hille, R. (2010) Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid. J Biol Chem. 285, 28044-53
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
Wang, H., and Gouaux, E. (2012) Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue. EMBO Rep. 13, 861-6
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
Zeller, M. J., Nuthanakanti, A., Li, K., Aubé, J., Serganov, A., and Weeks, K. M. (2022) Subsite Ligand Recognition and Cooperativity in the TPP Riboswitch: Implications for Fragment-Linking in RNA Ligand Discovery. ACS Chem Biol. 17, 438-448
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
Lee, S., Choi, J., Mohanty, J., Sousa, L. P., Tome, F., Pardon, E., Steyaert, J., Lemmon, M. A., Lax, I., and Schlessinger, J. (2018) Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.. Nature. 10.1038/nature25010
Knappenberger, A. John, Reiss, C. Wetheringt, and Strobel, S. A. (2018) Structures of two aptamers with differing ligand specificity reveal ruggedness in the functional landscape of RNA. Elife. 10.7554/eLife.36381
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
F Demircioglu, E., Sosa, B. A., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2016) Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Elife. 10.7554/eLife.17983
Song, G., and Springer, T. A. (2014) Structures of the Toxoplasma gliding motility adhesin. Proc Natl Acad Sci U S A. 111, 4862-7
Zhang, W., Dunkle, J. A., and Cate, J. H. D. (2009) Structures of the ribosome in intermediate states of ratcheting. Science. 325, 1014-7
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
Su, C. - C., Klenotic, P. A., Cui, M., Lyu, M., Morgan, C. E., and Yu, E. W. (2021) Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol. 19, e3001370

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