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Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Mannepalli, S., Bahna, F., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) γ-Protocadherin structural diversity and functional implications.. Elife. 10.7554/eLife.20930
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Liu, C., Sawaya, M. R., and Eisenberg, D. (2011) β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.. Nat Struct Mol Biol. 18, 49-55
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Chen, G., Liu, Y., Goetz, R., Fu, L., Jayaraman, S., Hu, M. - C., Moe, O. W., Liang, G., Li, X., and Mohammadi, M. (2018) α-Klotho is a non-enzymatic molecular scaffold for FGF23 hormone signalling.. Nature. 10.1038/nature25451
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Jaiganesh, A., De-la-Torre, P., Patel, A. A., Termine, D. J., Velez-Cortes, F., Chen, C., and Sotomayor, M. (2018) Zooming in on Cadherin-23: Structural Diversity and Potential Mechanisms of Inherited Deafness. Structure. 10.1016/j.str.2018.06.003
Li, Z., Lu, W., Beyett, T. S., Ficarro, S. B., Jiang, J., Tse, J., Kim, A. Yong- Ju, Marto, J. A., Che, J., Jänne, P. A., Eck, M. J., Zhang, T., and Gray, N. S. (2024) ZNL0325, a Pyrazolopyrimidine-Based Covalent Probe, Demonstrates an Alternative Binding Mode for Kinases. J Med Chem. 67, 2837-2848
Sankhala, R. S., Dussupt, V., Donofrio, G., Gromowski, G. D., De La Barrera, R. A., Larocca, R. A., Mendez-Rivera, L., Lee, A., Choe, M., Zaky, W., Mantus, G., Jensen, J. L., Chen, W. - H., Gohain, N., Bai, H., McCracken, M. K., Mason, R. D., Leggat, D., Slike, B. M., Tran, U., Jian, N., Abbink, P., Peterson, R., Mendes, E. Araujo, Franca, R. Freitas de, Calvet, G. Amaral, de Filippis, A. Maria Bisp, McDermott, A., Roederer, M., Hernandez, M., Albertus, A., Davidson, E., Doranz, B. J., Rolland, M., Robb, M. L., Lynch, R. M., Barouch, D. H., Jarman, R. G., Thomas, S. J., Modjarrad, K., Michael, N. L., Krebs, S. J., and M Joyce, G. (2023) Zika-specific neutralizing antibodies targeting inter-dimer envelope epitopes. Cell Rep. 42, 112942
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Peselis, A., and Serganov, A. (2018) ykkC riboswitches employ an add-on helix to adjust specificity for polyanionic ligands. Nat Chem Biol. 14, 887-894
Borowska, M. T., Dominik, P. K., S Anghel, A., Kossiakoff, A. A., and Keenan, R. J. (2015) A YidC-like Protein in the Archaeal Plasma Membrane. Structure. 23, 1715-1724
Nordeen, S. A., Turman, D. L., and Schwartz, T. U. (2020) Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nat Commun. 11, 6060
Gorynia, S., Lorenz, T. C., Costaguta, G., Daboussi, L., Cascio, D., and Payne, G. S. (2012) Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins. Mol Biol Cell. 23, 4416-29
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Ren, F., Logeman, B. L., Zhang, X., Liu, Y., Thiele, D. J., and Yuan, P. (2019) X-ray structures of the high-affinity copper transporter Ctr1. Nat Commun. 10, 1386
Krishnamurthy, H., and Gouaux, E. (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature. 481, 469-74
Althoff, T., Hibbs, R. E., Banerjee, S., and Gouaux, E. (2014) X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature. 512, 333-7
Penmatsa, A., Wang, K. H., and Gouaux, E. (2015) X-ray structures of Drosophila dopamine transporter in complex with nisoxetine and reboxetine. Nat Struct Mol Biol. 22, 506-508
Mansoor, S. E., Lü, W., Oosterheert, W., Shekhar, M., Tajkhorshid, E., and Gouaux, E. (2016) X-ray structures define human P2X(3) receptor gating cycle and antagonist action. Nature. 538, 66-71
Coleman, J. A., Green, E. M., and Gouaux, E. (2016) X-ray structures and mechanism of the human serotonin transporter. Nature. 532, 334-9
Sobolevsky, A. I., Rosconi, M. P., and Gouaux, E. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature. 462, 745-56
Morales-Perez, C. L., Noviello, C. M., and Hibbs, R. E. (2016) X-ray structure of the human α4β2 nicotinic receptor.. Nature. 538, 411-415
Jackson, M. R., Loll, P. J., and Jorns, M. Schuman (2019) X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation. Structure. 10.1016/j.str.2019.03.002
Penmatsa, A., Wang, K. H., and Gouaux, E. (2013) X-ray structure of dopamine transporter elucidates antidepressant mechanism. Nature. 503, 85-90
Goldman, P. J., Grove, T. L., Sites, L. A., McLaughlin, M. I., Booker, S. J., and Drennan, C. L. (2013) X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proc Natl Acad Sci U S A. 110, 8519-24
Van den Berg, B., Clemons, W. M., Collinson, I., Modis, Y., Hartmann, E., Harrison, S. C., and Rapoport, T. A. (2004) X-ray structure of a protein-conducting channel. Nature. 427, 36-44
Bai, Y., McCoy, J. G., Levin, E. J., Sobrado, P., Rajashankar, K. R., Fox, B. G., and Zhou, M. (2015) X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 524, 252-6
Sazinsky, M. H., Dunten, P. W., McCormick, M. S., DiDonato, A., and Lippard, S. J. (2006) X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase. Biochemistry. 45, 15392-404
Chen, P. Yang- Ting, DeColli, A. A., Meyers, C. L. Freel, and Drennan, C. L. (2019) X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. J Biol Chem. 294, 12405-12414

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