2020 Publications

  1. Afek, A., Shi, H., Rangadurai, A., Sahay, H., Senitzki, A., Xhani, S., Fang, M., Salinas, R., Mielko, Z., Pufall, M.A., Poon, G.M.K., Haran, T.E., Schumacher, M.A., Al-Hashimi, H.M., Gordân, R., 2020. DNA mismatches reveal conformational penalties in protein-DNA recognition. Nature 587, 291–296. doi:10.1038/s41586-020-2843-2

  2. Banda, D.M., Pereira, J.H., Liu, A.K., Orr, D.J., Hammel, M., He, C., Parry, M.A.J., Carmo-Silva, E., Adams, P.D., Banfield, J.F., Shih, P.M., 2020. Novel bacterial clade reveals origin of form I Rubisco. Nat. Plants 6, 1158–1166. doi:10.1038/s41477-020-00762-4

  3. Berry, K.N., Brett, T.J., 2020. Structural and biophysical analysis of the CLCA1 VWA domain suggests mode of TMEM16A engagement. Cell Rep. 30, 1141-1151.e3. doi:10.1016/j.celrep.2019.12.059

  4. Bhargava, H.K., Tabata, K., Byck, J.M., Hamasaki, M., Farrell, D.P., Anishchenko, I., DiMaio, F., Im, Y.J., Yoshimori, T., Hurley, J.H., 2020. Structural basis for autophagy inhibition by the human Rubicon-Rab7 complex. Proc Natl Acad Sci USA 117, 17003–17010. doi:10.1073/pnas.2008030117

  5. Broom, A., Rakotoharisoa, R.V., Thompson, M.C., Zarifi, N., Nguyen, E., Mukhametzhanov, N., Liu, L., Fraser, J.S., Chica, R.A., 2020. Ensemble-based enzyme design can recapitulate the effects of laboratory directed evolution in silico. Nat. Commun. 11, 4808. doi:10.1038/s41467-020-18619-x

  6. Brown, C. A., L. Hu, Z. Sun, M. P. Patel, S. Singh, J.R. Porter, B. Sankaran,  B.V. Prasad,  G. R. Bowman, and T. Palzkill,. 2020. “Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance .” J Biol Chem. 2020 May 22;295(21):7376-7390. doi: 10.1074/jbc.RA119.012489. Epub 2020 Apr 16. PMID: 32299911 PMCID: PMC7247304 DOI: 10.1074/jbc.RA119.012489

  7. Brunette, T.J., Bick, M.J., Hansen, J.M., Chow, C.M., Kollman, J.M., Baker, D., 2020. Modular repeat protein sculpting using rigid helical junctions. Proc Natl Acad Sci USA 117, 8870–8875. doi:10.1073/pnas.1908768117

  8. Campbell, A.C., Bogner, A.N., Mao, Y., Becker, D.F., Tanner, J.J., 2020a. Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-γ-semialdehyde dehydrogenase active site of bifunctional proline utilization A. Arch. Biochem. Biophys. 108727. doi:10.1016/j.abb.2020.108727

  9. Campbell, A.C., Robinson, R., Mena-Aguilar, D., Sobrado, P., Tanner, J.J., 2020b. Structural determinants of flavin dynamics in a class B monooxygenase. Biochemistry. doi:10.1021/acs.biochem.0c00783

  10. Campbell AC, Stiers KM, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ.Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics J Biol Chem. 2020 Sep 18;295(38):13239-13249. doi: 10.1074/jbc.RA120.014750. Epub 2020 Jul 28.  PMID: 32723870 PMCID: PMC7504930 (available on 2021-09-18) DOI: 10.1074/jbc.RA120.014750

  11. Chandrasekharan, N.P., Ravenburg, C.M., Roy, I.R., Monroe, J.D., Berndsen, C.E., 2020. Solution structure and assembly of β-amylase 2 from Arabidopsis thaliana. Acta Crystallogr. D Struct. Biol. 76, 357–365. doi:10.1107/S2059798320002016

  12. Chen, Z., Kibler, R.D., Hunt, A., Busch, F., Pearl, J., Jia, M., VanAernum, Z.L., Wicky, B.I.M., Dods, G., Liao, H., Wilken, M.S., Ciarlo, C., Green, S., El-Samad, H., Stamatoyannopoulos, J., Wysocki, V.H., Jewett, M.C., Boyken, S.E., Baker, D., 2020. De novo design of protein logic gates. Science 368, 78–84. doi:10.1126/science.aay2790

  13. Choudhary, D., Narui, Y., Neel, B.L., Wimalasena, L.N., Klanseck, C.F., De-la-Torre, P., Chen, C., Araya-Secchi, R., Tamilselvan, E., Sotomayor, M., 2020. Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception. Proc Natl Acad Sci USA 117, 24837–24848. doi:10.1073/pnas.1920444117

  14. Christensen, E.M., Bogner, A.N., Vandekeere, A., Tam, G.S., Patel, S.M., Becker, D.F., Fendt, S.-M., Tanner, J.J., 2020. In crystallo screening for proline analog inhibitors of the proline cycle enzyme PYCR1. J. Biol. Chem. 295, 18316–18327. doi:10.1074/jbc.RA120.016106

  15. Corpuz, J.C., Podust, L.M., Davis, T.D., Jaremko, M.J., Burkart, M.D., 2020. Dynamic visualization of type II peptidyl carrier protein recognition in pyoluteorin biosynthesis. RSC Chem. Biol. 1, 8–12. doi:10.1039/c9cb00015a

  16. Dai, J., Knott, G.J., Fu, W., Lin, T.W., Furst, A.L., Britt, R.D., Francis, M.B., 2020. Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins. ACS Nano. doi:10.1021/acsnano.0c07165

  17. de la Mora, E., Coquelle, N., Bury, C.S., Rosenthal, M., Holton, J.M., Carmichael, I., Garman, E.F., Burghammer, M., Colletier, J.-P., Weik, M., 2020. Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures. Proc Natl Acad Sci USA 117, 4142–4151. doi:10.1073/pnas.1821522117

  18. Divine, R., Dang, H.V., Ueda, G., Fallas, J.A., Vulovic, I., Sheffler, W., Saini, S., Zhao, Y.T., Raj, I.X., Morawski, P.A., Jennewein, M.F., Homad, L.J., Wan, Y.-H., Tooley, M.R., Seeger, F., Etemadi, A., Fahning, M.L., Lazarovits, J., Roederer, A., Walls, A.C., Stewart, L., Mazloomi, M., King, N.P., Campbell, D.J., McGuire, A.T., Stamatatos, L., Ruohola-Baker, H., Mathieu, J., Veesler, D., Baker, D., 2020. Designed proteins assemble antibodies into modular nanocages. BioRxiv. doi:10.1101/2020.12.01.406611

  19. Dominguez-Martin, M.A., Hammel, M., Gupta, S., Lechno-Yossef, S., Sutter, M., Rosenberg, D.J., Chen, Y., Petzold, C.J., Ralston, C.Y., Polívka, T., Kerfeld, C.A., 2020. Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP. Sci. Rep. 10, 15564. doi:10.1038/s41598-020-72383-y

  20. Dotas, R.R., Nguyen, T.T., Stewart, C.E., Ghirlando, R., Potoyan, D.A., Venditti, V., 2020. Hybrid thermophilic/mesophilic enzymes reveal a role for conformational disorder in regulation of bacterial enzyme I. J. Mol. Biol. 432, 4481–4498. doi:10.1016/j.jmb.2020.05.024

  21. Fedechkin, S.O., George, N.L., Nuñez Castrejon, A.M., Dillen, J.R., Kauvar, L.M., DuBois, R.M., 2020. Conformational flexibility in respiratory syncytial virus G neutralizing epitopes. J. Virol. 94. doi:10.1128/JVI.01879-19

  22. Flower, T.G., Buffalo, C.Z., Hooy, R.M., Allaire, M., Ren, X., Hurley, J.H., 2020a. Structure of SARS-CoV-2 ORF8, a rapidly evolving coronavirus protein implicated in immune evasion. BioRxiv. doi:10.1101/2020.08.27.270637

  23. Flower, T.G., Takahashi, Y., Hudait, A., Rose, K., Tjahjono, N., Pak, A.J., Yokom, A.L., Liang, X., Wang, H.-G., Bouamr, F., Voth, G.A., Hurley, J.H., 2020b. A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission. Nat. Struct. Mol. Biol. 27, 570–580. doi:10.1038/s41594-020-0426-4

  24. Gao, Z.-Z., Wang, Z.-K., Wei, L., Yin, G., Tian, J., Liu, C.-Z., Wang, H., Zhang, D.-W., Zhang, Y.-B., Li, X., Liu, Y., Li, Z.-T., 2020. Water-Soluble 3D Covalent Organic Framework that Displays an Enhanced Enrichment Effect of Photosensitizers and Catalysts for the Reduction of Protons to H2. ACS Appl. Mater. Interfaces 12, 1404–1411. doi:10.1021/acsami.9b19870

  25. Gorelik, A., Illes, K., Nagar, B., 2020. Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme. Structure 28, 426-436.e3. doi:10.1016/j.str.2020.02.001

  26. Hammel, M., Rosenberg, D.J., Bierma, J., Hura, G.L., Thapar, R., Lees-Miller, S.P., Tainer, J.A., 2020. Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog. Biophys. Mol. Biol. doi:10.1016/j.pbiomolbio.2020.09.003

  27. Hille, R., Young, T., Niks, D., Hakopian, S., Tam, T.K., Yu, X., Mulchandani, A., Blaha, G.M., 2020. Structure: Function Studies of the Cytosolic, Mo- and NAD+-Dependent Formate Dehydrogenase from Cupriavidus necator. Inorganics 8, 41. doi:10.3390/inorganics8070041

  28. Hoffmann, K.M., Goncuian, E.S., Karimi, K.L., Amendola, C.R., Mojab, Y., Wood, K.M., Prussia, G.A., Nix, J., Yamamoto, M., Lathan, K., Orion, I.W., 2020. Cofactor Complexes of DesD, a Model Enzyme in the Virulence-related NIS Synthetase Family. Biochemistry 59, 3427–3437. doi:10.1021/acs.biochem.9b00899

  29. Hongdusit, A., Zwart, P.H., Sankaran, B., Fox, J.M., 2020. Minimally disruptive optical control of protein tyrosine phosphatase 1B. Nat. Commun. 11, 788. doi:10.1038/s41467-020-14567-8

  30. Howitz, W.J., Wierzbicki, M., Cabanela, R.W., Saliba, C., Motavalli, A., Tran, N., Nowick, J.S., 2020. Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin19-36. J. Am. Chem. Soc. 142, 15870–15875. doi:10.1021/jacs.0c06143

  31. Hu, X., Kim, J.-K., Yu, C., Jun, H.-I., Liu, J., Sankaran, B., Huang, L., Qiao, F., 2020. Quality-Control Mechanism for Telomerase RNA Folding in the Cell. Cell Rep. 33, 108568. doi:10.1016/j.celrep.2020.108568

  32. Ibrahim, M., Fransson, T., Chatterjee, R., Cheah, M.H., Hussein, R., Lassalle, L., Sutherlin, K.D., Young, I.D., Fuller, F.D., Gul, S., Kim, I.-S., Simon, P.S., de Lichtenberg, C., Chernev, P., Bogacz, I., Pham, C.C., Orville, A.M., Saichek, N., Northen, T., Batyuk, A., Carbajo, S., Alonso-Mori, R., Tono, K., Owada, S., Bhowmick, A., Bolotovsky, R., Mendez, D., Moriarty, N.W., Holton, J.M., Dobbek, H., Brewster, A.S., Adams, P.D., Sauter, N.K., Bergmann, U., Zouni, A., Messinger, J., Kern, J., Yachandra, V.K., Yano, J., 2020. Untangling the sequence of events during the S2 → S3 transition in photosystem II and implications for the water oxidation mechanism. Proc Natl Acad Sci USA 117, 12624–12635. doi:10.1073/pnas.2000529117

  33. Jiao L, Shubbar M, Yang X, Zhang Q, Chen S, Wu Q, Chen Z, Rizo J, Liu X. A partially disordered region connects gene repression and activation functions of EZH2 Proc Natl Acad Sci U S A. 2020 Jul 21;117(29):16992-17002. doi: 10.1073/pnas.1914866117. Epub 2020 Jul 6.  PMID: 32631994 PMCID: PMC7382310 DOI: 10.1073/pnas.1914866117

  34. Jing, T., Zhao, B., Xu, P., Gao, X., Chi, L., Han, H., Sankaran, B., Li, P., 2020. The Structural Basis of IRF-3 Activation upon Phosphorylation. J. Immunol. 205, 1886–1896. doi:10.4049/jimmunol.2000026

  35. Kilgore, H.R., Latham, A.P., Ressler, V.T., Zhang, B., Raines, R.T., 2020. Structure and Dynamics of N-Glycosylated Human Ribonuclease 1. Biochemistry 59, 3148–3156. doi:10.1021/acs.biochem.0c00191

  36. Kolich, L.R., Chang, Y.-T., Coudray, N., Giacometti, S.I., MacRae, M.R., Isom, G.L., Teran, E.M., Bhabha, G., Ekiert, D.C., 2020. Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation. elife 9. doi:10.7554/eLife.60030

  37. Kosciuk, T., Price, I.R., Zhang, X., Zhu, C., Johnson, K.N., Zhang, S., Halaby, S.L., Komaniecki, G.P., Yang, M., DeHart, C.J., Thomas, P.M., Kelleher, N.L., Fromme, J.C., Lin, H., 2020. NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle. Nat. Commun. 11, 1067. doi:10.1038/s41467-020-14893-x

  38. Kumar, D., Yu, X., Crawford, S.E., Moreno, R., Jakana, J., Sankaran, B., Anish, R., Kaundal, S., Hu, L., Estes, M.K., Wang, Z., Prasad, B.V.V., 2020. 2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity. Sci. Adv. 6, eaay6410. doi:10.1126/sciadv.aay6410

  39. Laciak, A.R., Korasick, D.A., Gates, K.S., Tanner, J.J., 2020. Structural analysis of pathogenic mutations targeting Glu427 of ALDH7A1, the hot spot residue of pyridoxine-dependent epilepsy. J. Inherit. Metab. Dis. 43, 635–644. doi:10.1002/jimd.12184

  40. Lau, R.K., Ye, Q., Birkholz, E.A., Berg, K.R., Patel, L., Mathews, I.T., Watrous, J.D., Ego, K., Whiteley, A.T., Lowey, B., Mekalanos, J.J., Kranzusch, P.J., Jain, M., Pogliano, J., Corbett, K.D., 2020. Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity. Mol. Cell 77, 723-733.e6. doi:10.1016/j.molcel.2019.12.010

  41. Li, Q., Pellegrino, J., Lee, D.J., Tran, A.A., Chaires, H.A., Wang, R., Park, J.E., Ji, K., Chow, D., Zhang, N., Brilot, A.F., Biel, J.T., van Zundert, G., Borrelli, K., Shinabarger, D., Wolfe, C., Murray, B., Jacobson, M.P., Mühle, E., Chesneau, O., Fraser, J.S., Seiple, I.B., 2020. Synthetic group A streptogramin antibiotics that overcome Vat resistance. Nature 586, 145–150. doi:10.1038/s41586-020-2761-3

  42. Liau, N.P.D., Venkatanarayan, A., Quinn, J.G., Phung, W., Malek, S., Hymowitz, S.G., Sudhamsu, J., 2020. Dimerization induced by C-terminal 14-3-3 binding is sufficient for BRAF kinase activation. Biochemistry. doi:10.1021/acs.biochem.0c00517

  43. Lieu, R., Antonysamy, S., Druzina, Z., Ho, C., Kang, N.R., Pustilnik, A., Wang, J., Atwell, S., 2020. Rapid and robust antibody Fab fragment crystallization utilizing edge-to-edge beta-sheet packing. PLoS ONE 15, e0232311. doi:10.1371/journal.pone.0232311

  44. Lu, T.-W., Aoto, P.C., Weng, J.-H., Nielsen, C., Cash, J.N., Hall, J., Zhang, P., Simon, S.M., Cianfrocco, M.A., Taylor, S.S., 2020. Structural analyses of the PKA RIIβ holoenzyme containing the oncogenic DnaJB1-PKAc fusion protein reveal protomer asymmetry and fusion-induced allosteric perturbations in fibrolamellar hepatocellular carcinoma. PLoS Biol. 18, e3001018. doi:10.1371/journal.pbio.3001018

  45. Mena, E.L., Jevtić, P., Greber, B.J., Gee, C.L., Lew, B.G., Akopian, D., Nogales, E., Kuriyan, J., Rape, M., 2020. Structural basis for dimerization quality control. Nature 586, 452–456. doi:10.1038/s41586-020-2636-7

  46. Mendez, D., Bolotovsky, R., Bhowmick, A., Brewster, A.S., Kern, J., Yano, J., Holton, J.M., Sauter, N.K., 2020. Beyond integration: modeling every pixel to obtain better structure factors from stills. IUCrJ 7, 1151–1167. doi:10.1107/S2052252520013007

  47. Nikolova, E.N., Stanfield, R.L., Dyson, H.J., Wright, P.E., 2020. A conformational switch in the zinc finger protein kaiso mediates differential readout of specific and methylated DNA sequences. Biochemistry 59, 1909–1926. doi:10.1021/acs.biochem.0c00253

  48. Oltrogge, L.M., Chaijarasphong, T., Chen, A.W., Bolin, E.R., Marqusee, S., Savage, D.F., 2020. Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. Nat. Struct. Mol. Biol. 27, 281–287. doi:10.1038/s41594-020-0387-7

  49. Osko JD, Porter NJ, Narayana Reddy PA, Xiao YC, Rokka J, Jung M, Hooker JM, Salvino JM, Christianson DW. Exploring Structural Determinants of Inhibitor Affinity and Selectivity in Complexes with Histone Deacetylase 6 J Med Chem. 2020 Jan 9;63(1):295-308. doi: 10.1021/acs.jmedchem.9b01540. Epub 2019 Dec 19. PMID: 31793776

  50. Otten, R., Pádua, R.A.P., Bunzel, H.A., Nguyen, V., Pitsawong, W., Patterson, M., Sui, S., Perry, S.L., Cohen, A.E., Hilvert, D., Kern, D., 2020. How directed evolution reshapes the energy landscape in an enzyme to boost catalysis. Science 370, 1442–1446. doi:10.1126/science.abd3623

  51. Patterson, E.I., Nanson, J.D., Abendroth, J., Bryan, C., Sankaran, B., Myler, P.J., Forwood, J.K., 2020. Structural characterization of β-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites. Proteins 88, 47–56. doi:10.1002/prot.25765

  52. Piccoli L, Park YJ, Tortorici MA, Czudnochowski N, Walls AC, Beltramello M, Silacci-Fregni C, Pinto D, Rosen LE, Bowen JE, Acton OJ, Jaconi S, Guarino B, Minola A, Zatta F, Sprugasci N, Bassi J, Peter A, De Marco A, Nix JC, Mele F, Jovic S, Rodriguez BF, Gupta SV, Jin F, Piumatti G, Lo Presti G, Pellanda AF, Biggiogero M, Tarkowski M, Pizzuto MS, Cameroni E, Havenar-Daughton C, Smithey M, Hong D, Lepori V, Albanese E, Ceschi A, Bernasconi E, Elzi L, Ferrari P, Garzoni C, Riva A, Snell G, Sallusto F, Fink K, Virgin HW, Lanzavecchia A, Corti D, Veesler D. Mapping Neutalizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution SerologyCell. 2020 Nov 12;183(4):1024-1042.e21. doi: 10.1016/j.cell.2020.09.037. Epub 2020 Sep 16. PMID: 32991844

  53. Pinals, R.L., Yang, D., Rosenberg, D.J., Chaudhary, T., Crothers, A.R., Iavarone, A.T., Hammel, M., Landry, M., 2020. Quantitative protein corona composition and dynamics on carbon nanotubes in biological environments. Angew Chem Int Ed. doi:10.1002/anie.202008175

  54. Polizzi, N.F., DeGrado, W.F., 2020. A defined structural unit enables de novo design of small-molecule-binding proteins. Science 369, 1227–1233. doi:10.1126/science.abb8330

  55. Remesh, S.G., Verma, S.C., Chen, J.-H., Ekman, A.A., Larabell, C.A., Adhya, S., Hammel, M., 2020. Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat. Commun. 11, 2905. doi:10.1038/s41467-020-16724-5

  56. Russelburg, L.P., O’Shea Murray, V.L., Demir, M., Knutsen, K.R., Sehgal, S.L., Cao, S., David, S.S., Horvath, M.P., 2020. Structural basis for finding OG lesions and avoiding undamaged G by the DNA glycosylase muty. ACS Chem. Biol. 15, 93–102. doi:10.1021/acschembio.9b00639

  57. Sauter, N.K., Kern, J., Yano, J., Holton, J.M., 2020. Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction. Acta Crystallogr. D Struct. Biol. 76, 176–192. doi:10.1107/S2059798320000418

  58. Schellenberg, M.J., Appel, C.D., Riccio, A.A., Butler, L.R., Krahn, J.M., Liebermann, J.A., Cortés-Ledesma, F., Williams, R.S., 2020. Ubiquitin stimulated reversal of topoisomerase 2 DNA-protein crosslinks by TDP2. Nucleic Acids Res. 48, 6310–6325. doi:10.1093/nar/gkaa318

  59. Schmit, J.D., Bouchard, J.J., Martin, E.W., Mittag, T., 2020. Protein Network Structure Enables Switching between Liquid and Gel States. J. Am. Chem. Soc. 142, 874–883. doi:10.1021/jacs.9b10066

  60. Schumacher, M.A., Ohashi, T., Corbin, L., Erickson, H.P., 2020. High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP. Acta Crystallogr. F Struct. Biol. Commun. 76, 94–102. doi:10.1107/S2053230X20001132

  61. Schumann, B., Malaker, S.A., Wisnovsky, S.P., Debets, M.F., Agbay, A.J., Fernandez, D., Wagner, L.J.S., Lin, L., Li, Z., Choi, J., Fox, D.M., Peh, J., Gray, M.A., Pedram, K., Kohler, J.J., Mrksich, M., Bertozzi, C.R., 2020. Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells. Mol. Cell 78, 824-834.e15. doi:10.1016/j.molcel.2020.03.030

  62. Seacrist, C.D., Kuenze, G., Hoffmann, R.M., Moeller, B.E., Burke, J.E., Meiler, J., Blind, R.D., 2020. Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function. Structure 28, 830-846.e9. doi:10.1016/j.str.2020.04.020

  63. Sloutsky, R., Dziedzic, N., Dunn, M.J., Bates, R.M., Torres-Ocampo, A.P., Boopathy, S., Page, B., Weeks, J.G., Chao, L.H., Stratton, M.M., 2020. Heterogeneity in human hippocampal CaMKII transcripts reveals allosteric hub-dependent regulation. Sci. Signal. 13. doi:10.1126/scisignal.aaz0240

  64. Soeung, V., Lu, S., Hu, L., Judge, A., Sankaran, B., Prasad, B.V.V., Palzkill, T., 2020. A Drug-Resistant β-lactamase Variant Changes the Conformation of Its Active Site Proton Shuttle to Alter Substrate Specificity and Inhibitor Potency. J. Biol. Chem. doi:10.1074/jbc.RA120.016103

  65. Stachowski, T.R., Snell, M.E., Snell, E.H., 2020a. SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique. PLoS ONE 15, e0239702. doi:10.1371/journal.pone.0239702

  66. Stachowski, T.R., Snell, M.E., Snell, E.H., 2020b. Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states. IUCrJ 7, 238–252. doi:10.1107/S205225251901707X

  67. Steckelberg, A.-L., Vicens, Q., Costantino, D.A., Nix, J.C., Kieft, J.S., 2020. The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold. RNA 26, 1767–1776. doi:10.1261/rna.076224.120

  68. Taylor, D.M., Anglin, J., Park, S., Ucisik, M.N., Faver, J.C., Simmons, N., Jin, Z., Palaniappan, M., Nyshadham, P., Li, F., Campbell, J., Hu, L., Sankaran, B., Prasad, B.V.V., Huang, H., Matzuk, M.M., Palzkill, T., 2020. Identifying Oxacillinase-48 Carbapenemase Inhibitors Using DNA-Encoded Chemical Libraries. ACS Infect. Dis. 6, 1214–1227. doi:10.1021/acsinfecdis.0c00015

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