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2021

Johnson, R. A. et al. J. Am. Chem. Soc. 2021, 143(31), 12003–12013. https://pubs.acs.org/doi/10.1021/jacs.1c02622
Kudlacek, S. T., Metz, S., Thiono, D., Payne, A. M., Phan, T. T. N., Tian, S., Forsberg, L. J., Maguire, J., Seim, I., Zhang, S., Tripathy, A., Harrison, J., Nicely, N. I., Soman, S., McCracken, M. K., Gromowski, G. D., Jarman, R. G., Premkumar, L., de Silva, A. M., & Kuhlman, B. (2021). Designed, highly expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies. Science Advances7(42), eabg4084. https://doi.org/10.1126/sciadv.abg4084
Seim, I., Roden, C. A., & Gladfelter, A. S. (2021). Role of spatial patterning of N-protein interactions in SARS-CoV-2 genome packaging. Biophysical Journal120(14), 2771–2784. https://doi.org/10.1016/j.bpj.2021.06.018

2020

Boyce, M. W., Simke, W. C., Kenney, R. M., & Lockett, M. R. (2020). Generating linear oxygen gradients across 3D cell cultures with block-layered oxygen controlled chips (BLOCCs). Analytical Methods : Advancing Methods and Applications12(1), 18–24. https://doi.org/10.1039/C9AY01690B
Boyer, J. A., Spangler, C. J., Strauss, J. D., Cesmat, A. P., Liu, P., McGinty, R. K., & Zhang, Q. (2020). Structural basis of nucleosome-dependent cGAS inhibition. Science370(6515), 450–454. https://doi.org/10.1126/science.abd0609
Chu, I.-T., Speer, S. L., & Pielak, G. J. (2020). Rheostatic control of protein expression using tuner cells. Biochemistry59(6), 733–735. https://doi.org/10.1021/acs.biochem.9b01101
Haney, M. J., Zhao, Y., Fay, J., Duhyeong, H., Wang, M., Wang, H., Li, Z., Lee, Y. Z., Karuppan, M. K., El-Hage, N., Kabanov, A. V., & Batrakova, E. V. (2020). Genetically modified macrophages accomplish targeted gene delivery to the inflamed brain in transgenic Parkin Q311X(A) mice: importance of administration routes. Scientific Reports10(1), 11818. https://doi.org/10.1038/s41598-020-68874-7
Hobson, C. M., Kern, M., O’Brien, E. T., Stephens, A. D., Falvo, M. R., & Superfine, R. (2020). Correlating nuclear morphology and external force with combined atomic force microscopy and light sheet imaging separates roles of chromatin and lamin A/C in nuclear mechanics. Molecular Biology of the Cell31(16), 1788–1801. https://doi.org/10.1091/mbc.E20-01-0073
Huang, W., Carr, A. J., Hajicek, N., Sokolovski, M., Siraliev-Perez, E., Hardy, P. B., Pearce, K. H., Sondek, J., & Zhang, Q. (2020). A High-Throughput Assay to Identify Allosteric Inhibitors of the PLC-γ Isozymes Operating at Membranes. Biochemistry59(41), 4029–4038. https://doi.org/10.1021/acs.biochem.0c00511
Liu, M., Movahed, S., Dangi, S., Pan, H., Kaur, P., Bilinovich, S. M., Faison, E. M., Leighton, G. O., Wang, H., Williams, D. C., & Riehn, R. (2020). DNA looping by two 5-methylcytosine-binding proteins quantified using nanofluidic devices. Epigenetics & Chromatin13(1), 18. https://doi.org/10.1186/s13072-020-00339-7
Martinez-Chacin, R. C., Bodrug, T., Bolhuis, D. L., Kedziora, K. M., Bonacci, T., Ordureau, A., Gibbs, M. E., Weissmann, F., Qiao, R., Grant, G. D., Cook, J. G., Peters, J. M., Wade Harper, J., Emanuele, M. J., & Brown, N. G. (2020). Ubiquitin chain-elongating enzyme UBE2S activates the RING E3 ligase APC/C for substrate priming. Nature Structural & Molecular Biology27(6), 550–560. https://doi.org/10.1038/s41594-020-0424-6
Nelsen, E., Hobson, C. M., Kern, M. E., Hsiao, J. P., O’Brien Iii, E. T., Watanabe, T., Condon, B. M., Boyce, M., Grinstein, S., Hahn, K. M., Falvo, M. R., & Superfine, R. (2020). Combined atomic force microscope and volumetric light sheet system for correlative force and fluorescence mechanobiology studies. Scientific Reports10(1), 8133. https://doi.org/10.1038/s41598-020-65205-8
Potjewyd, F., Turner, A.-M. W., Beri, J., Rectenwald, J. M., Norris-Drouin, J. L., Cholensky, S. H., Margolis, D. M., Pearce, K. H., Herring, L. E., & James, L. I. (2020). Degradation of Polycomb Repressive Complex 2 with an EED-Targeted Bivalent Chemical Degrader. Cell Chemical Biology27(1), 47-56.e15. https://doi.org/10.1016/j.chembiol.2019.11.006
Rectenwald, J. M., Guduru, S. K. R., Dang, Z., Collins, L. B., Liao, Y.-E., Norris-Drouin, J. L., Cholensky, S. H., Kaufmann, K. W., Hammond, S. M., Kireev, D. B., Frye, S. V., & Pearce, K. H. (2020). Design and Construction of a Focused DNA-Encoded Library for Multivalent Chromatin Reader Proteins. Molecules (Basel, Switzerland)25(4). https://doi.org/10.3390/molecules25040979
Richeson, K. V., Bodrug, T., Sackton, K. L., Yamaguchi, M., Paulo, J. A., Gygi, S. P., Schulman, B. A., Brown, N. G., & King, R. W. (2020). Paradoxical mitotic exit induced by a small molecule inhibitor of APC/CCdc20. Nature Chemical Biology16(5), 546–555. https://doi.org/10.1038/s41589-020-0495-z
Skrajna, A., Goldfarb, D., Kedziora, K. M., Cousins, E. M., Grant, G. D., Spangler, C. J., Barbour, E. H., Yan, X., Hathaway, N. A., Brown, N. G., Cook, J. G., Major, M. B., & McGinty, R. K. (2020). Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding. Nucleic Acids Research48(17), 9415–9432. https://doi.org/10.1093/nar/gkaa544
Sonn-Segev, A., Belacic, K., Bodrug, T., Young, G., VanderLinden, R. T., Schulman, B. A., Schimpf, J., Friedrich, T., Dip, P. V., Schwartz, T. U., Bauer, B., Peters, J.-M., Struwe, W. B., Benesch, J. L. P., Brown, N. G., Haselbach, D., & Kukura, P. (2020). Quantifying the heterogeneity of macromolecular machines by mass photometry. Nature Communications11(1), 1772. https://doi.org/10.1038/s41467-020-15642-w
Stadmiller, S. S., Aguilar, J. S., Parnham, S., & Pielak, G. J. (2020). Protein-Peptide Binding Energetics under Crowded Conditions. The Journal of Physical Chemistry. B. https://doi.org/10.1021/acs.jpcb.0c05578
Stadmiller, S. S., Aguilar, J. S., Waudby, C. A., & Pielak, G. J. (2020). Rapid Quantification of Protein-Ligand Binding via 19F NMR Lineshape Analysis. Biophysical Journal118(10), 2537–2548. https://doi.org/10.1016/j.bpj.2020.03.031
Thomas, A., Thiono, D. J., Kudlacek, S. T., Forsberg, J., Premkumar, L., Tian, S., Kuhlman, B., de Silva, A. M., & Metz, S. W. (2020). Dimerization of dengue virus E subunits impacts antibody function and domain focus. Journal of Virology94(18). https://doi.org/10.1128/JVI.00745-20
Thurman, R., Siraliev-Perez, E., & Campbell, S. L. (2020). RAS ubiquitylation modulates effector interactions. Small GTPases11(3), 180–185. https://doi.org/10.1080/21541248.2017.1371267
2019
Anderson, C. J., Baird, M. R., Hsu, A., Barbour, E. H., Koyama, Y., Borgnia, M. J., & McGinty, R. K. (2019). Structural basis for recognition of ubiquitylated nucleosome by dot1l methyltransferase. Cell Reports26(7), 1681-1690.e5. https://doi.org/10.1016/j.celrep.2019.01.058
Bodrug, T., & Brown, N. G. (2019). UBE2S Learns Self-Control. Structure27(8), 1185–1187. https://doi.org/10.1016/j.str.2019.07.009
Eubanks, C. S., Zhao, B., Patwardhan, N. N., Thompson, R. D., Zhang, Q., & Hargrove, A. E. (2019). Visualizing RNA conformational changes via pattern recognition of RNA by small molecules. Journal of the American Chemical Society141(14), 5692–5698. https://doi.org/10.1021/jacs.8b09665
Giannetti, C. A., Busan, S., Weidmann, C. A., & Weeks, K. M. (2019). SHAPE Probing Reveals Human rRNAs Are Largely Unfolded in Solution. Biochemistry58(31), 3377–3385. https://doi.org/10.1021/acs.biochem.9b00076
Hajicek, N., Keith, N. C., Siraliev-Perez, E., Temple, B. R., Huang, W., Zhang, Q., Harden, T. K., & Sondek, J. (2019). Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations. ELife8. https://doi.org/10.7554/eLife.51700
Henderson, N. T., Pablo, M., Ghose, D., Clark-Cotton, M. R., Zyla, T. R., Nolen, J., Elston, T. C., & Lew, D. J. (2019). Ratiometric GPCR signaling enables directional sensing in yeast. PLoS Biology17(10), e3000484. https://doi.org/10.1371/journal.pbio.3000484
Johnson, R. A., Fulcher, L. M., Vang, K., Palmer, C. D., Grossoehme, N. E., & Spuches, A. M. (2019). In depth, thermodynamic analysis of Ca2+ binding to human cardiac troponin C: Extracting buffer-independent binding parameters. Biochimica et Biophysica Acta. Proteins and Proteomics1867(4), 359–366. https://doi.org/10.1016/j.bbapap.2019.01.004
Kudlacek, S. T., & Metz, S. W. (2019). Focused dengue vaccine development: outwitting nature’s design. Pathogens and Disease77(1). https://doi.org/10.1093/femspd/ftz003
Leighton, G., & Williams, D. C. (2019). The Methyl-CpG-Binding Domain 2 and 3 Proteins and Formation of the Nucleosome Remodeling and Deacetylase Complex. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2019.10.007
Marvin, C. M., Ding, S., White, R. E., Orlova, N., Wang, Q., Zywot, E. M., Vickerman, B. M., Harr, L., Tarrant, T. K., Dayton, P. A., & Lawrence, D. S. (2019). On Command Drug Delivery via Cell-Conveyed Phototherapeutics. Small (Germany)15(37), e1901442. https://doi.org/10.1002/smll.201901442
Patteson, J. B., Lescallette, A. R., & Li, B. (2019). Discovery and Biosynthesis of Azabicyclene, a Conserved Nonribosomal Peptide in Pseudomonas aeruginosa. Organic Letters21(13), 4955–4959. https://doi.org/10.1021/acs.orglett.9b01383
Piszkiewicz, S., Gunn, K. H., Warmuth, O., Propst, A., Mehta, A., Nguyen, K. H., Kuhlman, E., Guseman, A. J., Stadmiller, S. S., Boothby, T. C., Neher, S. B., & Pielak, G. J. (2019). Protecting activity of desiccated enzymes. Protein Science28(5), 941–951. https://doi.org/10.1002/pro.3604
Rectenwald, J. M., Hardy, P. B., Norris-Drouin, J. L., Cholensky, S. H., James, L. I., Frye, S. V., & Pearce, K. H. (2019). A General TR-FRET Assay Platform for High-Throughput Screening and Characterizing Inhibitors of Methyl-Lysine Reader Proteins. SLAS Discovery24(6), 693–700. https://doi.org/10.1177/2472555219844569
Speer, S. L., Guseman, A. J., Patteson, J. B., Ehrmann, B. M., & Pielak, G. J. (2019). Controlling and quantifying protein concentration in Escherichia coli. Protein Science28(7), 1307–1311. https://doi.org/10.1002/pro.3637
Wickenheisser, V. A., Zywot, E. M., Rabjohns, E. M., Lee, H. H., Lawrence, D. S., & Tarrant, T. K. (2019). Laser light therapy in inflammatory, musculoskeletal, and autoimmune disease. Current Allergy and Asthma Reports19(8), 37. https://doi.org/10.1007/s11882-019-0869-z
Zhu, C., Dukhovlinova, E., Council, O., Ping, L., Faison, E. M., Prabhu, S. S., Potter, E. L., Upton, S. L., Yin, G., Fay, J. M., Kincer, L. P., Spielvogel, E., Campbell, S. L., Benhabbour, S. R., Ke, H., Swanstrom, R., & Dokholyan, N. V. (2019). Rationally designed carbohydrate-occluded epitopes elicit HIV-1 Env-specific antibodies. Nature Communications10(1), 948. https://doi.org/10.1038/s41467-019-08876-w
Zhu, C., Han, Q., Samoshkin, A., Convertino, M., Linton, A., Faison, E. M., Ji, R.-R., Diatchenko, L., & Dokholyan, N. V. (2019). Stabilization of μ-opioid receptor facilitates its cellular translocation and signaling. Proteins87(10), 878–884. https://doi.org/10.1002/prot.25751

2018

Ankney, J. A., Muneer, A., & Chen, X. (2018). Relative and Absolute Quantitation in Mass Spectrometry-Based Proteomics. Annual Review of Analytical Chemistry (Palo Alto, Calif.)11(1), 49–77. https://doi.org/10.1146/annurev-anchem-061516-045357
Guseman, A. J., Perez Goncalves, G. M., Speer, S. L., Young, G. B., & Pielak, G. J. (2018). Protein shape modulates crowding effects. Proceedings of the National Academy of Sciences of the United States of America115(43), 10965–10970. https://doi.org/10.1073/pnas.1810054115
Guseman, A. J., Speer, S. L., Perez Goncalves, G. M., & Pielak, G. J. (2018). Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments. Biochemistry57(11), 1681–1684. https://doi.org/10.1021/acs.biochem.8b00061
Jiang, Y., Fay, J. M., Poon, C.-D., Vinod, N., Zhao, Y., Bullock, K., Qin, S., Manickam, D. S., Yi, X., Banks, W. A., & Kabanov, A. V. (2018). Nanoformulation of Brain-Derived Neurotrophic Factor with Target Receptor-Triggered-Release in the Central Nervous System. Advanced Functional Materials28(6). https://doi.org/10.1002/adfm.201703982
Kudlacek, S. T., Premkumar, L., Metz, S. W., Tripathy, A., Bobkov, A. A., Payne, A. M., Graham, S., Brackbill, J. A., Miley, M. J., de Silva, A. M., & Kuhlman, B. (2018). Physiological temperatures reduce dimerization of dengue and Zika virus recombinant envelope proteins. The Journal of Biological Chemistry293(23), 8922–8933. https://doi.org/10.1074/jbc.RA118.002658
Lerner, A. M., Yumerefendi, H., Goudy, O. J., Strahl, B. D., & Kuhlman, B. (2018). Engineering improved photoswitches for the control of nucleocytoplasmic distribution. ACS Synthetic Biology [Electronic Resource]7(12), 2898–2907. https://doi.org/10.1021/acssynbio.8b00368
Newby, J. M., Seim, I., Lysy, M., Ling, Y., Huckaby, J., Lai, S. K., & Forest, M. G. (2018). Technological strategies to estimate and control diffusive passage times through the mucus barrier in mucosal drug delivery. Advanced Drug Delivery Reviews124, 64–81. https://doi.org/10.1016/j.addr.2017.12.002
Pablo, M., Ramirez, S. A., & Elston, T. C. (2018). Particle-based simulations of polarity establishment reveal stochastic promotion of Turing pattern formation. PLoS Computational Biology14(3), e1006016. https://doi.org/10.1371/journal.pcbi.1006016
Patteson, J. B., Cai, W., Johnson, R. A., Santa Maria, K. C., & Li, B. (2018). Identification of the biosynthetic pathway for the antibiotic bicyclomycin. Biochemistry57(1), 61–65. https://doi.org/10.1021/acs.biochem.7b00943
Stadmiller, S. S., & Pielak, G. J. (2018a). Enthalpic stabilization of an SH3 domain by D2 O. Protein Science27(9), 1710–1716. https://doi.org/10.1002/pro.3477
Stadmiller, S. S., & Pielak, G. J. (2018b). The Expanding Zoo of In-Cell Protein NMR. Biophysical Journal115(9), 1628–1629. https://doi.org/10.1016/j.bpj.2018.09.017
Yan, C., Wang, F., Peng, Y., Williams, C. R., Jenkins, B., Wildonger, J., Kim, H.-J., Perr, J. B., Vaughan, J. C., Kern, M. E., Falvo, M. R., O’Brien, E. T., Superfine, R., Tuthill, J. C., Xiang, Y., Rogers, S. L., & Parrish, J. Z. (2018). Microtubule acetylation is required for mechanosensation in drosophila. Cell Reports25(4), 1051-1065.e6. https://doi.org/10.1016/j.celrep.2018.09.075