Publications

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Journal Article
Campiani, G., Cavella, C., Osko, J. D., Brindisi, M., Relitti, N., Brogi, S., A Saraswati, P., Federico, S., Chemi, G., Maramai, S., Carullo, G., Jaeger, B., Carleo, A., Benedetti, R., Sarno, F., Lamponi, S., Rottoli, P., Bargagli, E., Bertucci, C., Tedesco, D., Herp, D., Senger, J., Ruberti, G., Saccoccia, F., Saponara, S., Gorelli, B., Valoti, M., Kennedy, B., Sundaramurthi, H., Butini, S., Jung, M., Roach, K. M., Altucci, L., Bradding, P., Christianson, D. W., Gemma, S., and Prasse, A. (2021) Harnessing the Role of HDAC6 in Idiopathic Pulmonary Fibrosis: Design, Synthesis, Structural Analysis, and Biological Evaluation of Potent Inhibitors. J Med Chem. 64, 9960-9988
Deo, C., Abdelfattah, A. S., Bhargava, H. K., Berro, A. J., Falco, N., Farrants, H., Moeyaert, B., Chupanova, M., Lavis, L. D., and Schreiter, E. R. (2021) The HaloTag as a general scaffold for far-red tunable chemigenetic indicators. Nat Chem Biol. 17, 718-723
Deo, C., Abdelfattah, A. S., Bhargava, H. K., Berro, A. J., Falco, N., Farrants, H., Moeyaert, B., Chupanova, M., Lavis, L. D., and Schreiter, E. R. (2021) The HaloTag as a general scaffold for far-red tunable chemigenetic indicators. Nat Chem Biol. 17, 718-723
Saredi, G., Huang, H., Hammond, C. M., Alabert, C., Bekker-Jensen, S., Forne, I., Reverón-Gómez, N., Foster, B. M., Mlejnkova, L., Bartke, T., Cejka, P., Mailand, N., Imhof, A., Patel, D. J., and Groth, A. (2016) H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex.. Nature. 534, 714-718
Saredi, G., Huang, H., Hammond, C. M., Alabert, C., Bekker-Jensen, S., Forne, I., Reverón-Gómez, N., Foster, B. M., Mlejnkova, L., Bartke, T., Cejka, P., Mailand, N., Imhof, A., Patel, D. J., and Groth, A. (2016) H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex.. Nature. 534, 714-718
Mehta, R. S., Mayers, J. R., Zhang, Y., Bhosle, A., Glasser, N. R., Nguyen, L. H., Ma, W., Bae, S., Branck, T., Song, K., Sebastian, L., Pacheco, J. Avila, Seo, H. - S., Clish, C., Dhe-Paganon, S., Ananthakrishnan, A. N., Franzosa, E. A., Balskus, E. P., Chan, A. T., and Huttenhower, C. (2023) Gut microbial metabolism of 5-ASA diminishes its clinical efficacy in inflammatory bowel disease. Nat Med. 29, 700-709
Gantt, S. M. Lucy, Decroos, C., Lee, M. S., Gullett, L. E., Bowman, C. M., Christianson, D. W., and Fierke, C. A. (2016) General Base-General Acid Catalysis in Human Histone Deacetylase 8. Biochemistry. 55, 820-32
Liu, L., Wilcox, X. E., Fisher, A. J., Boyd, S. D., Zhi, J., Winkler, D. D., and Bulla, L. A. (2022) Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R, for Cry1A Toxins of . Biochemistry. 61, 752-766
Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
Richards, L. S., Flores, M. D., Millán, C., Glynn, C., Zee, C. - T., Sawaya, M. R., Gallagher-Jones, M., Borges, R. J., Usón, I., and Rodriguez, J. A. (2023) Fragment-Based Phasing of Peptidic Nanocrystals by MicroED. ACS Bio Med Chem Au. 3, 201-210
Fei, X., Ye, X., LaRonde, N. A., and Lorimer, G. H. (2014) Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form. Proc Natl Acad Sci U S A. 111, 12775-80
C Y Jeng, S., Trachman, R. J., Weissenboeck, F., Truong, L., Link, K. A., Jepsen, M. D. E., Knutson, J. R., Andersen, E. S., Ferré-D'Amaré, A. R., and Unrau, P. J. (2021) Fluorogenic aptamers resolve the flexibility of RNA junctions using orientation-dependent FRET. RNA. 27, 433-444
Truong, L., Kooshapur, H., Dey, S. Kumar, Li, X., Tjandra, N., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2021) The fluorescent aptamer Squash extensively repurposes the adenine riboswitch fold. Nat Chem Biol. 10.1038/s41589-021-00931-2
Anmangandla, A., Jana, S., Peng, K., Wallace, S. D., Bagde, S. R., Drown, B. S., Xu, J., Hergenrother, P. J., J Fromme, C., and Lin, H. (2023) A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain. ACS Chem Biol. 18, 1200-1207
Li, Y. L., Zee, C. - T., Lin, J. B., Basile, V. M., Muni, M., Flores, M. D., Munárriz, J., Kaner, R. B., Alexandrova, A. N., Houk, K. N., Tolbert, S. H., and Rubin, Y. (2020) Fjord-Edge Graphene Nanoribbons with Site-Specific Nitrogen Substitution. J Am Chem Soc. 142, 18093-18102
Moody, J. D., Levy, S., Mathieu, J., Xing, Y., Kim, W., Dong, C., Tempel, W., Robitaille, A. M., Dang, L. T., Ferreccio, A., Detraux, D., Sidhu, S., Zhu, L., Carter, L., Xu, C., Valensisi, C., Wang, Y., R Hawkins, D., Min, J., Moon, R. T., Orkin, S. H., Baker, D., and Ruohola-Baker, H. (2017) First critical repressive H3K27me3 marks in embryonic stem cells identified using designed protein inhibitor. Proc Natl Acad Sci U S A. 10.1073/pnas.1706907114
Moreno, M. V., Rockwell, N. C., Mora, M., Fisher, A. J., and J Lagarias, C. (2020) A far-red cyanobacteriochrome lineage specific for verdins. Proc Natl Acad Sci U S A. 10.1073/pnas.2016047117
Francis, J. William, Shao, Z., Narkhede, P., Trinh, A. Truc, Lu, J., Song, J., and Gozani, O. (2023) The FAM86 domain of FAM86A confers substrate specificity to promote EEF2-Lys525 methylation. J Biol Chem. 299, 104842
Do, T. D., LaPointe, N. E., Sangwan, S., Teplow, D. B., Feinstein, S. C., Sawaya, M. R., Eisenberg, D. S., and Bowers, M. T. (2014) Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. J Phys Chem B. 118, 7247-56
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Moremen, K. W., Ramiah, A., Stuart, M., Steel, J., Meng, L., Forouhar, F., Moniz, H. A., Gahlay, G., Gao, Z., Chapla, D., Wang, S., Yang, J. - Y., Prabhakar, P. Kumar, Johnson, R., Rosa, M. Dela, Geisler, C., Nairn, A. V., Seetharaman, J., Wu, S. - C., Tong, L., Gilbert, H. J., LaBaer, J., and Jarvis, D. L. (2017) Expression system for structural and functional studies of human glycosylation enzymes. Nat Chem Biol. 10.1038/nchembio.2539
Hollander, K., Chan, A. H., Frey, K. M., Hunker, O., Ippolito, J. A., Spasov, K. A., Yeh, Y. - H. J., Jorgensen, W. L., Ho, Y. - C., and Anderson, K. S. (2023) Exploring novel HIV-1 reverse transcriptase inhibitors with drug-resistant mutants: A double mutant surprise. Protein Sci. 32, e4814
Kearney, C., Olenginski, L. T., Hirn, T. D., Fowler, G. D., Tariq, D., Brewer, S. H., and Phillips-Piro, C. M. (2018) Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine. RSC Adv. 8, 13503-13512

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