Publications

Found 2797 results
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Brumshtein, B., Esswein, S. R., Landau, M., Ryan, C. M., Whitelegge, J. P., Phillips, M. L., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2014) Formation of amyloid fibers by monomeric light chain variable domains. J Biol Chem. 289, 27513-25
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
Ren, A., Rajashankar, K. R., and Patel, D. J. (2012) Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch. Nature. 486, 85-9
Xu, S., Uddin, M. Jashim, Banerjee, S., Duggan, K., Musee, J., Kiefer, J. R., Ghebreselasie, K., Rouzer, C. A., and Marnett, L. J. (2019) Fluorescent indomethacin-dansyl conjugates utilize the membrane-binding domain of cyclooxygenase-2 to block the opening to the active site. J Biol Chem. 10.1074/jbc.RA119.007405
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
R Wiseman, L., Zhang, Y., Lee, K. P. K., Harding, H. P., Haynes, C. M., Price, J., Sicheri, F., and Ron, D. (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell. 38, 291-304
Hamill, M. J., Jost, M., Wong, C., Elliott, S. J., and Drennan, C. L. (2011) Flavin-induced oligomerization in Escherichia coli adaptive response protein AidB. Biochemistry. 50, 10159-69
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
Bertram, J. H., Mulliner, K. M., Shi, K., Plunkett, M. H., Nixon, P., Serratore, N. A., Douglas, C. J., Aihara, H., and Barney, B. M. (2017) Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket. Appl Environ Microbiol. 10.1128/AEM.00018-17
Doamekpor, S. K., Schwer, B., Sanchez, A. M., Shuman, S., and Lima, C. D. (2015) Fission yeast RNA triphosphatase reads an Spt5 CTD code. RNA. 21, 113-23
Sanchez, A. M., Jacewicz, A., and Shuman, S. (2022) Fission yeast Duf89 and Duf8901 are cobalt/nickel-dependent phosphatase-pyrophosphatases that act via a covalent aspartyl-phosphate intermediate. J Biol Chem. 10.1016/j.jbc.2022.101851
Shen, Y., Li, F., Szewczyk, M. M., Halabelian, L., Chau, I., Eram, M. S., Seña, Cdela, Park, K. - S., Meng, F., Chen, H., Zeng, H., Dong, A., Wu, H., Trush, V. V., McLeod, D., Zepeda-Velázquez, C. A., Campbell, R. M., Mader, M. M., Watson, B. M., Schapira, M., Arrowsmith, C. H., Al-awar, R., Barsyte-Lovejoy, D., H Kaniskan, Ü., Brown, P. J., Vedadi, M., and Jin, J. (2021) A First-in-Class, Highly Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 6. J Med Chem. 64, 3697-3706
Herp, D., Ridinger, J., Robaa, D., Shinsky, S. A., Schmidtkunz, K., Yesiloglu, T. Z., Bayer, T., Steimbach, R. R., Herbst-Gervasoni, C. J., Merz, A., Romier, C., Sehr, P., Gunkel, N., Miller, A. K., Christianson, D. W., Oehme, I., Sippl, W., and Jung, M. (2022) First Fluorescent Acetylspermidine Deacetylation Assay for HDAC10 Identifies Selective Inhibitors with Cellular Target Engagement. Chembiochem. 10.1002/cbic.202200180
Beseiso, D., Chen, E. V., McCarthy, S. E., Martin, K. N., Gallagher, E. P., Miao, J., and Yatsunyk, L. A. (2022) The first crystal structures of hybrid and parallel four-tetrad intramolecular G-quadruplexes. Nucleic Acids Res. 50, 2959-2972
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
Huang, P. - T., Summers, B. James, Xu, C., Perilla, J. R., Malikov, V., Naghavi, M. H., and Xiong, Y. (2019) FEZ1 Is Recruited to a Conserved Cofactor Site on Capsid to Promote HIV-1 Trafficking. Cell Rep. 28, 2373-2385.e7
Debler, E. W., Ma, Y., Seo, H. - S., Hsia, K. - C., Noriega, T. R., Blobel, G., and Hoelz, A. (2008) A fence-like coat for the nuclear pore membrane. Mol Cell. 32, 815-26
Van Wagoner, R. M., and Clardy, J. (2006) FeeM, an N-acyl amino acid synthase from an uncultured soil microbe: structure, mechanism, and acyl carrier protein binding. Structure. 14, 1425-35
Perry, K. (2021) Featured Friend. Molecular Biology and Chemistry Seminar Series
Rana, M. S., Kumar, P., Lee, C. - J., Verardi, R., Rajashankar, K. R., and Banerjee, A. (2018) Fatty acyl recognition and transfer by an integral membrane S-acyltransferase. Science. 10.1126/science.aao6326
Tararina, M. A., Dam, K. K., Dhingra, M., Janda, K. D., Palfey, B. A., and Allen, K. N. (2021) Fast Kinetics Reveals Rate-Limiting Oxidation and the Role of the Aromatic Cage in the Mechanism of the Nicotine-Degrading Enzyme NicA2. Biochemistry. 60, 259-273
Wang, L., Yang, J. Kuk, Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Young, Yin, Q., Damko, E., Jang, S. Bok, Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., and Wu, H. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 17, 1324-9
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

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