Publications

Found 49 results
Filters: First Letter Of Title is F  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
F
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
Hangasky, J. A., Taabazuing, C. Y., Martin, C. B., Eron, S. J., and Knapp, M. J. (2017) The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O activation.. J Inorg Biochem. 166, 26-33
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
Ceccarelli, D. F., Ivantsiv, S., Mullin, A. Anne, Coyaud, E., Manczyk, N., Maisonneuve, P., Kurinov, I., Zhao, L., Go, C., Gingras, A. - C., Raught, B., Cordes, S., and Sicheri, F. (2019) FAM105A/OTULINL Is a Pseudodebuiquitinase of the OTU-Class that Localizes to the ER Membrane. Structure. 10.1016/j.str.2019.03.022
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
Cheng, S., Park, Y., Kurleto, J. D., Jeon, M., Zinn, K., Thornton, J. W., and zkan, E. Ö. (2019) Family of neural wiring receptors in bilaterians defined by phylogenetic, biochemical, and structural evidence. Proc Natl Acad Sci U S A. 10.1073/pnas.1818631116
Harrison, O. J., Brasch, J., Katsamba, P. S., Ahlsen, G., Noble, A. J., Dan, H., Sampogna, R. V., Potter, C. S., Carragher, B., Honig, B., and Shapiro, L. (2020) Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.. Cell Rep. 30, 2655-2671.e7
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
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
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
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
Perry, K. (2021) Featured Friend. Molecular Biology and Chemistry Seminar Series
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
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
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
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
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
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
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
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
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
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
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
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
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

Pages