Publications

Found 31 results
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Bunker, R. D., Mandal, K., Bashiri, G., Chaston, J. J., Pentelute, B. L., J Lott, S., Kent, S. B. H., and Baker, E. N. (2015) A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography. Proc Natl Acad Sci U S A. 112, 4310-5
Shelton, C. L., Conrady, D. G., and Herr, A. B. (2017) Functional consequences of B-repeat sequence variation in the staphylococcal biofilm protein Aap: deciphering the assembly code. Biochem J. 474, 427-443
Posternak, G., Tang, X., Maisonneuve, P., Jin, T., Lavoie, H., Daou, S., Orlicky, S., de Rugy, T. Goullet, Caldwell, L., Chan, K., Aman, A., Prakesch, M., Poda, G., Mader, P., Wong, C., Maier, S., Kitaygorodsky, J., Larsen, B., Colwill, K., Yin, Z., Ceccarelli, D. F., Batey, R. A., Taipale, M., Kurinov, I., Uehling, D., Wrana, J., Durocher, D., Gingras, A. - C., Al-awar, R., Therrien, M., and Sicheri, F. (2020) Functional characterization of a PROTAC directed against BRAF mutant V600E. Nat Chem Biol. 10.1038/s41589-020-0609-7
Hameed, U., Price, I., Ke, A., Wilson, D. B., and Mirza, O. (2017) Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization. Biochim Biophys Acta. 1865, 1237-1245
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
Chowdhury, C., Chun, S., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2016) The function of the PduJ microcompartment shell protein is determined by the genomic position of its encoding gene. Mol Microbiol. 101, 770-83
Avital-Shmilovici, M., Mandal, K., Gates, Z. P., Phillips, N. B., Weiss, M. A., and Kent, S. B. H. (2013) Fully convergent chemical synthesis of ester insulin: determination of the high resolution X-ray structure by racemic protein crystallography. J Am Chem Soc. 135, 3173-85
Schiltz, C. J., Adams, M. C., and Chappie, J. S. (2020) The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases. Nucleic Acids Res. 48, 2762-2776
Eser, B. E., Zhang, X., Chanani, P. K., Begley, T. P., and Ealick, S. E. (2016) From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis. J Am Chem Soc. 138, 3639-42
Morar, M., Hoskins, A. A., Stubbe, J. A., and Ealick, S. E. (2008) Formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima: structural insights into complex formation. Biochemistry. 47, 7816-30
Blaha, G., Stanley, R. E., and Steitz, T. A. (2009) Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science. 325, 966-70
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
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
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
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
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
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
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

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