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Homodimerization of coronin A through the C-terminal coiled-coil domain is essential for multicellular differentiation of <em>Dictyostelium discoideum</em>
Fiedler, T., Fabrice, T. N., Studer, V., Vinet, A., Faltova, L., Kammerer, R. A., … Pieters, J. (2020). Homodimerization of coronin A through the C-terminal coiled-coil domain is essential for multicellular differentiation of Dictyostelium discoideum. FEBS Letters, 594(13), 2116-2127. https://doi.org/10.1002/1873-3468.13787
The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in <em>Enterococcus faecalis</em> quorum sensing
Littlewood, S., Tattersall, H., Hughes, C. S., Hussain, R., Ma, P., Harding, S. E., … Phillips-Jones, M. K. (2020). The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensing. FEBS Letters, 594(3), 553-563. https://doi.org/10.1002/1873-3468.13634
Crystal structure of the human NLRP9 pyrin domain suggests a distinct mode of inflammasome assembly
Marleaux, M., Anand, K., Latz, E., & Geyer, M. (2020). Crystal structure of the human NLRP9 pyrin domain suggests a distinct mode of inflammasome assembly. FEBS Letters, 594(15), 2383-2395. https://doi.org/10.1002/1873-3468.13865
Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines
Savino, S., Jensen, S., Terwisscha van Scheltinga, A., & Fraaije, M. W. (2020). Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines. FEBS Letters, 594(17), 2819-2828. https://doi.org/10.1002/1873-3468.13854
Biophysical and structural insight into the USP8/14-3-3 interaction
Centorrino, F., Ballone, A., Wolter, M., & Ottmann, C. (2018). Biophysical and structural insight into the USP8/14-3-3 interaction. FEBS Letters, 592(7), 1211-1220. https://doi.org/10.1002/1873-3468.13017
Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction
Demmer, J. K., Bertsch, J., Öppinger, C., Wohlers, H., Kayastha, K., Demmer, U., … Müller, V. (2018). Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction. FEBS Letters, 592(3), 332-342. https://doi.org/10.1002/1873-3468.12971
Small-molecule stabilization of the p53 – 14-3-3 protein-protein interaction
Doveston, R. G., Kuusk, A., Andrei, S. A., Leysen, S., Cao, Q., Castaldi, M. P., … Ottmann, C. (2017). Small-molecule stabilization of the p53 – 14-3-3 protein-protein interaction. FEBS Letters, 591(16), 2449-2457. https://doi.org/10.1002/1873-3468.12723
Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands
Elegheert, J., Brigé, A., Van Beeumen, J., & Savvides, S. N. (2017). Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands. FEBS Letters, 591(20), 3391-3401. https://doi.org/10.1002/1873-3468.12833
Mutations in the tetramer interface of human glucose-6-phosphate dehydrogenase reveals kinetic differences between oligomeric states
Ranzani, A. T., & Cordeiro, A. T. (2017). Mutations in the tetramer interface of human glucose-6-phosphate dehydrogenase reveals kinetic differences between oligomeric states. FEBS Letters, 591(9), 1278-1284. https://doi.org/10.1002/1873-3468.12638
Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity
Siegrist, J., Netzer, J., Mordhorst, S., Karst, L., Gerhardt, S., Einsle, O., … Andexer, J. N. (2017). Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity. FEBS Letters, 591(2), 312-321. https://doi.org/10.1002/1873-3468.12530
Structure of OxyAtei: Completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade
Haslinger, K., & Cryle, M. J. (2016). Structure of OxyAtei: Completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade. FEBS Letters, 590(4), 571-581. https://doi.org/10.1002/1873-3468.12081
Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction
Scott, D. E., Marsh, M., Blundell, T. L., Abell, C., & Hyvönen, M. (2016). Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction. FEBS Letters, 590(8), 1094-1102. https://doi.org/10.1002/1873-3468.12139
A novel esterase subfamily with α/β-hydrolase fold suggested by structures of two bacterial enzymes homologous to L-homoserine O-acetyl transferases
Tölzer, C., Pal, S., Watzlawick, H., Altenbuchner, J., & Niefind, K. (2016). A novel esterase subfamily with α/β-hydrolase fold suggested by structures of two bacterial enzymes homologous to L-homoserine O-acetyl transferases. FEBS Letters, 590(1), 174-184. https://doi.org/10.1002/1873-3468.12031
X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis
Weidenweber, S., Marmulla, R., Ermler, U., & Harder, J. (2016). X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis. FEBS Letters, 590(9), 1375-1383. https://doi.org/10.1002/1873-3468.12165
C-di-AMP recognition by Staphylococcus aureus PstA
Müller, M., Hopfner, K. P., & Witte, G. (2015). C-di-AMP recognition by Staphylococcus aureus PstA. FEBS Letters, 589(1), 45-51. https://doi.org/10.1016/J.FEBSLET.2014.11.022
A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis
Fujishiro, T., Ermler, U., & Shima, S. (2014). A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis. FEBS Letters, 588(17), 2789-2793. https://doi.org/10.1016/j.febslet.2014.05.059
Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide
Reubold, T. F., Hahne, G., Wohlgemuth, S., & Eschenburg, S. (2014). Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide. FEBS Letters, 588(18), 3327-3332. https://doi.org/10.1016/j.febslet.2014.07.017
Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum
Rekittke, I., Olkhova, E., Wiesner, J., Demmer, U., Warkentin, E., Jomaa, H., & Ermler, U. (2013). Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum. FEBS Letters, 587(24), 3968-3972. https://doi.org/10.1016/j.febslet.2013.10.029
Establishing catalytic activity on an artificial (βα) 8-barrel protein designed from identical half-barrels
Sperl, J. M., Rohweder, B., Rajendran, C., & Sterner, R. (2013). Establishing catalytic activity on an artificial (βα) 8-barrel protein designed from identical half-barrels. FEBS Letters, 587(17), 2798-2805. https://doi.org/10.1016/j.febslet.2013.06.022
Boron-based phosphodiesterase inhibitors show novel binding of boron to PDE4 bimetal center
Freund, Y. R., Akama, T., Alley, M. R. K., Antunes, J., Dong, C., Jarnagin, K., … Zhou, Y. (2012). Boron-based phosphodiesterase inhibitors show novel binding of boron to PDE4 bimetal center. FEBS Letters, 586(19), 3410-3414. https://doi.org/10.1016/j.febslet.2012.07.058