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A set of closely related methyltransferases for site-specific tailoring of anthraquinone pigments
Huber, E. M., Kreling, L., Heinrich, A. K., Dünnebacke, M., Pöthig, A., Bode, H. B., & Groll, M. (2023). A set of closely related methyltransferases for site-specific tailoring of anthraquinone pigments. Structure, 31(5), 573-583.e5. https://doi.org/10.1016/j.str.2023.03.001
An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity
Beaumet, M., Dose, A., Bräuer, A., Mahy, J. P., Ghattas, W., Groll, M., & Hess, C. R. (2022). An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity. Journal of Inorganic Biochemistry, 235, 111914 (5 pp.). https://doi.org/10.1016/j.jinorgbio.2022.111914
A specialized polythioamide-binding protein confers antibiotic self-resistance in anaerobic bacteria
Gude, F., Molloy, E. M., Horch, T., Dell, M., Dunbar, K. L., Krabbe, J., … Hertweck, C. (2022). A specialized polythioamide-binding protein confers antibiotic self-resistance in anaerobic bacteria. Angewandte Chemie International Edition, 61(37), e202206168 (9 pp.). https://doi.org/10.1002/anie.202206168
Structural and mechanistic insights into C-S bond formation in gliotoxin
Scherlach, K., Kuttenlochner, W., Scharf, D. H., Brakhage, A. A., Hertweck, C., Groll, M., & Huber, E. M. (2021). Structural and mechanistic insights into C-S bond formation in gliotoxin. Angewandte Chemie International Edition, 60(25), 14188-14194. https://doi.org/10.1002/anie.202104372
A transmembrane crenarchaeal mannosyltransferase is involved in <em>N</em>-glycan biosynthesis and displays an unexpected minimal cellulose-synthase-like fold
Gandini, R., Reichenbach, T., Spadiut, O., Tan, T. C., Kalyani, D. C., & Divne, C. (2020). A transmembrane crenarchaeal mannosyltransferase is involved in N-glycan biosynthesis and displays an unexpected minimal cellulose-synthase-like fold. Journal of Molecular Biology, 432(16), 4658-4672. https://doi.org/10.1016/j.jmb.2020.06.016
Structural basis of HapE<sup>P88L</sup>-linked antifungal triazole resistance in <em>Aspergillus fumigatus</em>
Hortschansky, P., Misslinger, M., Mörl, J., Gsaller, F., Bromley, M. J., Brakhage, A. A., … Huber, E. M. (2020). Structural basis of HapEP88L-linked antifungal triazole resistance in Aspergillus fumigatus. Life Science Alliance, 3(7), e202000729 (12 pp.). https://doi.org/10.26508/lsa.202000729
Crystal structure of the translation recovery factor Trf from <em>Sulfolobus solfataricus</em>
Kaiser, M., Wurm, J. P., Märtens, B., Bläsi, U., Pogoryelov, D., & Wöhnert, J. (2020). Crystal structure of the translation recovery factor Trf from Sulfolobus solfataricus. FEBS Open Bio, 10(2), 221-228. https://doi.org/10.1002/2211-5463.12772
Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of <em>m</em>-cresol
Karavassili, F., Valmas, A., Dimarogona, M., Giannopoulou, A. E., Fili, S., Norrman, M., … Margiolaki, I. (2020). Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of m-cresol. Acta Crystallographica Section D: Structural Biology, 76, 366-374. https://doi.org/10.1107/S2059798320002545
Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase
Griese, J. J., Kositzki, R., Haumann, M., & Högbom, M. (2019). Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase. Journal of Biological Inorganic Chemistry, 24(2), 211-221. https://doi.org/10.1007/s00775-019-01639-4
Redox-induced structural changes in the di-iron and di-manganese forms of <em>Bacillus anthracis</em> ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
Grāve, K., Lambert, W., Berggren, G., Griese, J. J., Bennett, M. D., Logan, D. T., & Högbom, M. (2019). Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access. Journal of Biological Inorganic Chemistry, 24(6), 849-861. https://doi.org/10.1007/s00775-019-01703-z
Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins
Kutin, Y., Kositzki, R., Branca, R. M. M., Srinivas, V., Lundin, D., Haumann, M., … Griese, J. J. (2019). Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins. Journal of Biological Chemistry, 294(48), 18372-18386. https://doi.org/10.1074/jbc.RA119.010570
Molecular determinants of the mechanism and substrate specificity of <em>Clostridium difficile</em> proline-proline endopeptidase-1
Pichlo, C., Juetten, L., Wojtalla, F., Schacherl, M., Diaz, D., & Baumann, U. (2019). Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1. Journal of Biological Chemistry, 294(30), 11525-11535. https://doi.org/10.1074/jbc.RA119.009029
The structure of the catalytic domain of the ATP synthase from <i>Mycobacterium smegmatis</i> is a target for developing antitubercular drugs
Zhang, A. T., Montgomery, M. G., Leslie, A. G. W., Cook, G. M., & Walker, J. E. (2019). The structure of the catalytic domain of the ATP synthase from Mycobacterium smegmatis is a target for developing antitubercular drugs. Proceedings of the National Academy of Sciences of the United States of America PNAS, 116(10), 4206-4211. https://doi.org/10.1073/pnas.1817615116
Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties
Fuchs, A. C. D., Maldoner, L., Hipp, K., Hartmann, M. D., & Martin, J. (2018). Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties. Journal of Biological Chemistry, 293(3), 920-930. https://doi.org/10.1074/jbc.M117.815258
Ether cross-link formation in the R2-like ligand-binding oxidase
Griese, J. J., Branca, R. M. M., Srinivas, V., & Högbom, M. (2018). Ether cross-link formation in the R2-like ligand-binding oxidase. Journal of Biological Inorganic Chemistry, 23(6), 879-886. https://doi.org/10.1007/s00775-018-1583-3
(−)-Homosalinosporamide A and its mode of proteasome inhibition: an X-ray crystallographic study
Groll, M., Nguyen, H., Vellalath, S., & Romo, D. (2018). (−)-Homosalinosporamide A and its mode of proteasome inhibition: an X-ray crystallographic study. Marine Drugs, 16(7), 240 (9 pp.). https://doi.org/10.3390/md16070240
Generation of conformation-specific antibody fragments for crystallization of the multidrug resistance transporter MdfA
Jaenecke, F., Nakada-Nakura, Y., Nagarathinam, K., Ogasawara, S., Liu, K., Hotta, Y., … Tanabe, M. (2018). Generation of conformation-specific antibody fragments for crystallization of the multidrug resistance transporter MdfA. In A. Yamaguchi & K. Nishino (Eds.), Methods in molecular biology: Vol. 1700. Bacterial multidrug exporters. Methods and protocols (pp. 97-109). https://doi.org/10.1007/978-1-4939-7454-2_7
Outward open conformation of a Major Facilitator Superfamily multidrug/H&lt;sup&gt;+&lt;/sup&gt; antiporter provides insights into switching mechanism
Nagarathinam, K., Nakada-Nakura, Y., Parthier, C., Terada, T., Juge, N., Jaenecke, F., … Tanabe, M. (2018). Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism. Nature Communications, 9(1), 4005 (9 pp.). https://doi.org/10.1038/s41467-018-06306-x
Design, synthesis, and evaluation of cystargolide-based β-lactones as potent proteasome inhibitors
Niroula, D., Hallada, L. P., Le Chapelain, C., Ganegamage, S. K., Dotson, D., Rogelj, S., … Tello-Aburto, R. (2018). Design, synthesis, and evaluation of cystargolide-based β-lactones as potent proteasome inhibitors. European Journal of Medicinal Chemistry, 157, 962-977. https://doi.org/10.1016/j.ejmech.2018.08.052
The &lt;em&gt;Y. bercovieri&lt;/em&gt; Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers
Piasecka, A., Czapinska, H., Vielberg, M. T., Szczepanowski, R. H., Kiefersauer, R., Reed, S., … Bochtler, M. (2018). The Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers. Journal of Molecular Biology, 430(5), 611-627. https://doi.org/10.1016/j.jmb.2017.11.016
 

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