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Benziodarone and 6-hydroxybenziodarone are potent and selective inhibitors of transthyretin amyloidogenesis
Mizuguchi, M., Yokoyama, T., Okada, T., Nakagawa, Y., Fujii, K., Nabeshima, Y., & Toyooka, N. (2023). Benziodarone and 6-hydroxybenziodarone are potent and selective inhibitors of transthyretin amyloidogenesis. Bioorganic and Medicinal Chemistry, 90, 117370 (12 pp.). https://doi.org/10.1016/j.bmc.2023.117370
Fragment ligands of the m<sup>6</sup>A-RNA reader YTHDF2
Nai, F., Nachawati, R., Zálešák, F., Wang, X., Li, Y., & Caflisch, A. (2022). Fragment ligands of the m6A-RNA reader YTHDF2. ACS Medicinal Chemistry Letters, 13(9), 1500-1509. https://doi.org/10.1021/acsmedchemlett.2c00303
A non-helical region in transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition
Focht, D., Neumann, C., Lyons, J., Eguskiza Bilbao, A., Blunck, R., Malinauskaite, L., … Nissen, P. (2021). A non-helical region in transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition. EMBO Journal, 40(1), e105164 (13 pp.). https://doi.org/10.15252/embj.2020105164
Systematic engineering of optimized autonomous heavy-chain variable domains
Nilvebrant, J., Ereño-Orbea, J., Gorelik, M., Julian, M. C., Tessier, P. M., Julien, J. P., & Sidhu, S. S. (2021). Systematic engineering of optimized autonomous heavy-chain variable domains. Journal of Molecular Biology, 433(21), 167241 (18 pp.). https://doi.org/10.1016/j.jmb.2021.167241
Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern
Signor, L., Paris, T., Mas, C., Picard, A., Lutfalla, G., Boeri Erba, E., & Yatime, L. (2021). Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern. Journal of Structural Biology, 213(1), 107689 (16 pp.). https://doi.org/10.1016/j.jsb.2020.107689
Two RNA tunnel inhibitors bind in highly conserved sites in dengue virus NS5 polymerase: structural and functional studies
Arora, R., Liew, C. W., Soh, T. S., Otoo, D. A., Seh, C. C., Yue, K., … Lim, S. P. (2020). Two RNA tunnel inhibitors bind in highly conserved sites in dengue virus NS5 polymerase: structural and functional studies. Journal of Virology, 94(24), e01130-20 (17 pp.). https://doi.org/10.1128/JVI.01130-20
High-resolution crystal structures of a &quot;half sandwich&quot;-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K
Chiniadis, L., Bratsos, I., Bethanis, K., Karpusas, M., Giastas, P., & Papakyriakou, A. (2020). High-resolution crystal structures of a "half sandwich"-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K. Journal of Biological Inorganic Chemistry, 25, 635-645. https://doi.org/10.1007/s00775-020-01786-z
Recognition of different base tetrads by RHAU (DHX36): X-ray crystal structure of the G4 recognition motif bound to the 3′-end tetrad of a DNA G-quadruplex
Heddi, B., Cheong, V. V., Schmitt, E., Mechulam, Y., & Phan, A. T. (2020). Recognition of different base tetrads by RHAU (DHX36): X-ray crystal structure of the G4 recognition motif bound to the 3′-end tetrad of a DNA G-quadruplex. Journal of Structural Biology, 209(1), 107399 (8 pp.). https://doi.org/10.1016/j.jsb.2019.10.001
The hydride transfer process in NADP-dependent methylene-tetrahydromethanopterin dehydrogenase
Huang, G., Wagner, T., Demmer, U., Warkentin, E., Ermler, U., & Shima, S. (2020). The hydride transfer process in NADP-dependent methylene-tetrahydromethanopterin dehydrogenase. Journal of Molecular Biology, 432(7), 2042-2054. https://doi.org/10.1016/j.jmb.2020.01.042
Snapshots of PLP-substrate and PLP-product external aldimines as intermediates in two types of cysteine desulfurase enzymes
Nakamura, R., Hikita, M., Ogawa, S., Takahashi, Y., & Fujishiro, T. (2020). Snapshots of PLP-substrate and PLP-product external aldimines as intermediates in two types of cysteine desulfurase enzymes. FEBS Journal, 287(6), 1138-1154. https://doi.org/10.1111/febs.15081
Unexpected CK2β-antagonistic functionality of bisubstrate inhibitors targeting protein kinase CK2
Pietsch, M., Viht, K., Schnitzler, A., Ekambaram, R., Steinkrüger, M., Enkvist, E., … Niefind, K. (2020). Unexpected CK2β-antagonistic functionality of bisubstrate inhibitors targeting protein kinase CK2. Bioorganic Chemistry, 96, 103608 (8 pp.). https://doi.org/10.1016/j.bioorg.2020.103608
Structural states of Hdm2 and HdmX: X-ray elucidation of adaptations and binding interactions for different chemical compound classes
Kallen, J., Izaac, A., Chau, S., Wirth, E., Schoepfer, J., Mah, R., … Furet, P. (2019). Structural states of Hdm2 and HdmX: X-ray elucidation of adaptations and binding interactions for different chemical compound classes. ChemMedChem, 14(14), 1305-1314. https://doi.org/10.1002/cmdc.201900201
Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach
Kaur, H., Hartmann, J. B., Jakob, R. P., Zahn, M., Zimmermann, I., Maier, T., … Hiller, S. (2019). Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach. Journal of Biomolecular NMR, 73(6-7), 375-384. https://doi.org/10.1007/s10858-019-00250-8
The structure of an archaeal B-family DNA polymerase in complex with a chemically modified nucleotide
Kropp, H. M., Diederichs, K., & Marx, A. (2019). The structure of an archaeal B-family DNA polymerase in complex with a chemically modified nucleotide. Angewandte Chemie International Edition, 58(16), 5457-5461. https://doi.org/10.1002/anie.201900315
Structure of outward-facing PglK and molecular dynamics of lipid-linked oligosaccharide recognition and translocation
Perez, C., Mehdipour, A. R., Hummer, G., & Locher, K. P. (2019). Structure of outward-facing PglK and molecular dynamics of lipid-linked oligosaccharide recognition and translocation. Structure, 27(4), 669-678.e5. https://doi.org/10.1016/j.str.2019.01.013
A comprehensive analysis of the protein-ligand interactions in crystal structures of <em>Mycobacterium tuberculosis</em> EthR
Tanina, A., Wohlkönig, A., Soror, S. H., Flipo, M., Villemagne, B., Prevet, H., … Wintjens, R. (2019). A comprehensive analysis of the protein-ligand interactions in crystal structures of Mycobacterium tuberculosis EthR. Biochimica et Biophysica Acta: Proteins and Proteomics, 1867(3), 248-258. https://doi.org/10.1016/j.bbapap.2018.12.003
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
Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-&lt;em&gt;c&lt;/em&gt;]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase
Crespo, I., Giménez-Dejoz, J., Porté, S., Cousido-Siah, A., Mitschler, A., Podjarny, A., … Farrés, J. (2018). Design, synthesis, structure-activity relationships and X-ray structural studies of novel 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivatives as selective and potent inhibitors of human aldose reductase. European Journal of Medicinal Chemistry, 152, 160-174. https://doi.org/10.1016/j.ejmech.2018.04.015
Structural analysis of small-molecule binding to the BAZ2A and BAZ2B Bromodomains
Dalle Vedove, A., Spiliotopoulos, D., D'Agostino, V. G., Marchand, J. R., Unzue, A., Nevado, C., … Caflisch, A. (2018). Structural analysis of small-molecule binding to the BAZ2A and BAZ2B Bromodomains. ChemMedChem, 13(14), 1479-1487. https://doi.org/10.1002/cmdc.201800234
Evolutionary morphing of tryptophan synthase: functional mechanisms for the enzymatic channeling of indole
Fleming, J. R., Schupfner, M., Busch, F., Baslé, A., Ehrmann, A., Sterner, R., & Mayans, O. (2018). Evolutionary morphing of tryptophan synthase: functional mechanisms for the enzymatic channeling of indole. Journal of Molecular Biology, 430(24), 5066-5079. https://doi.org/10.1016/j.jmb.2018.10.013
 

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