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Channel activities of the full-length prion and truncated proteins
Wu, J., Wang, X., Lakkaraju, A., Sternke-Hoffmann, R., Qureshi, B. M., Aguzzi, A., & Luo, J. (2024). Channel activities of the full-length prion and truncated proteins. ACS Chemical Neuroscience, 15(1), 98-107. https://doi.org/10.1021/acschemneuro.3c00412
Fast imaging of millimeter-scale areas with beam deflection transmission electron microscopy
Zheng, Z., Own, C. S., Wanner, A. A., Koene, R. A., Hammerschmith, E. W., Silversmith, W. M., … Seung, H. S. (2024). Fast imaging of millimeter-scale areas with beam deflection transmission electron microscopy. Nature Communications, 15(1), 6860 (11 pp.). https://doi.org/10.1038/s41467-024-50846-4
Sequential chromogenic IHC: spatial analysis of lymph nodes identifies contact interactions between plasmacytoid dendritic cells and plasmablasts
Claudio, N., Nguyen, M. T., Wanner, A., & Pucci, F. (2023). Sequential chromogenic IHC: spatial analysis of lymph nodes identifies contact interactions between plasmacytoid dendritic cells and plasmablasts. Cancer Research Communications, 3(7), 1237-1247. https://doi.org/10.1158/2767-9764.CRC-23-0102
Oligomer dynamics of LL-37 truncated fragments probed by <em>α</em>-hemolysin pore and molecular simulations
Liu, C., Henning-Knechtel, A., Österlund, N., Wu, J., Wang, G., Gräslund, R. A. O., … Luo, J. (2023). Oligomer dynamics of LL-37 truncated fragments probed by α-hemolysin pore and molecular simulations. Small, 19(37), 2206232 (11 pp.). https://doi.org/10.1002/smll.202206232
Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases
Loch, R. A., Wang, H., Perálvarez-Marín, A., Berger, P., Nielsen, H., Chroni, A., & Luo, J. (2023). Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases. Computational and Structural Biotechnology Journal, 21, 1189-1204. https://doi.org/10.1016/j.csbj.2023.01.022
Single-molecule nanopore dielectrophoretic trapping of α-synuclein with lipid membranes
Wu, J., Yamashita, T., Hamilton, A. D., Thompson, S., & Luo, J. (2023). Single-molecule nanopore dielectrophoretic trapping of α-synuclein with lipid membranes. Cell Reports Physical Science, 4(2), 101243 (13 pp.). https://doi.org/10.1016/j.xcrp.2022.101243
Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation
Bavinton, C. E., Sternke-Hoffmann, R., Yamashita, T., Knipe, P. C., Hamilton, A. D., Luo, J., & Thompson, S. (2022). Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation. Chemical Communications, 58(33), 5132-5135. https://doi.org/10.1039/d2cc00212d
Michaelis-Menten quantification of ligand signaling bias applied to the promiscuous vasopressin V2 receptor
Heydenreich, F. M., Plouffe, B., Rizk, A., Milić, D., Zhou, J., Breton, B., … Veprintsev, D. B. (2022). Michaelis-Menten quantification of ligand signaling bias applied to the promiscuous vasopressin V2 receptor. Molecular Pharmacology, 102(3), 139-149. https://doi.org/10.1124/molpharm.122.000497
Evaluation of Zn<sup>2+</sup>- and Cu<sup>2+</sup>-binding affinities of native Cu,Zn-SOD1 and its G93A mutant by LC-ICP MS
Smirnova, J., Gavrilova, J., Noormägi, A., Valmsen, K., Pupart, H., Luo, J., … Palumaa, P. (2022). Evaluation of Zn2+- and Cu2+-binding affinities of native Cu,Zn-SOD1 and its G93A mutant by LC-ICP MS. Molecules, 27(10), 3160 (11 pp.). https://doi.org/10.3390/molecules27103160
In situ X-ray-assisted electron microscopy staining for large biological samples
Ströh, S., Hammerschmith, E. W., Tank, D. W., Seung, H. S., & Wanner, A. A. (2022). In situ X-ray-assisted electron microscopy staining for large biological samples. eLife, 11, e72147 (19 pp.). https://doi.org/10.7554/eLife.72147
Automated synapse-level reconstruction of neural circuits in the larval zebrafish brain
Svara, F., Förster, D., Kubo, F., Januszewski, M., dal Maschio, M., Schubert, P. J., … Baier, H. (2022). Automated synapse-level reconstruction of neural circuits in the larval zebrafish brain. Nature Methods, 19, 1357-1366. https://doi.org/10.1038/s41592-022-01621-0
Cu<sup>2+</sup> ions modulate the interaction between α-synuclein and lipid membranes
Wang, H., Mörman, C., Sternke-Hoffmann, R., Huang, C. Y., Prota, A., Ma, P., & Luo, J. (2022). Cu2+ ions modulate the interaction between α-synuclein and lipid membranes. Journal of Inorganic Biochemistry, 236, 111945 (10 pp.). https://doi.org/10.1016/j.jinorgbio.2022.111945
Multivariate effects of pH, salt, and Zn<sup>2+</sup> ions on Aβ<sub>40</sub> fibrillation
Wang, H., Wu, J., Sternke-Hoffmann, R., Zheng, W., Mörman, C., & Luo, J. (2022). Multivariate effects of pH, salt, and Zn2+ ions on Aβ40 fibrillation. Communications Chemistry, 5(1), 171 (12 pp.). https://doi.org/10.1038/s42004-022-00786-1
Identifying the role of co-aggregation of Alzheimer's amyloid-β with amorphous protein aggregates of non-amyloid proteins
Wu, J., Österlund, N., Wang, H., Sternke-Hoffmann, R., Pupart, H., Ilag, L. L., … Luo, J. (2022). Identifying the role of co-aggregation of Alzheimer's amyloid-β with amorphous protein aggregates of non-amyloid proteins. Cell Reports Physical Science, 3(9), 101028 (22 pp.). https://doi.org/10.1016/j.xcrp.2022.101028
Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ<sub>1-42</sub> aggregation
Zhang, Q., Liu, Y., Wu, J., Zeng, L., Wei, J., Fu, S., … Gao, Z. (2022). Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ1-42 aggregation. Inorganic Chemistry Frontiers, 9(7), 1520-1532. https://doi.org/10.1039/d1qi01434j
Editorial: the biochemistry of amyloids in neurodegenerative diseases, volume I
Gomes, C. M., Hoyer, W., & Luo, J. (2021). Editorial: the biochemistry of amyloids in neurodegenerative diseases, volume I. Frontiers in Neuroscience, 15, 819481 (2 pp.). https://doi.org/10.3389/fnins.2021.819481
Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L<sub>2,3</sub><sub>-</sub>edge soft X-ray absorption spectroscopy
Luo, J., Wang, H., Wu, J., Romankov, V., Daffé, N., & Dreiser, J. (2021). Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy. iScience, 24(12), 103465 (11 pp.). https://doi.org/10.1016/j.isci.2021.103465
Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone
Romantini, N., Alam, S., Dobitz, S., Spillmann, M., De Foresta, M., Schibli, R., … Berger, P. (2021). Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone. Proceedings of the National Academy of Sciences of the United States of America PNAS, 118(48), e2108776118 (8 pp.). https://doi.org/10.1073/pnas.2108776118
ATP impedes the inhibitory effect of Hsp90 on Aβ&lt;sub&gt;40&lt;/sub&gt; fibrillation
Wang, H., Lallemang, M., Hermann, B., Wallin, C., Loch, R., Blanc, A., … Luo, J. (2021). ATP impedes the inhibitory effect of Hsp90 on Aβ40 fibrillation. Journal of Molecular Biology, 433(2), 166717 (16 pp.). https://doi.org/10.1016/j.jmb.2020.11.016
Cryo-electron microscopy imaging of Alzheimer's amyloid-beta 42 oligomer displayed on a functionally and structurally relevant scaffold
Wu, J., Blum, T. B., Farrell, D. P., DiMaio, F., Abrahams, J. P., & Luo, J. (2021). Cryo-electron microscopy imaging of Alzheimer's amyloid-beta 42 oligomer displayed on a functionally and structurally relevant scaffold. Angewandte Chemie International Edition, 60(34), 18680-18687. https://doi.org/10.1002/anie.202104497