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Amytracker - References

2026

  • Labra, S. R., Compher, J., Prabhavalkar, A., Almaraz, M., Cedeño Kwong, C., Baal, C., Talantova, M., Dolatabadi, N., Piña-Sanz, J., Wang, Y., Yoon, L., Ghatak, S., Gao, Z., Zhang, Y., Trudler, D., Massey, L., Lin, W., Balistreri, A., Bula, M., Schork, N., Mandala, T., Head, S., Kelly, J. & Lipton, S. A. (2026). Autophagy Activators Normalize Aberrant Tau Proteostasis and Rescue Synapses in Human Familial Alzheimer’s Disease iPSC-Derived Cortical Organoids. Advanced Science 13(17), e14783. https://doi.org/10.1002/ADVS.202514783
  • Featherby, S. J., Faulkner, E. C., Gordon, A., & Ettelaie, C. (2026). Procoagulant Extracellular Vesicles Increase Neuronal Tau expression, Metabolism and Processing Through Tissue Factor and Protease Activated Receptor 2. Cellular and Molecular Neurobiology 46(1), 21-. https://doi.org/10.1007/S10571-025-01658-7
  • da Silva, I. A. N., Paulus, A., Skoryk, V., Su, K. Y., Herranz-Trillo, F., & Klementieva, O. (2026). Polystyrene nanoplastic exposure promotes amyloid misfolding and metabolic impairment at sublethal doses. A subcellular infrared imaging study. Environmental Science: Nano 13(4), 1948–1961. https://doi.org/10.1039/D5EN01181G
  • Ariyath, A., Arigo, F. D., Wallach, I., Fernando, W. M. A. D. B., Martins, R. N., & Bharadwaj, P. (2026). Novel Small-Molecule Analogues of IU1 Ameliorate Amyloid-β Mediated Toxicity in Alzheimer’s Disease Cell and Worm Models. International Journal of Molecular Sciences 27(4), 1963. https://doi.org/10.3390/IJMS27041963/S1
  • de Schepper, S., Konstantellos, V., Conway, J. A., Sokolova, D., Zaccagnini, L., Cowley, M. v., Sierksma, A., Yudina, M., Edmonds, M., Gavriouchkina, D., Geary, B., Wallis, A., Celikag, M., Baykam, Z., Vara-Pérez, M., Crowley, G., Hager, F. T., Bijnen, M., Posner, D., Luk, K., Cerovic, V., Clatworthy, M., Videlock, E., Jaunmuktane, Z., Movahedi, K., Greater, M. Chain, B. Alessi, D., Hong, S. & Bartels, T. (2026). Intestinal macrophages modulate synucleinopathy along the gut–brain axis. Nature 651(8104), 174–184. https://doi.org/10.1038/s41586-025-09984-y
  • Ferreon, J. C., Choi, K. J., Quan, M. D., Tsoi, P. S., Ferreon, C. C., Coskun, U., Liao, S. C. J., & Ferreon, A. C. M. (2026). Modulation of Biomolecular Aggregate Morphology and Condensate Infectivity. Biomolecules 16(4), 492.https://doi.org/10.3390/BIOM16040492/S1
  • Fischer, C. M., Edu, I. A., Šneideris, T., Baronaite, I., Toprakcioglu, Z., Deck, L. T., Qian, D., Scrutton, R., Dreyer, L., Wen, J., Otzen, D. E., Wu, S., Perrett, S., & Knowles, T. P. J. (2026). Reversibility and β-sheet formation are decoupled in tau condensate aging. PNAS 16(4), 492. https://doi.org/10.1073/PNAS.2522993123

2025

  • Zattoni, M., Bernegger, S., Weinbender, S., Altendorfer, B., Mrowetz, H., Benedetti, A., Poupardin, R., Unger, M. S., & Aigner, L. (2025). The involvement of microglia and the CXCL16-CXCR6 axis in the recruitment of CD8+ T cells to an amyloidogenic mouse brain. Scientific Reports, 15(1), 38221-. https://doi.org/10.1038/s41598-025-22137-5
  • Altendorfer, B., Benedetti, A., Mrowetz, H., Bernegger, S., Bretl, A., Preishuber-Pflügl, J., Bessa de Sousa, D. M., Ladek, A. M., Koller, A., le Faouder, P., Bertrand-Michel, J., Trost, A., & Aigner, L. (2025). Omega-3 EPA Supplementation Shapes the Gut Microbiota Composition and Reduces Major Histocompatibility Complex Class II in Aged Wild-Type and APP/PS1 Alzheimer’s Mice: A Pilot Experimental Study. Nutrients, 17(7), 1108. https://doi.org/10.3390/nu17071108
  • Lee, J., Chin, N., Zou, J., Mazli, W. N. A. B., Jarnik, M., Saidi, L., Xu, Y., Jeong, E., Suh, J., Replogle, J., Ward, M. E., Bonifacino, J. S., Zheng, W., Hao, L., & Ye, Y. (2025). CHIP protects lysosomes from CLN4 mutant-induced membrane damage. Nature Cell Biology, 27(9), 1465–1481. https://doi.org/10.1038/S41556-025-01738-2
  • Urbanek, A., Garland, E. F., Prescott, E. E., King, M. C., Olerinyova, A., Wareing, H. E., Georgieva, N., Bradshaw, E. L., Tzokov, S. B., Knight, A., Tartakovskii, A. I., Malm, T., Highley, J. R., & De, S. (2025). Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level. Advanced Science, 15(8). https://doi.org/10.1002/ADVS.202410229
  • do Amaral, M. J., Passos, A. R., Mohapatra, S., Freire, M. H., Wegmann, S., & Cordeiro, Y. (2025). X-Ray Photon Correlation Spectroscopy, Microscopy, and Fluorescence Recovery After Photobleaching to Study Phase Separation and Liquid-to-Solid Transition of Prion Protein Condensates. Bio-Protocol, 15(8). https://doi.org/10.21769/BIOPROTOC.5277
  • Zhan, X., Li, W., Hatterer, E., Courade, J. P., Piché, K., Klementieva, O., & Li, J. Y. (2025). Strain-Distinct α-Synuclein and Tau Cross-Seeding Uncovered by Correlative Approach with Optical Photothermal Infrared Sub-Micron Imaging. Journal of the American Chemical Society, 147(31), 27323–27340. https://doi.org/10.1021/JACS.5C02811
  • Horvath, I., Aning, O. A., Kk, S., Rehnberg, N., Chawla, S., Molin, M., Westerlund, F., & Wittung-Stafshede, P. (2025). Biological Amyloids Chemically Damage DNA. ACS Chemical Neuroscience, 16(3), 355–364. https://doi.org/10.1021/ACSCHEMNEURO.4C00461
  • Puthia, M., Marzinek, J. K., Vesela, K., Larsson, A., Schmidtchen, A., Bond, P. J., &amp Petrlova, J. (2025). Apolipoprotein E3 and E4 isoforms exhibit differing effects in countering endotoxins. Journal of Biological Chemistry, 301(3), 108236. https://doi.org/10.1016/j.jbc.2025.108236
  • Nozohouri, E., Noorani, B., Patel, D., Ahn, Y., Zoubi, S., & Bickel, U. (2025). Assessing blood-brain barrier (BBB) integrity in an Alzheimer’s disease mouse model: is the BBB globally or locally disrupted? Fluids and Barriers of the CNS, 22(1), 79. https://doi.org/10.1186/S12987-025-00685-2
  • Qin, J., Yang, Q., Ullate-Agote, A., Sampaio-Pinto, V., Florit, L., Dokter, I., Mathioudaki, C., Middelberg, L., Montero-Calle, P., Aguirre-Ruiz, P., de las Heras Rojo, J., Lei, Z., Qiu, Z., Wei, J., van der Harst, P., Prosper, F., Mazo, M. M., Iglesias-García, O., Minnema, M. C., … van Mil, A. (2025). Uncovering cell type-specific phenotypes using a novel human in vitro model of transthyretin amyloid cardiomyopathy. Stem Cell Research & Therapy 2025 16:1, 16(1), 1–17. https://doi.org/10.1186/S13287-025-04464-6
  • Kunnath, S. M., Arad, E., Zalk, R., Kass, I., Shahar, A., Batushansky, A., Rapaport, H., & Jelinek, R. (2025). Allosteric amyloid catalysis by coiled coil fibrils. Nature Communications, 16(1), 5071-. https://doi.org/10.1038/s41467-025-60379-z
  • Yan, X., Kuster, D., Mohanty, P., Nijssen, J., Pombo-García, K., Garcia Morato, J., Rizuan, A., Franzmann, T. M., Sergeeva, A., Ly, A. M., Liu, F., Passos, P. M., George, L., Wang, S. H., Shenoy, J., Danielson, H. L., Ozguney, B., Honigmann, A., Ayala, Y. M., … Hyman, A. A. (2025). Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates. Cell, 188(15), 4123-4140.e18. https://doi.org/10.1016/J.CELL.2025.04.039
  • Feng, J., Osmekhina, E., Timonen, J. V. I., & Linder, M. B. (2025). Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies. Applied and Environmental Microbiology, 91(3). https://doi.org/10.1128/AEM.01703-24
  • Olari, L. R., Liu, S., Arnold, F., Kühlwein, J., Gil Miró, M., Updahaya, A. R., Stürzel, C., Thal, D. R., Walther, P., Sparrer, K. M. J., Danzer, K. M., Münch, J., & Kirchhoff, F. (2025). α-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia. Nature Communications, 16(1), 1–18. https://doi.org/10.1038/s41467-025-56099-z
  • Huang, M., & McEwan, W. A. (2025). Sensitive detection and propagation of brain-derived tau assemblies in HEK293-based wild-type tau seeding assays. Journal of Biological Chemistry, 301(3), 108245. https://doi.org/10.1016/j.jbc.2025.108245

2024

  • Sanislav, O., Tetaj, R., Metali, Ratcliffe, J., Phillips, W., Klein, A. R., Sethi, A., Zhou, J., Mezzenga, R., Saxer, S. S., Charnley, M., Annesley, S. J., & Reynolds, N. P. (2024). Cell invasive amyloid assemblies from SARS-CoV-2 peptides can form multiple polymorphs with varying neurotoxicity. Nanoscale, 16(42), 19814–19827. https://doi.org/10.1039/D4NR03030C
  • Eroglu, M., Zocher, A., McAuley, J., Webster, R., Xiao, M. Z. X., Yu, B., Mok, C., & Derry, W. B. (2024). Noncanonical inheritance of phenotypic information by protein amyloids. Nature Cell Biology, 26(11), 1712–1724. https://doi.org/10.1038/s41556-024-01494-9
  • Koundal, S., Chen, X., Gursky, Z., Lee, H., Xu, K., Liang, F., Xie, Z., Xu, F., Lin, H. M., van Nostrand, W. E., Gu, X., Elkin, R., Tannenbaum, A., & Benveniste, H. (2024). Divergent brain solute clearance in rat models of cerebral amyloid angiopathy and Alzheimer’s disease. IScience, 27(12), 111463. https://doi.org/10.1016/j.isci.2024.111463
  • Farzadfard, A., Mason, T. O., Kunka, A., Mohammad-Beigi, H., Bjerregaard-Andersen, K., Folke, J., Aznar, S., Kallunki, P., & Buell, A. K. (2025). The Amplification of Alpha-Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions. Angewandte Chemie International Edition, 64(7), e202419173. https://doi.org/10.1002/ANIE.202419173
  • Hurtle, B., Donnelly, C. J., Zhang, X., & Thathiah, A. (2024). Live-cell visualization of tau aggregation in human neurons. Communications Biology, 7(1), 1–11. https://doi.org/10.1038/s42003-024-06840-z
  • Pinzi, L., Conze, C., Bisi, N., Torre, G. D., Soliman, A., Monteiro-Abreu, N., Trushina, N. I., Krusenbaum, A., Dolouei, M. K., Hellwig, A., Christodoulou, M. S., Passarella, D., Bakota, L., Rastelli, G., & Brandt, R. (2024). Quantitative live cell imaging of a tauopathy model enables the identification of a polypharmacological drug candidate that restores physiological microtubule interaction. Nature Communications, 15(1), 1679. https://doi.org/10.1038/s41467-024-45851-6
  • Šulskis, D., Žiaunys, M., Sakalauskas, A., Sniečkute, R., & Smirnovas, V. (2024). Formation of amyloid fibrils by the regulatory 14-3-3ζ protein. Open Biology, 14(1). https://doi.org/10.1098/rsob.230285
  • Dranseike, D., Ota, Y., Edwardson, T. G. W., Guzzi, E. A., Hori, M., Nakic, Z. R., Deshmukh, D. v., Levasseur, M. D., Mattli, K., Tringides, C. M., Zhou, J., Hilvert, D., Peters, C., & Tibbitt, M. W. (2024). Designed modular protein hydrogels for biofabrication. Acta Biomaterialia, 177, 107–117. https://doi.org/10.1016/J.ACTBIO.2024.02.019
  • Balana, A. T., Mahul-Mellier, A. L., Nguyen, B. A., Horvath, M., Javed, A., Hard, E. R., Jasiqi, Y., Singh, P., Afrin, S., Pedretti, R., Singh, V., Lee, V. M. Y., Luk, K. C., Saelices, L., Lashuel, H. A., & Pratt, M. R. (2024). O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology. Nature Chemical Biology, 20(5), 646–655. https://doi.org/10.1038/s41589-024-01551-2
  • Kreutzer, A. G., Parrocha, C. M. T., Haerianardakani, S., Guaglianone, G., Nguyen, J. T., Diab, M. N., Yong, W., Perez-Rosendahl, M., Head, E., & Nowick, J. S. (2024). Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer’s Disease and Associated Amyloid-Disease Brain Tissue. ACS Central Science, 10(1), 104–121. https://doi.org/10.1021/acscentsci.3c00592
  • Raymundo, J. R., Zhang, H., Smaldone, G., Zhu, W., Daly, K. E., Glennon, B. J., Pecoraro, G., Salvatore, M., Devine, W. A., Lo, C. W., Vitagliano, L., & Marneros, A. G. (2024). KCTD1/KCTD15 complexes control ectodermal and neural crest cell functions, and their impairment causes aplasia cutis. The Journal of Clinical Investigation, 134(4). https://doi.org/10.1172/JCI174138
  • Morelli, C., Faltova, L., Capasso Palmiero, U., Makasewicz, K., Papp, M., Jacquat, R. P. B., Pinotsi, D., & Arosio, P. (2024). RNA modulates hnRNPA1A amyloid formation mediated by biomolecular condensates. Nature Chemistry, 16(7), 1052–1061. https://doi.org/10.1038/s41557-024-01467-3
  • Kitamura, A., Fujimoto, A., Kawashima, R., Lyu, Y., Sasaki, K., Hamada, Y., Moriya, K., Kurata, A., Takahashi, K., Brielmann, R., Bott, L. C., Morimoto, R. I., & Kinjo, M. (2024). Hetero-oligomerization of TDP-43 carboxy-terminal fragments with cellular proteins contributes to proteotoxicity. Communications Biology, 7(1). https://doi.org/10.1038/s42003-024-06410-3
  • de Oliveira, D. H., Gowda, V., Sparrman, T., Gustafsson, L., Sanches Pires, R., Riekel, C., Barth, A., Lendel, C., & Hedhammar, M. (2024). Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-49111-5
  • Sun, H., Yang, B., Li, Q., Zhu, X., Song, E., Liu, C., Song, Y., & Jiang, G. (2024). Polystyrene nanoparticles trigger aberrant condensation of TDP-43 and amyotrophic lateral sclerosis-like symptoms. Nature Nanotechnology. https://doi.org/10.1038/s41565-024-01683-5
  • Li, B., Suresh, P., Brelstaff, J., Kedia, S., Bryant, C. E., & Klenerman, D. (2024). The delayed kinetics of Myddosome formation explains why amyloid-beta aggregates trigger Toll-like receptor 4 less efficiently than lipopolysaccharide. eLife, 13, RP92350. https://doi.org/10.7554/eLife.92350
  • Bacioglu, M., Schweighauser, M., Gray, D., Lövestam, S., Katsinelos, T., Quaegebeur, A., van Swieten, J., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., Goedert, M., Ghetti, B., & Spillantini, M. G. (2024). Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems. Acta Neuropathologica Communications, 12(1). https://doi.org/10.1186/s40478-024-01813-z
  • Eltom, K., Mothes, T., Libard, S., Ingelsson, M., & Erlandsson, A. (2024). Astrocytic accumulation of tau fibrils isolated from Alzheimer’s disease brains induces inflammation, cell-to-cell propagation and neuronal impairment. Acta Neuropathologica Communications, 12(1). https://doi.org/10.1186/s40478-024-01745-8

2023

  • Arad, E., Pedersen, K. B., Malka, O., Mambram Kunnath, S., Golan, N., Aibinder, P., Schiøtt, B., Rapaport, H., Landau, M., & Jelinek, R. (2023). Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-43624-1
  • Juliani do Amaral, M., Mohapatra, S., Ribeiro Passos, A., Sousa Lopes da Silva, T., Sampaio Carvalho, R., da Silva Almeida, M., Sá Pinheiro, A., Wegmann, S., & Cordeiro, Y. (2023). Copper drives prion protein phase separation and modulates aggregation. Science Advances, 9, eadi7347. https://doi.org/10.1126/sciadv.adi7347
  • Chandhok, S., Pereira, L., Momchilova, E. A., Marijan, D., Zapf, R., Lacroix, E., Kaur, A., Keymanesh, S., Krieger, C., & Audas, T. E. (2023). Stress-mediated aggregation of disease-associated proteins in amyloid bodies. Scientific Reports, 13(1). https://doi.org/10.1038/s41598-023-41712-2
  • Chia, S., Faidon Brotzakis, Z., Horne, R. I., Possenti, A., Mannini, B., Cataldi, R., Nowinska, M., Staats, R., Linse, S., Knowles, T. P. J., Habchi, J., & Vendruscolo, M. (2023). Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates. Mol. Pharmaceutics, 20, 183–193. https://doi.org/10.1021/acs.molpharmaceut.2c00548
  • Frenkel, A., Zecharia, E., Gómez-Pérez, D., Sendersky, E., Yegorov, Y., Jacob, A., Benichou, J. I. C., Stierhof, Y. D., Parnasa, R., Golden, S. S., Kemen, E., & Schwarz, R. (2023). Cell specialization in cyanobacterial biofilm development revealed by expression of a cell-surface and extracellular matrix protein. Npj Biofilms and Microbiomes 2023 9:1, 9(1), 1–10. https://doi.org/10.1038/s41522-023-00376-6
  • Gvazava, N., Konings, S. C., Cepeda-Prado, E., Skoryk, V., Umeano, C. H., Dong, J., Silva, I. A. N., Ottosson, D. R., Leigh, N. D., Wagner, D. E., & Klementieva, O. (2023). Label-Free High-Resolution Photothermal Optical Infrared Spectroscopy for Spatiotemporal Chemical Analysis in Fresh, Hydrated Living Tissues and Embryos. Journal of the American Chemical Society. https://doi.org/10.1021/jacs.3c08854
  • Petrlova, J., Hartman, E., Petruk, G., Lim, J. C. H., Adav, S. S., Kjellström, S., Puthia, M., & Schmidtchen, A. (2023). Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation. iScience, 26(10). https://doi.org/10.1016/j.isci.2023.107951
  • Kommaddi, R. P., Verma, A., Muniz-Terrera, G., Tiwari, V., Chithanathan, K., Diwakar, L., Gowaikar, R., Karunakaran, S., Malo, P. K., Graff-Radford, N. R., Day, G. S., Laske, C., Vöglein, J., Nübling, G., Ikeuchi, T., Kasuga, K., & Ravindranath, V. (2023). Sex difference in evolution of cognitive decline: studies on mouse model and the Dominantly Inherited Alzheimer Network cohort. Translational Psychiatry, 13(1), 1–12. https://doi.org/10.1038/s41398-023-02411-8
  • Ornithopoulou, E., Åstrand, C., Gustafsson, L., Crouzier, T., & Hedhammar, M. (2023). Self-Assembly of RGD-Functionalized Recombinant Spider Silk Protein into Microspheres in Physiological Buffer and in the Presence of Hyaluronic Acid. ACS Applied Bio Materials, 6(9), 3696–3705. https://doi.org/10.1021/acsabm.3c00373
  • Piroska, L., Fenyi, A., Thomas, S., Plamont, M.-A., Redeker, V., Melki, R., & Gueroui, Z. (2023). α-Synuclein liquid condensates fuel fibrillar α-synuclein growth. Science Advances, 9(33), eadg5663. https://doi.org/10.1126/sciadv.adg5663
  • Prater, C., Bai, Y., Konings, S. C., Martinsson, I., Swaminathan, V. S., Nordenfelt, P., Gouras, G., Borondics, F., & Klementieva, O. (2023). Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level. Journal of Medicinal Chemistry, 66(4), 2542–2549. https://doi.org/10.1021/acs.jmedchem.2c01359

2022

  • Cascella, R., Banchelli, M., Abolghasem Ghadami, S., Ami, D., Gagliani, M. C., Bigi, A., Staderini, T., Tampellini, D., Cortese, K., Cecchi, C., Natalello, A., Adibi, H., Matteini, P., & Chiti, F. (2022). An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature. Annals of Medicine, 55(1), 72–88. https://doi.org/10.1080/07853890.2022.2148734
  • Choi, M. L., Chappard, A., Singh, B. P., Maclachlan, C., Abramov, A. Y., Horrocks, M. H., & Gandhi, S. (2022). Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity. Nature Neuroscience. https://doi.org/10.1038/s41593-022-01140-3
  • de Luca, C. M. G., Consonni, A., Cazzaniga, F. A., Bistaffa, E., Bufano, G., Quitarrini, G., Celauro, L., Legname, G., Eleopra, R., Baggi, F., Giaccone, G., & Moda, F. (2022). The alpha-synuclein RT-QuIC products generated by the olfactory mucosa of patients with parkinson’s disease and multiple system atrophy induce inflammatory responses in SH-SY5Y cells. Cells, 11(1). https://doi.org/10.3390/cells11010087
  • Wood, J. I., Wong, E., Cummings, D. M., Hardy, J., Correspondence, F. A. E., Joghee, R., Balbaa, A., Vitanova, K. S., Stringer, K. M., Vanshoiack, A., Phelan, S.-L. J., Launchbury, F., Desai, S., Tripathi, T., Rg Hanrieder, J., & Edwards, F. A. (2022). Plaque contact and unimpaired Trem2 is required for the microglial response to amyloid pathology. Cell Reports. https://doi.org/10.1016/j.celrep.2022.111686
  • Petrlova, J., Samsudin, F., Bond, P. J., & Schmidtchen, A. (2022). SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. FEBS Letters. https://doi.org/10.1002/1873-3468.14490
  • Morten, M. J., Sirvio, L., Rupawala, H., Hayes, E. M., Franco, A., Radulescu, C., Ying, L., Barnes, S. J., Muga, A., & Ye, Y. (2022). Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies. PNAS. https://doi.org/10.1073/pnas.2205591119
  • Hochmair, J., Exner, C., Franck, M., Dominguez‐Baquero, A., Diez, L., Brognaro, H., Kraushar, M. L., Mielke, T., Radbruch, H., Kaniyappan, S., Falke, S., Mandelkow, E., Betzel, C., & Wegmann, S. (2022). Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates. The EMBO Journal, 41(11). https://doi.org/10.15252/EMBJ.2021108882
  • Kumar, S. T., Mahul-Mellier, A. L., Hegde, R. N., Rivière, G., Moons, R., de Opakua, A. I., Magalhães, P., Rostami, I., Donzelli, S., Sobott, F., Zweckstetter, M., & Lashuel, H. A. (2022). A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity. Science Advances, 8(17), 44. https://doi.org/10.1126/SCIADV.ABN0044
  • Lackie, R. E., de Miranda, A. S., Lim, M. P., Novikov, V., Madrer, N., Karunatilleke, N. C., Rutledge, B. S., Tullo, S., Brickenden, A., Maitland, M. E. R., Greenberg, D., Gallino, D., Luo, W., Attaran, A., Shlaifer, I., del Cid Pellitero, E., Schild-Poulter, C., Durcan, T. M., Fon, E. A., … Prado, M. A. M. (2022). Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo. Acta Neuropathologica. https://doi.org/10.1007/s00401-022-02491-8

2021

  • Graziotto, M. E., Adair, L. D., Kaur, A., Vérité, P., Ball, S. R., Sunde, M., Jacquemin, D., & New, E. J. (2021). Versatile naphthalimide tetrazines for fluorogenic bioorthogonal labelling. RSC Chemical Biology, 2(5), 1491–1498. https://doi.org/10.1039/D1CB00128K
  • Michno, W., Stringer, K. M., Enzlein, T., Passarelli, M. K., Escrig, S., Vitanova, K., Wood, J., Blennow, K., Zetterberg, H., Meibom, A., Hopf, C., Edwards, F. A., & Hanrieder, J. (2021). Following spatial Aβ aggregation dynamics in evolving Alzheimer’s disease pathology by imaging stable isotope labeling kinetics. Science Advances, 7(25), 4855–4871. https://doi.org/10.1126/SCIADV.ABG4855/
  • Aubi, O., Prestegård, K. S., Jung-KC, K., Shi, T. J. S., Ying, M., Grindheim, A. K., Scherer, T., Ulvik, A., McCann, A., Spriet, E., Thöny, B., & Martinez, A. (2021). The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase. Nature Communications 2021 12:1, 12(1), 1–16. https://doi.org/10.1038/s41467-021-22107-1
  • Frey, B., AlOkda, A., Jackson, M. P., Riguet, N., Duce, J. A., & Lashuel, H. A. (2021). Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get. Journal of Neurochemistry, 157(4), 872–888. https://doi.org/10.1111/jnc.15147
  • Frottin, F., Pérez-Berlanga, M., Hartl, F. U., & Hipp, M. S. (2021). Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model. ELife, 10. https://doi.org/10.7554/eLife.62718
  • Rimal, S., Li, Y., Vartak, R., Geng, J., Tantray, I., Li, S., Huh, S., Vogel, H., Glabe, C., Grinberg, L. T., Spina, S., Seeley, W. W., Guo, S., & Lu, B. (2021). Inefficient quality control of ribosome stalling during APP synthesis generates CAT-tailed species that precipitate hallmarks of Alzheimer’s disease. Acta Neuropathologica Communications, 9(1), 1–24. https://doi.org/10.1186/s40478-021-01268-6
  • Hofbauer, D., Mougiakakos, D., Mackensen, A., Ricagno, S., & Bruns, H. (2021). B2-microglobulin triggers NLRP3 inflammasome activation in tumor-associated macrophages to promote multiple myeloma progression. Immunity. https://doi.org/10.1016/j.immuni.2021.07.002
  • Johari, M., Sarparanta, J., Vihola, A., Jonson, P. H., Savarese, M., Jokela, M., Torella, A., Piluso, G., Said, E., Vella, N., Cauchi, M., Magot, A., Magri, F., Mauri, E., Kornblum, C., Reimann, J., Stojkovic, T., Romero, N. B., Luque, H., Huovinen, S., Lahermo, P., Donner, K., Comi, G. P., Nigro, V., Hackman, P., & Udd, B. (2021). Missense mutations in small muscle protein X-linked (SMPX) cause distal myopathy with protein inclusions. Acta Neuropathologica, 0123456789. https://doi.org/10.1007/s00401-021-02319-x

2020

  • Mahul-Mellier, A. L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020). The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America, 117(9), 4971–4982. https://doi.org/10.1073/pnas.1913904117
  • Ghosh, A., Mizuno, K., Tiwari, S. S., Proitsi, P., Gomez Perez-Nievas, B., Glennon, E., Martinez-Nunez, R. T., & Giese, K. P. (2020). Alzheimer’s disease-related dysregulation of mRNA translation causes key pathological features with ageing. Translational Psychiatry, 10(1), 1–18. https://doi.org/10.1038/s41398-020-00882-7

2019

  • Page, M. J., Thomson, G. J. A., Nunes, J. M., Engelbrecht, A. M., Nell, T. A., de Villiers, W. J. S., de Beer, M. C., Engelbrecht, L., Kell, D. B., & Pretorius, E. (2019). Serum amyloid A binds to fibrin(ogen), promoting fibrin amyloid formation. Scientific Reports, 9(1), 1–14. https://doi.org/10.1038/s41598-019-39056-x
  • Adams, B., Nunes, J. M., Page, M. J., Roberts, T., Carr, J., Nell, T. A., Kell, D. B., & Pretorius, E. (2019). Parkinson’s disease: A systemic inflammatory disease accompanied by bacterial inflammagens. Frontiers in Aging Neuroscience, 10(JUL), 1–17. https://doi.org/10.3389/fnagi.2019.00210
  • Frottin, F., Schueder, F., Tiwary, S., Gupta, R., Körner, R., Schlichthaerle, T., Cox, J., Jungmann, R., Hartl, F. U., & Hipp, M. S. (2019). The nucleolus functions as a phase-separated protein quality control compartment. Science, 365(6451), 342–347. https://doi.org/10.1126/science.aaw9157

2018

  • de Waal, G. M., Engelbrecht, L., Davis, T., de Villiers, W. J. S., Kell, D. B., & Pretorius, E. (2018). Correlative Light-Electron Microscopy detects lipopolysaccharide and its association with fibrin fibres in Parkinson’s Disease, Alzheimer’s Disease and Type 2 Diabetes Mellitus. Scientific Reports, 8(1), 1–12. https://doi.org/10.1038/s41598-018-35009-y
  • Pretorius, E., Page, M. J., Hendricks, L., Nkosi, N. B., Benson, S. R., & Kell, D. B. (2018). Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: Assessment with novel Amytracker TM stains. Journal of the Royal Society Interface, 15(139). https://doi.org/10.1098/rsif.2017.0941

2017

  • Sehlin, D., Fang, X. T., Meier, S. R., Jansson, M., & Syvänen, S. (2017). Pharmacokinetics, biodistribution and brain retention of a bispecific antibody-based PET radioligand for imaging of amyloid-β. Scientific Reports, 7(1), 1–9. https://doi.org/10.1038/s41598-017-17358-2
  • Pretorius, E., Page, M. J., Engelbrecht, L., Ellis, G. C., & Kell, D. B. (2017). Substantial fibrin amyloidogenesis in type 2 diabetes assessed using amyloid-selective fluorescent stains. Cardiovascular Diabetology, 16(1), 1–14. https://doi.org/10.1186/s12933-017-0624-5