EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains
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In neurodegenerative diseases, proteins fold into amyloid structures with distinct conformations (strains) that are characteristic of different diseases. However, there is a need to rapidly identify amyloid conformations in situ. Here, we use machine learning on the full information available in fluorescent excitation/emission spectra of amyloid-binding dyes to identify six distinct different conformational strains in vitro, as well as amyloid-β (Aβ) deposits in different transgenic mouse models. Our EMBER (excitation multiplexed bright emission recording) imaging method rapidly identifies conformational differences in Aβ and tau deposits from Down syndrome, sporadic and familial Alzheimer’s disease human brain slices. EMBER has in situ identified distinct conformational strains of tau inclusions in astrocytes, oligodendrocytes, and neurons from Pick’s disease. In future studies, EMBER should enable high-throughput measurements of the fidelity of strain transmission in cellular and animal neurodegenerative diseases models, time course of amyloid strain propagation, and identification of pathogenic versus benign strains.
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EMBER enables swift identification of conformational differences in Aβ and tau deposits in human brain slices derived from various neurodegenerative diseases, including sporadic and familial AD, Down syndrome, and PiD.
“Notably, EMBER enables the swift identification of conformational differences in Aβ and tau deposits in human brain slices derived from various neurodegenerative diseases, including sporadic and familial AD, Down syndrome, as well as PiD.”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [184]
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Deep Residual Learning for Image Recognition
He, K., Zhang, X., Ren, S., & Sun, J. (2016) · 2016 IEEE Conference on Computer Vision and Pattern Recognition (CVPR) · doi:10.1109/cvpr.2016.90 · Cited by 235,474 · see citing works
ImageNet classification with deep convolutional neural networks
Krizhevsky, A., Sutskever, I., & Hinton, G. E. (2017) · Communications of the ACM · doi:10.1145/3065386 · Cited by 112,155 · see citing works
Wold, S., Esbensen, K. H., & Geladi, P. L. M. (1987) · Chemometrics and Intelligent Laboratory Systems · doi:10.1016/0169-7439(87)80084-9 · Cited by 11,792 · see citing works
UMAP: Uniform Manifold Approximation and Projection
McInnes, L., Healy, J., Saul, N., & Großberger, L. (2018) · Journal of Open Source Software · doi:10.21105/joss.00861 · Cited by 9,826 · see citing works
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works
Deep Learning using Rectified Linear Units (ReLU)Preprint
Agarap, A. F. (2018) · arXiv (Cornell University) · doi:10.48550/arxiv.1803.08375 · Cited by 3,792 · see citing works
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · see citing works
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382 · see citing works
Cryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061 · see citing works
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works
Curli biogenesis and function.
Barnhart, M. M., & Chapman, M. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142106 · Cited by 1,223 · see citing works
ON THE BINDING OF CONGO RED BY AMYLOID
Puchtler, H., Sweat, F., & Levine, M. I. (1962) · Journal of Histochemistry & Cytochemistry · doi:10.1177/10.3.355 · Cited by 1,136 · see citing works
Synthesis and Evaluation of 11C-Labeled 6-Substituted 2-Arylbenzothiazoles as Amyloid Imaging Agents
Mathis, C. A., Wang, Y., Holt, D. P., Huang, G.-F., Debnath, M. L., & Klunk, W. E. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030026b · Cited by 976 · see citing works
Structural and functional characterization of two alpha-synuclein strains
Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Oliéric, V., Böckmann, A., Meier, B. H., et al. (2013) · Nature Communications · doi:10.1038/ncomms3575 · Cited by 890 · see citing works
Structure-based classification of tauopathies
Shi, Y., Zhang, W., Yang, Y., Murzin, A. G., Falcon, B., Kotecha, A., van Beers, M., Tarutani, A., Kametani, F., Garringer, H. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03911-7 · Cited by 878 · see citing works
Structures of filaments from Pick’s disease reveal a novel tau protein fold
Falcon, B., Zhang, W., Murzin, A. G., Murshudov, G. N., Garringer, H. J., Vidal, R., Crowther, R. A., Ghetti, B. F., Scheres, S. H. W., & Goedert, M. (2018) · Nature · doi:10.1038/s41586-018-0454-y · Cited by 837 · see citing works
Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy
Shahnawaz, M., Mukherjee, A., Pritzkow, S., Mendez, N., Rabadia, P., Liu, X., Hu, B., Schmeichel, A., Singer, W., Wu, G., et al. (2020) · Nature · doi:10.1038/s41586-020-1984-7 · Cited by 820 · see citing works
Yuan, P., Condello, C., Keene, C. D., Wang, Y., Bird, T. D., Paul, S. M., Luo, W., Colonna, M., Baddeley, D., & Grutzendler, J. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.003 · Cited by 817 · see citing works
Self-citationMaruyama, M., Shimada, H., Suhara, T., Shinotoh, H., Ji, B., Maeda, J., Zhang, M.-R., Trojanowski, J. Q., Lee, V. M.-Y., Ono, M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.037 · Cited by 760 · see citing works
Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease
Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works
Short peptides self-assemble to produce catalytic amyloids
Rufo, C. M., Moroz, Y. S., Moroz, O. V., Stöhr, J., Smith, T. A., Hu, X., DeGrado, W. F., & Korendovych, I. V. (2014) · Nature Chemistry · doi:10.1038/nchem.1894 · Cited by 667 · see citing works
Self-citationStructural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes
Qiang, W., Yau, W., Lu, J., Collinge, J., & Tycko, R. (2017) · Nature · doi:10.1038/nature20814 · Cited by 634 · see citing works
Novel tau filament fold in corticobasal degeneration
Zhang, W., Tarutani, A., Newell, K. L., Murzin, A. G., Matsubara, T., Falcon, B., Vidal, R., Garringer, H. J., Shi, Y., Ikeuchi, T., et al. (2020) · Nature · doi:10.1038/s41586-020-2043-0 · Cited by 546 · see citing works
Cryo-EM structures of amyloid-β 42 filaments from human brains
Yang, Y., Arseni, D., Zhang, W., Huang, M., Lövestam, S., Schweighauser, M., Kotecha, A., Murzin, A. G., Peak-Chew, S. Y., Macdonald, J., et al. (2022) · Science · doi:10.1126/science.abm7285 · Cited by 546 · see citing works
The fold of α-synuclein fibrils
Vilar, M., Chou, H., Lührs, T., Maji, S. K., Riek-Loher, D., Verel, R., Manning, G., Stahlberg, H., & Riek, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712179105 · Cited by 539 · see citing works
Kirschner, D. A., Abraham, C., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.83.2.503 · Cited by 517 · see citing works
A Unifying Role for Prions in Neurodegenerative Diseases
Prusiner, S. B. (2012) · Science · doi:10.1126/science.1222951 · Cited by 495 · see citing works
Ran, C., Xu, X., Raymond, S. B., Ferrara, B. J., Neal, K. L., Bacskai, B. J., Medarova, Z. O., & Moore, A. V. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9047043 · Cited by 487 · see citing works
Structures of α-synuclein filaments from human brains with Lewy pathology
Yang, Y., Shi, Y., Schweighauser, M., Zhang, X., Kotecha, A., Murzin, A. G., Garringer, H. J., Cullinane, P. W., Saito, Y., Foroud, T., et al. (2022) · Nature · doi:10.1038/s41586-022-05319-3 · Cited by 474 · see citing works
PET imaging of amyloid in Alzheimer's disease
Nordberg, A. K. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00853-1 · Cited by 462 · see citing works
Dementia in Down syndrome: unique insights for Alzheimer disease research
Lott, I. T., & Head, E. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0132-6 · Cited by 383 · see citing works
Tau filaments from multiple cases of sporadic and inherited Alzheimer's disease adopt a common fold
Falcon, B., Zhang, W., Schweighauser, M., Murzin, A. G., Vidal, R., Garringer, H. J., Ghetti, B., Scheres, S. H. W., & Goedert, M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1914-z · Cited by 362 · see citing works
Alzheimer's disease associated with Down syndrome: a genetic form of dementia
Fortea, J., Zaman, S. H., Hartley, S., Rafii, M. S., Head, E., & Carmona-Iragui, M. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00245-3 · Cited by 357 · see citing works
Åslund, A., Sigurdson, C. J., Klingstedt, T., Grathwohl, S. A., Bolmont, T., Dickstein, D. L., Glimsdal, E., Prokop, S., Lindgren, M., Konradsson, P., et al. (2009) · ACS Chemical Biology · doi:10.1021/cb900112v · Cited by 332 · see citing works
Shim, S., Strasfeld, D. B., Ling, Y. L., & Zanni, M. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700804104 · Cited by 315 · see citing works
α-Synuclein strains target distinct brain regions and cell types
Lau, A., So, R. W. L., Lau, H. H. C., Sang, J. C., Ruiz‐Riquelme, A., Fleck, S. C., Stuart, E., Menon, S. A., Visanji, N. P., Meisl, G., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0541-x · Cited by 304 · see citing works
Tau PET imaging: present and future directions
Saint‐Aubert, L., Lemoine, L., Chiotis, K., Leuzy, A., Rodriguez‐Vieitez, E., & Nordberg, A. K. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0162-3 · Cited by 283 · see citing works
Prion strain discrimination using luminescent conjugated polymers
Sigurdson, C. J., Nilsson, K. P. R., Hornemann, S., Manco, G., Polymenidou, M., Schwarz, P., Leclerc, M., Hammarström, P., Kurt Wüthrich, A., & Aguzzi, A. (2007) · Nature Methods · doi:10.1038/nmeth1131 · Cited by 273 · see citing works
Cryo-EM structures of tau filaments
Scheres, S. H. W., Zhang, W., Falcon, B., & Goedert, M. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.011 · Cited by 266 · see citing works
Rasmussen, J., Mahler, J., Beschörner, N., Kaeser, S. A., Häsler, L. M., Baumann, F., Nyström, S., Portelius, E., Blennow, K., Lashley, T., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713215114 · Cited by 228 · see citing works
Cellular and pathological heterogeneity of primary tauopathies
Chung, D. C., Roemer, S. F., Petrucelli, L., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00476-x · Cited by 219 · see citing works
Amyloid-like interactions within nucleoporin FG hydrogels
Ader, C., Frey, S., Maas, W. E., Schmidt, H. B., Görlich, D., & Baldus, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910163107 · Cited by 204 · see citing works
Deep clinical and neuropathological phenotyping of P ick disease
Irwin, D. J., Brettschneider, J., McMillan, C. T., Cooper, F. I., Olm, C. A., Arnold, S. E., Deerlin, V. M. V., Seeley, W. W., Miller, B. L., Lee, E. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24559 · Cited by 204 · see citing works
Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β
Cohen, M. L., Kim, C., Haldiman, T., ElHag, M., Mehndiratta, P., Termsarasab, P., Lissemore, F. M., Shea, M., Cohen, Y., Chen, W., et al. (2015) · Brain · doi:10.1093/brain/awv006 · Cited by 202 · see citing works
Taniguchi-Watanabe, S., Arai, T., Kametani, F., Nonaka, T., Masuda-Suzukake, M., Tarutani, A., Murayama, S., Saito, Y., Arima, K., Yoshida, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1503-3 · Cited by 200 · see citing works
Seidler, P. M., Murray, K. A., Boyer, D. R., Ge, P., Sawaya, M. R., Hu, C. J., Cheng, X., Abskharon, R. N. N., Pan, H., Deture, M. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32951-4 · Cited by 186 · see citing works
Cryo-EM structures of tau filaments from Alzheimer’s disease with PET ligand APN-1607
Shi, Y., Murzin, A. G., Falcon, B., Epstein, A., Machin, J., Tempest, P. A., Newell, K. L., Vidal, R., Garringer, H. J., Sahara, N., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02294-3 · Cited by 184 · see citing works
A new method for purification of recombinant human α-synuclein in Escherichia coli
Huang, C., Ren, G., Zhou, H., & Wang, C.-C. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.02.014 · Cited by 183 · see citing works
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
Jiang, Y. X., Cao, Q., Sawaya, M. R., Abskharon, R. N. N., Ge, P., Deture, M. A., Dickson, D. W., Fu, J. Y., Loo, R. R. O., Loo, J. A., et al. (2022) · Nature · doi:10.1038/s41586-022-04670-9 · Cited by 161 · see citing works
Condello, C., Lemmin, T., Stöhr, J., Nick, M., Wu, Y., Maxwell, A. M., Watts, J. C., Caro, C. D., Oehler, A., Keene, C. D., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714966115 · Cited by 145 · see citing works
Self-citationMolecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network
Nagy-Smith, K. J., Moore, E. W., Schneider, J. P., & Tycko, R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509313112 · Cited by 143 · see citing works
Araki, K., Yagi, N., Aoyama, K., Choong, C., Hayakawa, H., Fujimura, H., Nagai, Y., Goto, Y., & Mochizuki, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906124116 · Cited by 132 · see citing works
Wang, T., Jo, H., DeGrado, W. F., & Hong, M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02089 · Cited by 102 · see citing works
Self-citationDregni, A. J., Mandala, V. S., Wu, H., Elkins, M. R., Wang, H. K., Hung, I., DeGrado, W. F., & Hong, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906839116 · Cited by 100 · see citing works
Self-citationBerthelot, K., Lecomte, S., Estevez, Y., Salin, B., Bentaleb, A., Cullin, C., Deffieux, A., & Peruch, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048065 · Cited by 94 · see citing works
Inhibition of synucleinopathic seeding by rationally designed inhibitors
Sangwan, S., Sahay, S., Murray, K. A., Morgan, S., Guenther, E. L., Jiang, L., Williams, C. K., Vinters, H. V., Goedert, M., & Eisenberg, D. S. (2020) · eLife · doi:10.7554/elife.46775 · Cited by 79 · see citing works
A multispectral LED array for the reduction of background autofluorescence in brain tissue
Duong, H., & Han, M. (2013) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2013.08.018 · Cited by 76 · see citing works
Magnusson, K., Simon, R. A., Sjölander, D., Sigurdson, C. J., Hammarström, P., & Nilsson, K. P. R. (2014) · Prion · doi:10.4161/pri.29239 · Cited by 68 · see citing works
Harada, R., Okamura, N., Furumoto, S., Yoshikawa, T., Arai, H., Yanai, K., & Kudo, Y. (2013) · Molecular Imaging and Biology · doi:10.1007/s11307-013-0667-2 · Cited by 51 · see citing works
Kloepper, K. D., Woods, W. S., Sochacki, K. A., George, J. M., & Rienstra, C. M. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.02.009 · Cited by 51 · see citing works
Dregni, A. J., Wang, H. K., Wu, H., Duan, P., Jin, J., DeGrado, W. F., & Hong, M. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03314 · Cited by 50 · see citing works
Self-citationHonda, K., Fujishima, S., Ojida, A., & Hamachi, I. (2007) · ChemBioChem · doi:10.1002/cbic.200700146 · Cited by 48 · see citing works
Duan, P., Chen, K. J., Wijegunawardena, G., Dregni, A. J., Wang, H. K., Wu, H., & Hong, M. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12056 · Cited by 43 · see citing works
Liu, H., Kim, C., Haldiman, T., Sigurdson, C. J., Nyström, S., Nilsson, K. P. R., Cohen, M. L., Wısnıewskı, T., Hammarström, P., & Safar, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101267 · Cited by 38 · see citing works
Catalytic amyloids: Is misfolding folding?
Marshall, L. R., & Korendovych, I. V. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.06.010 · Cited by 36 · see citing works
Michno, W., Wehrli, P. M., Koutarapu, S., Marsching, C., Minta, K., Ge, J., Meyer, S. W., Zetterberg, H., Blennow, K., Henkel, C., et al. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15557 · Cited by 36 · see citing works
Maxwell, A. M., Yuan, P., Rivera, B. M., Schaaf, W., Mladinov, M., Prasher, V. P., Robinson, A. C., DeGrado, W. F., & Condello, C. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01298-0 · Cited by 23 · see citing works
Self-citationProtein-adaptive differential scanning fluorimetry using conformationally responsive dyes
Wu, T., Yu, J. C., Suresh, A., Gale-Day, Z. J., Alteen, M. G., Woo, A. S., Millbern, Z., Johnson, O. T., Carroll, E. C., Partch, C. L., et al. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02158-7 · Cited by 22 · see citing works
Conformationally responsive dyes enable protein-adaptive differential scanning fluorimetryPreprint
Wu, T., Yu, J., Suresh, A., Gale-Day, Z. J., Alteen, M. G., Woo, A. S., Millbern, Z., Johnson, O. T., Carroll, E. C., Partch, C. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.23.525251 · Cited by 11 · see citing works
Stacked binding of a small molecule PET tracer to Alzheimer’s tau paired helical filamentsPreprint
Merz, G. E., Chalkley, M. J., Tan, S. K., Tse, E., Lee, J., Prusiner, S. B., Paras, N. A., DeGrado, W. F., & Southworth, D. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.30.510175 · Cited by 5 · see citing works
Self-citation
Flagged first, then by citations
1 of the 71 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [14]M. L. Cohen, Rapidly progressive Alzheimer’s disease features distinct structures of amyloid-β. Brain 138, 1009– 1022 (2015). 25688081 PMC5014074
Cited by
Sorted by citations
Gaikwad, S., Senapati, S., Haque, M. A., & Kayed, R. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13490 · Cited by 117 · see citing works
Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments
Bai, Y., Zhang, S., Dong, H. Y., Liu, Y., Liu, C., & Zhang, X. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00494 · Cited by 71 · see citing works
Cascio, F. L., Park, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Shchankin, N., Jerez, C., Moreno, N., Bittar, A., Xavier, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07499-w · Cited by 35 · see citing works
Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer’s disease fold
Ghosh, U., Tse, E., Yang, H., Shi, M., Caro, C. D., Wang, F., Merz, G. E., Prusiner, S. B., Southworth, D. R., & Condello, C. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01806-y · Cited by 23 · see citing works
Self-citationBinding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils
Liu, K., Tao, Y., Zhao, Q., Xia, W., Li, X., Zhang, S., Yao, Y., Xiang, H., Han, C., Tan, L., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321633121 · Cited by 18 · see citing works
De novo design of peptides that bind specific conformers of α-synuclein
Wallace, H. M., Yang, H., Tan, S. K., Pan, H. S., Yang, R., Xu, J., Jo, H., Condello, C., Polizzi, N. F., & DeGrado, W. F. (2024) · Chemical Science · doi:10.1039/d3sc06245g · Cited by 11 · see citing works
Self-citationHolmes, B. B., Weigel, T. K., Chung, J. M., Kaufman, S. K., Apresa, B. I., Byrnes, J. R., Kumru, K. S., Vaquer‐Alicea, J., Gupta, A., Rose, I. V. L., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00883-4 · Cited by 13 · see citing works
Self-citationHigh-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs
Carroll, E. C., Yang, H., Powell, W. C., Charvat, A. F., Oehler, A., Jones, J. G., Montgomery, K. M., Yung, A., Millbern, Z., Taylor, A. I. P., et al. (2025) · Nature Chemistry · doi:10.1038/s41557-025-01889-7 · Cited by 10 · see citing works
Self-citationSpectral Fluorescence Pathology of Protein Misfolding Disorders
Stepanchuk, A. A., & Stys, P. K. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00798 · Cited by 9 · see citing works
Diverse influences on tau aggregation and implications for disease progressionPreprint
Alstyne, M. V., Pratt, J., & Parker, R. (2025) · Genes & Development · doi:10.1101/gad.352551.124 · Cited by 10 · see citing works
Klingstedt, T., Shirani, H., Parvin, F., Nyström, S., Hammarström, P., Graff, C., Ingelsson, M., Vidal, R., Ghetti, B. F., Sehlin, D., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108032 · Cited by 8 · see citing works
Marcatti, M., Tumurbaatar, B., Zhang, W. R., Scaduto, P., Guptarak, J., Kadamangudi, S., Schuetze, R., Fracassi, A., Kayed, R., & Taglialatela, G. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70550 · Cited by 6 · see citing works
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Methods for high throughput discovery of fluoroprobes that recognize tau fibril polymorphsPreprint
Carroll, E. C., Yang, H., Jones, J. G., Oehler, A., Charvat, A. F., Montgomery, K., Yung, A., Millbern, Z., Vinueza, N. R., DeGrado, W. F., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.02.610853 · Cited by 3 · see citing works
Self-citationChemical Approaches for Array Based Detection of Amyloids
Simon, P. M., Xu, Y., & Kaur, A. (2025) · Advanced Sensor Research · doi:10.1002/adsr.202500108 · Cited by 1 · see citing works
A functional amyloid scaffold shapes insect egg coatsPreprint
Konstantoulea, K., Kunach, P., Tagad, H. D., Diamond, M. I., & Louros, N. N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.727653 · Cited by 2 · see citing works
Ghosh, U., Tse, E., Yang, H., Shi, M., Caro, C. D., Wang, F., Merz, G. E., Prusiner, S. B., Southworth, D. R., & Condello, C. (2024) · Figshare · doi:10.6084/m9.figshare.26732911
Self-citationGhosh, U., Tse, E., Yang, H., Shi, M., Caro, C. D., Wang, F., Merz, G. E., Prusiner, S. B., Southworth, D. R., & Condello, C. (2024) · Figshare · doi:10.6084/m9.figshare.26732908
Self-citationXu, L., Yang, H., Leon, J., Li, X., Oehler, A., Modavi, C., Abate, A. R., & Condello, C. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.23.701345
Self-citation
- Authors
- Yang, H., Yuan, P., Wu, Y., Shi, M., Caro, C. D., Tengeiji, A., Yamanoi, S., Inoue, M., DeGrado, W. F., & Condello, C.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- DeGrado, William F.
- Condello, Carlo
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2023-03-16
- Volume
- 120
- Issue
- 12
- Pages
- e2300769120-e2300769120
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC10041141
- OpenAlex
- W4327566974
- Cited by
- 19
- References
- 71
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 8 · 2023: 2
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- HHS | NIH | National Institute on Aging (AG061874, AG002132)
- BrightFocus Foundation (A2020039F)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Keywords
- amyloid-beta, tau protein, amyloid conformation, machine learning, Pick's disease, Down syndrome, Alzheimer's disease, transgenic mouse model, astrocytes, oligodendrocytes, neurons, neurodegenerative diseases, strain transfer
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