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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Open accessAbstract
For several decades scientists have speculated that the key to understanding age-related neurodegenerative disorders may be found in the unusual biology of the prion diseases. Recently, owing largely to the advent of new disease models, this hypothesis has gained experimental momentum. In a remarkable variety of diseases, specific proteins have been found to misfold and aggregate into seeds that structurally corrupt like proteins, causing them to aggregate and form pathogenic assemblies ranging from small oligomers to large masses of amyloid. Proteinaceous seeds can therefore serve as self-propagating agents for the instigation and progression of disease. Alzheimer's disease and other cerebral proteopathies seem to arise from the de novo misfolding and sustained corruption of endogenous proteins, whereas prion diseases can also be infectious in origin. However, the outcome in all cases is the functional compromise of the nervous system, because the aggregated proteins gain a toxic function and/or lose their normal function. As a unifying pathogenic principle, the prion paradigm suggests broadly relevant therapeutic directions for a large class of currently intractable diseases.
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In the citing paper
“The recent discovery that specific misfolded and aggregated proteins can propagate and spread in a prion-like fashion has sparked considerable interest (67).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“In Parkinson’s disease and Lewy body disease, α-synuclein aggregates initially spread through the brainstem and olfactory bulb followed by limbic structures, and only thence to the neocortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“In each of these cases, the aggregates initially deposit at the ventral base of the forebrain and midbrain, and then extend rostrally and dorsally to the cortex.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [67]
In the citing paper
“While still a contentious topic [46], there is now substantial evidence that also supports the idea that propagation of pathological tau species occurs between cells [47–50].”
From Glial contributions to neurodegeneration in tauopathies (2017) · cites this paper as [50]
In the citing paper
“As aforementioned, the neuropathological lesions of not only AD but also PD/DLB and amyotrophic lateral sclerosis (ALS) are known to spread through the brain in a rather specific pattern, which also serves as a basis for the neuropathological staging of disease severity [203].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [203]
In the citing paper
“Importantly, the spatiotemporal spread of αSyn lesions in PD/DLB is nearly inverted to the spread of Aβ and tau pathology as observed in AD [203].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [203]
In the citing paper
“pathological neurofibrillary Tau aggregates show a pattern of accumulation that starts in the entorhinal cortex and spreads through connected pathways to cortical areas (Jucker and Walker, 2013)”
From Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease (2020) · cites this paper as Jucker and Walker, 2013
In the citing paper
“It has been suggested that alpha-synuclein could act like a prion protein during PD pathogenesis.In this theory pathologic, misfolded alpha-synuclein is an 'infectious' protein spreading pathology by forming a template that seeds misfolding for nearby alpha-synuclein protein, turning the previously healthy protein into a pathogenic protein (Jucker and Walker, 2013;Visanji et al., 2013).”
From The Gut-Brain Axis in Parkinson’s Disease: Possibilities for Food-Based Therapies (2017) · cites this paper as Jucker and Walker, 2013
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Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
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 6,497
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814
Phases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495
Cited by
Sorted by citations
Scheltens, P., Blennow, K., Breteler, M. M. B., de Strooper, B., Frisoni, G. B., Salloway, S., & Van der Flier, W. M. (2016) · The Lancet · doi:10.1016/s0140-6736(15)01124-1 · Cited by 3,125
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927
Lane, C. A., Hardy, J., & Schott, J. M. (2018) · European Journal of Neurology · doi:10.1111/ene.13439 · Cited by 2,616
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
Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120
How neuroinflammation contributes to neurodegeneration
Ransohoff, R. M. (2016) · Science · doi:10.1126/science.aag2590 · Cited by 1,967
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789
The New Neurometabolic Cascade of Concussion
Giza, C. C., & Hovda, D. A. (2014) · Neurosurgery · doi:10.1227/neu.0000000000000505 · Cited by 1,353
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Glymphatic failure as a final common pathway to dementia
Nedergaard, M., & Goldman, S. A. (2020) · Science · doi:10.1126/science.abb8739 · Cited by 1,145
Trial of Solanezumab for Mild Dementia Due to Alzheimer’s Disease
Honig, L. S., Vellas, B., Woodward, M., Boada, M., Bullock, R., Borrie, M., Hager, K., Andreasen, N., Scarpini, E., Liu-Seifert, H., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1705971 · Cited by 1,049
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., López‐Iglesias, C., Hoyer, W., Heise, H., et al. (2017) · Science · doi:10.1126/science.aao2825 · Cited by 1,055
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease
Venegas, C., Kumar, S., Franklin, B. S., Dierkes, T., Brinkschulte, R., Tejera, D., Vieira-Saecker, A., Schwartz, S., Santarelli, F., Kummer, M. P., et al. (2017) · Nature · doi:10.1038/nature25158 · Cited by 983
Goedert, M. (2015) · Science · doi:10.1126/science.1255555 · Cited by 1,028
Brain-Gut-Microbiota Axis in Alzheimer’s Disease
Kowalski, K., & Mulak, A. (2019) · Journal of Neurogastroenterology and Motility · doi:10.5056/jnm18087 · Cited by 826
TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis
Kleinberger, G., Yamanishi, Y., Suárez-Calvet, M., Czirr, E., Lohmann, E., Cuyvers, E., Struyfs, H., Pettkus, N., Wenninger-Weinzierl, A., Mazaheri, F., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009093 · Cited by 798
APP mouse models for Alzheimer’s disease preclinical studies.
Sasaguri, H., Nilsson, P., Hashimoto, S., Nagata, K., Saito, T., De Strooper, B., Hardy, J., Vassar, R., Winblad, B., & Saido, T. C. (2017) · The EMBO Journal · doi:10.15252/embj.201797397 · Cited by 793
Spreading of pathology in neurodegenerative diseases: a focus on human studies
Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790
Brain-Derived Neurotrophic Factor in Brain Disorders: Focus on Neuroinflammation
Lima Giacobbo, B., Doorduin, J., Klein, H. C., Dierckx, R. A. J. O., Bromberg, E., & de Vries, E. F. J. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1283-6 · Cited by 750
Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3
Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T.-I., Yin, X., Xiong, Y., Ge, P., Umanah, G. E., Brahmachari, S., Shin, J.-H., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 690
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
“During disease progression in AD, pathological neurofibrillary Tau aggregates show a pattern of accumulation that starts in the entorhinal cortex and spreads through connected pathways to cortical areas (Jucker and Walker, 2013).”
BackgroundNguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domínguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 680
Neuroinflammation Induces Neurodegeneration.
Kempuraj, D., Thangavel, R., Natteru, P., Selvakumar, G. P., Saeed, D., Zahoor, H., Zaheer, S., Iyer, S. S., & Zaheer, A. (2016) · PubMed · Cited by 675
Tau PET imaging in neurodegenerative tauopathies—still a challenge
Leuzy, A., Chiotis, K., Lemoine, L., Gillberg, P.-G., Almkvist, O., Rodriguez-Vieitez, E., & Nordberg, A. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0342-8 · Cited by 628
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Selective vulnerability in neurodegenerative diseases
Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585
Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
Altmeyer, M., Neelsen, K. J., Teloni, F., Pozdnyakova, I., Pellegrino, S., Grøfte, M., Rask, M., Streicher, W. W., Jungmichel, S., Nielsen, M. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9088 · Cited by 581
The road to restoring neural circuits for the treatment of Alzheimer's disease
Canter, R. G., Penney, J., & Tsai, L.-H. (2016) · Nature · doi:10.1038/nature20412 · Cited by 565
Loss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
Parhizkar, S., Arzberger, T., Brendel, M., Kleinberger, G., Deussing, M., Focke, C., Nuscher, B., Xiong, M., Ghasemigharagoz, A., Katzmarski, N., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0296-9 · Cited by 555
The gut microbiome in human neurological disease: A review
Tremlett, H., Bauer, K. C., Appel‐Cresswell, S., Finlay, B. B., & Waubant, E. (2017) · Annals of Neurology · doi:10.1002/ana.24901 · Cited by 535
Amyotrophic lateral sclerosis—a model of corticofugal axonal spread
Braak, H., Brettschneider, J., Ludolph, A. C., Lee, V. M., Trojanowski, J. Q., & Tredici, K. D. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.221 · Cited by 544
Current state of Alzheimer’s fluid biomarkers
Molinuevo, J. L., Ayton, S., Batrla, R., Bednar, M. M., Bittner, T., Cummings, J., Fagan, A. M., Hampel, H., Mielke, M. M., Mikulskis, A., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1932-x · Cited by 518
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 536
Synaptic degeneration in Alzheimer disease
Tzioras, M., McGeachan, R. I., Durrant, C. S., & Spires-Jones, T. L. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-022-00749-z · Cited by 504
Converging pathways in neurodegeneration, from genetics to mechanisms
Gan, L., Cookson, M. R., Petrucelli, L., & Spada, A. R. L. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0237-7 · Cited by 500
Fifty Shades of Brain: A Review on the Mechanical Testing and Modeling of Brain Tissue
Budday, S., Ovaert, T. C., Holzapfel, G. A., Steinmann, P., & Ellen Kuhl, A. (2019) · Archives of Computational Methods in Engineering · doi:10.1007/s11831-019-09352-w · Cited by 473
Defects in trafficking bridge Parkinson’s disease pathology and genetics
Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462
Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0238-6 · Cited by 450
Self-citationStancu, I.-C., Cremers, N., Vanrusselt, H., Couturier, J., Vanoosthuyse, A., Kessels, S., Lodder, C., Brône, B., Huaux, F., Octave, J.-N., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-01957-y · Cited by 447
Amyloid Polymorphism: Structural Basis and Neurobiological Relevance
Tycko, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.017 · Cited by 449
A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice
Sampson, T. R., Challis, C., Jain, N., Moiseyenko, A., Ladinsky, M. S., Shastri, G. G., Thron, T., Needham, B. D., Horvath, I., Debelius, J. W., et al. (2020) · eLife · doi:10.7554/elife.53111 · Cited by 439
Transmission of multiple system atrophy prions to transgenic mice
Watts, J. C., Giles, K., Oehler, A., Middleton, L. T., Dexter, D. T., Gentleman, S., DeArmond, S. J., & Prusiner, S. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318268110 · Cited by 455
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy
Li, Y., Zhao, C., Luo, F., Liu, Z., Gui, X., Luo, Z., Zhang, X., Li, D., Liu, C., & Li, X. (2018) · Cell Research · doi:10.1038/s41422-018-0075-x · Cited by 441
Interactions of pathological proteins in neurodegenerative diseases
Spires‐Jones, T. L., Attems, J., & Thal, D. R. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1709-7 · Cited by 435
Targeting protein aggregation for the treatment of degenerative diseases
Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4593 · Cited by 426
Glial contributions to neurodegeneration in tauopathies
Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409
A clinicopathological approach to the diagnosis of dementia
Elahi, F. M., & Miller, B. L. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.96 · Cited by 425
Jo, M., Lee, S., Jeon, Y., Kim, S., Kwon, Y., & Kim, H. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00513-7 · Cited by 427
Insulin and Insulin Resistance in Alzheimer’s Disease
Sędzikowska, A., & Szablewski, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189987 · Cited by 414
Review: Sporadic Parkinson's disease: development and distribution ofα‐synuclein pathology
Tredici, K. D., & Braak, H. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12298 · Cited by 416
Exploring Braak’s hypothesis of Parkinson’s disease
Rietdijk, C. D., Perez-Pardo, P., Garssen, J., van Wezel, R. J. A., & Kraneveld, A. D. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00037 · Cited by 395
Biological aging processes underlying cognitive decline and neurodegenerative disease
Gonzales, M. M., Garbarino, V. R., Pollet, E., Palavicini, J. P., Kellogg, D. L., Kraig, E., & Orr, M. E. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158453 · Cited by 426
Tagge, C. A., Fisher, A. M., Minaeva, O. V., Gaudreau, A., Moncaster, J. A., Zhang, X.-L., Wojnarowicz, M. W., Casey, N. F., Lu, H., Kokiko‐Cochran, O. N., et al. (2017) · Brain · doi:10.1093/brain/awx350 · Cited by 402
Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease
Bridi, J. C., & Hirth, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00080 · Cited by 396
α-synuclein in the pathophysiology of Alzheimer’s disease
Twohig, D., & Nielsen, H. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0320-x · Cited by 374
Braak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372
Updated TDP-43 in Alzheimer’s disease staging scheme
Josephs, K. A., Murray, M. E., Whitwell, J. L., Tosakulwong, N., Weigand, S. D., Petrucelli, L., Liesinger, A. M., Petersen, R. C., Parisi, J. E., & Dickson, D. W. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1537-1 · Cited by 382
Neurodegenerative Diseases: Expanding the Prion Concept
Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361
Self-citationAlzheimer's disease: From immunotherapy to immunoprevention
Jucker, M., & Walker, L. C. (2023) · Cell · doi:10.1016/j.cell.2023.08.021 · Cited by 353
Self-citationLoss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
Parhizkar, S., Arzberger, T., Brendel, M., Kleinberger, G., Deußing, M., Focke, C., Nuscher, B., Xiong, M., Ghasemigharagoz, A., Katzmarski, N., et al. (2019) · doi:10.7892/boris.125653 · Cited by 352
TREM2 deficiency impairs chemotaxis and microglial responses to neuronal injury
Mazaheri, F., Snaidero, N., Kleinberger, G., Madore, C., Daria, A., Werner, G., Krasemann, S., Capell, A., Trümbach, D., Wurst, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201743922 · Cited by 351
Observing crystal nucleation in four dimensions using atomic electron tomography
Zhou, J., Yang, Y., Yang, Y., Kim, D. S., Yuan, A. C., Tian, X., Ophus, C., Sun, F., Schmid, A. K., Nathanson, M. H., et al. (2019) · Nature · doi:10.1038/s41586-019-1317-x · Cited by 348
Microglia in Alzheimer's disease at single-cell level. Are there common patterns in humans and mice?
Chen, Y., & Colonna, M. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20202717 · Cited by 339
Mechanisms of Molecular Mimicry Involving the Microbiota in Neurodegeneration
Friedland, R. P. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142841 · Cited by 338
Type 2 diabetes as a protein misfolding disease
Mukherjee, A., Morales‐Scheihing, D., Butler, P. C., & Soto, C. A. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.04.005 · Cited by 349
Phase Separation: Linking Cellular Compartmentalization to Disease
Aguzzi, A., & Altmeyer, M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.004 · Cited by 343
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 338
Sequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD)
Brettschneider, J., Tredici, K. D., Irwin, D. J., Grossman, M., Robinson, J. L., Toledo, J. B., Fang, L., Deerlin, V. M. V., Ludolph, A. C., Lee, V. M. ‐., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1238-y · Cited by 328
Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies
Tardivel, M., Bégard, S., Bousset, L., Dujardin, S., Coens, A., Melki, R., Buée, L., & Colin, M. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0386-4 · Cited by 305
Mechanisms of secretion and spreading of pathological tau protein
Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304
Iraci, N., Leonardi, T., Gessler, F., Vega, B., & Pluchino, S. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020171 · Cited by 301
Endoplasmic reticulum stress and inflammation in the central nervous system
Sprenkle, N. T., Sims, S. G., Sánchez, C. L., & Meares, G. P. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0183-y · Cited by 305
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 308
A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 301
Simon, M. J., Wang, M. X., Ismail, O., Braun, M., Schindler, A. G., Reemmer, J., Wang, Z., Haveliwala, M. A., O’Boyle, R. P., Han, W., et al. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-00999-5 · Cited by 293
Serial propagation of distinct strains of Aβ prions from Alzheimer’s disease patients
Watts, J. C., Condello, C., Stöhr, J., Oehler, A., Lee, J., DeArmond, S. J., Lannfelt, L., Ingelsson, M., Giles, K., & Prusiner, S. B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408900111 · Cited by 291
Role of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278
Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein
Cho, S. Y., Yun, Y. S., Lee, S., Jang, D., Park, K.-Y., Kim, J. K., Kim, B. H., Kang, K., Kaplan, D. L., & Jin, H.-J. (2015) · Nature Communications · doi:10.1038/ncomms8145 · Cited by 277
Clearance of cerebral Aβ in Alzheimer’s disease: reassessing the role of microglia and monocytes
Zuroff, L. R., Daley, D. A., Black, K. L., & Koronyo‐Hamaoui, M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2463-7 · Cited by 292
Brain aging mechanisms with mechanical manifestations
Blinkouskaya, Y., Caçoilo, A., Gollamudi, T., Jalalian, S., & Weickenmeier, J. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111575 · Cited by 306
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272
TDP-43 pathology and neuronal loss in amyotrophic lateral sclerosis spinal cord
Brettschneider, J., Arai, K., Tredici, K. D., Toledo, J. B., Robinson, J. L., Lee, E. B., Kuwabara, S., Shibuya, K., Irwin, D. J., Fang, L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1299-6 · Cited by 279
Polanco, J. C., Scicluna, B. J., Hill, A. F., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709485 · Cited by 280
Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Tziortzouda, P., Bosch, L. V. D., & Hirth, F. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00431-1 · Cited by 285
Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine
Irwin, D. J., Cairns, N. J., Grossman, M., McMillan, C. T., Lee, E. B., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1380-1 · Cited by 278
Ocular indicators of Alzheimer’s: exploring disease in the retina
Hart, N. J., Koronyo, Y., Black, K. L., & Koronyo‐Hamaoui, M. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1613-6 · Cited by 264
Boluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 268
Synaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation
Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 277
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256
The therapeutic potential of chemical chaperones in protein folding diseases
Cortez, L. M., & Sim, V. L. (2014) · Prion · doi:10.4161/pri.28938 · Cited by 254
Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins
Flavin, W. P., Bousset, L., Green, Z. C., Chu, Y., Skarpathiotis, S., Chaney, M. J., Kordower, J. H., Melki, R., & Campbell, E. M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1722-x · Cited by 260
Structural basis of synaptic vesicle assembly promoted by α-synuclein
Fusco, G., Pape, T., Stephens, A. D., Mahou, P., Costa, A. R., Kaminski, C. F., Schierle, G. S. K., Vendruscolo, M., Veglia, G., Dobson, C. M., et al. (2016) · Nature Communications · doi:10.1038/ncomms12563 · Cited by 261
Unconventional Secretion Mediates the Trans-cellular Spreading of Tau
Katsinelos, T., Zeitler, M., Dimou, E., Karakatsani, A., Müller, H., Nachman, E., Steringer, J. P., de Almodóvar, C. R., Nickel, W., & Jahn, T. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.056 · Cited by 274
Kang, U. J., Boehme, A. K., Fairfoul, G., Shahnawaz, M., Ma, T. C., Hutten, S. J., Green, A. J. E., & Soto, C. A. (2019) · Movement Disorders · doi:10.1002/mds.27646 · Cited by 253
Porta, S., Xu, Y., Restrepo, C. R., Kwong, L. K., Zhang, B., Brown, H. J., Lee, E. B., Trojanowski, J. Q., & Lee, V. M.-Y. (2018) · Nature Communications · doi:10.1038/s41467-018-06548-9 · Cited by 248
The glymphatic system: implications for drugs for central nervous system diseases
Lohela, T. J., Lilius, T. O., & Nedergaard, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00500-9 · Cited by 254
Arterial stiffness and vascular aging: mechanisms, prevention, and therapy
Herzog, M. J., Müller, P., Lechner, K., Stiebler, M., Arndt, P., Kunz, M., Ahrens, D., Schmeißer, A., Schreiber, S., & Braun-Dullaeus, R. C. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02346-0 · Cited by 275
Usenovic, M., Niroomand, S., Drolet, R. E., Yao, L., Gaspar, R. C., Hatcher, N. G., Schachter, J., Renger, J. J., & Parmentier-Batteur, S. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.1523-15.2015 · Cited by 245
Rajasekhar, K., Chakrabarti, M., & Govindaraju, T. (2015) · Chemical Communications · doi:10.1039/c5cc05264e · Cited by 243
Metadata
- Authors
- Jucker, M., & Walker, L. C.
- Affiliations
- Hertie Institute for Clinical Brain Research (DE)
- Emory University (US)
- Corresponding author
- Jucker, Mathias
- Walker, Lary C.
- Venue
- Nature
- Published
- 2013-09-04
- Volume
- 501
- Issue
- 7465
- Pages
- 45-51
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3963807
- OpenAlex
- W2034147064
- Cited by
- 1,663
- References
- 126
- Citations by year
- 2026: 82 · 2025: 113 · 2024: 114 · 2023: 111 · 2022: 119 · 2021: 161 · 2020: 140 · 2019: 153 · 2018: 131 · 2017: 166 · 2016: 147 · 2015: 119 · 2014: 101 · 2013: 6
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DZNE Pub (submittedVersion)
- Funders
- National Institutes of Health (P51OD011132)
- National Institute on Aging (R21AG040589)
- National Center for Research Resources (P51RR165, P51RR000165)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- protein aggregation, seeded aggregation, neurodegenerative diseases, prion disease, Alzheimer's disease, Parkinson's disease, Creutzfeldt-Jakob disease, protein misfolding, amyloid, oligomers, proteinopathies, disease models, neurodegeneration therapy
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Humans, Prions, tau Proteins, Prion Diseases, Neurodegenerative Diseases, alpha-Synuclein
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