Cited by 797Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingAmyotrophic Lateral Sclerosis Research

The DOI matches its Crossref record; 186 of the 187 references it cites were found in a registry or an index.

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Open access

Brettschneider, Johannes, Tredici, Kelly Del, Lee, Virginia M.-Y., Trojanowski, John Q.·2015·Nature Reviews Neuroscience

DOI 10.1038/nrn3887PMC PMC4312418

Open this paper in CoChat — free account

Abstract

The progression of many neurodegenerative diseases is thought to be driven by the template-directed misfolding, seeded aggregation and cell-cell transmission of characteristic disease-related proteins, leading to the sequential dissemination of pathological protein aggregates. Recent evidence strongly suggests that the anatomical connections made by neurons - in addition to the intrinsic characteristics of neurons, such as morphology and gene expression profile - determine whether they are vulnerable to degeneration in these disorders. Notably, this common pathogenic principle opens up opportunities for pursuing novel targets for therapeutic interventions for these neurodegenerative disorders. We review recent evidence that supports the notion of neuron-neuron protein propagation, with a focus on neuropathological and positron emission tomography imaging studies in humans.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1038/nrn3887

Cites

186 of 186 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Self-citation
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Self-citation
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,221
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B
Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496
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
Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172
Self-citation
α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice
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
Self-citation
Neurodegenerative Tauopathies
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Self-citation
The spectrum of disease in chronic traumatic encephalopathy
McKee, A. C., Stein, T. D., Nowinski, C. J., Stern, R. A., Daneshvar, D. H., Alvarez, V. E., Lee, H.-S., Hall, G., Wojtowicz, S. M., Baugh, C. M., et al. (2013) · Brain · doi:10.1093/brain/aws307 · Cited by 2,098
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892
Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803
Idiopathic Parkinson's disease: possible routes by which vulnerable neuronal types may be subject to neuroinvasion by an unknown pathogen
Braak, H., R�b, U., Gai, W. P., & Del Tredici, K. (2003) · Journal of Neural Transmission · doi:10.1007/s00702-002-0808-2 · Cited by 1,683
Self-citation
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569
Self-citation
Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567
Self-citation
Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.
Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427
Gastric α-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's disease-related brain pathology
Braak, H., de Vos, R. A. I., Bohl, J., & Del Tredici, K. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2005.11.012 · Cited by 1,354
Self-citation
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252
Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1
Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,250
100 years of Lewy pathology
Goedert, M., Spillantini, M. G., Del Tredici, K., & Braak, H. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.242 · Cited by 1,190
Self-citation
Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,136
Self-citation
Use of Florbetapir-PET for Imaging β-Amyloid Pathology
Clark, C. M. (2011) · JAMA · doi:10.1001/jama.2010.2008 · Cited by 1,117
Cell-produced α-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115
Stages of pTDP‐43 pathology in amyotrophic lateral sclerosis
Brettschneider, J., Del Tredici, K., Toledo, J. B., Robinson, J. L., Irwin, D. J., Grossman, M., Suh, E., Van Deerlin, V. M., Wood, E. M., Baek, Y., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23937 · Cited by 1,065
Self-citation
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994
Anatomical correlates of the distribution of the pathological changes in the neocortex in Alzheimer disease.
Pearson, R. C., Esiri, M. M., Hiorns, R. W., Wilcock, G. K., & Powell, T. P. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4531 · Cited by 987
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986
Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Direct evidence of Parkinson pathology spread from the gastrointestinal tract to the brain in rats
Holmqvist, S., Chutna, O., Bousset, L., Aldrin-Kirk, P., Li, W., Björklund, T., Wang, Z.-Y., Roybon, L., Melki, R., & Li, J.-Y. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1343-6 · Cited by 925
TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916
Multi-organ distribution of phosphorylated α-synuclein histopathology in subjects with Lewy body disorders
Arizona Parkinson’s Disease Consortium, Beach, T. G., Adler, C. H., Sue, L. I., Vedders, L., Lue, L., White III, C. L., Akiyama, H., Caviness, J. N., Shill, H. A., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0664-3 · Cited by 911
Exosomal cell-to-cell transmission of alpha synuclein oligomers
Danzer, K. M., Kranich, L. R., Ruf, W. P., Cagsal‐Getkin, O., Winslow, A. R., Zhu, L., Vanderburg, C. R., & McLean, P. J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-42 · Cited by 880
Direct Transfer of α-Synuclein from Neuron to Astroglia Causes Inflammatory Responses in Synucleinopathies
Lee, H.-J., Suk, J.-E., Patrick, C., Bae, E.-J., Cho, J.-H., Rho, S., Hwang, D., Masliah, E., & Lee, S.-J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.081125 · Cited by 877
Prion-like spreading of pathological α-synuclein in brain
Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867
Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859
α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 826
Identifying the amylome, proteins capable of forming amyloid-like fibrils
Goldschmidt, L., Teng, P. K., Riek, R., & Eisenberg, D. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915166107 · Cited by 814
The pathological process underlying Alzheimer’s disease in individuals under thirty
Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812
Self-citation
Brain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 792
Where Does Parkinson Disease Pathology Begin in the Brain?
Del Tredici, K., Rüb, U., de Vos, R. A. I., Bohl, J. R. E., & Braak, H. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.5.413 · Cited by 773
Self-citation
Imaging of Tau Pathology in a Tauopathy Mouse Model and in Alzheimer Patients Compared to Normal Controls
Maruyama, 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
Self-citation
A network diffusion model of disease progression in dementia
Raj, A., Kuceyeski, A., & Weiner, M. (2012) · Neuron · doi:10.1016/j.neuron.2011.12.040 · Cited by 723
Predicting Regional Neurodegeneration from the Healthy Brain Functional Connectome
Zhou, J., Gennatas, E. D., Kramer, J. H., Miller, B. L., & Seeley, W. W. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.004 · Cited by 706
Unified staging system for Lewy body disorders: correlation with nigrostriatal degeneration, cognitive impairment and motor dysfunction
the Arizona Parkinson’s Disease Consortium, Beach, T. G., Adler, C. H., Lue, L., Sue, L. I., Bachalakuri, J., Henry-Watson, J., Sasse, J., Boyer, S., Shirohi, S., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0538-8 · Cited by 698
Early Clinical PET Imaging Results with the Novel PHF-Tau Radioligand [F18]-T808
Chien, D. T., Szardenings, A. K., Bahri, S., Walsh, J. C., Mu, F., Xia, C. A., Shankle, W. R., Lerner, A. J., Su, M., Elizarov, A. M., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130098 · Cited by 683
Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680
Self-citation
Lewy body extracts from Parkinson disease brains trigger α‐synuclein pathology and neurodegeneration in mice and monkeys
Recasens, A., Dehay, B., Bové, J., Carballo‐Carbajal, I., Doveró, S., Pérez‐Villalba, A., Fernagut, P., Blesa, J., Parent, A., Perier, C., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24066 · Cited by 670
Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664
Self-citation
18 F‐flutemetamol amyloid imaging in Alzheimer disease and mild cognitive impairment: A phase 2 trial
Vandenberghe, R. R., Laere, K. V., Ivanoiu, A., Salmon, É., Bastin, C., Triau, E., Hasselbalch, S. G., Law, I. G., Andersen, A., Kørner, A., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22068 · Cited by 664
Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice
Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655
Early clinical PET imaging results with the novel PHF-tau radioligand [F-18]-T807
Chien, D. T., Bahri, S., Szardenings, A. K., Walsh, J. C., Mu, F., Su, M.-Y., Shankle, W. R., Elizarov, A., & Kolb, H. C. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-122059 · Cited by 651
Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641
Self-citation
Cerebral amyloid-β PET with florbetaben (18F) in patients with Alzheimer's disease and healthy controls: a multicentre phase 2 diagnostic study
Barthel, H., Gertz, H., Dresel, S. H. J., Peters, O., Bartenstein, P., Büerger, K., Hiemeyer, F. J., Wittemer‐Rump, S., Seibyl, J. P., Reininger, C. B., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70077-1 · Cited by 600
Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis
Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568
Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552
Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains
Nonaka, T., Masuda‐Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., Yoshida, M., Murayama, S., Mann, D. M. A., Akiyama, H., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.007 · Cited by 547
TDP-43 in Familial and Sporadic Frontotemporal Lobar Degeneration with Ubiquitin Inclusions
Cairns, N. J., Neumann, M., Bigio, E. H., Holm, I. E., Troost, D., Hatanpaa, K. J., Foong, C., White, C. L., Schneider, J. A., Kretzschmar, H. A., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070182 · Cited by 545
Self-citation
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
Self-citation
Small Misfolded Tau Species Are Internalized via Bulk Endocytosis and Anterogradely and Retrogradely Transported in Neurons
Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537
Parkinson's disease: the presence of Lewy bodies in Auerbach's and Meissner's plexuses
Wakabayashi, K., Takahashi, H., Takeda, S., Ohama, E., & Ikuta, F. (1988) · Acta Neuropathologica · doi:10.1007/bf00687767 · Cited by 528
Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
Münch, C., O’Brien, J., & Bertolotti, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017275108 · Cited by 475
The Transcellular Spread of Cytosolic Amyloids, Prions, and Prionoids
Aguzzi, A., & Rajendran, L. (2009) · Neuron · doi:10.1016/j.neuron.2009.12.016 · Cited by 473
Assembly-dependent endocytosis and clearance of extracellular a-synuclein
Lee, H.-J., Suk, J.-E., Bae, E.-J., Lee, J.-H., Paik, S. R., & Lee, S.-J. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.017 · Cited by 470
Alpha-synuclein in colonic submucosa in early untreated Parkinson’s disease
Shannon, K. M., Keshavarzian, A., Mutlu, E., Dodiya, H. B., Daian, D., Jaglin, J. A., & Kordower, J. H. (2012) · Movement Disorders · doi:10.1002/mds.23838 · Cited by 469
Protein transfer at the blood cerebrospinal fluid barrier and the quantitation of the humoral immune response within the central nervous system
Reiber, H., & Felgenhauer, K. (1987) · Clinica Chimica Acta · doi:10.1016/0009-8981(87)90250-6 · Cited by 462
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
Identification and Rescue of α-Synuclein Toxicity in Parkinson Patient–Derived Neurons
Chung, C. Y., Khurana, V., Auluck, P. K., Tardiff, D. F., Mazzulli, J. R., Soldner, F., Baru, V., Lou, Y., Freyzon, Y., Cho, S., et al. (2013) · Science · doi:10.1126/science.1245296 · Cited by 454
Isogenic Human iPSC Parkinson’s Model Shows Nitrosative Stress-Induced Dysfunction in MEF2-PGC1α Transcription
Ryan, S. D., Dolatabadi, N., Chan, S. F., Zhang, X., Akhtar, M. W., Parker, J., Soldner, F., Sunico, C. R., Nagar, S., Talantova, M. V., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.009 · Cited by 445
Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
Deng, H., Shi, Y., Furukawa, Y., Zhai, H., Fu, R., Liu, E., Gorrie, G., Khan, M. S., Hung, W.-Y., Bigio, E. H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602046103 · Cited by 432
Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers
De Felice, F. G., Wu, D., Lambert, M. P., Fernandez, S. J., Velasco, P. T., Lacor, P. N., Bigio, E. H., Jerecic, J., Acton, P. J., Shughrue, P. J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.029 · Cited by 432
Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
Ren, P.-H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., & Kopito, R. R. (2009) · Nature Cell Biology · doi:10.1038/ncb1830 · Cited by 427
Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms
Grad, L. I., Yerbury, J. J., Turner, B. J., Guest, W. C., Pokrishevsky, E., O’Neill, M. A., Yanai, A., Silverman, J. M., Zeineddine, R., Corcoran, L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312245111 · Cited by 414
Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis
Braak, H., & Braak, E. (1996) · Acta Neuropathologica · doi:10.1007/s004010050508 · Cited by 406
Norepinephrine: A Neuromodulator That Boosts the Function of Multiple Cell Types to Optimize CNS Performance
O’Donnell, J., Zeppenfeld, D., McConnell, E., Pena, S., & Nedergaard, M. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0818-x · Cited by 399
Prion-like acceleration of a synucleinopathy in a transgenic mouse model
Mougenot, A.-L. J., Nicot, S., Bencsik, A. A., Morignat, E., Verchère, J., Lakhdar, L., Legastelois, S., & Baron, T. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.022 · Cited by 399
Alzheimer's disease and Aβ toxicity: from top to bottom
Small, D. H., Mok, S. S., & Bornstein, J. C. (2001) · Nature reviews. Neuroscience · doi:10.1038/35086072 · Cited by 398
Evidence for Seeding of β-Amyloid by Intracerebral Infusion of Alzheimer Brain Extracts in β-Amyloid Precursor Protein-Transgenic Mice
Kane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., Roher, A. E., & Walker, L. C. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03606.2000 · Cited by 394
Neuron‐to‐neuron transmission of α‐synuclein fibrils through axonal transport
Freundt, E. C., Maynard, N., Clancy, E. K., Roy, S., Bousset, L., Sourigues, Y., Covert, M. W., Melki, R., Kirkegaard, K., & Brahic, M. (2012) · Annals of Neurology · doi:10.1002/ana.23747 · Cited by 394
Regional variability of imaging biomarkers in autosomal dominant Alzheimer's disease
Benzinger, T. L. S., Blazey, T., Jack, C. R., Koeppe, R. A., Su, Y., Xiong, C., Raichle, M. E., Snyder, A. Z., Ances, B. M., Bateman, R. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317918110 · Cited by 391
The olfactory vector hypothesis of neurodegenerative disease: Is it viable?
Doty, R. L. (2008) · Annals of Neurology · doi:10.1002/ana.21327 · Cited by 391
Sequence of Aβ-protein deposition in the human medial temporal lobe
Thal, D. R., Rüb, U., Schultz, C., Sassin, I., Ghebremedhin, E., Del Tredici, K., Braak, E., & Braak, H. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.8.733 · Cited by 370
Self-citation
Molecular Mechanisms of Prion Pathogenesis
Aguzzi, A., Sigurdson, C. J., & Heikenwaelder, M. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.154326 · Cited by 366
Staging TDP-43 pathology in Alzheimer’s disease
Josephs, K. A., Murray, M. E., Whitwell, J. L., Parisi, J. E., Petrucelli, L., Jack, C. R., Petersen, R. C., & Dickson, D. W. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1211-9 · Cited by 366
Astrocytic expression of Parkinson's disease-related A53T α-synuclein causes neurodegeneration in mice
Gu, X., Long, C.-X., Sun, L., Xie, C., Lin, X. Z., & Cai, H. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-12 · Cited by 351
Seeded Aggregation and Toxicity of α-Synuclein and Tau
Nonaka, T., Watanabe, S., Iwatsubo, T., & Hasegawa, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148460 · Cited by 348
Phosphorylated TDP-43 in Alzheimer’s disease and dementia with Lewy bodies
Arai, T., Mackenzie, I. R. A., Hasegawa, M., Nonoka, T., Niizato, K., Tsuchiya, K., Iritani, S., Onaya, M., & Akiyama, H. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0480-1 · Cited by 345
Molecular imaging with Pittsburgh Compound B confirmed at autopsy: a case report.
Bacskai, B. J., Frosch, M. P., Freeman, S. H., Raymond, S. B., Augustinack, J. C., Johnson, K. A., Irizarry, M. C., Klunk, W. E., Mathis, C. A., DeKosky, S. T., et al. (2007) · PubMed · doi:10.1001/archneur.64.3.431 · Cited by 341
18F-THK523: a novel in vivo tau imaging ligand for Alzheimer's disease
Fodero‐Tavoletti, M. T., Okamura, N., Furumoto, S., Mulligan, R. S., Connor, A. R., McLean, C., Cao, D., Rigopoulos, A., Cartwright, G. A., O'Keefe, G. J., et al. (2011) · Brain · doi:10.1093/brain/awr038 · Cited by 340
Antibody-Aided Clearance of Extracellular α-Synuclein Prevents Cell-to-Cell Aggregate Transmission
Bae, E.-J., Lee, H.-J., Rockenstein, E., Ho, D.-H., Park, E.-B., Yang, N.-Y., Desplats, P., Masliah, E., & Lee, S.-J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1292-12.2012 · Cited by 339
Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice
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
The human entorhinal cortex: normal morphology and lamina-specific pathology in various diseases
Braak, H., & Braak, E. (1992) · Neuroscience Research · doi:10.1016/0168-0102(92)90014-4 · Cited by 334
α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration
Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 334
Self-citation
The Transthyretin Amyloidoses: From Delineating the Molecular Mechanism of Aggregation Linked to Pathology to a Regulatory-Agency-Approved Drug
Johnson, S. M., Connelly, S., Fearns, C., Powers, E. T., & Kelly, J. W. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.060 · Cited by 332
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
Self-citation
Insights into prion strains and neurotoxicity
Aguzzi, A., Heikenwälder, M. F., & Polymenidou, M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2204 · Cited by 327
Parkinson's disease: an immunohistochemical study of Lewy body-containing neurons in the enteric nervous system
Wakabayashi, K., Takahashi, H., Ohama, E., & Ikuta, F. (1990) · Acta Neuropathologica · doi:10.1007/bf00294234 · Cited by 324
Neuronal cytoskeletal changes are an early consequence of repetitive head injury
Geddes, J. F., Vowles, G. H., Nicoll, J. A. R., & Révész, T. (1999) · Acta Neuropathologica · doi:10.1007/s004010051066 · Cited by 323
Transsynaptic progression of amyloid-β-induced neuronal dysfunction within the entorhinal-hippocampal network
Harris, J. A., Devidze, N., Verret, L., Ho, K., Halabisky, B., Thwin, M. T., Kim, D., Hamto, P., Lo, I., Yu, G.-Q., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.020 · Cited by 319
Incidence of Dementia With Lewy Bodies and Parkinson Disease Dementia
Savica, R., Grossardt, B. R., Bower, J. H., Boeve, B. F., Ahlskog, J. E., & Rocca, W. A. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.3579 · Cited by 317
The Binding of 2-(4′-Methylaminophenyl)Benzothiazole to Postmortem Brain Homogenates Is Dominated by the Amyloid Component
Klunk, W. E., Wang, Y., Huang, G.-F., Debnath, M. L., Holt, D. P., Shao, L., Hamilton, R. L., Ikonomović, M. D., DeKosky, S. T., & Mathis, C. A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-06-02086.2003 · Cited by 306
Lewy pathology in the submandibular gland of individuals with incidental Lewy body disease and sporadic Parkinson’s disease
Tredici, K. D., Hawkes, C. H., Ghebremedhin, E., & Braak, H. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0665-2 · Cited by 303
Self-citation
Parkinson's Disease: The Dual Hit Theory Revisited
Hawkes, C. H., Del Tredici, K., & Braak, H. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04365.x · Cited by 303
Self-citation
Transplanted dopaminergic neurons develop PD pathologic changes: A second case report
Kordower, J. H., Chu, Y., Hauser, R. A., Olanow, C. W., & Freeman, T. B. (2008) · Movement Disorders · doi:10.1002/mds.22369 · Cited by 301
Mouse Model of Multiple System Atrophy α-Synuclein Expression in Oligodendrocytes Causes Glial and Neuronal Degeneration
Yazawa, I., Giasson, B. I., Sasaki, R., Zhang, B., Joyce, S., Uryu, K., Trojanowski, J. Q., & Lee, V. M.-Y. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.032 · Cited by 301
Self-citation
Neuroanatomy and Pathology of Sporadic Parkinson's Disease
Braak, H., & Tredici, K. D. (2008) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-540-79850-7 · Cited by 297
Self-citation
The anterior olfactory nucleus in Parkinson's disease
Pearce, R. K. B., Hawkes, C. H., & Daniel, S. E. (1995) · Movement Disorders · doi:10.1002/mds.870100309 · Cited by 289
Novel 18F-Labeled Arylquinoline Derivatives for Noninvasive Imaging of Tau Pathology in Alzheimer Disease
Okamura, N., Furumoto, S., Harada, R., Tago, T., Yoshikawa, T., Fodero‐Tavoletti, M. T., Mulligan, R. S., Villemagne, V. L., Akatsu, H., Yamamoto, T., et al. (2013) · Journal of Nuclear Medicine · doi:10.2967/jnumed.112.117341 · Cited by 289
Neuron-to-neuron wild-type Tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies
Dujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 284
Alpha‐synuclein transfers from neurons to oligodendrocytes
Reyes, J. F., Rey, N. L., Bousset, L., Melki, R., Brundin, P., & Angot, É. (2013) · Glia · doi:10.1002/glia.22611 · Cited by 283
Intermolecular transmission of superoxide dismutase 1 misfolding in living cells
Grad, L. I., Guest, W. C., Yanai, A., Pokrishevsky, E., O’Neill, M. A., Gibbs, E., Semenchenko, V., Yousefi, M., Wishart, D. S., Plotkin, S. S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102645108 · Cited by 281
Population based epidemiology of amyotrophic lateral sclerosis using capture-recapture methodology
Huisman, M. H. B., de Jong, S. W., van Doormaal, P. T. C., Weinreich, S. S., Schelhaas, H. J., van der Kooi, A. J., de Visser, M., Veldink, J. H., & van den Berg, L. H. (2011) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2011.244939 · Cited by 277
Non-invasive assessment of Alzheimer’s disease neurofibrillary pathology using 18F-THK5105 PET
Okamura, N., Furumoto, S., Fodero‐Tavoletti, M. T., Mulligan, R. S., Harada, R., Yates, P. A., Pejoska, S., Kudo, Y., Masters, C. L., Yanai, K., et al. (2014) · Brain · doi:10.1093/brain/awu064 · Cited by 273
Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo
Angot, E., Steiner, J. A., Lema Tomé, C. M., Ekström, P., Mattsson, B., Björklund, A., & Brundin, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039465 · Cited by 270
Glial cells in amyotrophic lateral sclerosis
Philips, T., & Rothstein, J. D. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.05.015 · Cited by 266
Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis
Shaw, P. J., & Eggett, C. J. (2000) · Journal of Neurology · doi:10.1007/bf03161151 · Cited by 262
Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype
Josephs, K. A., Whitwell, J. L., Knopman, D. S., Hu, W. T., Stroh, D. A., Baker, M., Rademakers, R., Boeve, B. F., Parisi, J. E., Smith, G. E., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000304041.09418.b1 · Cited by 258
The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth
Fallini, C., Bassell, G. J., & Rossoll, W. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds205 · Cited by 247
Spreading of Neurodegenerative Pathology via Neuron-to-Neuron Transmission of -Amyloid
Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244
Axonal and transneuronal transport in the transmission of neurological disease: Potential role in system degenerations, including alzheimer's disease
Saper, C., Wainer, B. H., & German, D. C. (1987) · Neuroscience · doi:10.1016/0306-4522(87)90063-7 · Cited by 239
A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions
Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K., & Nukina, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231209 · Cited by 239
Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition
Langer, F., Eisele, Y. S., Fritschi, S. K., Staufenbiel, M., Walker, L. C., & Jucker, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3088-11.2011 · Cited by 237
Gastrointestinal dysfunction in Parkinson's disease
Edwards, L., Quigley, E., & Pfeiffer, R. (1992) · Neurology · doi:10.1212/wnl.42.4.726 · Cited by 226
Predicting Alzheimer disease with β‐amyloid imaging: Results from the Australian imaging, biomarkers, and lifestyle study of ageing
Rowe, C. C., Bourgeat, P., Ellis, K. A., Brown, B., Lim, Y. Y., Mulligan, R., Jones, G., Maruff, P., Woodward, M., Price, R., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24040 · Cited by 222
Characterization of Lewy body pathology in 12‐ and 16‐year‐old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease
Li, J., Englund, E. M., Widner, H., Rehncrona, S., Björklund, A., Lindvall, O., & Brundin, P. (2010) · Movement Disorders · doi:10.1002/mds.23012 · Cited by 221
Diffusion tensor imaging of white matter degeneration in Alzheimer’s disease and mild cognitive impairment
Amlien, I. K., & Fjell, A. M. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.02.017 · Cited by 219
Neuroprotective and neurotoxic properties of glial cells in the pathogenesis of Alzheimer's disease
Farfara, D., Lifshitz, V., & Frenkel, D. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00314.x · Cited by 216
Grading of neuropathology in multiple system atrophy: Proposal for a novel scale
Jellinger, K. A., Seppi, K., & Wenning, G. K. (2005) · Movement Disorders · doi:10.1002/mds.20537 · Cited by 203
The impact of reactive oxygen species and genetic mitochondrial mutations in Parkinson's disease
Zuo, L., & Motherwell, M. S. (2013) · Gene · doi:10.1016/j.gene.2013.07.085 · Cited by 200
Diffusion tensor imaging analysis of sequential spreading of disease in amyotrophic lateral sclerosis confirms patterns of TDP-43 pathology
Kassubek, J., Müller, H.-P., Tredici, K. D., Brettschneider, J., Pinkhardt, E. H., Lulé, D. E., Böhm, S., Braak, H., & Ludolph, A. C. (2014) · Brain · doi:10.1093/brain/awu090 · Cited by 198
Self-citation
A highly selective and specific PET tracer for imaging of tau pathologies
Zhang, W., Arteaga, J., Cashion, D. K., Chen, G., Gangadharmath, U., Gomez, L. F., Kasi, D., Lam, C., Liang, Q., Liu, C., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-120712 · Cited by 195
Lewy pathology and neurodegeneration in premotor Parkinson's disease
Tredici, K. D., & Braak, H. (2012) · Movement Disorders · doi:10.1002/mds.24921 · Cited by 187
Self-citation
Laminar, tangential and regional organization of the noradrenergic innervation of monkey cortex: Dopamine-β-hydroxylase immunohistochemistry
Morrison, J. H., Foote, S. L., O’Connor, D., & Bloom, F. E. (1982) · Brain Research Bulletin · doi:10.1016/0361-9230(82)90144-7 · Cited by 186
Prion-like spread of protein aggregates in neurodegeneration
Polymenidou, M., & Cleveland, D. W. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20120741 · Cited by 184
Aβ-independent processes—rethinking preclinical AD
Chételat, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.21 · Cited by 184
Beyond the prion principle
Aguzzi, A. (2009) · Nature · doi:10.1038/459924a · Cited by 179
Transfer of host-derived alpha synuclein to grafted dopaminergic neurons in rat
Kordower, J. H., Dodiya, H. B., Kordower, A. M., Terpstra, B. T., Paumier, K. L., Madhavan, L., Sortwell, C. E., Steece‐Collier, K., & Collier, T. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.001 · Cited by 176
Alzheimer's disease β‐secretase BACE1 is not a neuron‐specific enzyme
Roßner, S., Lange‐Dohna, C., Zeitschel, U., & Perez-Polo, J. R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02857.x · Cited by 174
Evaluation of Potential Infectivity of Alzheimer and Parkinson Disease Proteins in Recipients of Cadaver-Derived Human Growth Hormone
Irwin, D. J., Abrams, J. Y., Schonberger, L. B., Leschek, E., Mills, J. L., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1933 · Cited by 172
Self-citation
Spinal cord lesions in sporadic Parkinson’s disease
Tredici, K. D., & Braak, H. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1028-y · Cited by 169
Self-citation
Glial dysfunction in the pathogenesis of α-synucleinopathies: emerging concepts
Fellner, L., Jellinger, K. A., Wenning, G. K., & Stefanova, N. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0833-z · Cited by 162
TDP-43 pathological changes in early onset familial and sporadic Alzheimer’s disease, late onset Alzheimer’s disease and Down’s Syndrome: association with age, hippocampal sclerosis and clinical phenotype
Davidson, Y. S., Raby, S., Foulds, P. G., Robinson, A., Thompson, J. C., Sikkink, S. K., Yusuf, I. H., Amin, H., DuPlessis, D., Troakes, C., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0879-y · Cited by 157
Induction of β(A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate
Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., & Bruton, C. J. (1994) · Molecular Neurobiology · doi:10.1007/bf02778005 · Cited by 153
Is Parkinson's disease a primary olfactory disorder?
Hawkes, C. H. (1999) · QJM · doi:10.1093/qjmed/92.8.473 · Cited by 152
Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis
Chen, A. K.-H., Lin, R. Y., Hsieh, E. Z.-J., Tu, P., Chen, R. P. ‐., Liao, T., Chen, W., Wang, C., & Huang, J. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9066207 · Cited by 145
Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
Clavaguera, F., Hench, J., Lavenir, I., Schweighauser, G., Frank, S., Goedert, M., & Tolnay, M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1231-5 · Cited by 143
Seeded strain‐like transmission of β‐amyloid morphotypes in APP transgenic mice
Heilbronner, G., Eisele, Y. S., Langer, F., Kaeser, S. A., Novotny, R., Nagarathinam, A., Åslund, A., Hammarström, P., Nilsson, K. P. R., & Jucker, M. (2013) · EMBO Reports · doi:10.1038/embor.2013.137 · Cited by 143
Epidemiology and genetics of frontotemporal dementia/Pick's disease
Bird, T. D., Knopman, D. S., Swieten, J. C. V., Rosso, S. M., Feldman, H., Tanabe, H., Graff‐Radford, N. R., Geschwind, D. H., Verpillat, P., & Hutton, M. L. (2003) · Annals of Neurology · doi:10.1002/ana.10572 · Cited by 137
Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease
Hu, W. T., Josephs, K. A., Knopman, D. S., Boeve, B. F., Dickson, D. W., Petersen, R. C., & Parisi, J. E. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0400-4 · Cited by 136
Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
Mori, F., Tanji, K., Zhang, H., Nishihira, Y., Tan, C., Takahashi, H., & Wakabayashi, K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0396-9 · Cited by 135
Interaction between pathogenic proteins in neurodegenerative disorders
Jellinger, K. A. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01507.x · Cited by 132
Exogenous seeding of cerebral β‐amyloid deposition in βAPP‐transgenic rats
Rosen, R. F., Fritz, J. J., Dooyema, J. M., Cintron, A. F., Hamaguchi, T., Lah, J. J., LeVine, H., Jucker, M., & Walker, L. C. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07551.x · Cited by 126
Signs of Degeneration in 12–22-Year Old Grafts of Mesencephalic Dopamine Neurons in Patients with Parkinson's Disease
Kurowska, Z., Englund, E. M., Widner, H., Lindvall, O., Li, J., & Brundin, P. (2011) · Journal of Parkinson s Disease · doi:10.3233/jpd-2011-11004 · Cited by 124
Neurofibrillary tangle‐like tau pathology induced by synthetic tau fibrils in primary neurons over‐expressing mutant tau
Guo, J., & Lee, V. M. ‐. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.051 · Cited by 117
Self-citation
TDP-43 skeins show properties of amyloid in a subset of ALS cases
Robinson, J. L., Geser, F., Stieber, A., Umoh, M. E., Kwong, L. K., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1055-8 · Cited by 113
Self-citation
Volume versus wiring transmission in the brain: A new theoretical frame for neuropsychopharmacology
Agnati, L. F., Bjelke, B., & Fuxé, K. (1995) · Medicinal Research Reviews · doi:10.1002/med.2610150104 · Cited by 107
Evidence for the experimental transmission of cerebral beta-amyloidosis to primates.
Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., & Bruton, C. J. (1993) · Europe PMC (PubMed Central) · Cited by 106
Transport and diffusion of Tau protein in neurons
Scholz, T., & Mandelkow�, E. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1610-7 · Cited by 105
Lewy body pathology in fetal grafts
Chu, Y., & Kordower, J. H. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05229.x · Cited by 104
Early AD pathology in a [C-11]PiB-negative case: a PiB-amyloid imaging, biochemical, and immunohistochemical study
Ikonomović, M. D., Abrahamson, E. E., Price, J. C., Hamilton, R. L., Mathis, C. A., Paljug, W. R., Debnath, M. L., Cohen, A. D., Mizukami, K., DeKosky, S. T., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0943-2 · Cited by 87
The Fluorescent Congo Red Derivative, (Trans, Trans)−1-Bromo-2,5-Bis-(3-Hydroxycarbonyl-4-Hydroxy)Styrylbenzene (BSB), Labels Diverse β-Pleated Sheet Structures in Postmortem Human Neurodegenerative Disease Brains
Schmidt, M. L., Schuck, T., Sheridan, S., Kung, M., Kung, H. F., Zhuang, Z., Bergeron, C., Lamarche, J. S., Skovronsky, D., Giasson, B. I., et al. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61769-5 · Cited by 86
Self-citation
Cellular mechanisms of protein aggregate propagation
Holmes, B. B., & Diamond, M. I. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a3ee0 · Cited by 80
TDP-43 pathology in primary progressive aphasia and frontotemporal dementia with pathologic Alzheimer disease
Bigio, E. H., Mishra, M., Hatanpaa, K. J., White, C. L., Johnson, N., RADEMAKER, A. W., Weitner, B. B., Deng, H., Dubner, S., Weıntraub, S., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0681-2 · Cited by 80
From Top to Bottom
Riemer, K., Stieglitz, S., & Meske, C. (2015) · Business & Information Systems Engineering · doi:10.1007/s12599-015-0375-3 · Cited by 72
Patterns of alpha-synuclein pathology in incidental cases and clinical subtypes of Parkinson's disease
van de Berg, W. D. J., Hepp, D. H., Dijkstra, A. A., Rozemüller, A. J. M., Berendse, H. W., & Foncke, E. M. J. (2011) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(11)70011-6 · Cited by 69
The Slow Axonal Transport of the Microtubule-Associated Protein Tau and the Transport Rates of Different Isoforms and Mutants in Cultured Neurons
Utton, M. A., Connell, J. W., Asuni, A. A., van Slegtenhorst, M., Hutton, M. L., de Silva, R., Lees, A. J., Miller, C. C. J., & Anderton, B. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06394.2002 · Cited by 66
Unmyelinated axons are more vulnerable to degeneration than myelinated axons of the cardiac nerve in Parkinson's disease
Orimo, S., Uchihara, T., Kanazawa, T., Itoh, Y., Wakabayashi, K., Kakita, A., & Takahashi, H. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01194.x · Cited by 62
The cost of an action potential
Aiello, G. L., & Bach‐y‐Rita, P. (2000) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(00)00308-3 · Cited by 59
Astrocyte signaling and neurodegeneration
Brambilla, L., Martorana, F., & Rossi, D. (2013) · Prion · doi:10.4161/pri.22512 · Cited by 58
Evolutional Aspects of Alzheimer's Disease Pathogenesis
Braak, H., & Tredici, K. D. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129029 · Cited by 54
Self-citation
Human Prion Diseases: From Kuru to Variant Creutzfeldt-Jakob Disease
Sikorska, B., & Liberski, P. P. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_17 · Cited by 51
AA-Amyloidosis Can Be Transferred by Peripheral Blood Monocytes
Sponarova, J., Nyström, S. N., & Westermark, G. T. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003308 · Cited by 49
Animal models of multiple system atrophy
Fernagut, P., & Tison, F. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.09.044 · Cited by 39
Comparative aspects of volume transmission, with sidelight on other forms of intercellular communication
Nieuwenhuys, R. (2000) · Progress in brain research · doi:10.1016/s0079-6123(00)25006-1 · Cited by 31
Alzheimer's disease under strain
Aguzzi, A. (2014) · Nature · doi:10.1038/512032a · Cited by 31
Neurodegenerative lesions: Seeding and spreading
Duyckaerts, C. J. (2013) · Revue Neurologique · doi:10.1016/j.neurol.2013.07.018 · Cited by 24

Flagged first, then by citations

1 of the 187 references couldn’t be matched to a known paper.

Sorted by citations

Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
Gut microbiota regulate motor deficits and neuroinflammation in a model of Parkinson's disease
Sampson, T. R., Debelius, J. W., Thron, T., Janssen, S., Shastri, G. G., Ilhan, Z. E., Challis, C., Schretter, C. E., Rocha, S., Gradinaru, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.018 · Cited by 3,622
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Non-motor features of Parkinson disease
Schapira, A. H. V., Chaudhuri, K. R., & Jenner, P. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.62 · Cited by 2,053

See all 797

Authors: Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q.
Affiliations: Universität Ulm (DE)
University of Pennsylvania (US)
Corresponding author: Trojanowski, John Q.
ORCID: Tredici, Kelly Del
Lee, Virginia M.-Y.
Trojanowski, John Q.
Venue: Nature Reviews Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2015-01-15
Volume: 16
Issue: 2
Pages: 109-120
ISSN: 1471-003X (ISSN-L)
1471-0048
DOI: 10.1038/nrn3887
PMC: PMC4312418
OpenAlex: W1973319971
Cited by: 790
References: 187
Citations by year: 2026: 40 · 2025: 64 · 2024: 50 · 2023: 54 · 2022: 63 · 2021: 78 · 2020: 79 · 2019: 86 · 2018: 83 · 2017: 88 · 2016: 70 · 2015: 35
FWCI: 11.31
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature reviews. Neuroscience (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Aging (P30AG010124, P01AG017586)
National Institute of Neurological Disorders and Stroke (P50NS053488)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: neurodegenerative diseases, protein aggregation, seeded aggregation, cell-to-cell transmission, neuropathology, positron emission tomography, therapeutic target
MeSH terms: Brain, Humans, Neurons, Disease Progression, Neurodegenerative Diseases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks