Intercellular Spread of Protein Aggregates in Neurodegenerative Disease
Open accessAbstract
Most neurodegenerative diseases are characterized by the accumulation of protein aggregates, some of which are toxic to cells. Mounting evidence demonstrates that in several diseases, protein aggregates can pass from neuron to neuron along connected networks, although the role of this spreading phenomenon in disease pathogenesis is not completely understood. Here we briefly review the molecular and histopathological features of protein aggregation in neurodegenerative disease, we summarize the evidence for release of proteins from donor cells into the extracellular space, and we highlight some other mechanisms by which protein aggregates might be transmitted to recipient cells. We also discuss the evidence that supports a role for spreading of protein aggregates in neurodegenerative disease pathogenesis and some limitations of this model. Finally, we consider potential therapeutic strategies to target spreading of protein aggregates in the treatment of neurodegenerative diseases.
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
Cites
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?
Proteins involved in neurodegenerative diseases may normally be intracellular or extracellular, but all are present in the extracellular space.
“while proteins involved in neurodegenerative diseases may normally be either intracellular or extracellular in nature, all are present in the extracellular space.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [76]
Sampling of CSF and extracellular fluid has documented that amyloid-β, tau, and α-synuclein are present outside the cytosol.
“Sampling of CSF and extracellular fluid have documented that amyloid-ß, tau and a-synuclein are all present outside the cytosol.”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [76]
These proteins lack N-terminal signal sequences, so unconventional mechanisms must be responsible for their release.
“These proteins all lack N-terminal signal sequences, so that unconventional mechanisms must be responsible for their release (76).”
From Glymphatic failure as a final common pathway to dementia (2020) · cites this paper as [76]
One curious feature of the pathology of neurodegenerative diseases is the apparent spread of cellular abnormalities to anatomically connected brain regions.
“While seemingly a cell-intrinsic phenomenon, one of the curious features of the pathology of these diseases is the apparent spread of the cellular abnormalities to anatomically connected brain regions.”
From Asynchronous, contagious and digital aging (2021) · cites this paper as [59]
Cell-to-cell spreading of cellular dysfunction is increasingly recognized in the pathogenesis of neurodegenerative diseases.
“The notion of cell-to-cell spreading of cellular dysfunction is of course not limited to the biology of senescence. This is becoming an increasingly recognized phenomenon in the pathogenesis of neurodegenerative diseases.59”
From Asynchronous, contagious and digital aging (2021) · cites this paper as [59]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Ngolab, J., Trinh, I., Rockenstein, E., Mante, M., Florio, J., Trejo, M., Masliah, D., Adame, A., Masliah, E., & Rissman, R. A. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0445-5 · Cited by 200 · see citing works
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 1× · see citing works
“The initial location of amyloid plaque accumulation in AD does not overlap with the site of early neuron loss, although the pattern of accumulation of neurofibrillary tangle pathology does track more closely with neurodegeneration (Braak & Braak 1991).”
BackgroundStaging 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 · see citing works
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240 · see citing works
Extracellular vesicles: Exosomes, microvesicles, and friends
Raposo, G., & Stoorvogel, W. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211138 · Cited by 8,099 · see citing works
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
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 · see citing works
Iliff, J. J., Wang, M., Liao, Y., Plogg, B. A., Peng, W., Gundersen, G. A., Benveniste, H., Vates, G. E., Deane, R., Goldman, S. A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003748 · Cited by 5,824 · see citing works
Sleep Drives Metabolite Clearance from the Adult Brain
Xie, L., Kang, H., Xu, Q., Chen, M. J., Liao, Y., Thiyagarajan, M., O’Donnell, J., Christensen, D. J., Nicholson, C., Iliff, J. J., et al. (2013) · Science · doi:10.1126/science.1241224 · Cited by 5,411 · see citing works
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · see citing works
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · see citing works
A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409 · see citing works
The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · see citing works
Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works
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 · see citing works
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 · see citing works
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376 · see citing works
Buckner, R. L., Snyder, A. Z., Shannon, B. J., LaRossa, G., Sachs, R., Fotenos, A. F., Sheline, Y. I., Klunk, W. E., Mathis, C. A., Morris, J. C., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2177-05.2005 · Cited by 2,140 · see citing works
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 · see citing works
Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,047 · see citing works
Nanotubular Highways for Intercellular Organelle Transport
Rustom, A., Saffrich, R., Markovic, I., Walther, P., & Gerdes, H.-H. (2004) · Science · doi:10.1126/science.1093133 · Cited by 2,038 · see citing works
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · cited 1× · see citing works
“Failure of lysosomal degradation and autophagy pathways has been implicated in the pathogenesis of synucleinopathies as well, although the precise mechanism of αSyn internalization in neurons also remains unclear (Cuervo et al. 2004).”
BackgroundLi, 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 · see citing works
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 · see citing works
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722 · see citing works
Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories
Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656 · see citing works
Depletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works
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 · see citing works
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424 · see citing works
Self-citationHolmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416 · cited 1× · see citing works
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript status were generally lacking (Holmes et al. 2008), and an early trial, AN1792, was halted due to a serious adverse event of meningoencephalitis in multiple participants (Senior 2002).”
BackgroundAlzheimer’s disease β-amyloid peptides are released in association with exosomes
Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., & Simons, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603838103 · Cited by 1,343 · see citing works
Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265 · see citing works
Self-citationImpairment of Glymphatic Pathway Function Promotes Tau Pathology after Traumatic Brain Injury
Iliff, J. J., Chen, M. J., Plog, B. A., Zeppenfeld, D. M., Soltero, M., Yang, L., Singh, I., Deane, R., & Nedergaard, M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3020-14.2014 · Cited by 1,159 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., & Baekelandt, V. (2015) · Nature · doi:10.1038/nature14547 · Cited by 1,130 · see citing works
Selective neuronal vulnerability in Parkinson disease
Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,121 · see citing works
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 · see citing works
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 1,087 · see citing works
Ash, P. E. A., Bieniek, K. F., Gendron, T. F., Caulfield, T. R., Lin, W.-L., DeJesus‐Hernandez, M., van Blitterswijk, M., Jansen‐West, K. R., Paul, J. W., Rademakers, R., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.004 · Cited by 1,079 · see citing works
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 · see citing works
Sperling, R. A., LaViolette, P. S., O'Keefe, K., O'Brien, J., Rentz, D. M., Pihlajamaki, M., Marshall, G., Hyman, B. T., Selkoe, D. J., Hedden, T., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.07.003 · Cited by 1,027 · see citing works
Huntington disease: natural history, biomarkers and prospects for therapeutics
Ross, C. A., Aylward, E. H., Wild, E. J., Langbehn, D. R., Long, J. D., Warner, J. H., Scahill, R. I., Leavitt, B. R., Stout, J. C., Paulsen, J. S., et al. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.24 · Cited by 1,016 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897 · see citing works
the TBI/CTE group, McKee, A. C., Cairns, N. J., Dickson, D. W., Folkerth, R. D., Dirk Keene, C., Litvan, I., Perl, D. P., Stein, T. D., Vonsattel, J.-P., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1515-z · Cited by 885 · see citing works
Neuronal activity regulates the regional vulnerability to amyloid-β deposition
Bero, A. W., Yan, P., Roh, J. H., Cirrito, J. R., Stewart, F. R., Raichle, M. E., Lee, J.-M., & Holtzman, D. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2801 · Cited by 880 · see citing works
Self-citationLee, 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 · see citing works
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 · see citing works
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 · see citing works
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 852 · see citing works
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 · see citing works
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 798 · see citing works
Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease
Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782 · see citing works
Self-citationWhere 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 · see citing works
Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3
Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T., Yin, X., Xiong, Y., Ge, P., Umanah, G. K. E., Brahmachari, S., Shin, J., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 739 · see citing works
Scherzinger, E., Sittler, A., Schweiger, K., Heiser, V., Lurz, R., Hasenbank, R., Bates, G. P., Lehrach, H. R., & Wanker, E. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4604 · Cited by 707 · see citing works
Tu, P., Galvin, J. E., Baba, M., Giasson, B., Tomita, T., Leight, S., Nakajo, S., Iwatsubo, T., Trojanowski, J. Q., & Lee, V. M. ‐. (1998) · Annals of Neurology · doi:10.1002/ana.410440324 · Cited by 686 · see citing works
Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
Bosco, D. A., Morfini, G. A., Karabacak, M., Song, Y., Gros‐Louis, F., Pasinelli, P., Goolsby, H., Fontaine, B. A., Lemay, N., McKenna-Yasek, D. M., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2660 · Cited by 685 · see citing works
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
Prusiner, S. B., Woerman, A. L., Mordes, D. A., Watts, J. C., Rampersaud, R., Berry, D. B., Patel, S. S., Oehler, A., Lowe, J. K., Kravitz, S. N., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514475112 · Cited by 679 · see citing works
The release and trans-synaptic transmission of Tau via exosomes
Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674 · see citing works
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 · see citing works
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659 · see citing works
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 629 · see citing works
Prions hijack tunnelling nanotubes for intercellular spread
Gousset, K., Schiff, E., Langevin, C., Marijanovic, Z., Caputo, A., Browman, D., Chenouard, N., de Chaumont, F., Martino, A., Enninga, J., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1841 · Cited by 616 · see citing works
Detection of Blast-Related Traumatic Brain Injury in U.S. Military Personnel
Mac Donald, C. L., Johnson, A. M., Cooper, D., Nelson, E. C., Werner, N. J., Shimony, J. S., Snyder, A. Z., Raichle, M. E., Witherow, J. R., Fang, R., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1008069 · Cited by 599 · see citing works
Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works
Self-citationClinical presentation of chronic traumatic encephalopathy
Stern, R. A., Daneshvar, D. H., Baugh, C. M., Seichepine, D. R., Montenigro, P. H., Riley, D. O., Fritts, N. G., Stamm, J. M., Robbins, C. A., McHale, L., et al. (2013) · Neurology · doi:10.1212/wnl.0b013e3182a55f7f · Cited by 564 · see citing works
Verghese, P. B., Castellano, J. M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C., & Holtzman, D. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220484110 · Cited by 556 · see citing works
Self-citationEffects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease
Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542 · see citing works
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 · see citing works
A Method for the Acute and Rapid Degradation of Endogenous Proteins
Clift, D., McEwan, W. A., Labzin, L. I., Konieczny, V., Mogessie, B., James, L. C., & Schuh, M. (2017) · Cell · doi:10.1016/j.cell.2017.10.033 · Cited by 531 · see citing works
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 520 · see citing works
Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A. K., Levina, V., Halloran, M. A., Gleeson, P. A., Blair, I. P., Soo, K. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu068 · Cited by 478 · see citing works
PrionsPreprint
Colby, D. W., & Prusiner, S. B. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006833 · Cited by 469 · see citing works
Biology and Genetics of Prions Causing Neurodegeneration
Prusiner, S. B. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155524 · Cited by 455 · see citing works
Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · see citing works
Antibody against early driver of neurodegeneration cis P-tau blocks brain injury and tauopathy
Kondo, A., Shahpasand, K., Mannix, R., Qiu, J., Moncaster, J., Chen, C.-H., Yao, Y., Lin, Y.-M., Driver, J. A., Sun, Y., et al. (2015) · Nature · doi:10.1038/nature14658 · Cited by 445 · see citing works
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 433 · see citing works
Tunneling-nanotube development in astrocytes depends on p53 activation
Wang, Y., Cui, J., Sun, X., & Zhang, Y. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.147 · Cited by 416 · see citing works
Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes
Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414 · see citing works
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 410 · see citing works
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 407 · see citing works
Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works
Paumier, K. L., Luk, K. C., Manfredsson, F. P., Kanaan, N. M., Lipton, J. W., Collier, T. J., Steece‐Collier, K., Kemp, C. J., Celano, S. L., Schulz, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.06.003 · Cited by 386 · see citing works
Wang, I.-F., Guo, B.-S., Liu, Y.-C., Wu, C.-C., Yang, C.-H., Tsai, K.-J., & Shen, C.-K. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206362109 · Cited by 377 · see citing works
Narasimhan, S., Guo, J. L., Changolkar, L., Stieber, A., McBride, J. D., Silva, L. V., He, Z., Zhang, B., Gathagan, R. J., Trojanowski, J. Q., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1230-17.2017 · Cited by 374 · see citing works
Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371 · see citing works
Exosome secretion is a key pathway for clearance of pathological TDP-43
Iguchi, Y., Eid, L., Parent, M., Soucy, G., Bareil, C., Riku, Y., Kawai, K., Takagi, S., Yoshida, M., Katsuno, M., et al. (2016) · Brain · doi:10.1093/brain/aww237 · Cited by 360 · see citing works
Purified and synthetic Alzheimer’s amyloid beta (Aβ) prions
Stöhr, J., Watts, J. C., Mensinger, Z. L., Oehler, A., Grillo, S. K., DeArmond, S. J., Prusiner, S. B., & Giles, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206555109 · Cited by 359 · see citing works
Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
Masliah, E., Hansen, L., Adame, A., Crews, L. A., Bard, F., Lee, C., Seubert, P. A., Games, D., Kirby, L., & Schenk, D. (2005) · Neurology · doi:10.1212/01.wnl.0000148590.39911.df · Cited by 355 · see citing works
Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351 · see citing works
Self-citationHuman Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339 · see citing works
TDP-43 is intercellularly transmitted across axon terminals
Feiler, M. S., Strobel, B., Freischmidt, A., Helferich, A. M., Kappel, J., Brewer, B. M., Li, D., Thal, D. R., Walther, P., Ludolph, A. C., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201504057 · Cited by 329 · see citing works
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 324 · see citing works
α‐Synuclein pathology does not predict extrapyramidal symptoms or dementia
Parkkinen, L., Kauppinen, T., Pirttilä, T., Autere, J. M., & Alafuzoff, I. I. (2004) · Annals of Neurology · doi:10.1002/ana.20321 · Cited by 315 · see citing works
Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage
Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works
Danzer, K. M., Ruf, W. P., Putcha, P., Joyner, D., Hashimoto, T., Glabe, C. C., Hyman, B. T., & McLean, P. J. (2010) · The FASEB Journal · doi:10.1096/fj.10-164624 · Cited by 309 · see citing works
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 · see citing works
CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease
Sánchez‐Juan, P., Green, A. J. E., Ladogana, A., Cuadrado‐Corrales, N., Sáanchez-Valle, R., Mitrováa, E., Stoeck, K., Sklaviadis, T., Kulczycki, J., Hess, K., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000230159.67128.00 · Cited by 295 · see citing works
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 290 · see citing works
Cognitive differences in dementia patients with autopsy-verified AD, Lewy body pathology, or both
Kraybill, M., Larson, E. B., Tsuang, D. W., Teri, L. L., McCormick, W. C., Bowen, J. D., Kukull, W. A., Leverenz, J. B., & Cherrier, M. M. (2005) · Neurology · doi:10.1212/01.wnl.0000165987.89198.65 · Cited by 286 · see citing works
Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
Bauer, P. O., Goswami, A., Wong, H. K., Okuno, M., Kurosawa, M., Yamada, M., Miyazaki, H., Matsumoto, G., Kino, Y., Nagai, Y., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1608 · Cited by 280 · see citing works
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 278 · see citing works
Immunotherapy Targeting Pathological Tau Prevents Cognitive Decline in a New Tangle Mouse Model
Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4363-10.2010 · Cited by 272 · see citing works
Minakaki, G., Menges, S., Kittel, A., Emmanouilidou, E., Schaeffner, I., Barkovits, K., Bergmann, A., Rockenstein, E., Adame, A., Marxreiter, F., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1395992 · Cited by 272 · see citing works
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 259 · see citing works
Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K. A., Barnham, K. J., Masters, C. L., & Hill, A. F. (2008) · The FASEB Journal · doi:10.1096/fj.07-9357com · Cited by 253 · see citing works
A critical evaluation of current staging of α-synuclein pathology in Lewy body disorders
Jellinger, K. A. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.07.006 · Cited by 229 · see citing works
Mandler, M., Valera, E., Rockenstein, E. M., Weninger, H., Patrick, C., Adame, A., Santic, R., Meindl, S., Vigl, B., Smrzka, O. W., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1256-4 · Cited by 228 · see citing works
Lewis, J. M., & Dickson, D. W. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1507-z · Cited by 221 · see citing works
Biomarkers of Alzheimer's disease
Craig‐Schapiro, R., Fagan, A. M., & Holtzman, D. M. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.10.003 · Cited by 217 · see citing works
Self-citationCell number changes in Alzheimer's disease relate to dementia, not to plaques and tangles
Andrade-Moraes, C. H., de Oliveira-Pinto, A. V., Castro-Fonseca, E., da Silva, C. G., Guimarães, D. M., Szczupak, D., Parente-Bruno, D. R., Carvalho, L. R. B., Polichiso, L., Valério‐Gomes, B., et al. (2013) · Brain · doi:10.1093/brain/awt273 · Cited by 213 · see citing works
Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes
Costanzo, M., Abounit, S., Marzo, L., Danckaert, A., Chamoun, Z., Roux, P., & Zurzolo, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.126086 · Cited by 210 · see citing works
Tunneling nanotubes, an emerging intercellular communication route in development
Gerdes, H., Rustom, A., & Wang, X. (2012) · Mechanisms of Development · doi:10.1016/j.mod.2012.11.006 · Cited by 209 · see citing works
Evolving basic, pathological and clinical concepts in PD
Kalia, L. V., & Lang, A. E. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.249 · Cited by 208 · see citing works
Abounit, S., Wu, J. W., Duff, K., Victoria, G. S., & Zurzolo, C. (2016) · Prion · doi:10.1080/19336896.2016.1223003 · Cited by 206 · see citing works
Gao, L., Tang, H., Nie, K., Wang, L., Zhao, J., Gan, R., Huang, J., Zhu, R., Feng, S., Duan, Z., et al. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2014.961454 · Cited by 204 · see citing works
Fontaine, S. N., Zheng, D., Sabbagh, J. J., Martin, M. D., Chaput, D., Darling, A. L., Trotter, J. H., Stothert, A. R., Nordhues, B. A., Lussier, A. L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593489 · Cited by 203 · see citing works
Cell-to-Cell Transmission of Dipeptide Repeat Proteins Linked to C9orf72-ALS/FTD
Westergard, T., Jensen, B. K., Wen, X., Cai, J., Kropf, E., Iacovitti, L., Pasinelli, P., & Trotti, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.032 · Cited by 202 · see citing works
Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation
McEwan, W. A., Falcon, B., Vaysburd, M., Clift, D., Oblak, A. L., Ghetti, B., Goedert, M., & James, L. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607215114 · Cited by 201 · see citing works
Geser, F., Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01091.x · Cited by 195 · see citing works
Mutant huntingtin is present in neuronal grafts in huntington disease patients
Cicchetti, F., Lacroix, S., Cisbani, G., Vallières, N., Saint‐Pierre, M., St‐Amour, I., Tolouei, R., Skepper, J. N., Hauser, R. A., Mantovani, D., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24174 · Cited by 193 · see citing works
Human-to-mouse prion-like propagation of mutant huntingtin protein
Jeon, I., Cicchetti, F., Cisbani, G., Lee, S., Li, E., Bae, J., Lee, N., Li, L., Im, W., Kim, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1582-9 · Cited by 193 · see citing works
De novo induction of amyloid-β deposition in vivo
Morales, R., Duran-Aniotz, C. A., Castilla, J., Estrada, L. D., & Soto, C. A. (2011) · Molecular Psychiatry · doi:10.1038/mp.2011.120 · Cited by 190 · see citing works
Ding, X., Ma, M., Teng, J., Teng, R. K. F., Zhou, S. Y., Yin, J., Fonkem, E., Huang, J. H., Wu, E., & Wang, X. (2015) · Oncotarget · doi:10.18632/oncotarget.4680 · Cited by 177 · see citing works
Post-translational modification of α-synuclein in Parkinson׳s disease
Barrett, P. J., & Greenamyre, J. T. (2015) · Brain Research · doi:10.1016/j.brainres.2015.06.002 · Cited by 175 · see citing works
(1911) · JAMA · doi:10.1001/jama.1911.02560030051032 · Cited by 175 · see citing works
Extracellular Tau Levels Are Influenced by Variability in Tau That Is Associated with Tauopathies
Karch, C. M. M., Jeng, A. T., & Goate, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380642 · Cited by 171 · see citing works
Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies
Peng, C., Gathagan, R. J., & Lee, V. M. ‐. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.07.018 · Cited by 164 · see citing works
Assessment of α-Synuclein Secretion in Mouse and Human Brain Parenchyma
Emmanouilidou, E., Elenis, D., Papasilekas, T., Stranjalis, G., Gerozissis, K., Ioannou, P. C., & Vekrellis, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022225 · Cited by 163 · see citing works
Smith, A. J., & Verkman, A. S. (2017) · The FASEB Journal · doi:10.1096/fj.201700999 · Cited by 160 · see citing works
Bi, M., Ittner, A., Ke, Y. D., Götz, J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026860 · Cited by 153 · see citing works
Vulnerability of Select Neuronal Types to Alzheimer's Disease
BRAAK, H., DEL TREDICI, K., SCHULTZ, C., & BRAAK, E. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05560.x · Cited by 150 · see citing works
Ayers, J. I., Fromholt, S., O’Neal, V., Diamond, J., & Borchelt, D. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1514-0 · Cited by 149 · see citing works
Neuronal spread of scrapie agent and targeting of lesions within the retino-tectal pathway
Fraser, H. (1982) · Nature · doi:10.1038/295149a0 · Cited by 147 · see citing works
West, T., Hu, Y., Verghese, P. B., Bateman, R. J., Braunstein, J. B., Fogelman, I., Budur, K., Florian, H., Mendonca, N., & Holtzman, D. M. (2017) · PubMed · doi:10.14283/jpad.2017.36 · Cited by 132 · see citing works
Self-citationExperimental transmissibility of mutant SOD1 motor neuron disease
Ayers, J. I., Fromholt, S., Koch, M., DeBosier, A., McMahon, B., Xu, G. M., & Borchelt, D. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1342-7 · Cited by 123 · see citing works
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 121 · see citing works
Tau as a Biomarker of Neurodegenerative Diseases
Schraen‐Maschke, S., Sergeant, N., Dhaenens, C., Bombois, S., Deramecourt, V., Caillet‐Boudin, M., Pasquier, F., Maurage, C., Sablonnière, B., Vanmechelen, E., et al. (2008) · Biomarkers in Medicine · doi:10.2217/17520363.2.4.363 · Cited by 121 · see citing works
Parkinson disease and incidental Lewy body disease
Iacono, D., Geraci-Erck, M., Rabin, M., Adler, C. H., Serrano, G. E., Beach, T. G., & Kurlan, R. (2015) · Neurology · doi:10.1212/wnl.0000000000002102 · Cited by 116 · see citing works
Brotherton, T. E., Li, Y., Cooper, D., Gearing, M., Julien, J., Rothstein, J. D., Boylan, K., & Glass, J. D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115009109 · Cited by 114 · see citing works
Delenclos, M., Trendafilova, T., Mahesh, D., Baine, A.-M. T., Moussaud, S., Yan, I. K., Patel, T. C., & McLean, P. J. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00172 · Cited by 114 · see citing works
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705091114 · Cited by 114 · see citing works
Kanaan, N. M., Cox, K. K., Alvarez, V. E., Stein, T. D., Poncil, S., & McKee, A. C. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlv001 · Cited by 108 · see citing works
Misfolded SOD1 is not a primary component of sporadic ALS
Cruz, S. D., Bui, A., Saberi, S., Lee, S. K., Stauffer, J. E., McAlonis‐Downes, M., Schulte, D. J., Pizzo, D. P., Parone, P. A., Cleveland, D. W., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1688-8 · Cited by 106 · see citing works
Astrocytic inclusions in progressive supranuclear palsy and corticobasal degeneration
Yoshida, M. (2014) · Neuropathology · doi:10.1111/neup.12143 · Cited by 100 · see citing works
Astrocyte-to-neuron intercellular prion transfer is mediated by cell-cell contact
Victoria, G. S., Arkhipenko, A., Zhu, S., Syan, S., & Zurzolo, C. (2016) · Scientific Reports · doi:10.1038/srep20762 · Cited by 94 · see citing works
Pokrishevsky, E., Grad, L. I., & Cashman, N. R. (2016) · Scientific Reports · doi:10.1038/srep22155 · Cited by 92 · see citing works
Prion aggregates transfer through tunneling nanotubes in endocytic vesicles
Zhu, S., Victoria, G. S., Marzo, L., Ghosh, R., & Zurzolo, C. (2015) · Prion · doi:10.1080/19336896.2015.1025189 · Cited by 89 · see citing works
Immunotherapy in Parkinson’s Disease: Micromanaging Alpha-Synuclein Aggregation
George, S., & Brundin, P. (2015) · Journal of Parkinson s Disease · doi:10.3233/jpd-150630 · Cited by 89 · see citing works
Liu, H., Sanelli, T. R., Horne, P., Pioro, E. P., Strong, M. J., Rogaeva, E. A., Bilbao, J. M., Zinman, L. H., & Robertson, J. (2009) · Annals of Neurology · doi:10.1002/ana.21704 · Cited by 88 · see citing works
Dosing in phase II trial of Alzheimer's vaccine suspended
Senior, K. (2002) · The Lancet Neurology · doi:10.1016/s1474-4422(02)00023-6 · Cited by 88 · see citing works
The Prion-Like Properties of Amyloid-β Assemblies: Implications for Alzheimer's DiseasePreprint
Walker, L. C., Schelle, J., & Jucker, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024398 · Cited by 88 · see citing works
Brody, D. L., Jiang, H., Wildburger, N. C., & Esparza, T. J. (2017) · Alzheimer s Research & Therapy · doi:10.1186/s13195-017-0293-3 · Cited by 84 · see citing works
Steele, J., Ju, S., Lachenmayer, M. L., Liken, J., Stock, A., Kim, S. Y., Delgado, L. M., Alfaro, I. E., Bernales, S., Verdile, G., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.115 · Cited by 77 · see citing works
Huber, B. R., Meabon, J. S., Hoffer, Z. S., Zhang, J., Hoekstra, J. G., Pagulayan, K. F., McMillan, P. J., Mayer, C. L., Banks, W. A., Kraemer, B. C., et al. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.01.022 · Cited by 76 · see citing works
GABA transmission via ATP-dependent K + channels regulates α-synuclein secretion in mouse striatum
Emmanouilidou, E., Minakaki, G., Keramioti, M. V., Xylaki, M., Balafas, E., Chrysanthou‐Piterou, M., Kloukina, I., & Vekrellis, K. (2016) · Brain · doi:10.1093/brain/awv403 · Cited by 76 · see citing works
SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation
Zeineddine, R., Pundavela, J., Corcoran, L., Stewart, E. M., Do‐Ha, D., Bax, M., Guillemin, G. J., Vine, K. L., Hatters, D. M., Ecroyd, H. W., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0053-4 · Cited by 75 · see citing works
Kim, J., Kim, T.-Y., Cho, K.-S., Kim, H., & Koh, J. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.07.011 · Cited by 74 · see citing works
Asymmetry of post-mortem neuropathology in behavioural-variant frontotemporal dementia
Irwin, D. J., McMillan, C. T., Xie, S. X., Rascovsky, K., Deerlin, V. M. V., Coslett, H. B., Hamilton, R. H., Aguirre, G. K., Lee, E. B., Lee, V. M. ‐., et al. (2017) · Brain · doi:10.1093/brain/awx319 · Cited by 74 · see citing works
Long-Distance Calls Between Cells Connected by Tunneling Nanotubules
Önfelt, B., Purbhoo, M. A., Nedvetzki, S., Sowinski, S., & Davis, D. M. (2005) · Science s STKE · doi:10.1126/stke.3132005pe55 · Cited by 56 · see citing works
Grad, L. I., Pokrishevsky, E., Silverman, J. M., & Cashman, N. R. (2014) · Prion · doi:10.4161/19336896.2014.983398 · Cited by 55 · see citing works
Ciura, S., Sellier, C., Campanari, M., Charlet‐Berguerand, N., & Kabashi, E. (2016) · Autophagy · doi:10.1080/15548627.2016.1189070 · Cited by 51 · see citing works
Antibody Therapeutics Targeting Aβ and TauPreprint
Gallardo, G., & Holtzman, D. M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024331 · Cited by 51 · see citing works
Self-citationPokrishevsky, E., Hong, R. H., Mackenzie, I. R., & Cashman, N. R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184384 · Cited by 42 · see citing works
Rangel, A., Race, B., Phillips, K. L., Striebel, J. F., Kurtz, N., & Chesebro, B. W. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-8 · Cited by 39 · see citing works
Chronic Traumatic Encephalopathy: Is Latency in Symptom Onset Explained by Tau Propagation?Preprint
Kriegel, J., Papadopoulos, Z., & McKee, A. C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024059 · Cited by 36 · see citing works
Evidence for sortilin modulating regional accumulation of human tau prions in transgenic mice
Johnson, N. R., Condello, C., Guan, S., Oehler, A., Becker, J., Gavidia, M., Carlson, G. A., Giles, K., & Prusiner, S. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717193114 · Cited by 26 · see citing works
Embryonic Mutant Huntingtin Aggregate Formation in Mouse Models of Huntington’s Disease
Osmand, A. P., Bichell, T. J., Bowman, A. B., & Bates, G. P. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160217 · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 · see citing works
Exercise sustains the hallmarks of health
Qiu, Y., Fernández-García, B., Lehmann, H. I., Li, G., Kroemer, G., López-Otín, C., & Xiao, J. (2023) · Journal of Sport and Health Science · doi:10.1016/j.jshs.2022.10.003 · Cited by 270 · see citing works
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Willbold, D., Strodel, B., Schroeder, G. F., Hoyer, W., & Heise, H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00196 · Cited by 222 · see citing works
Dural lymphatics regulate clearance of extracellular tau from the CNS
Patel, T. K., Habimana-Griffin, L., Gao, X., Xu, B. J., Achilefu, S., Alitalo, K. K., McKee, C. A., Sheehan, P. W., Musiek, E. S., Xiong, C., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0312-x · Cited by 215 · see citing works
Self-citationConformational strains of pathogenic amyloid proteins in neurodegenerative diseases
Li, D., & Liu, C. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00603-7 · Cited by 122 · see citing works
A growth-factor-activated lysosomal K+ channel regulates Parkinson’s pathology
Wie, J., Liu, Z., Song, H., Tropea, T. F., Yang, L., Wang, H., Liang, Y., Cang, C., Aranda, K., Lohmann, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03185-z · Cited by 120 · see citing works
Asynchronous, contagious and digital aging
Rando, T. A., & Wyss-Coray, T. (2021) · Nature Aging · doi:10.1038/s43587-020-00015-1 · Cited by 121 · see citing works
Contribution of astrocytes to neuropathology of neurodegenerative diseases
Acıoğlu, Ç., Li, L., & Elkabes, S. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147291 · Cited by 115 · see citing works
The prion-like spreading of α-synuclein: From in vitro to in vivo models of Parkinson’s disease
Vargas, J., Grudina, C., & Zurzolo, C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.01.012 · Cited by 106 · see citing works
TIA1 regulates the generation and response to toxic tau oligomers
Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 99 · see citing works
Cell models for Alzheimer’s and Parkinson’s disease: At the interface of biology and drug discovery
Cetin, S., Knez, D., Gobec, S., Kos, J., & Pišlar, A. H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112924 · Cited by 87 · see citing works
Diverse CMT2 neuropathies are linked to aberrant G3BP interactions in stress granules
Cui, Q., Bi, H., Lv, Z., Wu, Q., Hua, J., Gu, B., Huo, C., Tang, M., Chen, Y., Chen, C., et al. (2023) · Cell · doi:10.1016/j.cell.2022.12.046 · Cited by 84 · see citing works
Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration
Nakamura, T., Oh, C.-K., Zhang, X., & Lipton, S. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.002 · Cited by 82 · see citing works
Friend or foe: The role of stress granule in neurodegenerative disease
Cui, Q., Liu, Z., & Bai, G. (2024) · Neuron · doi:10.1016/j.neuron.2024.04.025 · Cited by 82 · see citing works
Zhang, J., & Wang, R. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111180 · Cited by 77 · see citing works
Insights into the Functions of LncRNAs in Drosophila
Li, K., Tian, Y., Yuan, Y., Fan, X., Yang, M., He, Z., & Yang, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184646 · Cited by 74 · see citing works
Fornari, S., Schäfer, A., Ellen Kuhl, A., & Goriely, A. (2019) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2019.110102 · Cited by 57 · see citing works
Castro, M. F. G., Miculán, E., Herrera, M. G., Ruera, C. N., Perez, F., Prieto, E. D., Barrera, E., Pantano, S., Carasi, P., & Chirdo, F. G. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00031 · Cited by 57 · see citing works
Development of New Strategies Using Extracellular Vesicles Loaded with Exogenous Nucleic Acid
Orefice, N. S. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12080705 · Cited by 56 · see citing works
Ha, N., Choi, Y. I., Jung, N., Song, J. Y., Bae, D. K., Kim, M. C., Lee, Y. J., Song, H., Kwak, G., Jeong, S., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15231 · Cited by 55 · see citing works
“Repair Me if You Can”: Membrane Damage, Response, and Control from the Viral Perspective
Daussy, C. F., & Wodrich, H. (2020) · Cells · doi:10.3390/cells9092042 · Cited by 52 · see citing works
Jellinger, K. A. (2019) · Journal of Neural Transmission · doi:10.1007/s00702-019-02028-6 · Cited by 55 · see citing works
Relevance of Autophagy and Mitophagy Dynamics and Markers in Neurodegenerative Diseases
Giorgi, C., Bouhamida, E., Danese, A., Previati, M., Pinton, P., & Patergnani, S. (2021) · Biomedicines · doi:10.3390/biomedicines9020149 · Cited by 50 · see citing works
The age pigment lipofuscin causes oxidative stress, lysosomal dysfunction, and pyroptotic cell death
Baldensperger, T., Jung, T., Heinze, T., Schwerdtle, T., Höhn, A., & Grune, T. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.10.311 · Cited by 51 · see citing works
Chen, S., Nazeri, A., Baek, H., Ye, D., Yang, Y., Yuan, J., Rubin, J. B., & Chen, H. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x211046129 · Cited by 50 · see citing works
Cooper, J. F., Guasp, R. J., Arnold, M. L., Grant, B. D., & Driscoll, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101410118 · Cited by 49 · see citing works
Sen, T., & Thummer, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00564-w · Cited by 50 · see citing works
Neuron‐glia interactions: Molecular basis of alzheimer’s disease and applications of neuroproteomics
Ibrahim, A. M., Pottoo, F. H., Dahiya, E. S., Khan, F. A., & Kumar, J. B. S. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14838 · Cited by 45 · see citing works
Selective Neuronal Death in Neurodegenerative Diseases: The Ongoing Mystery.
Subramaniam, S. (2019) · Europe PMC (PubMed Central) · Cited by 40 · see citing works
Connecting the Dots: Macromolecular Crowding and Protein Aggregation
Siddiqui, G. A., & Naeem, A. (2022) · Journal of Fluorescence · doi:10.1007/s10895-022-03082-2 · Cited by 39 · see citing works
Hearing Loss in Neurological Disorders
Li, S., Cheng, C., Lü, L., Ma, X., Zhang, X., Li, A., Chen, J., Qian, X., & Gao, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.716300 · Cited by 39 · see citing works
Wang, Y., Arnold, M. L., Smart, A. J., Wang, G., Androwski, R. J., Morera, A., Nguyen, K. C. Q., Schweinsberg, P. J., Bai, G., Cooper, J. F., et al. (2023) · eLife · doi:10.7554/elife.82227 · Cited by 34 · see citing works
Donnelly, K. M., DeLorenzo, O. R., Zaya, A., Pisano, G. E., Thu, W. M., Luo, L., Kopito, R. R., & Pearce, M. M. P. (2020) · eLife · doi:10.7554/elife.58499 · Cited by 37 · see citing works
Serum Uric Acid Levels and Non-Motor Symptoms in Parkinson’s Disease
van Wamelen, D. J., Taddei, R. N., Calvano, A., Titova, N., Leta, V., Shtuchny, I. V., Jenner, P. G., Martínez‐Martín, P., Катунина, Е. А., & Chaudhuri, К. R. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-201988 · Cited by 35 · see citing works
Axonal mRNA translation in neurological disorders
Lin, J. Q., van Tartwijk, F. W., & Holt, C. E. (2020) · RNA Biology · doi:10.1080/15476286.2020.1822638 · Cited by 33 · see citing works
Rhes protein transits from neuron to neuron and facilitates mutant huntingtin spreading in the brain
Ramírez-Jarquín, U. N., Sharma, M., Shahani, N., Li, Y., Boregowda, S. V., & Subramaniam, S. (2022) · Science Advances · doi:10.1126/sciadv.abm3877 · Cited by 32 · see citing works
Mullane, K., & Williams, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.027 · Cited by 32 · see citing works
Pharmacological Tools to Modulate Autophagy in Neurodegenerative Diseases
Suresh, S., Chakravorty, A., Giridharan, M., Garimella, L., & Manjithaya, R. R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.023 · Cited by 32 · see citing works
Balasubramaniam, M., Ayyadevara, S., Ganne, A., Kakraba, S., Penthala, N. R., Du, X., Crooks, P. A., Griffin, S. T., & Reis, R. J. S. (2019) · iScience · doi:10.1016/j.isci.2019.09.026 · Cited by 31 · see citing works
Hernández, E. R., Sánchez-Maldonado, C., Chávez, M. Á. M., Hernández-Zimbrón, L. F., Patricio-Martínez, A., Zenteno, E., & Limón, I. D. (2020) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2020.1750955 · Cited by 31 · see citing works
Maszka, P., Kwaśniak-Butowska, M., Cysewski, D., Sławek, J. W., Smolenski, R. T., & Tomczyk, M. (2023) · Metabolites · doi:10.3390/metabo13030369 · Cited by 30 · see citing works
Neuronal Glial Crosstalk: Specific and Shared Mechanisms in Alzheimer’s Disease
Chavda, V. K., Singh, K., Patel, V., Mishra, M., & Mishra, A. K. (2022) · Brain Sciences · doi:10.3390/brainsci12010075 · Cited by 29 · see citing works
Rajendran, R., Raghavan, R. P., Al-Sehemi, A. G., Uddin, M. S., Aleya, L., & Mathew, B. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-17931-3 · Cited by 29 · see citing works
Arnold, M. L., Cooper, J. F., Androwski, R. J., Ardeshna, S., Melentijevic, I., Smart, A. J., Guasp, R. J., Nguyen, K. C. Q., Bai, G., Hall, D. H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39700-1 · Cited by 29 · see citing works
Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases
Gracia, L., Lora, G., Blair, L. J., & Jinwal, U. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01263 · Cited by 28 · see citing works
Lysosomal peptidases—intriguing roles in cancer progression and neurodegeneration
Kos, J., Mitrović, A., Nanut, M. P., & Pišlar, A. H. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13372 · Cited by 28 · see citing works
Arnold, M. L., Cooper, J. F., Grant, B. D., & Driscoll, M. (2020) · Journal of Visualized Experiments · doi:10.3791/61368 · Cited by 22 · see citing works
High Altitude Cerebral Edema: Improving Treatment Options
Zelmanovich, R., Pierre, K., Felisma, P., Cole, D., Goldman, M., & Lucke-Wold, B. P. (2022) · Biologics · doi:10.3390/biologics2010007 · Cited by 26 · see citing works
Tau accumulation in degradative organelles is associated to lysosomal stress
Piovesana, E., Magrin, C., Ciccaldo, M., Sola, M., Bellotto, M., Molinari, M., Papin, S., & Paganetti, P. (2023) · Scientific Reports · doi:10.1038/s41598-023-44979-7 · Cited by 26 · see citing works
Clusterin is a Potential Therapeutic Target in Alzheimer’s Disease
Palihati, N., Tang, Y., Yin, Y., Yu, D., Liu, G., Quan, Z., Ni, J., Yan, Y., & Qing, H. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03801-1 · Cited by 25 · see citing works
Ageing promotes microglial accumulation of slow-degrading synaptic proteins
Guldner, I. H., Wagner, V., Losada, P. M., Shi, S. M., Golub, S. W., Hevler, J. F., Chen, K. S., Meese, B. T., Ghoochani, A., Pulido, E. H., et al. (2026) · Nature · doi:10.1038/s41586-025-09987-9 · Cited by 25 · see citing works
[Retracted] Glymphatic System: Emerging Therapeutic Target for Neurological Diseases
Xuan, X., Zhou, G., Chen, C., Shao, A., Zhou, Y., Li, X., & Zhou, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6189170 · Cited by 24 · see citing works
RetractedJiang, L., Zhang, X.-L., & Hu, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212380 · Cited by 24 · see citing works
Longitudinal imaging highlights preferential basal ganglia circuit atrophy in Huntington’s disease
Liu, C.-F., Laurent Younes, B., Tong, X. J., Hinkle, J. T., Wang, M., Phatak, S., Xu, X., Bu, X., Looi, V., Bang, J., et al. (2023) · Brain Communications · doi:10.1093/braincomms/fcad214 · Cited by 23 · see citing works
Watabe, K., Niida‐Kawaguchi, M., Tada, M., Kato, Y., Murata, M., Tanji, K., Wakabayashi, K., Yamada, M., Kakita, A., & Shibata, N. (2022) · Neuropathology · doi:10.1111/neup.12840 · Cited by 21 · see citing works
Dhakal, S., Robang, A. S., Bhatt, N. N., Puangmalai, N., Fung, L., Kayed, R., Paravastu, A. K., & Rangachari, V. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102498 · Cited by 23 · see citing works
Chen, Z. S., & Chan, H. Y. E. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.251193 · Cited by 22 · see citing works
Silva-Pilipich, N., Smerdou, C., & Vanrell, L. (2021) · Microorganisms · doi:10.3390/microorganisms9091956 · Cited by 21 · see citing works
Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases
Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 22 · see citing works
Multiple system atrophy - a clinicopathological update
Jellinger, K. A. (2020) · Free Neuropathology · doi:10.17879/freeneuropathology-2020-2813 · Cited by 20 · see citing works
Vahed, M., Sweeney, A., Shirasawa, H., & Vahed, M. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107128 · Cited by 19 · see citing works
The Involvement of RAGE and Its Ligands during Progression of ALS in SOD1 G93A Transgenic Mice
Nowicka, N., Szymanska, K., Juranek, J. K., Zglejc‐Waszak, K., Korytko, A., Załęcki, M., Chmielewska‐Krzesińska, M., Wa̧sowicz, K., & Wojtkiewicz, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042184 · Cited by 18 · see citing works
He, C., Tang, Y., Chen, X., Long, T., He, Y.-N., Wei, J., Wu, J., Lan, C., Yu, L., Huang, F., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154548 · Cited by 17 · see citing works
Therapeutic innovation in Parkinson’s disease: a 2020 update on disease-modifying approaches
Colombo, D., Pnevmatikou, P., Melloni, E., & Keywood, C. (2020) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2020.1800454 · Cited by 17 · see citing works
Current Understanding of Protein Aggregation in Neurodegenerative Diseases
Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 18 · see citing works
A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization
Azimi, F. C., Dean, T. T., Minari, K., Basso, L. G. M., Vance, T. D. R., & Serrão, V. H. B. (2023) · Biomolecules · doi:10.3390/biom13071130 · Cited by 16 · see citing works
Subach, O. M., Barykina, N. V., Chefanova, E. S., Vlaskina, A. V., Sotskov, V. P., Ivashkina, O. I., Anokhin, K. V., & Subach, F. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010111 · Cited by 15 · see citing works
Bendifallah, M., Redeker, V., Monsellier, É., Bousset, L., Bellande, T., & Melki, R. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.04.091 · Cited by 15 · see citing works
A new fibrillization mechanism of β-lactoglobulin in glycine solutions
Jaklin, M., Hritz, J., & Hribar-Lee, B. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.06.182 · Cited by 14 · see citing works
Upadhyay, A., Sundaria, N., Dhiman, R., Prajapati, V. K., Prasad, A., & Mishra, A. (2021) · The Neuroscientist · doi:10.1177/1073858421989582 · Cited by 12 · see citing works
Axonal mRNA localization and local translation in neurodegenerative disease
Li, H., Wang, Y., Zhang, Y., Shen, M., Li, H.-Y., Yu, Z., & Chen, G. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.308074 · Cited by 12 · see citing works
Transdiagnostic prevention in youth mental health, Part I: rationale, shared risk factors
Holt, D. J., Choi, K. W., DeTore, N. R., & Balogun‐Mwangi, O. (2025) · Neuropsychopharmacology · doi:10.1038/s41386-025-02233-w · Cited by 11 · see citing works
Lei, T., Xiao, Z., Bi, W., Cai, S., Yang, Y., & Du, H. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101769 · Cited by 11 · see citing works
Conserved components of the macroautophagy machinery in Caenorhabditis elegans
Zhang, H., & Meléndez, A. (2025) · Genetics · doi:10.1093/genetics/iyaf007 · Cited by 10 · see citing works
Neurodegeneration as Ecosystem Failure: A New Paradigm for Prevention and Treatment
Velikic, G. S., Šupić, G., Marić, D., Puletić, M., Kos, M. O., Vojvodić, D., & Maric, D. M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211207 · Cited by 10 · see citing works
Consequence of Dementia and Cognitive Impairment by Primary Nucleation Pathway
Singh, A., Ansari, V. A., Ansari, T. M., Hasan, S. M., Ahsan, F., Singh, K., Wasim, R., Maheshwari, S., & Ahmad, A. (2023) · Hormone and Metabolic Research · doi:10.1055/a-2052-8462 · Cited by 10 · see citing works
Decoding the Cellular Trafficking of Prion-like Proteins in Neurodegenerative Diseases
Hu, C., Yan, Y., Jin, Y., Yang, J. H., Xi, Y., & Zhong, Z. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01115-9 · Cited by 11 · see citing works
Is pseudoexfoliation glaucoma a neurodegenerative disorder?
Padhy, B., & Alone, D. P. (2021) · Journal of Biosciences · doi:10.1007/s12038-021-00217-8 · Cited by 9 · see citing works
Control Intracellular Protein Condensates with Light
Li, M., Huang, W., Duan, L., & Sun, F. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00305 · Cited by 8 · see citing works
The Molecular Architecture of Neurodegeneration: An Integrative Overview of Convergent Mechanisms
Aranda-Abreu, G. E., Rojas-Durán, F., Hernández‐Aguilar, M. E., Herrera‐Covarrubias, D., Tlapa-Monge, L. R., & Mestizo-Gutiérrez, S. L. (2026) · NeuroSci · doi:10.3390/neurosci7010007 · Cited by 9 · see citing works
CCDC50 mediates the clearance of protein aggregates to prevent cellular proteotoxicity
Ye, Y., Jia, P., Miao, J., Wang, Y., Li, Z., Lin, Y., He, M., Liu, S., Zheng, B., Wu, J., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2367183 · Cited by 7 · see citing works
Ma, P., Zhang, R., Xu, L., Liu, H., & Xiao, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.791288 · Cited by 7 · see citing works
The Search for a Universal Treatment for Defined and Mixed Pathology Neurodegenerative Diseases
O’Day, D. H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413424 · Cited by 6 · see citing works
A Drosophila model for mechanistic investigation of tau protein spread
Bankapalli, K., Thomas, R. E., Vincow, E. S., Milstein, G., Fisher, L. V., & Pallanck, L. J. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050858 · Cited by 6 · see citing works
Chen, X., & Zhang, M. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.1027 · Cited by 6 · see citing works
Polyoxometalates’ Progress for the Treatment of Alzheimer’s Disease
Aureliano, M., Mateus, J., & Rijo, D. M. (2025) · The biochemist · doi:10.3390/biochem5040041 · Cited by 7 · see citing works
Sternberg, Z. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03684-2 · Cited by 6 · see citing works
Wang, G., Guasp, R. J., Salam, S., Chuang, E., Morera, A., Smart, A. J., Jimenez, D., Shekhar, S., Friedman, E., Melentijevic, I., et al. (2024) · eLife · doi:10.7554/elife.95443.3 · Cited by 5 · see citing works
Jellinger, K. A. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1638908 · Cited by 5 · see citing works
Insolubilome profiling defines molecular features that influence protein insolubility with aging
Stephan, A., Graça, F. A., Pagala, V., Hunt, L. C., Chuang, C.-L., Grime, J., Alford, D., Wang, X., High, A. A., Peng, J., et al. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.01.015 · Cited by 4 · see citing works
COVID-19: Energy, Protein Folding & Prion Disease
Thorp, K. E., Thorp, J. A., Thorp, E. M., BS, F. W., Thorp, M. M., JD MACP. Law Firm of Margery M. Thorp, P., Walker, P. R., & BSME, M. (2022) · The Gazette of Medical Sciences · doi:10.46766/thegms.neuro.22083101 · Cited by 4 · see citing works
Sengupta, P., & Mukhopadhyay, D. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.97002 · Cited by 4 · see citing works
Role of Antioxidant Vitamins in Neurogenesis
Roy‐Chowdhury, S., Bhavsar, D., Singh, J., & Mardon, A. A. (2021) · Journal of Undergraduate Life Sciences · doi:10.33137/juls.v15i1.37312 · Cited by 4 · see citing works
Wang, G., Guasp, R. J., Salam, S., Chuang, E., Morera, A., Smart, A. J., Jimenez, D., Shekhar, S., Friedman, E., Melentijevic, I., et al. (2024) · eLife · doi:10.7554/elife.95443 · Cited by 4 · see citing works
Decoding stress granules dynamics: Implications for neurodegenerative disease
Wang, Z., Yang, C., Wang, X., Liu, X., Liu, H., Liu, X., Liu, H., Zhang, L., Shen, H., Zhang, L., et al. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102758 · Cited by 3 · see citing works
Aberrant TDP‐43 phosphorylation: a key wind gap from TDP‐43 to TDP‐43 proteinopathy
Huang, Z., Ba, Z., Huang, N., Li, Y., & Luo, Y. (2021) · Ibrain · doi:10.1002/j.2769-2795.2021.tb00074.x · Cited by 4 · see citing works
Sharbafshaaer, M., Pepe, R., Notariale, R., Canale, F., Tessitore, A., Tedeschi, G., & Trojsi, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157644 · Cited by 3 · see citing works
Zhan, A., Zhong, K., & Zhang, K. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151582 · Cited by 2 · see citing works
A Perspective on Studies of Phage DNA Packaging Dynamics
Serwer, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147854 · Cited by 2 · see citing works
Computational design of rasagiline derivatives: Searching for enhanced antioxidant capability
Reina, M., Guzmán‐López, E. G., & Galano, A. (2022) · International Journal of Quantum Chemistry · doi:10.1002/qua.27011 · Cited by 2 · see citing works
- Authors
- Davis, A. A., Leyns, C. E. G., & Holtzman, D. M.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2018-10-06
- Volume
- 34
- Issue
- 1
- Pages
- 545-568
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- PMC
- PMC6350082
- OpenAlex
- W2883506729
- Cited by
- 131
- References
- 174
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 14 · 2023: 16 · 2022: 24 · 2021: 20 · 2020: 20 · 2019: 13 · 2018: 2
- FWCI
- 1.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (K08NS101118)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- protein aggregates, neurodegenerative diseases, intercellular spread, prion-like propagation, extracellular protein release, treatment options, neurodegeneration
- MeSH terms
- Chronic Traumatic Encephalopathy, Alzheimer Disease, Amyotrophic Lateral Sclerosis, Humans, Huntington Disease, Neurons, Parkinson Disease, Prion Diseases, Neurodegenerative Diseases, Frontotemporal Dementia, Protein Aggregation, Pathological, Protein Aggregates
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
