The DOI matches its Crossref record; 111 of the 111 references it cites were found in a registry or an index; none of the 24 sources its claims cite is checked for support yet.
Pathogenic protein seeding in alzheimer disease and other neurodegenerative disorders
Open accessAbstract
The misfolding and aggregation of specific proteins is a seminal occurrence in a remarkable variety of neurodegenerative disorders. In Alzheimer disease (the most prevalent cerebral proteopathy), the two principal aggregating proteins are β‐amyloid (Aβ) and tau. The abnormal assemblies formed by conformational variants of these proteins range in size from small oligomers to the characteristic lesions that are visible by optical microscopy, such as senile plaques and neurofibrillary tangles. Pathologic similarities with prion disease suggest that the formation and spread of these proteinaceous lesions might involve a common molecular mechanism—corruptive protein templating. Experimentally, cerebral β‐amyloidosis can be exogenously induced by exposure to dilute brain extracts containing aggregated Aβ seeds. The amyloid‐inducing agent probably is Aβ itself, in a conformation generated most effectively in the living brain. Once initiated, Aβ lesions proliferate within and among brain regions. The induction process is governed by the structural and biochemical nature of the Aβ seed, as well as the attributes of the host, reminiscent of pathogenically variant prion strains. The concept of prionlike induction and spreading of pathogenic proteins recently has been expanded to include aggregates of tau, α‐synuclein, huntingtin, superoxide dismutase‐1, and TDP‐43, which characterize such human neurodegenerative disorders as frontotemporal lobar degeneration, Parkinson/Lewy body disease, Huntington disease, and amyotrophic lateral sclerosis. Our recent finding that the most effective Aβ seeds are small and soluble intensifies the search in bodily fluids for misfolded protein seeds that are upstream in the proteopathic cascade, and thus could serve as predictive diagnostics and the targets of early, mechanism‐based interventions. Establishing the clinical implications of corruptive protein templating will require further mechanistic and epidemiologic investigations. However, the theory that many chronic neurodegenerative diseases can originate and progress via the seeded corruption of misfolded proteins has the potential to unify experimental and translational approaches to these increasingly prevalent disorders. Ann Neurol 2011;70:532–540
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
This review argues that many neurodegenerative proteopathies, including Alzheimer’s disease, progress by prion-like corruptive protein templating, in which misfolded protein seeds induce and spread aggregation of Aβ, tau, α-synuclein, and other proteins. It synthesizes experimental seeding evidence and discusses implications for biomarkers, therapeutics, and possible iatrogenic transmission, while noting that clinical implications remain uncertain.
Key findings
- In Alzheimer’s disease, Aβ aggregation is implicated as an early trigger; cerebral Aβ deposition precedes clinical symptoms by a decade or more, and tauopathy correlates strongly with cognitive decline. Oligomeric Aβ, ranging from dimers to dodecamers or larger, may be more deleterious than histologically obvious plaques and cerebral amyloid angiopathy.
- Cerebral β-amyloidosis can be experimentally induced in APP-transgenic mice by intracerebral infusion of brain extracts containing minute amounts of aggregated Aβ. Evidence includes that seeding requires aggregated human-sequence Aβ, is impeded by anti-Aβ immunodepletion, is ineffective in non-transgenic mice, mirrors the donor deposit phenotype, and is abrogated by formic acid denaturation.
- The most potent Aβ seeds appear to be small and soluble, including proteinase K-sensitive species in the 100,000×g soluble fraction; sonication enhances seeding. In contrast, aggregated synthetic Aβ has not significantly induced cerebral Aβ deposition in APP-transgenic mice.
- Tau tangles can be exogenously induced by brain extract containing abnormal tau filaments in Alz17 mice, with time- and region-dependent spread; prion-like propagation has also been implicated for α-synuclein, SOD1, TDP-43, and polyglutamine aggregates. Human prion disease transmission has occurred in fewer than 700 known cases.
Methods
- Narrative review; no new primary data are reported. It synthesizes human neuropathology, genetics, imaging, and transgenic mouse/cell-culture seeding experiments.
- The main analysis is a conceptual synthesis of evidence for corruptive protein templating across Alzheimer’s disease, prion disease, tauopathies, synucleinopathies, amyotrophic lateral sclerosis/frontotemporal lobar degeneration, and Huntington’s disease.
- No systematic search strategy, meta-analysis, or quantitative pooling is described.
Limitations
- Stated: many questions remain, clinical implications are uncertain, and much research on this phenomenon is fragmentary. The paper also states that there is no direct evidence linking non-prion neurodegenerative diseases to seeds arising outside the central nervous system or taken up from the environment.
- Stated: final evidence is lacking that in vivo tau induction occurs via prion-like corruptive templating rather than, for example, activation of a signaling cascade; the mode of cell-to-cell transfer of aggregates is unclear. Transmission of non-prion proteopathies by tainted instruments is a theoretical possibility not demonstrated in humans.
- Evident: as a narrative review, it does not provide systematic search criteria, quantitative synthesis, or primary experimental validation, and some cited findings are described as in press or not fully detailed.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
0 of 24 cited sources checked · 0 supported · 0 flagged
In the paper
“Our recent finding that the most effective Aβ seeds are small and soluble”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Abstract
What the sources say
- Not checked yetcites [54] Langer F Eisele YS Fritschi S Staufenbiel M Walker LC Jucker M Soluble Aβ seeds are potent inducers of cerebral β-amyloid deposition J Neuroscience 2011 in press PMC3229270 21994365 source
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Using a paradigm similar to in vivo Aβ-seeding, neurofibrillary (tau) tangles can be exogenously induced by the intracerebral infusion of brain extract containing abnormal tau filaments into mice bearing a human tau transgene63.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Induction and spread of tau filaments in experimental animals
What the sources say
- Not checked yetcites [63] Clavaguera F Bolmont T Crowther RA Transmission and spreading of tauopathy in transgenic mouse brain Nat Cell Biol 2009 11 909 13 19503072 PMC2726961 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The seeded proliferation of misfolded proteins, a concept that arose and evolved in the prion field, holds considerable explanatory power for the pathogenesis of many of the neurodegenerative diseases that afflict our burgeoning elderly population.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Conclusion
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes? Based: unclearA conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“While the transmission of non-prion proteopathies by tainted instruments thus is a theoretical possibility, proof of such a phenomenon (which could be obscured by a protracted incubation period) has not been demonstrated in humans.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Clinical, Practical and Theoretical Implications
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Experimentally, β-amyloid induction can be triggered in transgenic mice by intracerebrally implanted stainless steel wires coated with minute amounts of brain extract rich in aggregated Aβ52 (Fig 2).”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Clinical, Practical and Theoretical Implications
What the sources say
- Not checked yetcites [52] Eisele YS Bolmont T Heikenwalder M Induction of cerebral beta-amyloidosis: intracerebral versus systemic Abeta inoculation Proc Natl Acad Sci U S A 2009 106 12926 31 19622727 PMC2722323 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesThe paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“Once initiated, Aβ lesions proliferate within and among brain regions.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Abstract
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“the (slight) risk of prion transmission by instruments used on patients with undiagnosed prion disease106”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Clinical, Practical and Theoretical Implications
What the sources say
- Not checked yetcites [106] Ward HJ Everington D Croes EA Sporadic Creutzfeldt-Jakob disease and surgery: a case-control study using community controls Neurology 2002 59 543 8 12196646 source
Strength:plain· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“Experimentally, cerebral β-amyloidosis can be exogenously induced by exposure to dilute brain extracts containing aggregated Aβ seeds.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Abstract
What the sources say
- Not checked yetcites [49] Kane MD Lipinski WJ Callahan MJ Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta -amyloid precursor protein-transgenic mice J Neurosci 2000 20 3606 11 10804202 PMC6772682 source
- Not checked yetcites [50] Walker LC Callahan MJ Bian F Durham RA Roher AE Lipinski WJ Exogenous induction of cerebral beta-amyloidosis in betaAPP-transgenic mice Peptides 2002 23 1241 7 12128081 source
- Not checked yetcites [51] Meyer-Luehmann M Coomaraswamy J Bolmont T Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host Science 2006 313 1781 4 16990547 source
- Not checked yetcites [52] Eisele YS Bolmont T Heikenwalder M Induction of cerebral beta-amyloidosis: intracerebral versus systemic Abeta inoculation Proc Natl Acad Sci U S A 2009 106 12926 31 19622727 PMC2722323 source
- Not checked yetcites [53] Watts JC Giles K Grillo SK Lemus A DeArmond SJ Prusiner SB Bioluminescence imaging of Abeta deposition in bigenic mouse models of Alzheimer’s disease Proc Natl Acad Sci U S A 2011 108 2528 33 21262831 PMC3038719 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesNone of the sources cited for this claim have been checked yet.
In the paper
“In cell culture, however, the prion-like propagation of α-synuclein lesions has been demonstrated80, 81”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Induction and spread of protein aggregates linked to other neurodegenerative diseases
What the sources say
- Not checked yetcites [80] Desplats P Lee HJ Bae EJ Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein Proc Natl Acad Sci U S A 2009 106 13010 5 19651612 PMC2722313 source
- Not checked yetcites [81] Hansen C Angot E Bergstrom AL alpha-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells J Clin Invest 2011 121 715 25 21245577 PMC3026723 source
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The induction and proliferation of proteinaceous aggregates by corruptive protein templating appears to be a common feature of multiple, clinically diverse disorders, although many questions remain to be addressed (Table 1).”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Clinical, Practical and Theoretical Implications
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: Findings from transgenic mouse and cell culture models of protein seeding are representative of the pathogenic process in human neurodegenerative diseases.
- Probably not a substantial claim. 2
- It may state two separate claims as one. 1
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The theoretical framework underlying this paradigm recently has expanded to include an extraordinary array of neurological and systemic disorders.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Conclusion
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✗ Based: failsProbably not a substantial claim. The paper’s conclusions may not depend on it. The paper may give no reason why it holds.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“the clinical implications remain uncertain”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Conclusion
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesProbably not a substantial claim.
In the paper
“In AD, cerebral β-amyloid deposition begins in humans at least a decade prior to the onset of cognitive decline, and hence is an early and predictive indicator of the disease4.”
§ Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders > Clinical, Practical and Theoretical Implications
What the sources say
- Not checked yetcites [4] Holtzman DM Morris JC Goate AM Alzheimer’s disease: the challenge of the second century Sci Transl Med 2011 3 77sr1 21471435 PMC3130546
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper relies on this without support.
Findings from transgenic mouse and cell culture models of protein seeding are representative of the pathogenic process in human neurodegenerative diseases.
“Establishing the clinical implications of corruptive protein templating will require further mechanistic and epidemiologic investigations.”
The paper relies on this without support.
Cerebral proteopathies are growing in prevalence.
“the growing prevalence of cerebral proteopathies necessitates a comprehensive quest”
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?
The cited source says what the claim attributes to it.
In the citing paper
“A synapse-centred hypothesis also does not preclude the spreading hypothesis [34, 66], which could be either a downstream pathological event or a potential trigger of Tau-related excitotoxicity and synaptic failure.”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [66]
In the citing paper
“The fact that the amyloid tap turns itself off before clinical changes appreciably manifest, we feel, also argues against the idea that Aβ perpetuates itself in a prion-like fashion [261].”
From The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives (2014) · cites this paper as [261]
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedNeuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 3×
“Whereas the degree of tauopathy correlates strongly with cognitive decline in AD 6-8 , genetic, pathologic and biochemical evidence implicates the aggregation of A β as a critical, early trigger in the chain of events that leads to tauopathy, neuronal dysfunction and dementia 9 .”
BackgroundThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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 · cited 1×
“In the brain, the a-synuclein–rich lesions that typify Lewy body disease/Parkinson disease first arise in the lower brainstem (notably the dorsal motor nucleus of the vagus nerve), and in the anterior olfactory nucleus and the olfactory bulb; they subsequently appear in a predictable sequence in mesencephalic and neoc…”
BackgroundSoluble 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
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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 · cited 2×
“Crosssectional autopsy studies indicate that b-amyloid (Ab) plaques (A) first appear in the neocortex, followed by the allocortex and finally subcortical regions.(21) In the brain, neurofibrillary tangles (B) occur first in the locus coeruleus and transentorhinal area and then spread to the amygdala and interconnected…”
BackgroundMethodSynapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 625
Sato, K., Mano, T., Matsuda, H., Senda, M., Ihara, R., Suzuki, K., Arai, H., Ishii, K., Ito, K., Ikeuchi, T., et al. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.101957 · Cited by 12
“These results are consistent with the well-known pathological progression of AD (Braak and Braak, 1991; Frisoni et al., 2010; Jucker and Walker, 2011), as well as the distribution of structural atrophy in MCIconverters relative to non-converters: baseline atrophy in medial temporal structures including the entorhinal…”
Spreading proteins in neurodegeneration: where do they take us?
Mallucci, G. R. (2013) · Brain · doi:10.1093/brain/awt072 · Cited by 12
“…conformers in vivo, and a number of elegant experiments followed confirming that mutant tau, amyloid-b and mutant -synuclein cause spread in regional pathology and disease progression in mouse models (Clavaguera et al., 2009; Jucker and Walker, 2011; Luk et al., 2012a; Mougenot et al., 2012).”
BackgroundBasheer, N., Buée, L., Brion, J., Smolek, T., Muhammadi, M. K., Hritz, J., Hromádka, T., Dewachter, I., Wegmann, S., Landrieu, I., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01748-5 · Cited by 12
“These aggregates can break into smaller pieces or serve as a surface for secondary nucleation, resulting in further aggregation along interconnected neuronal networks in a stereotypical manner [61, 83, 112].”
BackgroundCellular Prion Protein and Amyloid-β Oligomers in Alzheimer’s Disease—Are There Connections?
Fułek, M., Hachiya, N., Gachowska, M., Beszłej, J. A., Bartoszewska, E., Kurpas, D., Kurpiński, T., Adamska, H., Poręba, R., Urban, S., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052097 · Cited by 17
“This is the first report of the possibility of transmitting cerebral A β amyloidosis from one person to another [61].”
Exosomes as Future Therapeutic Tools and Targets for Corneal Diseases
Gamez, J., Zha, D., Ebrahimi, S. M., White, S. V., Ljubimov, A. V., & Saghizadeh, M. (2025) · Cells · doi:10.3390/cells14130959 · Cited by 12
“While Exos have beneficial effects on recipient cells, their implication in disease states, such as cancer, can promote metastasis and angiogenesis [88], and in neurodegenerative diseases, such as Alzheimer’s, can carry misfolded beta-amyloid protein, potentially spreading pathology [89].”
Mahady, L. J., Perez, S. E., Malek‐Ahmadi, M. H., & Mufson, E. J. (2023) · The Journal of Comparative Neurology · doi:10.1002/cne.25466 · Cited by 11
“…1987; Hyman et al., 1988; Pearson, 1996;Pearsonetal.,1985;Rübetal.,2000;Saperetal.,1987;Shukla& Bridges, 1999; Thal, Holzer, et al., 2000) led to the hypothesis that tau propagates along synaptically connected circuits using a “prion-like” transneuronalprocess(Fornarietal.,2019;Jucker&Walker,2011).”
MethodTowards Optimization of Arylamides As Novel, Potent, and Brain-Penetrant Antiprion Lead Compounds
Li, Z., Rao, S., Gever, J. R., et al. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300454k · Cited by 11
Soltani, N., & Gholami, M. R. (2016) · ChemPhysChem · doi:10.1002/cphc.201601000 · Cited by 11
Chen, C., Liu, Y., Zhang, J., Zhang, M., Zheng, J., Teng, Y., & Liang, G. (2015) · Chemometrics and Intelligent Laboratory Systems · doi:10.1016/j.chemolab.2015.04.009 · Cited by 9
Cannabinoids – a new therapeutic strategy in neurology
Sîrbu, C. A., Manole, A. M., Vasile, M., Toma, G. S., Dobrican, L. R., Varvara, D. G., & Vasiliu, O. (2022) · Romanian Journal of Military Medicine · doi:10.55453/rjmm.2022.125.3.1 · Cited by 16
Copper metabolism-related Genes in entorhinal cortex for Alzheimer's disease
Zhang, Y., Yang, Y.-S., Wang, C., Chen, W.-C., Chen, X.-L., Wu, F., & He, H.-F. (2023) · Scientific Reports · doi:10.1038/s41598-023-44656-9 · Cited by 12
McDonnell, G. E. (2014) · Elsevier eBooks · doi:10.1533/9780857096692.2.346 · Cited by 11
Variability and Coupling of Olfactory Identification and Episodic Memory in Older Adults
Knight, J. E., Bennett, D. A., & Piccinin, A. M. (2018) · The Journals of Gerontology Series B · doi:10.1093/geronb/gby058 · Cited by 10
“The progression of neuritic plaques is less predictable than that of neurofibrillary tangles (Serrano-Pozo, Frosch, Masliah, & Hyman, 2011), but also affects main and secondary olfactory brain areas early on (Jucker & Walker, 2011; Seubert, Freiherr, Djordjevic, & Lundström, 2013).”
BackgroundInfluentialProceedings: Cell Therapies for Parkinson's Disease From Discovery to Clinic
Canet-Aviles, R., Lomax, G. P., Feigal, E. G., & Priest, C. A. (2014) · Stem Cells Translational Medicine · doi:10.5966/sctm.2014-0146 · Cited by 9
Hornemann, S., Schwarz, P., Rushing, E. J., Connolly, M. D., Zuckermann, R. N., Yam, A. Y.-W., & Aguzzi, A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216013 · Cited by 10
Cost-Reducing Traits for Agonistic Head Collisions: A Case for Neurophysiology
Tobiansky, D. J., Long, K. M., Hamden, J. E., Brawn, J. D., & Fuxjager, M. J. (2021) · Integrative and Comparative Biology · doi:10.1093/icb/icab034 · Cited by 9
Srivastava, A., & Balaji, P. V. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.09.020 · Cited by 9
“…now includes the following: (i) templating: structured aggregates promote the conversion of soluble protein species into similar aggregates (Jucker and Walker, 2011; Eisele et al., 2015; Knowles et al., 2014), (ii) fragmentation: new aggregates are generated by fragmentation of fibrils…”
BackgroundInfluentialFu, H., Yu, L., Cui, M., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.04.028 · Cited by 9
Therapeutic Approaches to Prion Diseases
Gandini, A., & Bolognesi, M. L. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.06.013 · Cited by 9
Deng, J., Liu, B., Tao, Q., Luo, Y., Zhu, Y., Huang, X., & Yue, F. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.04.002 · Cited by 8
Corti, M. (2024) · Brain Multiphysics · doi:10.1016/j.brain.2024.100098 · Cited by 8
“For what concerns the amyloid-β protein, we impose initial misfolding protein concentrations in the neocortex [42], as reported in Figure 4d.”
MethodGuidolin, D., Agnati, L. F., Albertin, G., Tortorella, C., & Fuxé, K. (2012) · Electrophoresis · doi:10.1002/elps.201200290 · Cited by 8
Popov, I. A., Indeykina, M. I., Игоревич, П. С., Starodubtseva, N. L., Kononikhin, A. S., Nikolaeva, M. I., Kukaev, E., Kostyukevich, Y., Kozin, S. A., Makarov, A. А., et al. (2014) · Molecular Biology · doi:10.1134/s0026893314040098 · Cited by 8
MacLea, K. S. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.012 · Cited by 8
“From these and other observations (e.g., Jucker & Walker 2011; 852 Eisenberg & Jucker 2012), it appears clear that the line separating the infectious prions 853 from the non-infectious amyloids or pathologic aggregates is thinner than previously 854 thought.”
BackgroundWang, C., Wang, X., Wang, D., et al. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.03.055 · Cited by 8
Koss, D. J., Robinson, L., Mietelska‐Porowska, A., Gąsiorowska, A., Sepčić, K., Turk, T., Jaspars, M., Niewiadomska, G., Scott, R. H., Platt, B., et al. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1949-4 · Cited by 8
Calcagno, D., Perina, M. L., Distefano, A., Parravano, M., Licciardello, A., Tuccitto, N., & Grasso, G. (2025) · Chemistry - Methods · doi:10.1002/cmtd.202400034 · Cited by 7
Brennan, G. S., & Goriely, A. (2025) · Journal of Mathematical Biology · doi:10.1007/s00285-024-02179-5 · Cited by 10
Prionerkrankungen — welche Rolle spielen sie heute?
Ponto, C., & Zerr, I. (2013) · InFo Neurologie + Psychiatrie · doi:10.1007/s15005-013-0230-3 · Cited by 7
“Des Weiteren konnte experimentell (in vitro) bewiesen werden, dass es möglich ist, mittels winziger, intrazerebral oder intraperitoneal applizierter Mengen von aggregiertem Aβ eine Kaskade in Gang zu setzen, deren Endpunkt eine zerebrale β-Amyloidose darstellt [20, 21].”
BackgroundSalimi, A., Chatterjee, S., & Lee, J. Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041930 · Cited by 7
“AD patients exhibit a higher risk of developing T2D and vice versa [6].”
BackgroundDiscovery and Development of Cyclic Peptide Proteasome Stimulators
Nelson, S. L., Harris, T., Muli, C. S., Maresh, M. E., Baker, B., Smith, C., Neumann, C., Trader, D. J., & Parkinson, E. I. (2023) · ChemBioChem · doi:10.1002/cbic.202300671 · Cited by 7
On the issue of transmissibility of Alzheimer disease
Schmidt, C., Karch, A., Korth, C., & Zerr, I. (2012) · Prion · doi:10.4161/pri.22502 · Cited by 8
“The concept of “seeded proliferation of misfolded proteins” in Alzheimer disease is already part of the current scientific paradigm.(3) This implies that AD might harbor the potential for being communicable.”
BackgroundModelling cerebrovascular pathology and the spread of amyloid beta in Alzheimer’s disease
Ahern, A., Thompson, T., Oliveri, H., Lorthois, S., & Goriely, A. (2025) · Proceedings of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rspa.2024.0548 · Cited by 8
Kozin, S. A., & Makarov, A. А. (2015) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro2015115115-9 · Cited by 6
Hawas, A. M., Rashed, L. A., & Mohamed, M. A. E. H. (2020) · Brazilian Archives of Biology and Technology · doi:10.1590/1678-4324-2020180687 · Cited by 7
“br/babt increase of Aβ in the brain of AD patients is related to the increased production or reduced clearance, accompanied by inflammation [43], oxidative stress [44], NFT formation [45], neuronal loss [46] and ultimately results in AD-related cognitive impairment [47].”
BackgroundPal, S., & Melnik, R. (2021) · Lecture notes in computer science · doi:10.1007/978-3-030-77977-1_42 · Cited by 7
Seeding and Cross-seeding in Amyloid Diseases
Westermark, P., & Westermark, G. T. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_4 · Cited by 7
Prion-like mechanisms in epileptogenesis
Orzi, F., Casolla, B., Rocchi, R., et al. (2012) · Neurological Sciences · doi:10.1007/s10072-012-1148-0 · Cited by 6
“A number of findings have recently suggested prion-like mechanisms as a prime mover in degenerative processes [22, 23].”
BackgroundMURAKOSHI, Y., Takahashi, T., & Mihara, H. (2013) · Chemistry - A European Journal · doi:10.1002/chem.201202762 · Cited by 6
Guan, L., Hao, Y., Chen, L., Wei, M., Jiang, Q., Liu, W., Zhang, Y., Zhang, J., Feng, F., & Qu, W. (2016) · RSC Advances · doi:10.1039/c5ra21313d · Cited by 6
Protein Misfolding in Neurodegenerative Diseases: The Key Pending Questions
Soto, C. A., & Mitchell, C. (2013) · Cited by 6
Chernova, T. A., Yang, Z., Karpova, T., Shanks, J. R., Shcherbik, N., Wilkinson, K. D., & Chernoff, Y. O. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145038 · Cited by 6
“Interactions between various amyloidogenic proteins have also been reported in mammalian systems, and some human amyloidoses (including Alzheimer’s disease) involve formation of amyloids by more than one protein [25,26].”
BackgroundNon-human primates in prion diseases
Comoy, E. E., Mikol, J., & Deslys, J. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03644-7 · Cited by 6
“…diseases including Alzheimer (AD), Parkinson (PD), Huntington diseases, and amyotrophic lateral sclerosis (ALS) presented mechanisms of aggregation and self-propagation reminiscent of those of prion protein (Jucker and Walker 2011, 2013); these diseases are now considered as prion-like diseases.”
BackgroundLeite, R. E. P., & Grinberg, L. T. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400192 · Cited by 6
Soto-Ospina, A., Marín, P. A., Bedoya, G., Falla, D. S., & Lanau, A. V. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.649990 · Cited by 6
“…in Molecular Biosciences | www.frontiersin.org June 2021 | Volume 8 | Article 6499901 ORIGINAL RESEARCH published: 02 June 2021 doi: 10.3389/fmolb.2021.649990 (Aβ) peptide in Alzheimer’s disease (AD) (Myers, 2004; Paulsen, 2011; Jucker and Walker, 2012; Jucker and Walker, 2013).”
InfluentialMcDonnell, G., & Comoy, E. E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-08-102565-9.00018-2 · Cited by 6
Strain conformation controls the specificity of cross-species prion transmission in the yeast model
Grizel, A. V., Rubel, A. A., & Chernoff, Y. O. (2016) · Prion · doi:10.1080/19336896.2016.1204060 · Cited by 7
Amyloid-based biomaterials: addressing global health, food security and environmental challenges
Su, H., Gao, Z., Liang, Y., et al. (2026) · Chemical Communications · doi:10.1039/d5cc06214d · Cited by 5
Tan, F. H., Azzam, G., Najimudin, N., Shamsuddin, S., & Zainuddin, A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03368-x · Cited by 5
“Consequently, augmented HSP concentrations are used as biomarkers for conditions such as central nervous system ischemia and AD which are considered protein-misfolding diseases or proteopathy [51].”
BackgroundHassan, M. S. O., Vahid, A. A., Sahayaraj, A. E., Viswanathan, R., & Vijayan, V. (2023) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.3c00912 · Cited by 5
Fiori, J., Naldi, M., & Andrisano, V. (2013) · European Journal of Mass Spectrometry · doi:10.1255/ejms.1255 · Cited by 5
“Monomer (1), dimer (2), trimer (3) and tetramer (4).”
BackgroundAngstmann, C. N., Donnelly, I. C., Henry, B. I., et al. (2016) · Mathematical Modelling of Natural Phenomena · doi:10.1051/mmnp/20161139 · Cited by 5
Imaging Nucleation, Growth and Heterogeneity in Self-Assembled Amyloid Phases
Anthony, N. R., Berland, K. M., Mehta, A. K., Lynn, D. G., & Childers, W. S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00003-1 · Cited by 5
Hao, Y.-N., Lu, Q., Zhai, Y.-H., Wang, H.-Y., Wu, M., Hu, M.-M., Yang, B., Wang, Z., Wu, Z., & Qi, J. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.10.003 · Cited by 5
Pal, S., & Melnik, R. (2021) · International Conference on Computational Methods for Coupled Problems in Science and Engineering (COUPLED PROBLEMS) · doi:10.23967/coupled.2021.038 · Cited by 5
“On the other hand, the tau staging for the AD begins in the locus coeruleus and transentorhinal regions [11, 15, 17, 18], as follows from [19].”
Differences in Tau Seeding in Newborn and Adult Wild-Type Mice
Ferrer, I., Andrés‐Benito, P., Garcia‐Esparcia, P., López‐González, I., Valiente, D., Jordán, M., Carmona, M., Sala‐Jarque, J., Gil, V., & del Rı́o, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094789 · Cited by 5
Rodacka, A., Strumillo, J., Puchała, M., Serafin, E., & Bartosz, G. (2019) · International Journal of Radiation Biology · doi:10.1080/09553002.2019.1642539 · Cited by 5
Tao, L., Hu, M., Zhang, X., Wang, X., Zhang, Y., Chen, X., Tang, J., & Wang, J. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.116090 · Cited by 4
Xie, J., Tandon, R., & Mitchell, C. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031062 · Cited by 5
Brain Network Functional Connectivity in Alzheimer’s Disease and Frontotemporal Dementia
Zhou, J. H., Ng, K. K., & Liu, S. (2020) · Springer eBooks · doi:10.1007/978-3-030-41874-8_25 · Cited by 4
Klotz, S., & Gelpí, E. (2021) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-021-00848-4 · Cited by 4
A New Interpretative Paradigm for Conformational Protein Diseases
Agnati, L. F., Guidolin, D., Woods, A. S., Ciruela, F., Carone, C., Vallelunga, A., Escuela, D. O. B., Genedani, S., & Fuxé, K. (2013) · Current Protein and Peptide Science · doi:10.2174/1389203711314020006 · Cited by 4
Prospects and Challenges for Alzheimer Therapeutics
Wolfe, M. S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00023-x · Cited by 5
A network thermodynamic analysis of amyloid aggregation along competing pathways
Ghosh, P., Pateras, J., Rangachari, V., & Vaidya, A. (2020) · Applied Mathematics and Computation · doi:10.1016/j.amc.2020.125778 · Cited by 4
“Addition of sub-stochiometric amounts of preformed amyloid aggregates as seeds accelerates aggregation [9, 17, 26].”
BackgroundPleasure Gone Awry? A New Conceptualization of Chronic Pain and Addiction
Hardcastle, V. G. (2013) · Review of Philosophy and Psychology · doi:10.1007/s13164-013-0170-3 · Cited by 4
Transmissible Spongiform Encephalopathies
Glatzel, M., & Aguzzi, A. (2015) · ASM Press eBooks · doi:10.1128/9781555817381.ch109 · Cited by 4
Prion propagation and inositol polyphosphates
Wickner, R. B., Edskes, H. K., Bezsonov, E. E., Son, M., & Ducatez, M. (2017) · Current Genetics · doi:10.1007/s00294-017-0788-2 · Cited by 4
“2015; Junker and Walker 2011; Kraus et al.”
Кленяева, А. Н., Chuprov‐Netochin, R. N., Marusich, E., Tatarnikova, O. G., Орлов, М. А., & Bobkova, N. V. (2014) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747814020111 · Cited by 4
Testing Amyloid Cross-Toxicity in the Vertebrate Brain
Henrı́quez, G., Méndez, L., Schmid, A. N., Guerrero, E. D., Collins, S. A., Castañeda, E., & Narayan, M. (2020) · ACS Omega · doi:10.1021/acsomega.0c01819 · Cited by 3
An Artificial Intelligence‐Based Motion Trajectory Prediction of Fibrous Matters
Yang, S., & Ling, S. (2021) · Advanced Intelligent Systems · doi:10.1002/aisy.202100136 · Cited by 3
Development of amyloid beta gold nanorod aggregates as optoacoustic probes
Soliman, M. G., Davies, H. A., Sharkey, J. W., Lévy, R., & Madine, J. (2022) · PLoS ONE · doi:10.1371/journal.pone.0259608 · Cited by 4
Björk, L., Shirani, H., Todarwal, Y., Linares, M., Vidal, R., Ghetti, B. F., Norman, P., Klingstedt, T., & Nilsson, K. P. R. (2023) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202300583 · Cited by 3
Gene Targeted Transgenic Mouse Models in Prion Research
Diack, A. B., Alibhai, J. D., & Manson, J. C. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.06.008 · Cited by 3
Reporters of Amyloid Structural Polymorphism
LeVine, H., Nilsson, K. P. R., Nilsson, R., & Hammarström, P. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00007-9 · Cited by 3
Nonamyloid Pet Biomarkers and Alzheimer'S Disease: Current and Future Perspectives
Schilling, L. P., Leuzy, A., Zimmer, E. R., Gauthier, S. G., & Rosa‐Neto, P. (2014) · Future Neurology · doi:10.2217/fnl.14.40 · Cited by 4
Hromádková, L., Kupčík, R., Jankovičová, B., Roušar, T., Řı́pová, D., & Bı́lková, Z. (2015) · Journal of Separation Science · doi:10.1002/jssc.201501045 · Cited by 3
Transmissible Spongiform Encephalopathies
Wısnıewskı, T., & Goñi, F. (2016) · Springer eBooks · doi:10.1007/978-3-319-33189-8_7 · Cited by 5
Fischer, F. U., Initiative, A. D. N., Wolf, D. G. F., & Fellgiebel, A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170147 · Cited by 3
Bourdenx, M., Dehay, B., & Bézard, E. (2015) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)30882-9 · Cited by 6
“Une autre critique globale pouvant être adressée à ces études est l’utilisation d’agrégats synthétiques d’α-syn qui sont généralement considérés comme faiblement pathogènes [37].”
Wang, Z., Wang, G., & Xie, K. (2020) · Current Opinion in Anaesthesiology · doi:10.1097/aco.0000000000000915 · Cited by 3
Insights into Network of Hot Spots of Aggregation in Nucleophosmin 1
Florio, D., Manna, S. L., Natale, C. D., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314704 · Cited by 3
“Amyloids can be divided into three main groups [1]: (1) pathological amyloids, which were the first to be discovered [2,3]; (2) artificial amyloids, often deriving from natural or de novo conceived sequences [4–6]; (3) naturally occurring functional amyloids, which perform a wide range of biological functions in diver…”
BackgroundConnectome-mediated prediction of future tau-PET burden in Alzheimer’s diseasePreprint
Damasceno, P. F., Joie, R. L., Shcherbinin, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.11.246496 · Cited by 3
“It appears that tau follows a so-called “trans-neuronal spread” mechanism whereby proteins misfold, triggering misfolding of adjacent same-species proteins, and thereupon a cascade along neuronal pathways via transsynaptic or trans-neuronal spread follows [13-17].”
BackgroundAmyloid Cross-Interactions through the Lens of Simulations: The Case of Aβ–IAPP
Xenophontos, X., Vlachou, A., Hunt, R. K., & Tamamis, P. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c04536 · Cited by 2
Sousa, G. J. A., Sá, R. A., Gomes, M. A. S. M., Edwards, G. A., Moreno‐González, I., & de Sousa, R. J. A. (2026) · Neuroinformatics · doi:10.1007/s12021-025-09763-0 · Cited by 2
“According to experimental and clinical investigations, TBI can cause tau protein misfolding, phosphorylation, and aggregation, resulting in tauopathy-like neuronal and glial inclusions (Arendt et al., 2016; Jucker & Walker, 2011; Yoshiyama et al., 2007).”
Report from the Tau Front: Cantoblanco 2013
Hall, G. F. (2014) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000e133 · Cited by 2
“Perhaps the largest influence on the direction of recent NDD research has been the idea that oligomer formation may itself be the agent of interneuronal lesion spreading via a “prionlike” mechanism [22-26].”
BackgroundComputational 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 3
Uncovering systems-level molecular similarities between Alzheimer’s and Parkinson’s diseases
Fallahi, H., Radak, M., & Yadegari, Z. S. (2023) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-023-01484-8 · Cited by 2
Nutrition and neurodegenerative diseases: Alzheimer's disease and others
Bianchi, V. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-91747-6.00013-5 · Cited by 2
Kumar, D., Singh, G., Tarun, Dhanawat, M., Gupta, S., Morsy, M. A., Nair, A. B., & Matouk, A. I. (2024) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/0118715303273145240110100341 · Cited by 2
Pin1 Protects Against Alzheimer's Disease: One Goal, Multiple Mechanisms
Pastorino, L., Kondo, A., Zhen, X., & Lu, K. P. (2013) · InTech eBooks · doi:10.5772/55085 · Cited by 2
“Plaques are forms of aggregated, fibrillar material called amyloid, insoluble fibrous protein aggregations organized in β-sheet strands that deposits in the outer part of the brain [17-19].”
BackgroundThe Prion-Like Aspect of Alzheimer Pathology
Fritschi, S. K., Eftekharzadeh, B., Manfredi, G., Hamaguchi, T., Heilbronner, G., Nagarathinam, A., Langer, F., Eisele, Y. S., Walker, L. C., & Jucker, M. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_5 · Cited by 2
Self-citationBrooks, P. L., Visanji, N. P., Hazrati, L., & Lang, A. E. (2012) · Basal Ganglia · doi:10.1016/j.baga.2012.05.004 · Cited by 2
“In the last few years the suggestion that PD, and indeed other neurodegenerative disorders, may be mediated by a process analogous to that of prion disorders has gained significant momentum [8–15].”
BackgroundMattei, T. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00075 · Cited by 2
“In fact, several recent studies (Jucker and Walker, 2011; Hall and Patuto, 2012; Kanouchi et al., 2012) have suggested that the basic proteins implied in a variety of neurodegenerative diseases [like betaamyloid and tau proteins in Alzheimer’s disease (AD), α-synuclein in Parkinson Disease and…”
Unresolved Questions in Alzheimer's Research: Will Biomarkers Help?
Zetterberg, H. (2013) · Biomarkers in Medicine · doi:10.2217/bmm.13.120 · Cited by 2
5. Prion Diseases: The Present Status and Prospect of Overcoming
Mizusawa, H. (2015) · Nihon Naika Gakkai Zasshi · doi:10.2169/naika.104.1783 · Cited by 2
Why Are Humans Vulnerable to Alzheimer’s Disease?
Glass, D. J., & Arnold, S. E. (2016) · Springer eBooks · doi:10.1007/978-3-319-29716-3_21 · Cited by 2
“If the pathogenic protein propagation process [65] is substantiated as an important mode of AD pathology transmission, as it is in prion diseases, the recommendation of Li et al.”
BackgroundDistribution of Transmissible Amyloid Proteins in the Liver with Apolipoprotein A-II Amyloidosis
Liu, Y., Sawashita, J., Wang, Y., Li, L., Miyahara, H., Ding, X., Yang, M., & Higuchi, K. (2016) · SOAR (Shinshu University) · Cited by 2
The Pattern of Cortical Lesions in Preclinical Stages
Braak, H., & Tredici, K. D. (2014) · Advances in anatomy, embryology and cell biology · doi:10.1007/978-3-319-12679-1_7 · Cited by 3
A Risk Coefficient for Radiation-Induced Dementia
Busby, C. C. (2018) · Advances in Alzheimer s Disease · doi:10.4236/aad.2018.72002 · Cited by 3
“The main component of the plaques, an accumulation of an amyloid beta peptide derived from the cleavage of an amyloid precursor protein (APP), is associated with inflammation [18], oxidative stress [19] [20], NFT formation [21], neuron loss [22] and the overall effect is AD-related cognitive impairment [23].”
BackgroundSabaté, R. (2014) · Prion · doi:10.4161/pri.29238 · Cited by 2
Metadata
- Authors
- Jucker, M., & Walker, L. C.
- Affiliations
- Emory University (US)
- Corresponding author
- Jucker, Mathias
- Venue
- Annals of Neurology
- Publisher
- Wiley
- Published
- 2011-10
- Volume
- 70
- Issue
- 4
- Pages
- 532-540
- ISSN
- 0364-5134 (ISSN-L)
- 1531-8249
- PMC
- PMC3203752
- OpenAlex
- W2018852249
- Semantic Scholar
- a083431598aa8300a06d560a5e6377c2d187348a
- Cited by
- 622
- References
- 111
- Citations by year
- 2026: 9 · 2025: 22 · 2024: 16 · 2023: 26 · 2022: 30 · 2021: 25 · 2020: 45 · 2019: 47 · 2018: 39 · 2017: 47 · 2016: 46 · 2015: 63 · 2014: 58 · 2013: 85 · 2012: 57
- FWCI
- 7.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annals of Neurology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DZNE Pub (submittedVersion)
- Funders
- U.S. Public Health Service (NCRR RR-00165)
- National Institute on Aging (P01AG026423, P50AG025688)
- National Center for Research Resources (P51RR000165)
- 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 › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, tau protein, prion-like propagation, protein aggregation, neurodegenerative diseases, frontotemporal lobar degeneration, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, alpha-synuclein, TDP-43, superoxide dismutase 1, huntingtin, amyloid seeding, diagnostic biomarkers
- MeSH terms
- Alzheimer Disease, Animals, DNA-Binding Proteins, Humans, Prions, Proteins, Amyloid beta-Peptides, tau Proteins, 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.
A language model drew the claims from the paper on 2026-10-10, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-10 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
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
