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
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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.
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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”
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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]
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“…is an upregulation in AD-specific neuropathology including increases in Aβ42 peptide deposition and senile plaque formation, neurofibrillary tangling and a progressive inflammatory neurodegeneration (Lukiw, 2007; Cui et al., 2007; Lee et al., 2011; Alexandrov et al., 2011; Jucker and Walker, 2011).”
BackgroundJiang, Q., Wang, L., Guan, Y., Xu, H., Niu, Y., Han, L., Wei, Y., Li, L., Chu, J., Wang, Q., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.022 · Cited by 42
Gouras, G. K., Willén, K., & Tampellini, D. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.06.004 · Cited by 39
CSF biomarkers in neurodegenerative and vascular dementias
Llorens, F., Schmitz, M., Ferrer, I., & Zerr, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.03.003 · Cited by 44
“It is known that misfolded Ab oligomers act as seeds inducing other Ab peptides to undergo oligomerization and aggregation in a prionlike manner (Jucker and Walker, 2011; Prado and Baron, 2012; Rosen et al., 2012).”
BackgroundStrain-specific Fibril Propagation by an Aβ Dodecamer
Dean, D. N., Das, P. K., Rana, P., Burg, F., Levites, Y., Morgan, S. E., Ghosh, P., & Rangachari, V. (2017) · Scientific Reports · doi:10.1038/srep40787 · Cited by 36
“Although termed dodecamer, LFAOs have been shown to be rather disperse oligomers that more appropriately could be described as oligomeric ‘cloud’ 12 .”
InfluentialPrion‐like protein aggregates exploit the RHO GTPase to cofilin‐1 signaling pathway to enter cells
Zhong, Z., Grasso, L., Sibilla, C., Stevens, T. J., Barry, N. P., & Bertolotti, A. (2018) · The EMBO Journal · doi:10.15252/embj.201797822 · Cited by 43
“There is now abundant literature showing that the diverse proteins associated with neurodegenerative diseases share the defining features of prions (Brundin et al , 2010; Frost & Diamond, 2010; Goedert et al , 2010; Jucker & Walker, 2011; Mu¨nch & Bertolotti, 2012).”
Anti-amyloid Therapy of Alzheimer’s Disease: Current State and Prospects
Kozin, S. A., Barykin, E. P., Mitkevich, V. A., & Makarov, A. А. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918090079 · Cited by 39
Jiang, N., Li, S., Xie, S., Li, Z., Wang, K. D. G., Wang, X., & Kong, L. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.10.004 · Cited by 39
Wegenast‐Braun, B. M., Skodras, A., Bayraktar, G., Mahler, J., Fritschi, S. K., Klingstedt, T., Mason, J. J., Hammarström, P., Nilsson, K. P. R., Liebig, C., et al. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.08.031 · Cited by 38
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“…Lateralposteriorthalamicnucleus;MD,Mediodorsalthalamicnucleus;MGB, Medialgeniculatebody;MMT,Mamillothalamictract(Vicqd’Azyr );PC,Paracentralthalamicnucleus;PF, propagation of this process along anatomical pathways, are a chronic prion-like neurodegenerative disorder [2, 5, 16, 34, 35].”
Eleuteri, S., Giovanni, S. D., Rockenstein, E. M., Mante, M., Adame, A., Trejo, M., Wrasidlo, W., Wu, F., Fraering, P. C., Masliah, E., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.017 · Cited by 40
Human Amylin: From Pathology to Physiology and Pharmacology
Ling, W., Huang, Y., Qiao, Y.-C., Zhang, X., & Zhao, H. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190328111833 · Cited by 37
Kaur, G., & Prakash, A. K. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.108255 · Cited by 36
Bayesian Physics-Based Modeling of Tau Propagation in Alzheimer's Disease
Schäfer, A., Peirlinck, M., Linka, K., Ellen Kuhl, A., & (ADNI), T. A. D. N. I. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.702975 · Cited by 38
Reprogramming energetic metabolism in Alzheimer's disease
Vallée, A., Lecarpentier, Y., Guillevin, R., & Vallée, J.-N. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.10.033 · Cited by 38
“and energetic dysregulation with oxidative stress [1,2].”
Prion Properties of SOD1 in Amyotrophic Lateral Sclerosis and Potential TherapyPreprint
Sibilla, C., & Bertolotti, A. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a024141 · Cited by 37
Linsley, J. W., Shah, K. D., Castello, N. A., Chan, M. Y., Haddad, D., Doric, Z., Wang, S., Leks, W., Mancini, J., Oza, V. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25549-9 · Cited by 37
Molecular hydrogen therapy for neurological diseases
Ramanathan, D., Huang, L., Wilson, T. A., & Boling, W. (2022) · Medical Gas Research · doi:10.4103/2045-9912.359677 · Cited by 37
Proteostasis in neurodegenerative diseases
Kinger, S., Jagtap, Y. A., Kumar, P., Choudhary, A., Prasad, A., Prajapati, V. K., Kumar, A., Mehta, G., & Mishra, A. (2024) · Advances in clinical chemistry · doi:10.1016/bs.acc.2024.04.002 · Cited by 34
Dopamine‐induced α‐synuclein oligomers show self‐ and cross‐propagation properties
Planchard, M. S., Exley, S. E., Morgan, S. E., & Rangachari, V. (2014) · Protein Science · doi:10.1002/pro.2521 · Cited by 35
“Recently, we established that some off-pathway oligomers of amyloid-b(1-42) (Ab42) are capable of undergoing replication by self-propagation similar to that of mammilian prions.”
BackgroundInfluentialAltered Serum IgG Levels to α-Synuclein in Dementia with Lewy Bodies and Alzheimer’s Disease
Koehler, N. K. U., Stransky, E., Shing, M., Gaertner, S., Meyer, M., Schreitmüller, B., Leyhe, T., Laske, C., Maetzler, W., Kahle, P., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064649 · Cited by 38
Xu, F., Fu, Z., Dass, S., Kotarba, A. E., Davis, J., Smith, S. O., & Nostrand, W. E. V. (2016) · Nature Communications · doi:10.1038/ncomms13527 · Cited by 36
A patent review of butyrylcholinesterase inhibitors and reactivators 2010–2017
Andrisano, V., Naldi, M., Simone, A. D., & Bartolini, M. (2018) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2018.1476494 · Cited by 35
Lo, A. C., Iscru, E., Blum, D. L., Tesseur, I. C., Callaerts‐Vegh, Z., Buée, L., Strooper, B. D., Balschun, D., & D’Hooge, R. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122296 · Cited by 39
“Amyloid and tau neuropathology both develop along distinct stages, but appear to affect parts of the brain differentially [6].”
Kulikova, A. A., Makarov, A. А., & Kozin, S. A. (2015) · Molecular Biology · doi:10.1134/s0026893315020065 · Cited by 35
Human prion diseases: Molecular, cellular and population biology
Head, M. W. (2013) · Neuropathology · doi:10.1111/neup.12016 · Cited by 35
Yang, J., Wang, X., Liu, J., Chi, W., Zhang, L., Xiao, L., & Yan, J. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c04042 · Cited by 35
Coordination of Zn 2+ and Cu 2+ to the membrane disrupting fragment of amylin
Rowińska‐Żyrek, M. (2016) · Dalton Transactions · doi:10.1039/c6dt00628k · Cited by 33
Role of water in protein folding, oligomerization, amyloidosis and miniprotein
Vajda, T., & Perczel, A. (2014) · Journal of Peptide Science · doi:10.1002/psc.2671 · Cited by 34
Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease
Kozin, S. A., Mitkevich, V. A., & Makarov, A. А. (2016) · Mendeleev Communications · doi:10.1016/j.mencom.2016.07.001 · Cited by 33
Autophagy impairment: a crossroad between neurodegeneration and tauopathies
Nassif, M., & Hetz, C. A. (2012) · BMC Biology · doi:10.1186/1741-7007-10-78 · Cited by 33
“Accumulation of phosphorylated Tau in neurofibrillary tangles represents one of the major hallmarks of AD and other tauopathies, including frontotemporal dementia [9].”
BackgroundNeural correlates of episodic memory in the Memento cohort
Epelbaum, S., Bouteloup, V., Mangin, J., Corte, V. L., Migliaccio, R., Bertin, H., Habert, M. O., Fischer, C., Azouani, C., Fillon, L., et al. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.03.010 · Cited by 39
Prion-like Mechanisms in Alzheimer's Disease
Yin, R., Tan, L., Jiang, T., & Yu, J. (2014) · Current Alzheimer Research · doi:10.2174/156720501108140910121425 · Cited by 33
Baloh, R. H. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a269b · Cited by 33
Cerebral Waste Accumulation and Glymphatic Clearance as Mechanisms of Human Neurological Diseases
Janigro, D. (2016) · Journal of Neurology and Neuromedicine · doi:10.29245/2572.942x/2016/7.1082 · Cited by 32
TDP-1/TDP-43 potentiates human α-Synuclein (HASN) neurodegeneration in Caenorhabditis elegans
Shen, L., Wang, C., Chen, L., Leung, K. L., Lo, E., Lakso, M., & Wong, G. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165876 · Cited by 32
CHAMBERS, J. K., Uchida, K., Harada, T., Tsuboi, M., Sato, M., Kubo, M., Kawaguchi, H., Miyoshi, N., Tsujimoto, H., & Nakayama, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046452 · Cited by 31
Insights into Mechanisms of Chronic Neurodegeneration
Diack, A. B., Alibhai, J. D., Barron, R. M., Bradford, B. M., Piccardo, P., & Manson, J. C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17010082 · Cited by 31
“The accumulation and aggregation of PrPSc occurs long before detectable neurodegeneration [63,69] and the spread of misfolded protein between distinct brain regions is thought to determine the specific brain regions that undergo neurodegeneration (reviewed in [40,70]).”
BackgroundThe ubiquitin-proteasome system and microvascular complications of diabetes.
Aghdam, S. Y., & Sheibani, N. (2013) · Europe PMC (PubMed Central) · Cited by 32
Pérez‐Torres, C. J., Reynolds, J. O., & Pautler, R. G. (2013) · Magnetic Resonance in Medicine · doi:10.1002/mrm.24665 · Cited by 30
“At the molecular level, both amyloid and tau begin as soluble monomers that eventually become insoluble deposits (19,23).”
BackgroundGanz, T., Fainstein, N., Elad, A., Lachish, M., Goldfarb, S., Einstein, O., & Ben‐Hur, T. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02369-8 · Cited by 31
“Since microbial endotoxins are powerful TLR4 agonists and stimulate microglia as well (27), we hypothesized that: (1) infectious agents and PAMP may accelerate neurodegeneration in the AD brain; (2) microglia may play a central role in this process; and (3) microglial modulation may protect the brain from PAMP-induced…”
BackgroundRüb, U., Stratmann, K., Heinsen, H., Seidel, K., Bouzrou, M., & Korf, H. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161102 · Cited by 31
“the brain, (2) these aggregates would propagate in a transneuronal manner along anatomical pathways, (3) the local templated conversion of the native and soluble cytoplasmic tau proteins would be induced in the next nerve cell of the affected neuronal chain and leads to its self-aggregation, and (4) the newly synthesi…”
InfluentialYusuf, M., Khan, M., Robaian, M. A., & Khan, R. A. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0250 · Cited by 32
“The misfolding and peculiar polymerization of β-amyloid, including the misfolding of the tau protein in the nervous system, has been primarily attributed to the pathogenesis of Alzheimer’s disease (Jucker and Walker, 2011).”
Wu, D., Faria, A. V., Laurent Younes, B., Mori, S., Brown, T., Johnson, H. J., Paulsen, J. S., Ross, C. A., Miller, M. I., & the PREDICT‐HD Investigators and Coordinators of the Huntington Study Group (2017) · Human Brain Mapping · doi:10.1002/hbm.23713 · Cited by 29
“Pathology could also spread via excitotoxicity or loss of trophic factor support or other mechanisms [Jucker and Walker, 2011; Ross et al., 2014].”
BackgroundMalik, H. H., Javaid, S., Rasool, M. F., Samad, N., Ahamad, S. R., Alqahtani, F., & Imran, I. (2020) · Medicina · doi:10.3390/medicina56030144 · Cited by 29
“Contributing pathophysiological factors are extracellular deposition of insoluble β-amyloid clumps, intracellular neurofibrillary tangles and oxidative stress followed by neuronal degeneration and impaired neurotransmission in the hippocampus [4].”
BackgroundAlzheimer's Disease and Prion Protein
Zhou, J. (2013) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2013.v2.2.35 · Cited by 31
Ito, K., Hutmacher, M. M., & Corrigan, B. (2012) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-012-9271-3 · Cited by 29
“Neuropathological observations of the postmortem AD brain include the presence of senile plaques—containing primarily b-amyloid (Ab) peptide aggregates—and tangles comprised of highly phosphorylated s proteins, and it is considered that Ab lesions proliferate within and among brain regions once initiated [16].”
Implications for Alzheimer’s disease of an atomic resolution structure of amyloid-β(1–42) fibrils
Eisenberg, D. S., & Sawaya, M. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610806113 · Cited by 30
Genesis of tramsmissible protein states via deformed templating
Makarava, N., & Baskakov, I. V. (2012) · Prion · doi:10.4161/pri.19930 · Cited by 28
Computational modeling of the relationship between amyloid and disease
Hall, D. R., & Edskes, H. K. (2012) · Biophysical Reviews · doi:10.1007/s12551-012-0091-x · Cited by 29
“Our aim is to discuss recent progress in the computational modeling of a diverse range of amyloid related diseases collectively known as the amyloidoses (Pepys 2006; Norrby 2011; Jucker and Walker 2011; Merlini and Bellotti 2003).”
BackgroundWang, Z.-M., Li, X., Xue, G., Xu, W., Wang, X., & Kong, L. (2015) · RSC Advances · doi:10.1039/c5ra22296f · Cited by 29
Guo, X., Tang, P., Chen, L., Liu, P., Hou, C., Zhang, X., Liu, Y., Li, C., Li, X., & Li, R. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00228 · Cited by 34
“Abnormal protein aggregation is a universal pathogenesis of neurodegenerative diseases such as AD, Huntington’s disease (HD) and Parkinson’s disease (PD) (Hardy and Selkoe, 2002; Brundin et al., 2010; Zuccato et al., 2010; Jucker and Walker, 2011).”
BackgroundCorlier, F. W., Rivals, I., Lagarde, J., Hamelin, L., Corne, H., Dauphinot, L., Ando, K., Cossec, J., Fontaine, G., Dorothée, G., et al. (2015) · Translational Psychiatry · doi:10.1038/tp.2015.87 · Cited by 28
Schipanski, A., Oberhauser, F. B., Neumann, M., Lange, S., Szalay, B., Krasemann, S., van Leeuwen, F. W., Galliciotti, G., & Glatzel, M. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.04.002 · Cited by 28
“Disequilibrium between generation and degradation of misfolded proteins is critically involved in the pathophysiology of dementias (Jucker and Walker, 2011; Lomas and Carrell, 2002).”
Yu, Q., Reale, M., Kamal, M. A., Holloway, H. W., Luo, W., Sambamurti, K., Ray, B., Lahiri, D. K., Rogers, J. T., & Greig, N. H. (2013) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/1871523011312020003 · Cited by 28
Yates, E. A., & Legleiter, J. A. (2014) · Biochemistry · doi:10.1021/bi500792f · Cited by 26
Legname, G., & Scialò, C. (2020) · Prion · doi:10.1080/19336896.2020.1854034 · Cited by 29
Increased retention of tau PET ligand [18F]-AV1451 in Alzheimer’s Disease Psychosis
Gomar, J. J., Tan, G., Halpern, J. H., Gordon, M. L., GREENWALD, B. S., & Koppel, J. L. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-01850-z · Cited by 27
α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties
Mehra, S., Ahlawat, S., Kumar, H., Datta, D., Navalkar, A., Singh, N., Patel, K., Gadhe, L. G., Kadu, P., Kumar, R., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167761 · Cited by 25
Campos, H. C., Ribeiro, D. E., Hashiguchi, D., Glaser, T., Milanis, M. D. S., Gimenes, C., Suchecki, D., Arida, R. M., Ulrich, H., & Longo, B. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1132825 · Cited by 30
“, 2006) and hyperlocomotion in the open field test (Jucker and Walker, 2011; Cheng et al., 2014; Wang et al., 2020).”
BackgroundEpelbaum, S., Youssef, I., Lacor, P. N., Chaurand, P., Duplus, E., Brugg, B., Duyckaerts, C. J., & Delatour, B. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.005 · Cited by 30
“, 2012,Braak and Braak, 1997) are characteristic of the spreading of cerebral ß-amyloidosis (Jucker and Walker, 2011).”
BackgroundPotential Novel Approaches to Understand the Pathogenesis and Treat Alzheimer’s Disease
Drummond, E., Goñi, F., Liu, S., Prelli, F., Scholtzova, H., & Wısnıewskı, T. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179909 · Cited by 26
Replacement of huntingtin exon 1 by trans-splicing
Rindt, H., Yen, P., Thebeau, C. N., Peterson, T. S., Weisman, G. A., & Lorson, C. L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1083-5 · Cited by 26
“This raises the question whether expanded polyQ amyloids may also play a role in the propagation of the pathology from initially localized foci [57, 58].”
Cryo-EM Analysis of the Effect of Seeding with Brain-derived Aβ Amyloid Fibrils
Pfeiffer, P. B., Ugrina, M., Schwierz, N., Sigurdson, C. J., Schmidt, M., & Fändrich, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168422 · Cited by 26
Kumar, A., Pate, K. M., Moss, M. A., Dean, D. N., & Rangachari, V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111492 · Cited by 26
A Multi-layered Variable Selection Strategy for QSAR Modeling of Butyrylcholinesterase Inhibitors
Kumar, V., De, P., Ojha, P. K., Saha, A., & Roy, K. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200616142753 · Cited by 25
Prion-based memory of heat stress in yeast
Chernova, T. A., Chernoff, Y. O., & Wilkinson, K. D. (2017) · Prion · doi:10.1080/19336896.2017.1328342 · Cited by 26
“Formation of a yeast prion de novo can be induced by a transient overproduction of the prion-forming protein or its PrD.20,30 However, typically this process is efficient only if there is another Q/N-rich protein aggregate in the same cell.31-34 For example, de novo formation of the Sup35 prion, [PSIC] after transient…”
BackgroundTunesi, M., Fusco, F., Fiordaliso, F., Corbelli, A., Biella, G., & Raimondi, M. T. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00146 · Cited by 26
“In addition, dynamic conditions may better reproduce pathology-relevant features, such as protein seeding and spreading across cells, that is relevant also for FTLD (Jucker and Walker, 2011).”
Background
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
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