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]
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
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Items 301–400 of 625
Zhang, Y., Tang, Y., Zhang, D., Liu, Y., He, J., Chang, Y., & Zheng, J. (2020) · Chinese Journal of Chemical Engineering · doi:10.1016/j.cjche.2020.09.033 · Cited by 24
Amyloid β and tau pathology in brains of aged pinniped species (sea lion, seal, and walrus)
Takaichi, Y., CHAMBERS, J. K., Takahashi, K., Soeda, Y., Koike, R., Katsumata, E., Kita, C., Matsuda, F., HARITANI, M., Takashima, A., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01104-3 · Cited by 26
“Rodent Aβ displays three amino acid differences in its N-terminal region from human Aβ [28], and one amino acid located in the N-terminal region of cat Aβ protein differed from that of human Aβ [27].”
BackgroundFurukawa, Y., & Nukina, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.011 · Cited by 25
Heinzel, S., Gold, M., Deuschle, C., Bernhard, F. P., Maetzler, W., Berg, D., & Dodel, R. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114566 · Cited by 26
“a-Syn aggregates into neurons and may lead to Lewy body pathology and the progressive degeneration of dopaminergic neurons [3, 4].”
BackgroundStructural connectivity centrality changes mark the path toward Alzheimer's disease
Peraza, L. R., Díaz‐Parra, A., Kennion, O., Moratal, D., Taylor, J., Kaiser, M., Bauer, R., & Initiative, A. D. N. (2019) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2018.12.004 · Cited by 24
“The presence of neurofibrillary tangles and amyloid plaques is the main pathological hallmark of AD [3,6,7].”
BackgroundNavale, G. R., Ahmed, I., Lim, M. H., & Ghosh, K. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202401991 · Cited by 24
Dean, D. N., Pate, K. M., Moss, M. A., & Rangachari, V. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00161 · Cited by 23
Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23
AAV Vector-Mediated Antibody Delivery (A-MAD) in the Central Nervous System
Marino, M., & Holt, M. G. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.870799 · Cited by 24
Narrative on Hydrogen Therapy and its Clinical Applications: Safety and Efficacy
Ahmad, A., Baig, A. A., Hussain, M., Saeed, M. U., Bilal, M., Ahmed, N., Chopra, H., Hassan, M. S., Rachamalla, M., Putnala, S. K., et al. (2022) · Current Pharmaceutical Design · doi:10.2174/1381612828666220728104200 · Cited by 25
Snord 3A: A Molecular Marker and Modulator of Prion Disease Progression
Cohen, E., Avrahami, D., Frid, K., Canello, T., Levy‐Lahad, E., Zeligson, S., Perlberg, S., Chapman, J., Cohen, O. S., Kahana, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054433 · Cited by 23
“also described for conditions such as Alzheimer’s and Parkinson [3], and their associated proteins, Tau, a-synuclein and Ab [4], [5].”
BackgroundMoving Away from Amyloid Beta to Move on in Alzheimer Research
Moreno‐Treviño, M. G., Castillo-López, J., & Meester, I. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00002 · Cited by 24
“First, senile plaques and neurofibrillary tangles display dissimilar spatiotemporal distribution (Jucker and Walker, 2011).”
BackgroundThe role of hydrogen in Alzheimer’s disease
Tan, X., Shen, F., Dong, W.-L., Yang, Y., & Chen, G. (2018) · Medical Gas Research · doi:10.4103/2045-9912.248270 · Cited by 23
Animal Models of Alzheimer’s Disease
Newman, M., Kretzschmar, D., Khan, I., Chen, M., Verdile, G., & Lardelli, M. T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809468-6.00040-1 · Cited by 25
Kim, H., Kim, S., Cho, B., Shin, J., & Kim, J. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00319-9 · Cited by 22
“Background Alzheimer’s disease (AD) is an age-dependent neurodegenerative disorder, characterized by cognitive decline and memory loss [1, 2].”
BackgroundReinhardt, A., Feuillette, S., Cassar, M., Callens, C., Thomassin, H., Birman, S., Lecourtois, M., Antoniewski, C., & Tricoire, H. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00226 · Cited by 23
“A common hallmark of several of these agingassociated neurodegenerative disorders that emerged from these early studies, is the existence of fibrillar aggregates of aggregationprone proteins that may trap other cellular compounds (Jucker and Walker, 2011).”
BackgroundGeorge, S., Rönnbäck, A., Gouras, G. K., Petit, G. H., Grueninger, F., Winblad, B., Graff, C., & Brundin, P. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-17 · Cited by 23
“The reduction of Aβ pathology we observed could also be the result of reduced transport of misfolded Aβ species that are released and cause prion-like seeding in interconnected regions [2,38].”
InfluentialEfficient GSH delivery using PAMAM-GSH into MPP-induced PC12 cellular model for Parkinson’s disease
Sun, H., Wang, Y., Hao, T., Wang, C., Wang, Q., & Jiang, X. (2016) · Regenerative Biomaterials · doi:10.1093/rb/rbw032 · Cited by 23
“Parkinson’s disease (PD) is a common progressive neurodegenerative disease, which is characterized by clinical features including bradykinesia, rigidity, tremor and postural instability [1] as well as loss of dopamine-secreting neurons within substantia nigra [2] and the accumulation of misfolded a-synuclein into intr…”
BackgroundRubin, K., & Glazer, S. (2016) · Immunobiology · doi:10.1016/j.imbio.2016.09.017 · Cited by 22
“Poor mucosal BP immunity, in turn, is held to increase the risk of SCBPC infection, and thus AD.”
Zn(II) - pramlintide: Stability, binding sites and unexpected aggregation
Łoboda, D., & Rowińska‐Żyrek, M. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.06.008 · Cited by 22
Communicability distance reveals hidden patterns of Alzheimer’s disease
Lella, E., & Estrada, E. (2020) · Network Neuroscience · doi:10.1162/netn_a_00143 · Cited by 24
“The molecular basis of these different stages appear to be linked to the presence of β-amyloid (Aβ) in senile plaques and cerebral amyloid angiopathy, as well as tau proteins (tau) in neurofibrillary tangles [12, 13, 14].”
BackgroundDohi, K., Satoh, K., Miyamoto, K., Momma, S., Fukuda, K., Higuchi, R., Ohtaki, H., & Banks, W. A. (2017) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.16-87 · Cited by 23
Pal, S., & Melnik, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-11242-4 · Cited by 22
Amyloid-β Activates Microglia and Regulates Protein Expression in a Manner Similar to Prions
Tu, J., Chen, B., Yang, L., Qi, K., Lu, J. N., & Zhao, D. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0553-2 · Cited by 23
Host immune defence, amyloid-β peptide and Alzheimer disease
Golde, T. E. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.105 · Cited by 23
Pandya, S., Initiative, A. D. N., Kuceyeski, A. F., & Raj, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160090 · Cited by 24
“…this network spread has been revealed to involve a transneuronal “prion-like” mechanism [21, 42], whereby implicated proteins misfold, trigger misfolding of adjacent same-species proteins, and thereupon cascade along neuronal pathways via transsynaptic or transneuronal spread [18, 20, 21, 43, 44].”
Rui, M., Rossino, G., Coniglio, S., Monteleone, S., Scuteri, A., Malacrida, A., Rossi, D., Catenacci, L., Sorrenti, M., Paolillo, M., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.010 · Cited by 23
Igel‐Egalon, A., Laferrière, F., Moudjou, M., Bohl, J., Mezache, M., Knäpple, T., Herzog, L., Reine, F., Jas-Duval, C., Doumic, M., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0608-y · Cited by 19
“Considering that suPrPB can condense into B2(41) and according to detailed-balance (2), one can establish the reaction model describing the formation of Bi assemblies from the neoformed suPrPB: 2suPrP"B2 ð5Þ”
BackgroundSpatial Propagation of Protein Polymerization
Cohen, S. I. A., Rajah, L., Yoon, C. H., Buell, A. K., White, D. A., Sperling, R. A., Vendruscolo, M., Terentjev, E. M., Dobson, C. M., Weitz, D. A., et al. (2014) · Physical Review Letters · doi:10.1103/physrevlett.112.098101 · Cited by 20
Cortical morphometry and neural dysfunction in Huntington’s disease: a review
Tan, B., Shishegar, R., Poudel, G. R., Fornito, A., & Georgiou‐Karistianis, N. (2020) · European Journal of Neurology · doi:10.1111/ene.14648 · Cited by 24
Shift of the insoluble content of the proteome in the aging mouse brain
Molzahn, C. M., Kuechler, E. R., Zemlyankina, I., Nierves, L. A., Ali, T., Cole, G., Wang, J., Albu, R. F., Zhu, M., Cashman, N. R., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310057120 · Cited by 22
“The cortex was selected due to susceptibility to amyloid aggregation early in AD (16).”
Switching On/Off Amyloid Plaque Formation in Transgenic Animal Models of Alzheimer’s Disease
Kozin, S. A., Kechko, O. I., Adzhubei, A. A., Makarov, A. А., & Mitkevich, V. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010072 · Cited by 21
Hill, W. J. L. J. M. (2014) · Journal of Aging Science · doi:10.4172/2329-8847.1000119 · Cited by 23
“In summary, at least 7 independent lines of research currently support the contention that miRNAs may be involved in the pathological spreading of AD, including the following empirical observations: (i) their similarity in structure, function and pathological mechanism to viroids, the smallest infectious agent known,…”
BackgroundZhang, G., Shen, Y., Phipps, J., Sun, L., & Ma, S. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.216059 · Cited by 21
“The progression of this pathology is correlated with the functional and anatomical coupling of brain regions [95].”
2‐Aminothiazoles with Improved Pharmacotherapeutic Properties for Treatment of Prion Disease
Li, Z., Silber, B. M., Rao, S., et al. (2013) · ChemMedChem · doi:10.1002/cmdc.201300007 · Cited by 20
Amyloidogenesis: What Do We Know So Far?
Alraawi, Z., Banerjee, N., Mohanty, S., & Kumar, T. K. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213970 · Cited by 22
Mitigation of cerebellar neuropathy in globoid cell leukodystrophy mice by AAV-mediated gene therapy
Lin, D., Hsiao, C., Lee, A. Y.-L., Ho, C., Liu, H., Wang, T.-J., Jian, Y.-R., Hsu, J.-C., Huang, Z., Lee, T., et al. (2015) · Gene · doi:10.1016/j.gene.2015.06.049 · Cited by 20
Antiprion compounds that reduce PrPSc levels in dividing and stationary-phase cells
Silber, B. M., Gever, J. R., Li, Z., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.09.022 · Cited by 20
Goñi, F., Martá-Ariza, M., Herline, K., Peyser, D. K., Boutajangout, A., Mehta, P. D., Drummond, E., Prelli, F., & Wısnıewskı, T. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0337-3 · Cited by 20
Genomics: New Light on Alzheimer’s Disease Research
Jung, Y. J., Kim, Y. H., Bhalla, M., Lee, S. B., & Seo, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123771 · Cited by 19
“As in other forms of proteopathy, this could further trigger the aggregation of other proteins by causing defects in the cellular machinery required for protein homeostasis [35].”
BackgroundNew protein deposition tracers in the pipeline
Jovalekic, A., Koglin, N., Mueller, A., & Stephens, A. W. (2016) · EJNMMI Radiopharmacy and Chemistry · doi:10.1186/s41181-016-0015-3 · Cited by 19
“While the evolution of AD neuropathology depends on interactions between Aβ and tau (Jucker & Walker 2011), the relative contributions of the two proteins in the development of AD remain unclear.”
BackgroundShi, J., Pei, J., Liu, E., & Zhang, L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173871 · Cited by 22
Kozin, S. A., Barykin, E. P., Telegin, G. B., Чернов, А. С., Adzhubei, A. A., Radko, S. P., Mitkevich, V. A., & Makarov, A. А. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00518 · Cited by 20
Takahashi, F., Zhang, C., Hohjoh, H., Raveney, B. J. E., Yamamura, T., Hayashi, N., & Oki, S. (2022) · iScience · doi:10.1016/j.isci.2022.104278 · Cited by 22
“Recent molecular genetic research has successfully unveiled a series of risk factors such as TDP-43, Amyloid b, and a-synuclein, which are schematically relevant to pathogenesis of ALS, AD, PD, respectively (Jucker and Walker, 2011).”
BackgroundKruppa, A. J., Ott, S., Chandraratna, D., Irving, J. A., Page, R. M., Speretta, E., Seto, T., Camargo, L. M., Marciniak, S. J., Lomas, D. A., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.07.019 · Cited by 19
Wang, Q., Chen, S., Wang, J., Shang, H., & Chen, X. (2024) · Brain Sciences · doi:10.3390/brainsci14100990 · Cited by 18
“Alzheimer’s disease (AD) is characterized by a convoluted pathology mechanism [1,2].”
BackgroundCalcium Signalling in Neurological Disorders, with Insights from Miniature Fluorescence Microscopy
Sun, D., Amiri, M., Meng, Q., Unnithan, R. R., & French, C. R. (2024) · Cells · doi:10.3390/cells14010004 · Cited by 20
Dyer-Reaves, K., Goodman, A. M., Nelson, A. R., & McMahon, L. L. (2019) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2019.00027 · Cited by 17
HspB5 Activates a Neuroprotective Glial Cell Response in Experimental Tauopathy
Hampton, D. W., Amor, S., Story, D., Torvell, M., Bsibsi, M., van Noort, J. M., & Chandran, S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00574 · Cited by 17
Molecular Pathology of Alzheimer's Disease
Castellani, R. J., & Perry, G. L. (2013) · Colloquium Series on Neurobiology of Alzheimer s Disease · doi:10.4199/c00095ed1v01y201310alz001 · Cited by 19
Alzheimer's disease models and functional genomics—How many needles are there in the haystack?
Götz, J., Matamales, M., Götz, N. N., Ittner, L. M., & Eckert, A. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00320 · Cited by 19
“It will be inevitable to discuss another form of dementia, FTLD-Tau, as it shares important clinical and histopathological features with AD (Jucker and Walker, 2011).”
BackgroundThe air–water interface determines the outcome of seeding during amyloidogenesis
Trigg, B., Lee, C. F., Vaux, D. J., & Jean, L. (2013) · Biochemical Journal · doi:10.1042/bj20130605 · Cited by 18
Inhaled Xenon Washout as a Biomarker of Alzheimer’s Disease
Hane, F. T., Li, T., Plata, J. A., Hassan, A. A., Granberg, K., & Albert, M. S. (2018) · Diagnostics · doi:10.3390/diagnostics8020041 · Cited by 20
“This observation is consistent with previous reports indicating that AD pathology begins near the rostral regions of the brain and slowly migrates towards the caudal regions of the brain [79].”
Protective effects of curcumin in APPswe transfected SH-SY5Y cells.
Yin, W., Zhang, X., & Yu, L. (2012) · PubMed · doi:10.3969/j.issn.1673-5374.2012.06.001 · Cited by 18
“Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized pathologically by the loss of synapses and neurons, the formation of neurofibrillary tangles, and the accumulation of amyloid-beta (Aβ) deposits [1] .”
BackgroundGentier, R. J. G., Verheijen, B. M., Zamboni, M., Stroeken, M. M. A., Hermes, D. J. H. P., Küsters, B., Steinbusch, H. W. M., Hopkins, D. A., & van Leeuwen, F. W. (2015) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2015.00026 · Cited by 18
Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion
Espargaró, A., Busquets, M. A., Estelrich, J., & Sabaté, R. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00029 · Cited by 18
“Like classical prions, these proteins form distinct conformers in vivo, and Aβ, mutant τ, and mutant α-syn can cause the spread of regional pathology and disease progression in mouse models (Aguzzi and Rajendran, 2009; Clavaguera et al., 2009; Jucker and Walker, 2011; Luk et al., 2012; Mougenot et al., 2012; Stöhr et…”
BackgroundPrion potentiation after life-long dormancy in mice devoid of PrP
Martin, D., Reine, F., Herzog, L., Igel‐Egalon, A., Aron, N., Michel, C., Moudjou, M., Fichet, G., Quadrio, I., Perret‐Liaudet, A., et al. (2021) · Brain Communications · doi:10.1093/braincomms/fcab092 · Cited by 18
Deng, Y., Li, W., Niu, L., Luo, X., Li, J., Zhang, Y. E., Liu, H., He, J., & Wan, W. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136209 · Cited by 17
Structure and Aggregation Mechanisms in Amyloids
Almeida, Z. L., & Brito, R. M. M. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamolscs.1.2020.9 · Cited by 17
Prions and Prion-Like Pathogens in Neurodegenerative Disorders
Peggion, C., Sorgato, M. C., & Bertoli, A. (2014) · Pathogens · doi:10.3390/pathogens3010149 · Cited by 17
“oligomers, was based on both clinical observations of AD pathology (in humans and animal models), and on intracerebral inoculation of AD brain extracts (in nonhuman primates and human APP-expressing transgenic mice) resulting in accelerated Aβ deposition [43–49].”
Autophagy Modulation in Disease Therapy: Where Do We Stand?
Nelson, M. P., & Shacka, J. J. (2013) · Current Pathobiology Reports · doi:10.1007/s40139-013-0032-9 · Cited by 17
Convergence of Synapses, Endosomes, and Prions in the Biology of Neurodegenerative Diseases
Gouras, G. K. (2013) · International Journal of Cell Biology · doi:10.1155/2013/141083 · Cited by 17
“A more recent development in research on neurodegenerative diseases is the surprising realization that other disease-linked aggregation prone proteins, such as Aβ [46, 47],α-synuclein [48, 49], and tau [29], can also propagate in experimental systems.”
BackgroundOlfactory bulb integrity in frontotemporal dementia and Alzheimer’s disease
Carnemolla, S. E., Kumfor, F., Liang, C. T., Foxe, D., Ahmed, R. M., & Piguet, O. (2022) · Journal of Alzheimer’s Disease · doi:10.3233/jad-220080 · Cited by 16
Goñi, F., Martá-Ariza, M., Peyser, D. K., Herline, K., & Wısnıewskı, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-10393-z · Cited by 16
AA amyloid in human food chain is a possible biohazard
Rising, A., Gherardi, P., Chen, G., Johansson, J., Oskarsson, M. E., Westermark, G. T., & Westermark, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-00588-w · Cited by 16
García-García, A., Rojas, S., & Rodríguez‐Diéguez, A. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb00427a · Cited by 16
Fan, X., Zhang, X., Yan, J., Xu, H., Zhao, W., Ding, F., Huang, F., & Sun, Y. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c00859 · Cited by 16
Biomarker evidence for uncoupling of amyloid build‐up and toxicity in Alzheimer's disease
Zetterberg, H., & Blennow, K. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.07.002 · Cited by 16
“This cascade may be initiated by high concentrations of misfolded Ab within cellular compartments [28] or from extracellular seeds [27].”
BackgroundTime is of the essence: microRNAs and age-associated neurodegeneration
Aw, S., & Cohen, S. M. (2012) · Cell Research · doi:10.1038/cr.2012.59 · Cited by 16
Phosphoinositides: Two-Path Signaling in Neuronal Response to Oligomeric Amyloid β Peptide
Uranga, R. M., Alza, N. P., Conde, M. A., Antollini, S. S., & Salvador, G. A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9885-3 · Cited by 16
Li, Y., Yan, L., Cai, J., Zhang, W., Li, L., Du, Z., Dong, C., Meunier, B., & Chen, H. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111585 · Cited by 16
Mass spectrometric studies of the variety of beta‐amyloid proteoforms in Alzheimer's disease
Zakharova, N. V., Kononikhin, A. S., Indeykina, M. I., Bugrova, A. E., Strelnikova, P. A., Игоревич, П. С., Kozin, S. A., Popov, I. A., Mitkevich, V. A., Makarov, A. А., et al. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21775 · Cited by 16
Li, J.-M., Xue, Z.-Q., Deng, S.-H., Luo, X.-G., Patrylo, P. R., Rose, G. W., Cai, H., Cai, Y., & Yan, X.-X. (2013) · Neurotoxicity Research · doi:10.1007/s12640-012-9355-2 · Cited by 16
“Because of their amphiphilic nature, Ab peptides tend to aggregate into large insoluble forms leading to the formation of extracellular plaques, a hallmark neuropathology in Alzheimer’s disease (AD) (Braak et al. 2011; Jucker and Walker 2011).”
Natale, G., Pompili, E., Biagioni, F., Paparelli, S., Lenzi, P., & Fornai, F. (2013) · European Journal of Histochemistry · doi:10.4081/ejh.2013.e5 · Cited by 16
Gilson, V., Mbebi, C., Sellal, F., & de Barry, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142529 · Cited by 17
“It has been suggested similarities between prion diseases and AD involving intracellular transport of misfolded particles [49, 50] before”
BackgroundSabaté, R. (2014) · Prion · doi:10.4161/19336896.2014.968464 · Cited by 14
Simonetti, F., Zhong, W., Hutten, S., Uliana, F., Schifferer, M., Rezaei, A., Ramirez, L. M., Hochmair, J., Sankar, R., Gopalan, A. B., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00590-2 · Cited by 22
“These mechanisms give rise to the stereotypical spreading of protein aggregates throughout the brain, which has been observed for the prion protein (PrP), Tau, α - synuclein and TDP-43 (Dujardin and Hyman, 2019; Jucker and Walker, 2011; Polymenidou and Cleveland, 2011; Uemura et al, 2020).”
WNT/β-catenin Pathway: a Possible Link Between Hypertension and Alzheimer’s Disease
Vallée, A., Vallée, J.-N., & Lecarpentier, Y. (2022) · Current Hypertension Reports · doi:10.1007/s11906-022-01209-1 · Cited by 16
Mutant α-synuclein propagates via the lymphatic system of the brain in the monomeric state
Fujita, K., Homma, H., Jin, M., Yoshioka, Y., Jin, X., Saito, Y., Tanaka, H., & Okazawa, H. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112962 · Cited by 14
Preventing the Spread of Alzheimer’s Disease Neuropathology: A Role for Calcilytics?
Chiarini, A., Gardenal, E., Whitfield, J., Chakravarthy, B., Armato, U., & Prà, I. D. (2015) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201016666150505123813 · Cited by 14
Spreading of Pathology in Alzheimer’s Disease
Lv, Z., Tan, C., Yu, J., & Tan, L. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9765-2 · Cited by 15
“The typical changes of AD in histopathology are neuritic plaque (senile plaques), NFTs, neuronal loss, and gliosis, and usually AD is characterized with the progressive cognitive disorder and behavior impairment (Jucker and Walker 2011).”
BackgroundInfluentialZhao, H., Li, S., Li, Z., Yang, S., Li, D., Zheng, J., Gao, H., Yun, L., Gu, Y., Li, L., et al. (2020) · Aging · doi:10.18632/aging.102970 · Cited by 15
“Alzheimer's disease (AD), the most prevalent neurodegenerative disorder, is characterized by the presence of extracellular amyloid plaques composed of amyloid-β (Aβ) and intracellular neurofibrillary tangles [1, 2].”
BackgroundProtein Microgels from Amyloid Fibril Networks
Roode, L. W. Y., Shimanovich, U., Wu, S., Perrett, S., & Knowles, T. P. J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9791-2_7 · Cited by 16
The Role of α-sheet in Amyloid Oligomer Aggregation and Toxicity.
Bi, T., & Daggett, V. (2018) · Europe PMC (PubMed Central) · Cited by 16
Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease
Kozin, S. A. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923140055 · Cited by 14
“It is commonly recognized that conformational transformation and aggregation of the monomeric Aβ molecules occur via a seeding mechanism [33-35].”
BackgroundSynthesis and functional survey of new Tacrine analogs modified with nitroxides or their precursors
Kálai, T., Altman, R., Maezawa, I., Balog, M., Morisseau, C. H. P., Petrlová, J., Hammock, B. D., Jin, L., Trudell, J. R., Voss, J. C., et al. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.03.026 · Cited by 14
Exploring the Potential of Neuroproteomics in Alzheimer's Disease
Uddin, M. S., Kabir, M. T., Jakaria, M., Sobarzo‐Sánchez, E., Barreto, G. E., Perveen, A., Hafeez, A., Bin-Jumah, M. N., Abdel‐Daim, M. M., & Ashraf, G. M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200603112030 · Cited by 17
Lin, M.-S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00260 · Cited by 17
“Conformational changes in these proteins are resistant to proteolysis resulting in the formation of so-called inclusion bodies in the brain (Jucker and Walker, 2011).”
BackgroundContext dependence of protein misfolding and structural strains in neurodegenerative diseases
Mehta, A. K., Rosen, R. F., Childers, W. S., Gehman, J. D., Walker, L. C., & Lynn, D. G. (2013) · Biopolymers · doi:10.1002/bip.22283 · Cited by 14
Self-citationSteinacker, P., Berner, C., Thal, D. R., Attems, J., Ludolph, A. C., & Otto, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0130-x · Cited by 14
“synucleopathies and Alzheimer’s disease [21-24].”
Benarroch, E. E. (2023) · Neurology · doi:10.1212/wnl.0000000000206736 · Cited by 12
Liu, X., TYLER, L. K., Cam‐CAN, Davis, S. W., Rowe, J. B., & Tsvetanov, K. A. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.06.001 · Cited by 17
Choi, Y., Kim, S.-M., Heo, Y., Lee, G., Kang, J. Y., & Yoon, D. S. (2020) · Nanotechnology · doi:10.1088/1361-6528/abba58 · Cited by 13
Macha, B., Kulkarni, R., Bagul, C., Garige, A. K., Akkinepally, R. R., & Garlapati, A. (2021) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02670-w · Cited by 13
The Evolution of Functional Amyloids and Their Impact on Host–Microbe Interactions
Kolli, D., Rout, S. K., Riek, R., & Chapman, M. R. (2025) · Advanced Science · doi:10.1002/advs.202510109 · Cited by 17
Updated insights on ASK1 signaling: mechanisms, regulation, and therapeutic potential in diseases
Thakur, D., Nandi, A., Gaur, Y. K., Chandrabose, K., Waiker, D. K., Gupta, G. D., & Sharma, K. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05330-y · Cited by 13
“Through this information, we come to know that ASK1 plays a key role in the pathogenesis of AD [173].”
Yaguchi, H., Takeuchi, A., Horiuchi, K., et al. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.10.038 · Cited by 12
Role of viruses, prions and miRNA in neurodegenerative disorders and dementia
Sohrab, S. S., Suhail, M., Ali, A., Kamal, M. A., Husen, A., Ahmad, F., Azhar, E. I., & Greig, N. H. (2018) · VirusDisease · doi:10.1007/s13337-018-0492-y · Cited by 12
Scialò, C., & Legname, G. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.008 · Cited by 12
Aryl Diazonium Chemistry for the Surface Functionalization of Glassy Biosensors
Zheng, W., van den Hurk, R., Cao, Y., et al. (2016) · Biosensors · doi:10.3390/bios6010008 · Cited by 12
“Prions play a significant role in diseases, such as the Creutzfeldt-Jakob disease and transmissible spongiform encephalopathies [8,9].”
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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