ArticleFrontiers in aging neuroscience2017
Age-Dependent Protein Aggregation Initiates Amyloid-β Aggregation.
Article in Frontiers in aging neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Viral Induced Oxidative and Inflammatory Response in Alzheimer's Disease Pathogenesis with Identification of Potential Drug Candidates: A Systematic Review using Systems Biology Approach.Current neuropharmacology · 2019Pooled it
- Combating ageing beyond the cell: Emerging roles of extracellular proteostasis.The FEBS journal · 2026Review
- Article
- Chronic Vanadium Exposure Promotes Aggregation of Alpha-Synuclein, Tau and Amyloid Beta in Mouse Brain.Journal of neurochemistry · 2025Article
- Amyloid β accelerates age-related proteome-wide protein insolubility.GeroScience · 2024Article
- Protein fibril aggregation on red blood cells: a potential biomarker to distinguish neurodegenerative diseases from healthy aging.Brain communications · 2024Article
- An adaptive stress response that confers cellular resilience to decreased ubiquitination.Nature communications · 2023Article
- A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.PLoS biology · 2023Article
- An evaluation of aging measures: from biomarkers to clocks.Biogerontology · 2023Review
- Long-Term Effects of SARS-CoV-2 in the Brain: Clinical Consequences and Molecular Mechanisms.Journal of clinical medicine · 2023Review
- New Pathways Identify Novel Drug Targets for the Prevention and Treatment of Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Direct and Indirect Effects of Filamin A on Tau Pathology in Neuronal Cells.Molecular neurobiology · 2023Article
- Computational assessment of the impact of Cu(II) and Al(III) on β-amyloidFrontiers in neuroscience · 2023Article
- Mutant Ataxin-2 Expression in Aged Animals Aggravates Neuropathological Features Associated with Spinocerebellar Ataxia Type 2.International journal of molecular sciences · 2022Article
- The Immune System as a Therapeutic Target for Alzheimer's Disease.Life (Basel, Switzerland) · 2022Review
- Comparative Study of Protein Aggregation Propensity and Mutation Tolerance Between Naked Mole-Rat and Mouse.Genome biology and evolution · 2022Article
- Modeling Alzheimer's Disease inBiomedicines · 2022Review
- Article
- Article
- Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aging is the most important risk factor for neurodegenerative diseases associated with pathological protein aggregation such as Alzheimer's disease. Although aging is an important player, it remains unknown which molecular changes are relevant for disease initiation. Recently, it has become apparent that widespread protein aggregation is a common feature of aging. Indeed, several studies demonstrate that 100s of proteins become highly insoluble with age, in the absence of obvious disease processes. Yet it remains unclear how these misfolded proteins aggregating with age affect neurodegenerative diseases. Importantly, several of these aggregation-prone proteins are found as minor components in disease-associated hallmark aggregates such as amyloid-β plaques or neurofibrillary tangles. This co-localization raises the possibility that age-dependent protein aggregation directly contributes to pathological aggregation. Here, we show for the first time that highly insoluble proteins from aged
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Registered trials
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