ReviewMolecular neurobiology2007
Heat shock proteins and amateur chaperones in amyloid-Beta accumulation and clearance in Alzheimer's disease.
Review in Molecular neurobiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
45 citing papers in PubMed.
- Protein Modifications and Quality Control System: Target for Alzheimer's Disease Therapy.International journal of molecular sciences · 2026Review
- Diverse influences on tau aggregation and implications for disease progression.Genes & development · 2025Review
- Endocytic Pathways Unveil the Role of Syndecans in the Seeding and Spreading of Pathological Protein Aggregates: Insights into Neurodegenerative Disorders.International journal of molecular sciences · 2025Review
- Article
- Readdressing the Localization of Apolipoprotein E (APOE) in Mitochondria-Associated Endoplasmic Reticulum (ER) Membranes (MAMs): An Investigation of the Hepatic Protein-Protein Interactions of APOE with the Mitochondrial Proteins Lon Protease (LONP1), Mitochondrial Import Receptor Subunit TOM40 (TOMM40) and Voltage-Dependent Anion-Selective Channel 1 (VDAC1).International journal of molecular sciences · 2024Article
- From Small Peptides to Large Proteins against Alzheimer'sDisease.Biomolecules · 2022Review
- Patient-Derived Fibroblasts With Presenilin-1 Mutations, That Model Aspects of Alzheimer's Disease Pathology, Constitute a Potential Object for Early Diagnosis.Frontiers in aging neuroscience · 2022Article
- Human stefin B: from its structure, folding, and aggregation to its function in health and disease.Frontiers in molecular neuroscience · 2022Review
- Trichostatin A ameliorates Alzheimer's disease-related pathology and cognitive deficits by increasing albumin expression and Aβ clearance in APP/PS1 mice.Alzheimer's research & therapy · 2021Article
- High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90.The Journal of biological chemistry · 2020Article
- Comprehensive Review on Alzheimer's Disease: Causes and Treatment.Molecules (Basel, Switzerland) · 2020Review
- Increased levels of Stress-inducible phosphoprotein-1 accelerates amyloid-β deposition in a mouse model of Alzheimer's disease.Acta neuropathologica communications · 2020Article
- Exploring the Promise of Targeting Ubiquitin-Proteasome System to Combat Alzheimer's Disease.Neurotoxicity research · 2020Review
- Histidyl-Proline Diketopiperazine Isomers as Multipotent Anti-Alzheimer Drug Candidates.Biomolecules · 2020Article
- Structural Interaction of Apolipoprotein A-I Mimetic Peptide with Amyloid-β Generates Toxic Hetero-oligomers.Journal of molecular biology · 2020Article
- Genomic Variation, Evolvability, and the Paradox of Mental Illness.Frontiers in psychiatry · 2020Article
- Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins.European biophysics journal : EBJ · 2017Article
- The blood-brain barrier in Alzheimer's disease.Neurobiology of disease · 2017Review
- The amyloid interactome: Exploring protein aggregation.PloS one · 2017Article
- Cystatin C in aging and in Alzheimer's disease.Ageing research reviews · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pathologic lesions of Alzheimer's disease (AD) are characterized by accumulation of protein aggregates consisting of intracellular or extracellular misfolded proteins. The amyloid-beta (Abeta) protein accumulates extracellularly in senile plaques and cerebral amyloid angiopathy, whereas the hyperphosphorylated tau protein accumulates intracellularly as neurofibrillary tangles. "Professional chaperones", such as the heat shock protein family, have a function in the prevention of protein misfolding and subsequent aggregation. "Amateur" chaperones, such as apolipoproteins and heparan sulfate proteoglycans, bind amyloidogenic proteins and may affect their aggregation process. Professional and amateur chaperones not only colocalize with the pathological lesions of AD, but may also be involved in conformational changes of Abeta, and in the clearance of Abeta from the brain via phagocytosis or active transport across the blood-brain barrier. Thus, both professional and amateur chaperones may be involved in the aggregation, accumulation, persistence, and clearance of Abeta and tau and in other Abeta-associated reactions such as inflammation associated with AD lesions, and may, therefore, serve as potential targets for therapeutic intervention.
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