ReviewJournal of molecular medicine (Berlin, Germany)2013
The role of amyloidogenic protein oligomerization in neurodegenerative disease.
Review in Journal of molecular medicine (Berlin, Germany), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Lysine-Targeting Inhibitors of Amyloidogenic Protein Aggregation: A Promise for Neurodegenerative Proteinopathies.JACS Au · 2025Review
- Development and Implementation of an Internal Quality Control Sample to Standardize Oligomer-Based Diagnostics of Alzheimer's Disease.Diagnostics (Basel, Switzerland) · 2023Article
- Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.Scientific reports · 2021Article
- Understanding and controlling amyloid aggregation with chirality.Current opinion in chemical biology · 2021Review
- Article
- Lipid Membranes Influence the Ability of Small Molecules To Inhibit Huntingtin Fibrillization.Biochemistry · 2019Article
- Effect of Varying Concentrations of Docosahexaenoic Acid on Amyloid Beta (1⁻42) Aggregation: An Atomic Force Microscopy Study.Molecules (Basel, Switzerland) · 2018Article
- Sphingomyelin and GM1 Influence Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.ACS omega · 2018Article
- AmyPro: a database of proteins with validated amyloidogenic regions.Nucleic acids research · 2018Article
- Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.Journal of molecular biology · 2017Article
- Review
- Multiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington's disease model system.Scientific reports · 2016Article
- Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation.Nature structural & molecular biology · 2015Article
- Standardization and quality control in quantifying non-enzymatic oxidative protein modifications in relation to ageing and disease: Why is it important and why is it hard?Redox biology · 2015Review
- Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism.Biomolecules · 2015Article
- Evaluation of Nanoparticle Tracking for Characterization of Fibrillar Protein Aggregates.AIChE journal. American Institute of Chemical Engineers · 2014Article
- Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell.The Journal of biological chemistry · 2014Article
- Understanding neuronal dysfunction and loss in neurodegenerative disease.Journal of molecular medicine (Berlin, Germany) · 2013Article
- On the subject of rigor in the study of amyloid β-protein assembly.Alzheimer's research & therapy · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A common pathological hallmark in many neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease, is the formation of fibrillar protein aggregates referred to as amyloids. The amyloidogenic aggregates were long thought to be toxic, but mounting evidence supports the notion that a variety of amyloid aggregate intermediates to fibril formation, termed oligomers, may in fact be the primary culprit leading to neuronal dysfunction and cell death. While amyloid formation is a complex, heterogeneous process, aggregates formed by diverse, diseases-related proteins share many conformational similarities, suggesting common toxic mechanisms among these diseases. Ideally, similar therapeutic strategies may be applicable. This review focuses on the potential role of amyloidogenic oligomers in neurodegenerative disease, highlighting some promising therapeutic strategies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.