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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Christian Haass, Dennis J. Selkoe. Nature Reviews Molecular Cell Biology, 2007-01-24
Topic: Amyloid, tau and blood-test diagnosis
This article discusses how distinct protein aggregates found in various neurodegenerative disorders appear to cause these conditions. It explains that small soluble oligomers during the aggregation process can cause synaptic dysfunction, while large insoluble deposits may act as reservoirs. These concepts are illustrated by Alzheimer's disease, where specific protein oligomers negatively impact synaptic structure and plasticity. Furthermore, findings across other neurodegenerative diseases suggest that a similar neuronal dysfunction is driven by diffusible oligomers of misfolded proteins.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Haass, C., & Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm2101
Vancouver
Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nature Reviews Molecular Cell Biology. 2007. doi:10.1038/nrm2101. PMID: 17245412.
BibTeX
@article{haass2007-17245412,
author = {Haass, Christian and Selkoe, Dennis J.},
title = {{Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide}},
journal = {Nature Reviews Molecular Cell Biology},
year = {2007},
doi = {10.1038/nrm2101},
pmid = {17245412},
url = {https://doi.org/10.1038/nrm2101}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
Key findings
- Small intermediates - soluble oligomers - in the aggregation process can confer synaptic dysfunction, whereas large, insoluble deposits might function as reservoirs of the bioactive oligomers.
- Amyloid beta-protein oligomers adversely affect synaptic structure and plasticity.
- Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.
Why it matters
A review of soluble protein oligomers in neurodegeneration, drawing lessons from the Alzheimer's amyloid beta peptide.
How this study scored 53/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it. We have no data on strength of evidence, so that was left out: it earned 50 of the 95 points we could judge it on, which is 53 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Nature Reviews Molecular Cell Biology) |
| Journal's citation record | 4 / 4 | Nature Reviews Molecular Cell Biology: journal h-index 622 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | — / 5 | No evidence rating recorded — left out of this score |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2007 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 7 / 7 | Cited 4,746 times (OpenAlex, 2026-10-10) |
| Citations per year | 5 / 5 | 226.0 citations a year over 21 year(s) since 2007 |
| Impact for its field and year | 4 / 6 | Cited 18.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 4 / 4 | Cited 461 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Dennis J. Selkoe: h-index 174 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Ludwig-Maximilians-Universität München: institution h-index 1,224 (OpenAlex) |
| Multicenter collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 17245412) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 50 / 95 | Scored on 19 of 20 parts. We have no data for the rest, so they are left out: 50 of the 95 points we could judge it on is 53 out of 100. |
| Total | 53 / 100 | — |
What each of these 20 components measures, and what this score is not →
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