Evidence map›Paper›PMID 20642866›Full record

ArticleAlzheimer's research & therapy2010

The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?

Kerensa Broersen, Frederic Rousseau, Joost Schymkowitz

Open access · goldAbstract read
In one paragraph

Article in Alzheimer's research & therapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 169 citations in OpenAlex.

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  6. Exploring the AβFrontiers in molecular biosciences · 2024
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  12. Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane.Proceedings of the National Academy of Sciences of the United States of America · 2021
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1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kerensa BroersenSwitch Laboratory, Flanders Institute for Biotechnology (VIB) and Vrije Universiteit Brussel (VUB), Pleinlaan 2, Brussels 1050, Belgium. kbroerse@vub.ac.be.
Frederic Rousseau
Joost Schymkowitz
Vrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many researchers refocused on detecting a specific molecular assembly of defined size thatis the main trigger of Alzheimer's disease. The result has been the identification of a host of molecular assemblies containing from two up to a hundred molecules of the amyloid beta peptide, which were all found to impair memory formation in mice. This clearly demonstrates that size is insufficient to define toxicity and peptide conformation has to be taken into account. In this review we discuss the interplay between oligomer size and peptide conformation as the key determinants of the neurotoxicity of the amyloid beta peptide.

Identifiers

PMID20642866
PMCPMC2949586
OpenAlexW2165292497

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.