Evidence map›Paper›PMID 38416693›Full record

ArticleACS chemical neuroscience2024

A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions.

Sean Chia, Rodrigo Lessa Cataldi, Francesco Simone Ruggeri, Ryan Limbocker, Itzel Condado-Morales, Katarina Pisani, Andrea Possenti, Sara Linse, Tuomas P J Knowles, Johnny Habchi and 2 more

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
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

12 authors at 2 institutions in 2 countries.

Sean ChiaCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.
Rodrigo Lessa CataldiCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.
Francesco Simone RuggeriCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0002-1232-1907
Ryan LimbockerCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0002-6030-6656
Itzel Condado-MoralesCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0001-7592-4556
Katarina PisaniCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.
Andrea PossentiCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.
Sara LinseDepartment of Biochemistry & Structural Biology, Center for Molecular Protein Science, Lund University, PO box 124, 221 00 Lund, Sweden.ORCID 0000-0001-9629-7109
Tuomas P J KnowlesCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0002-7879-0140
Johnny HabchiCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.
Benedetta ManniniCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0001-6812-7348
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.ORCID 0000-0002-3616-1610
University of Cambridge · GBLund University · SE

Funding

Wellcome Trust
6 · The paper itself

Abstract

Oligomeric assemblies of the amyloid β peptide (Aβ) have been investigated for over two decades as possible neurotoxic agents in Alzheimer's disease. However, due to their heterogeneous and transient nature, it is not yet fully established which of the structural features of these oligomers may generate cellular damage. Here, we study distinct oligomer species formed by Aβ40 (the 40-residue form of Aβ) in the presence of four different metal ions (Al

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesHumansIonsMetalsPeptide FragmentsAmyloid beta-PeptidesIonsMetalsPeptide FragmentsAlzheimer’s diseaseamyloid-β peptidemetal ionsprotein aggregationprotein misfoldingprotein oligomers

Identifiers

PMID38416693
PMCPMC10958495
OpenAlexW4392242863

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.