Evidence map›Paper›PMID 22736768›Full record

ArticleThe Journal of biological chemistry2012

Specific recognition of biologically active amyloid-β oligomers by a new surface plasmon resonance-based immunoassay and an in vivo assay in Caenorhabditis elegans.

Matteo Stravalaci, Antonio Bastone, Marten Beeg, Alfredo Cagnotto, Laura Colombo, Giuseppe Di Fede, Fabrizio Tagliavini, Laura Cantù, Elena Del Favero, Michele Mazzanti and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-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

27 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. Article
  4. Article
  5. Neurodegeneration-related genes influencemicroPublication biology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Brain sciences · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers.Journal of Alzheimer's disease : JAD · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

14 authors at 4 institutions in 1 country.

Matteo StravalaciDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri, 20156 Milan, Italy.
Antonio Bastone
Marten Beeg
Alfredo Cagnotto
Laura Colombo
Giuseppe Di Fede
Fabrizio Tagliavini
Laura Cantù
Elena Del Favero
Michele Mazzanti
Roberto Chiesa
Mario Salmona
Luisa Diomede
Marco Gobbi
Mario Negri Institute for Pharmacological Research · ITUniversity of Milan · ITFondazione IRCCS Istituto Neurologico Carlo Besta · ITDulbecco Telethon Institute · IT

Funding

Telethon GGP10120
6 · The paper itself

Abstract

Soluble oligomers of the amyloid-β (Aβ) peptide play a key role in the pathogenesis of Alzheimer's disease, but their elusive nature makes their detection challenging. Here we describe a novel immunoassay based on surface plasmon resonance (SPR) that specifically recognizes biologically active Aβ oligomers. As a capturing agent, we immobilized on the sensor chip the monoclonal antibody 4G8, which targets a central hydrophobic region of Aβ. This SPR assay allows specific recognition of oligomeric intermediates that rapidly appear and disappear during the incubation of synthetic Aβ(1-42), discriminating them from monomers and higher order aggregates. The species recognized by SPR generate ionic currents in artificial lipid bilayers and inhibit the physiological pharyngeal contractions in Caenorhabditis elegans, a new method for testing the toxic potential of Aβ oligomers. With these assays we found that the formation of biologically relevant Aβ oligomers is inhibited by epigallocatechin gallate and increased by the A2V mutation, previously reported to induce early onset dementia. The SPR-based immunoassay provides new opportunities for detection of toxic Aβ oligomers in biological samples and could be adapted to study misfolding proteins in other neurodegenerative disorders.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAnimalsAntibodies, Monoclonal, Murine-DerivedCaenorhabditis elegansCaenorhabditis elegans ProteinsSurface Plasmon ResonanceAmyloidAmyloid beta-PeptidesAntibodies, Monoclonal, Murine-DerivedCaenorhabditis elegans Proteins

Identifiers

PMID22736768
PMCPMC3431664
OpenAlexW1968409781

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.