Evidence map›Paper›PMID 21268584›Full record

ArticleBiochemistry2011

A kinetic aggregation assay allowing selective and sensitive amyloid-β quantification in cells and tissues.

Deguo Du, Amber N Murray, Ehud Cohen, Hyun-Eui Kim, Ryan Simkovsky, Andrew Dillin, Jeffery W Kelly

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Mucin-TypeFrontiers in chemistry · 2022
    Article
  3. Perspectives on theToxins · 2021
    Review
  4. Review
  5. Review
  6. Review
  7. Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016
    Review
  8. Conversion of Synthetic Aβ to In Vivo Active Seeds and Amyloid Plaque Formation in a Hippocampal Slice Culture Model.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  9. Article
  10. Article
  11. Article
  12. Proteopathic tau seeding predicts tauopathy in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Mechanisms of transthyretin inhibition of β-amyloid aggregation in vitro.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  14. Article
  15. Article
  16. Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  17. Review
  18. Soluble Aβ seeds are potent inducers of cerebral β-amyloid deposition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
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

7 authors.

Deguo DuHoward Hughes Medical Institute, Molecular and Cell Biology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, United States.
Amber N Murray
Ehud Cohen
Hyun-Eui Kim
Ryan Simkovsky
Andrew Dillin
Jeffery W Kelly

Funding

TRAFFICKING AND ABETA AGGREGATIONP01AG031097 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2009 to 2013
$10.2M
NIA NIH HHS AG031097NIA NIH HHS P01 AG031097
6 · The paper itself

Abstract

The process of amyloid-β (Aβ) fibril formation is genetically and pathologically linked to Alzheimer's disease (AD). Thus, a selective and sensitive method for quantifying Aβ fibrils in complex biological samples allows a variety of hypotheses to be tested. Herein, we report the basis for a quantitative in vitro kinetic aggregation assay that detects seeding-competent Aβ aggregates in mammalian cell culture media, in Caenorhabditis elegans lysate, and in mouse brain homogenate. Sonicated, proteinase K-treated Aβ fibril-containing tissue homogenates or cell culture media were added to an initially monomeric Aβ(1-40) reporter peptide to seed an in vitro nucleated aggregation reaction. The reduction in the half-time (t(50)) of the amyloid growth phase is proportional to the quantity of seeding-competent Aβ aggregates present in the biological sample. An ion-exchange resin amyloid isolation strategy from complex biological samples is demonstrated as an alternative for improving the sensitivity and linearity of the kinetic aggregation assay.

Indexed as

AmyloidAmyloid beta-PeptidesAnimalsBrain ChemistryCaenorhabditis elegansEndopeptidase KKineticsMicePeptide FragmentsAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Endopeptidase KPeptide Fragments

Identifiers

PMID21268584
PMCPMC3051019

What OpenQuestion holds

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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.