Evidence map›Paper›PMID 22489141›Full record

ReviewInternational journal of molecular sciences2012

Unraveling the early events of amyloid-β protein (Aβ) aggregation: techniques for the determination of Aβ aggregate size.

N Elizabeth Pryor, Melissa A Moss, Christa N Hestekin

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Polyallylamine Binds to Aβ Amyloid and Inhibits Antibody Recognition.International journal of molecular sciences · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. AβACS chemical neuroscience · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Sensors and actuators. B, Chemical · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors.

N Elizabeth PryorRalph E. Martin Department of Chemical Engineering, 3202 Bell Engineering Center, University of Arkansas, Fayetteville, AR 72701, USA.
Melissa A MossDepartment of Chemical Engineering, 2C02 Swearingen Engineering Center, University of South Carolina, Columbia, SC 29208, USA.
Christa N HestekinRalph E. Martin Department of Chemical Engineering, 3202 Bell Engineering Center, University of Arkansas, Fayetteville, AR 72701, USA.

Funding

Center for Protein Structure and FunctionP30GM103450 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2012 to 2014
$3.2M
RESEARCH PILOT PROJECT PROGRAMP30RR031154 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI HINTON, JAMES F · 2010 to 2011
$2.2M
NCRR NIH HHS 1P30RR031154-02NCRR NIH HHS P30 RR031154NIGMS NIH HHS P30 GM103450
6 · The paper itself

Abstract

The aggregation of proteins into insoluble amyloid fibrils coincides with the onset of numerous diseases. An array of techniques is available to study the different stages of the amyloid aggregation process. Recently, emphasis has been placed upon the analysis of oligomeric amyloid species, which have been hypothesized to play a key role in disease progression. This paper reviews techniques utilized to study aggregation of the amyloid-β protein (Aβ) associated with Alzheimer's disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric Aβ species formed during the early stages of aggregation, including native-PAGE, SDS-PAGE, Western blotting, capillary electrophoresis, mass spectrometry, fluorescence correlation spectroscopy, light scattering, size exclusion chromatography, centrifugation, enzyme-linked immunosorbent assay, and dot blotting.

Indexed as

Protein Aggregation, PathologicalAlzheimer DiseaseAmyloid beta-PeptidesBlotting, WesternChromatography, GelDisease ProgressionElectrophoresis, CapillaryElectrophoresis, Polyacrylamide GelHumansParticle SizeProtein AggregatesProtein MultimerizationProtein Structure, QuaternaryScattering, RadiationSpectrometry, FluorescenceSpectrometry, Mass, Electrospray IonizationAmyloid beta-PeptidesProtein Aggregatesamyloidcapillary electrophoresiscentrifugationfluorescence correlation spectroscopylight scatteringmass spectrometryoligomerpolyacrylamide gel electrophoresissize exclusion chromatographyWestern blotting

Identifiers

PMID22489141
PMCPMC3317702

What OpenQuestion holds

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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.