Evidence map›Paper›PMID 27810329›Full record

ArticleAnalytical biochemistry2017

Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes.

Eric Y Hayden, Joseph L Conovaloff, Ashley Mason, Gal Bitan, David B Teplow

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytical biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
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  10. Review
  11. Article
  12. Energetics of cosolvent effect on peptide aggregation.Biophysics and physicobiology · 2019
    Review
  13. Article
  14. Article
  15. The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018
    Review
  16. Article
  17. 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

5 authors.

Eric Y HaydenDepartment of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095, United States.
Joseph L ConovaloffDepartment of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095, United States.
Ashley MasonDepartment of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095, United States.
Gal BitanDepartment of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095, United States.
David B TeplowDepartment of Neurology, David Geffen School of Medicine, and Molecular Biology Institute and Brain Research Institute, University of California, Los Angeles, CA 90095, United States. Electronic address: dteplow@mednet.ucla.edu.

Funding

PROTEIN CHEMISTRY COREP01AG027818 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 2006 to 2010
$7.6M
STRUCTURAL/KINETIC ANALYSIS OF ABETA FIBRILLOGENESISR01NS038328 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 1999 to 2014
$4.0M
3D Structure of Amyloid beta-Protein AssembliesR01AG018921 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 2002 to 2006
$1.9M
Physical Biochemistry and Biology of Amyloid Beta-ProteinR01AG041295 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 2011 to 2015
$1.6M
NIA NIH HHS P01 AG027818NIA NIH HHS R01 AG018921NIA NIH HHS R01 AG041295NINDS NIH HHS R01 NS038328
6 · The paper itself

Abstract

Evidence suggests that amyloid β-protein (Aβ) oligomers may be seminal pathogenic agents in Alzheimer's disease (AD). If so, developing oligomer-targeted therapeutics requires an understanding of oligomer structure. This has been difficult due to the instability of these non-covalently associated Aβ assemblies. We previously used rapid, zero-length, in situ chemical cross-linking to stabilize oligomers of Aβ40. These enabled us to isolate pure, stable populations of dimers, trimers, and tetramers and to determine their structure-activity relationships. However, equivalent methods applied to Aβ42 did not produce stable oligomers. We report here that the use of an Aβ42 homologue, [F10, Y42]Aβ42, coupled with sequential denaturation/dissociation and gel electrophoresis procedures, provides the means to produce highly pure, stable populations of oligomers of sizes ranging from dimer through dodecamer that are suitable for structure-activity relationship determination.

Indexed as

Amyloid beta-PeptidesHumansPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide FragmentsAlzheimer's diseaseAmyloid β-proteinIsolationOligomersProtein functionProtein structure

Identifiers

PMID27810329
PMCPMC5474095

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Registered trials

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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.