Evidence map›Paper›PMID 27917876›Full record

ArticleScientific reports2016

Soluble Amyloid-beta Aggregates from Human Alzheimer's Disease Brains.

Thomas J Esparza, Norelle C Wildburger, Hao Jiang, Mihika Gangolli, Nigel J Cairns, Randall J Bateman, David L Brody

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
8.8field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.

  1. Utility of cortical tissue analysis in normal pressure hydrocephalus.Cerebral cortex (New York, N.Y. : 1991) · 2024
    Pooled it
  2. Article
  3. Anti-amyloid antibody equilibrium binding to Aβ aggregates from human Alzheimer's disease brain.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
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  9. Article
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  16. Article
  17. Structural polymorphism and cytotoxicity of brain-derived β-amyloid extracts.Protein science : a publication of the Protein Society · 2023
    Review
  18. Review
  19. Review
  20. Review

17 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Thomas J EsparzaDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
Norelle C WildburgerDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
Hao JiangDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
Mihika GangolliDepartment of Biomedical Engineering, Washington University, St. Louis, Missouri, USA.
Nigel J CairnsDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
Randall J BatemanDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
David L BrodyDepartment of Neurology, 660 South Euclid Avenue, Box 8111, Washington University, St. Louis, Missouri, USA.
Washington University in St. Louis · US

Funding

Smartphone-Based "Burst" Cognitive AssessmentsP01AG003991 · NIA · WASHINGTON UNIVERSITY · PI Tammie Lee Smith Benzinger · 1985 to 2026
$69.5M
WASHINGTON UNIVERSITY ALZHEIMERS DISEASE RESEARCH CENTERP50AG005681 · NIA · WASHINGTON UNIVERSITY · PI MORRIS, JOHN · 1985 to 2019
$52.1M
The natural history of AB accumulation in preclinical ADP01AG026276 · NIA · WASHINGTON UNIVERSITY · PI SCHINDLER, SUZANNE ELIZABETH · 2005 to 2025
$49.5M
Mechanisms Underlying Tauopathy Following Traumatic Brain InjuryR01NS065069 · NINDS · WASHINGTON UNIVERSITY · PI BRODY, DAVID L · 2009 to 2017
$3.3M
NIA NIH HHS P01 AG003991NIA NIH HHS P01 AG026276NIA NIH HHS P50 AG005681NINDS NIH HHS R01 NS065069
6 · The paper itself

Abstract

Soluble amyloid-beta (Aβ) aggregates likely contribute substantially to the dementia that characterizes Alzheimer's disease. However, despite intensive study of in vitro preparations and animal models, little is known about the characteristics of soluble Aβ aggregates in the human Alzheimer's disease brain. Here we present a new method for extracting soluble Aβ aggregates from human brains, separating them from insoluble aggregates and Aβ monomers using differential ultracentrifugation, and purifying them >6000 fold by dual antibody immunoprecipitation. The method resulted in <40% loss of starting material, no detectible ex vivo aggregation of monomeric Aβ, and no apparent ex vivo alterations in soluble aggregate sizes. By immunoelectron microscopy, soluble Aβ aggregates typically appear as clusters of 10-20 nanometer diameter ovoid structures with 2-3 amino-terminal Aβ antibody binding sites, distinct from previously characterized structures. This approach may facilitate investigation into the characteristics of native soluble Aβ aggregates, and deepen our understanding of Alzheimer's dementia.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBrainBrain ChemistryFemaleHumansMaleProtein Aggregation, PathologicalSolubilityAmyloid beta-Peptides

Identifiers

PMID27917876
PMCPMC5137165
OpenAlexW2560590017

What OpenQuestion holds

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LicenceCC BY
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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.