Evidence map›Paper›PMID 25604547›Full record

ReviewActa neuropathologica2015

Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.

Kirsten L Viola, William L Klein

Open access · greenAbstract readReview
In one paragraph

Review in Acta neuropathologica, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 339 papers.

0numbers the graph read from it
0cells of the map it votes in
339citing papers in PubMed
30.7field-weighted citation impact, top 1% 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

339 citing papers in PubMed, 606 citations in OpenAlex.

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  4. Preclinical and clinical biomarker studies of CT1812: A novel approach to Alzheimer's disease modification.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2021
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279 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

2 authors at 1 institution in 1 country.

Kirsten L ViolaNeurobiology, Northwestern University, Evanston, IL, 60208, USA.
William L Klein
Northwestern University · US

Funding

Abeta oligomers (ADDLs)in Alzheimers Disease pathologyR01AG022547 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2003 to 2010
$1.9M
ADDLs, synapses & the molecular etiology of Alzheimer's diseaseR01AG029460 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2007 to 2009
$916k
A novel, nanoparticle-based molecular MRI probe for early Alzheimer's diagnosticsR21AG045637 · NIA · NORTHWESTERN UNIVERSITY · PI KLEIN, WILLIAM L · 2014 to 2015
$419k
NIA NIH HHS AG022547NIA NIH HHS AG029460NIA NIH HHS AG045637NIA NIH HHS R01 AG022547NIA NIH HHS R01 AG029460NIA NIH HHS R21 AG045637
6 · The paper itself

Abstract

Protein aggregation is common to dozens of diseases including prionoses, diabetes, Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in understanding the structural basis for these proteinopathies. Precedent for this shift has come from investigation of soluble Aβ oligomers (AβOs), toxins now widely regarded as instigating neuron damage leading to Alzheimer's dementia. Toxic AβOs accumulate in AD brain and constitute long-lived alternatives to the disease-defining Aβ fibrils deposited in amyloid plaques. Key experiments using fibril-free AβO solutions demonstrated that while Aβ is essential for memory loss, the fibrillar Aβ in amyloid deposits is not the agent. The AD-like cellular pathologies induced by AβOs suggest their impact provides a unifying mechanism for AD pathogenesis, explaining why early stage disease is specific for memory and accounting for major facets of AD neuropathology. Alternative ideas for triggering mechanisms are being actively investigated. Some research favors insertion of AβOs into membrane, while other evidence supports ligand-like accumulation at particular synapses. Over a dozen candidate toxin receptors have been proposed. AβO binding triggers a redistribution of critical synaptic proteins and induces hyperactivity in metabotropic and ionotropic glutamate receptors. This leads to Ca(2+) overload and instigates major facets of AD neuropathology, including tau hyperphosphorylation, insulin resistance, oxidative stress, and synapse loss. Because different species of AβOs have been identified, a remaining question is which oligomer is the major pathogenic culprit. The possibility has been raised that more than one species plays a role. Despite some key unknowns, the clinical relevance of AβOs has been established, and new studies are beginning to point to co-morbidities such as diabetes and hypercholesterolemia as etiological factors. Because pathogenic AβOs appear early in the disease, they offer appealing targets for therapeutics and diagnostics. Promising therapeutic strategies include use of CNS insulin signaling enhancers to protect against the presence of toxins and elimination of the toxins through use of highly specific AβO antibodies. An AD-dependent accumulation of AβOs in CSF suggests their potential use as biomarkers and new AβO probes are opening the door to brain imaging. Overall, current evidence indicates that Aβ oligomers provide a substantive molecular basis for the cause, treatment and diagnosis of Alzheimer's disease.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsHumansNeuronsAmyloid beta-Peptides

Identifiers

PMID25604547
PMCPMC4390393
OpenAlexW2055775253

What OpenQuestion holds

Textmetadata
LicenceTDM
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.