Evidence map›Paper›PMID 9065490›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997

Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia.

D R McDonald, K R Brunden, G E Landreth

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
7.4field-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

112 citing papers in PubMed, 317 citations in OpenAlex.

  1. β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026
    Review
  2. Alterations in the inflammatory homeostasis of aging-related cardiac dysfunction and Alzheimer's diseases.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
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  12. [EJNMMI research · 2022
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  18. Chronic copper exposure directs microglia towards degenerative expression signatures in wild-type and J20 mouse model of Alzheimer's disease.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2020
    Article
  19. Article
  20. Review

52 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

3 authors at 2 institutions in 1 country.

D R McDonaldAlzheimer Research Laboratory, Department of Neurology and Neurosciences, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
K R Brunden
G E Landreth
Case Western Reserve University · USUniversity School · US

Funding

VISUAL DYSFUNCTIONS IN ALZHEIMER'S DISEASEP50AG008012 · NIA · CASE WESTERN RESERVE UNIVERSITY · PI HERRUP, KARL · 1988 to 2005
$11.1M
NIA NIH HHS AG08012NIA NIH HHS P50 AG008012
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a devastating neurological disorder characterized by loss of cognitive skills and progressive dementia. The pathological hallmark of AD is the presence of numerous senile plaques throughout the hippocampus and cerebral cortex associated with degenerating axons, neurofibrillary tangles, and gliosis. The core of the senile plaque primarily is composed of the 39-43 amino acid beta-amyloid peptide (Abeta), which forms fibrils of beta-pleated sheets. Although considerable genetic evidence implicates Abeta in the pathogenesis of AD, a direct causal link remains to be established. Senile plaques are foci of local inflammatory processes, as evidenced by the presence of numerous activated microglia and acute phase proteins. Abeta has been shown to elicit inflammatory responses in microglia; however, the intracellular events mediating these effects are largely unknown. We report that exposure of microglia and THP1 monocytes to fibrillar Abeta led to time- and dose-dependent increases in protein tyrosine phosphorylation of a population of proteins similar to that elicited by classical immune stimuli such as immune complexes. The tyrosine kinases Lyn, Syk, and FAK were activated on exposure of microglia and THP1 monocytes to Abeta, resulting in the tyrosine kinase-dependent generation of superoxide radicals. The present data support a role for oxidative damage in the pathogenesis of AD, provide an important mechanistic link between Abeta and the generation of reactive oxygen intermediates, and identify molecular targets for therapeutic intervention in AD.

Indexed as

Amyloid beta-PeptidesEnzyme PrecursorsHumansIntracellular Signaling Peptides and ProteinsKineticsMicrogliaMonocytesPeptide FragmentsPhosphoproteinsPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgGSignal TransductionSuperoxidesSyk KinaseTumor Cells, CulturedAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (25-35)Enzyme PrecursorsIntracellular Signaling Peptides and ProteinsPeptide FragmentsPhosphoproteinsPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgGSuperoxidesSyk KinaseSYK protein, human

Identifiers

PMID9065490
PMCPMC6573513
OpenAlexW2159027833

What OpenQuestion holds

Textmetadata
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.