Evidence map›Paper›PMID 25888324›Full record

ReviewMolecular brain2015

Glutamate receptors function as scaffolds for the regulation of β-amyloid and cellular prion protein signaling complexes.

Alison Hamilton, Gerald W Zamponi, Stephen S G Ferguson

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Molecular brain, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  8. PET molecular imaging for pathophysiological visualization in Alzheimer's disease.European journal of nuclear medicine and molecular imaging · 2023
    Review
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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.

Alison HamiltonJ. Allyn Taylor Centre for Cell Biology, Robarts Research Institute, University of Western Ontario, 100 Perth Dr, London, Ontario, N6A 5 K8, Canada. ahamil58@uwo.ca.
Gerald W ZamponiDepartment of Physiology & Pharmacology, Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada. Zamponi@ucalgary.ca.
Stephen S G FergusonJ. Allyn Taylor Centre for Cell Biology, Robarts Research Institute, University of Western Ontario, 100 Perth Dr, London, Ontario, N6A 5 K8, Canada. ferguson@robarts.ca.
Western University · CAUniversity of Calgary · CA

Funding

Canadian Institutes of Health Research MOP-119437
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a progressive neurodegenerative disorder that affects 36 million people worldwide, but currently has no effective treatment options. One of the original hallmarks of AD are plaques comprised of beta amyloid (Aβ) and neurofibrillary tangles comprised of phosphorylated Tau protein. However, it is soluble oligomeric Aβ which is more closely correlated with cognitive decline and is therefore considered to be the neurotoxic species. Oligomeric Aβ has recently been shown to form complexes with the glycosylphosphatidylinositol (GPI)-anchored membrane protein, cellular prion protein (PrP(c)), and these complexes are believed to play an important role in the progression of AD pathogenesis. Glutamate, the major excitatory neurotransmitter is responsible for mediating learning and memory under normal physiological conditions. However, the dysregulation of glutamatergic signaling has also been implicated in a number of neurodegenerative diseases including AD. Glutamate acts via both ionotropic glutamate receptors (iGluR) and metabotropic glutamate receptors (mGluR), each of which have been implicated in AD. There is now growing evidence to suggest that mGluR5 may contribute the AD pathogenesis by acting as scaffolds for the PrP(c)/Aβ oligomer complex, enabling the propagation of neurotoxic signaling in AD. In addition, PrP(c) and Aβ oligomer signaling via NMDARs may also contribute to AD pathology. The current review overviews our current understanding of the role of PrP(c) and Aβ oligomers in regulating glutamate receptor signaling, as well as highlights the importance of understanding these signaling complexes to develop more effective therapeutic strategies to treat AD.

Indexed as

Signal TransductionAmyloid beta-PeptidesAnimalsHumansModels, BiologicalPrPC ProteinsReceptors, GlutamateReceptors, N-Methyl-D-AspartateAmyloid beta-PeptidesPrPC ProteinsReceptors, GlutamateReceptors, N-Methyl-D-Aspartate

Identifiers

PMID25888324
PMCPMC4395978
OpenAlexW2169763883

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.