Evidence map›Paper›PMID 28344547›Full record

ReviewFrontiers in molecular neuroscience2017

APP Function and Lipids: A Bidirectional Link.

Marcus O W Grimm, Janine Mett, Heike S Grimm, Tobias Hartmann

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 103 citations in OpenAlex.

  1. Trial
  2. Special Issue "Molecular Insight into Alzheimer's Disease".International journal of molecular sciences · 2026
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1 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

4 authors at 1 institution in 1 country.

Marcus O W GrimmExperimental Neurology, Saarland UniversityHomburg/Saar, Germany; Neurodegeneration and Neurobiology, Saarland UniversityHomburg/Saar, Germany; Deutsches Institut für DemenzPrävention (DIDP), Saarland UniversityHomburg/Saar, Germany.
Janine MettExperimental Neurology, Saarland University Homburg/Saar, Germany.
Heike S GrimmExperimental Neurology, Saarland University Homburg/Saar, Germany.
Tobias HartmannExperimental Neurology, Saarland UniversityHomburg/Saar, Germany; Neurodegeneration and Neurobiology, Saarland UniversityHomburg/Saar, Germany; Deutsches Institut für DemenzPrävention (DIDP), Saarland UniversityHomburg/Saar, Germany.
Saarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular neuritic plaques, composed of aggregated amyloid-β (Aβ) peptides, are one of the major histopathological hallmarks of Alzheimer's disease (AD), a progressive, irreversible neurodegenerative disorder and the most common cause of dementia in the elderly. One of the most prominent risk factor for sporadic AD, carrying one or two aberrant copies of the apolipoprotein E (ApoE) ε4 alleles, closely links AD to lipids. Further, several lipid classes and fatty acids have been reported to be changed in the brain of AD-affected individuals. Interestingly, the observed lipid changes in the brain seem not only to be a consequence of the disease but also modulate Aβ generation. In line with these observations, protective lipids being able to decrease Aβ generation and also potential negative lipids in respect to AD were identified. Mechanistically, Aβ peptides are generated by sequential proteolytic processing of the amyloid precursor protein (APP) by β- and γ-secretase. The α-secretase appears to compete with β-secretase for the initial cleavage of APP, preventing Aβ production. All APP-cleaving secretases as well as APP are transmembrane proteins, further illustrating the impact of lipids on Aβ generation. Beside the pathological impact of Aβ, accumulating evidence suggests that Aβ and the APP intracellular domain (AICD) play an important role in regulating lipid homeostasis, either by direct effects or by affecting gene expression or protein stability of enzymes involved in the

Indexed as

Abeta cholesterolAICDAPP processinggangliosideslipidsPUFAsphingolipidssulfatides

Identifiers

PMID28344547
PMCPMC5344993
OpenAlexW2594288299

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.