Evidence map›Paper›PMID 40739894›Full record

ReviewScience progress

A synapse perspective on the function of the amyloid precursor protein.

Pia Kruse, Amelie Eichler, Larissa Klukas, Maximilian Lenz

Abstract readReview
In one paragraph

Review in Science progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Pia KruseInstitute of Neuroanatomy and Cell Biology, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-1742-1608
Amelie EichlerInstitute of Neuroanatomy and Cell Biology, Hannover Medical School, Hannover, Germany.ORCID 0000-0001-7990-654X
Larissa KlukasInstitute of Neuroanatomy and Cell Biology, Hannover Medical School, Hannover, Germany.ORCID 0009-0008-4265-7576
Maximilian LenzInstitute of Neuroanatomy and Cell Biology, Hannover Medical School, Hannover, Germany.ORCID 0000-0003-3147-4949

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amyloid precursor protein (APP) is a transmembrane protein widely expressed throughout the brain, where it plays critical roles in both physiological and pathological states. APP undergoes complex post-translational processing by various secretases, a process that can lead to amyloid plaque formation via its amyloidogenic pathway. Consequently, APP has been extensively studied in the context of Alzheimer's disease (AD). However, emerging evidence highlights its physiological functions and the diverse roles of its cleavage fragments. This review explores the dual role of APP and its fragments, focusing on their contributions to synaptic structure, function, and plasticity. We summarize the mechanisms by which APP and its fragments influence synaptic dynamics and plasticity in the hippocampal CA1 region. These insights underline the importance of APP beyond amyloidogenesis, emphasizing its role in fundamental neurobiological processes and potential implications for understanding early AD-related synaptic dysfunction.

Indexed as

Alzheimer DiseaseAmyloid beta-Protein PrecursorSynapsesAnimalsHumansNeuronal PlasticityProtein Processing, Post-TranslationalAmyloid beta-Protein PrecursorAbetaAlzheimer's diseaseAmyloid precursor proteinsynaptic plasticitysynaptic transmission

Identifiers

PMID40739894
PMCPMC12317227

What OpenQuestion holds

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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.