Evidence map›Paper›PMID 35563046›Full record

ReviewInternational journal of molecular sciences2022

Role of Intracellular Amyloid β as Pathway Modulator, Biomarker, and Therapy Target.

Lucia Gallego Villarejo, Lisa Bachmann, David Marks, Maite Brachthäuser, Alexander Geidies, Thorsten Müller

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.8field-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

33 citing papers in PubMed, 46 citations in OpenAlex.

  1. Arsenic Promotes Intracellular AβBiological trace element research · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Intracellular amyloidosis in peripheral nerve and skeletal muscle.Journal of neuropathology and experimental neurology · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Altered Protein Palmitoylation as Disease Mechanism in Neurodegenerative Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Review
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Lucia Gallego VillarejoDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.
Lisa BachmannDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.
David MarksDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0002-1002-786X
Maite BrachthäuserDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0001-9903-4240
Alexander GeidiesDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.ORCID 0000-0001-5650-3035
Thorsten MüllerDepartment of Molecular Biochemistry, Cell Signalling, Ruhr University Bochum, 44801 Bochum, Germany.
Ruhr University Bochum · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The β- and γ-secretase-driven cleavage of the amyloid precursor protein (APP) gives rise to the amyloid β peptide, which is believed to be the main driver of neurodegeneration in Alzheimer's disease (AD). As it is prominently detectable in extracellular plaques in post-mortem AD brain samples, research in recent decades focused on the pathological role of extracellular amyloid β aggregation, widely neglecting the potential meaning of very early generation of amyloid β inside the cell. In the last few years, the importance of intracellular amyloid β (iAβ) as a strong player in neurodegeneration has been indicated by a rising number of studies. In this review, iAβ is highlighted as a crucial APP cleavage fragment, able to manipulate intracellular pathways and foster neurodegeneration. We demonstrate its relevance as a pathological marker and shed light on initial studies aiming to modulate iAβ through pharmacological treatment, which has been shown to have beneficial effects on cognitive properties in animal models. Finally, we display the relevance of viral infections on iAβ generation and point out future directions urgently needed to manifest the potential relevance of iAβ in Alzheimer's disease.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsBiomarkersPlaque, AmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesBiomarkersAlzheimer’s diseaseamyloidAPPintracellular amyloid βneurodegeneration

Identifiers

PMID35563046
PMCPMC9103247
OpenAlexW4224301527

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.