Evidence map›Paper›PMID 23943322›Full record

ArticleBioEssays : news and reviews in molecular, cellular and developmental biology2013

A new molecular explanation for age-related neurodegeneration: the Tyr682 residue of amyloid precursor protein.

Carmela Matrone

Open access · bronzeAbstract read
In one paragraph

Article in BioEssays : news and reviews in molecular, cellular and developmental biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Phosphorylation Signaling in APP Processing in Alzheimer's Disease.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. APP Receptor? To Be or Not To Be.Trends in pharmacological sciences · 2016
    Review
  12. Article
  13. Article
  14. Review
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Carmela MatroneDepartment of Medical Biochemistry, University of Aarhus, Aarhus, Denmark.
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Emerging evidence supports the role for the intracellular domains of amyloid precursor protein (APP) in the physiology and function of APP. In this short report, I discuss the hypothesis that mutation of Tyr682 on the Y682 ENPTY687 C-terminal motif of APP may be directly or indirectly associated with alterations in APP functioning and activity, leading to neuronal defects and deficits. Mutation of Tyr682 induces an early and progressive age-dependent cognitive and locomotor decline that is associated with a loss of synaptic connections, a decrease in cholinergic tone, and defects in NGF signaling. These findings support a model in which APP-C-terminal domain exerts a pathogenic function in neuronal development and decline, and suggest that Tyr682 potentially could modulate the properties of APP metabolites in humans.

Indexed as

Amino Acid MotifsAlzheimer DiseaseAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsDisease Models, AnimalHumansMiceMolecular Sequence DataMutationPhosphorylationSignal TransductionAmyloid beta-Protein Precursorabeta peptidesadaptor proteinsAPPneurodegenerationNGFTyr682YENPTY domain

Identifiers

PMID23943322
PMCPMC4033529
OpenAlexW1796059154

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.