Evidence map›Paper›PMID 15126698›Full record

ReviewJournal of molecular neuroscience : MN2004

Signal transduction therapeutics: relevance for Alzheimer's disease.

Odete A B da Cruz e Silva, Margarida Fardilha, Ana Gabriela Henriques, Sandra Rebelo, Sandra Vieira, Edgar F da Cruz e Silva

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular neuroscience : MN, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. S655 phosphorylation enhances APP secretory traffic.Molecular and cellular biochemistry · 2009
    Article
  11. Review
  12. Tyr687 dependent APP endocytosis and Abeta production.Journal of molecular neuroscience : MN · 2007
    Article
  13. Protein phosphorylation and APP metabolism.Neurochemical research · 2003
    Review
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 1 institution in 1 country.

Odete A B da Cruz e SilvaCentro de Biologia Celular, Universidade de Aveiro, Aveiro, Portugal. odetecs@bio.ua.pt
Margarida Fardilha
Ana Gabriela Henriques
Sandra Rebelo
Sandra Vieira
Edgar F da Cruz e Silva
University of Aveiro · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is now widely accepted that abnormal processing of the Alzheimer's amyloid precursor protein (APP) can contribute significantly to Alzheimer's disease (AD). APP can be processed proteolytically to give rise to several fragments, including toxic beta-amyloid (Abeta) fragments that are subsequently deposited as amyloid plaques in brains of AD patients. Data from several groups have revealed that APP processing can be regulated by phosphorylation and phosphorylation-dependent events. Consequently, the key players controlling such signal transduction cascades, the protein kinases and phosphatases, as well as their corresponding regulatory proteins, take on added importance. By characterizing how altered cell signaling might contribute to APP processing, one can identify potential targets for signal transduction therapeutics. Here, we review APP phosphorylation and phosphorylation-dependent events in APP processing, with particular focus on phosphatases that impact on APP processing, and their binding and regulatory proteins. Particular attention is given to protein phosphatase 1 (PP1), as it seems to have a central role not only in the regulation of APP cleavage events but also in the molecular control of neurotransmission and in age-related memory deterioration. The development of specific drugs targeting protein phosphatase binding proteins would constitute potential therapeutic agents with a high degree of specificity. The identification of such targets provides novel therapeutic avenues for normal aging and for neurodegenerative conditions such as AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsDrug DesignHumansPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Phosphatase 1Signal TransductionAmyloid beta-PeptidesAmyloid beta-Protein PrecursorPhosphoprotein PhosphatasesProtein Phosphatase 1

Identifiers

PMID15126698
OpenAlexW2312781316

What OpenQuestion holds

Textmetadata
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.