Evidence map›Paper›PMID 21912928›Full record

ReviewExperimental brain research2012

Analysis of amyloid precursor protein function in Drosophila melanogaster.

Burkhard Poeck, Roland Strauss, Doris Kretzschmar

Abstract readReview
PubMed Publisher
In one paragraph

Review in Experimental brain research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. A Role forFrontiers in cellular neuroscience · 2019
    Article
  7. Article
  8. Article
  9. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  10. Article
  11. Review
  12. Role ofFrontiers in molecular neuroscience · 2016
    Review
  13. Article
  14. Review
  15. The full-length form of the Drosophila amyloid precursor protein is involved in memory formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  16. Article
  17. Article
  18. Origins of amyloid-β.BMC genomics · 2013
    Article
  19. 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

3 authors at 2 institutions in 2 countries.

Burkhard PoeckInstitut für Zoologie III-Neurobiologie, Johannes Gutenberg-Universität Mainz, Colonel Kleinmann-Weg 2, 55099 Mainz, Germany.
Roland Strauss
Doris Kretzschmar
Johannes Gutenberg University Mainz · DEOregon Health & Science University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid precursor proteins (APPs) are evolutionary conserved from nematodes to man (Jacobsen and Iverfeldt in Cell Mol Life Sci 66:2299-2318, 2009) suggesting an important physiological function of these proteins. Human APP is a key factor in the pathogenesis of Alzheimer's Disease because its proteolytic processing results in the production of the neurotoxic Aβ-peptide, which accumulates in the amyloid plaques characteristic for this disease (Selkoe in Physiol Rev 81(2):741-766, 2001). However, the processing also leads to the production of several other fragments and the role of these products, as well as the function of the full-length protein is so far not well understood. The functional analysis of APP in vertebrates has been hampered by the fact that two close relatives, APLP1 and APLP2, exist and that knock-out mice for APP only show subtle defects. In contrast, invertebrates like Caenorhabditis elegans and Drosophila express only one APP-like protein but whereas a null mutation in the C. elegans APL-1 protein is lethal, flies lacking APPL (Amyloid Precursor Protein-like) are viable but show synaptic defects and behavioral abnormalities. Together with the analyses of flies that express APP proteins ectoptically or xenotopically, these studies show that APP proteins are involved in neuronal differentiation, neuritic outgrowth, and synapse formation. In addition, they play a role in long-term memory formation and maintaining brain integrity in adult flies.

Indexed as

Amino Acid SequenceAmyloid beta-Protein PrecursorAnimalsCell DifferentiationDrosophila melanogasterDrosophila ProteinsHumansMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsNeuronsSynapsesAmyloid beta-Protein PrecursorAppl protein, DrosophilaDrosophila ProteinsMembrane ProteinsNerve Tissue Proteins

Identifiers

PMID21912928
OpenAlexW2020880976

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.