Evidence map›Paper›PMID 28197076›Full record

ReviewFrontiers in molecular neuroscience2017

Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.

Klemens Wild, Alexander August, Claus U Pietrzik, Stefan Kins

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Polyoxometalates bind multiple targets involved in Alzheimer's disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  4. Astrocyte-to-neuron HNature metabolism · 2025
    Article
  5. Article
  6. Article
  7. Amyloid-International journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Is brain iron trafficking part of the physiology of the amyloid precursor protein?Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  14. Review
  15. Copper signalling: causes and consequences.Cell communication and signaling : CCS · 2018
    Review
  16. Review
  17. Direct evidence of amyloid precursor-like protein 1Molecular biology of the cell · 2017
    Article
  18. A Trishistidine Pseudopeptide with Ability to Remove Both CuChemistry (Weinheim an der Bergstrasse, Germany) · 2017
    Article
  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

4 authors at 3 institutions in 1 country.

Klemens WildHeidelberg University Biochemistry Center (BZH), University of Heidelberg Heidelberg, Germany.
Alexander AugustDivision of Human Biology and Human Genetics, Technical University of Kaiserslautern Kaiserslautern, Germany.
Claus U PietrzikInstitute for Pathobiochemistry, University Medical Center of the Johannes Gutenberg-University Mainz Mainz, Germany.
Stefan KinsDivision of Human Biology and Human Genetics, Technical University of Kaiserslautern Kaiserslautern, Germany.
University of Kaiserslautern · DEHeidelberg University · DEUniversity Medical Center of the Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is ultimately linked to the amyloid precursor protein (APP). However, current research reveals an important synaptic function of APP and APP-like proteins (APLP1 and 2). In this context various neurotrophic and neuroprotective functions have been reported for the APP proteolytic fragments sAPPα, sAPPβ and the monomeric amyloid-beta peptide (Aβ). APP is a metalloprotein and binds copper and zinc ions. Synaptic activity correlates with a release of these ions into the synaptic cleft and dysregulation of their homeostasis is linked to different neurodegenerative diseases. Metal binding to APP or its fragments affects its structure and its proteolytic cleavage and therefore its physiological function at the synapse. Here, we summarize the current data supporting this hypothesis and provide a model of how these different mechanisms might be intertwined with each other.

Indexed as

Alzheimer’s diseaseamyloid precursor protein (APP)coppersynaptic transmissionzinc

Identifiers

PMID28197076
PMCPMC5281630
OpenAlexW2581164166

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.