Evidence map›Paper›PMID 31201463›Full record

ReviewCellular and molecular life sciences : CMLS2019

Regulation of the alternative β-secretase meprin β by ADAM-mediated shedding.

Franka Scharfenberg, Fred Armbrust, Liana Marengo, Claus Pietrzik, Christoph Becker-Pauly

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Interaction between resveratrol and SIRT1: role in neurodegenerative diseases.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Degradome of soluble ADAM10 and ADAM17 metalloproteases.Cellular and molecular life sciences : CMLS · 2020
    Article
  12. Article
  13. Metalloproteinases in nervous system function and pathology: introduction.Cellular and molecular life sciences : CMLS · 2019
    Review
  14. 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

5 authors at 2 institutions in 1 country.

Franka ScharfenbergUnit for Degradomics of the Protease Web, Biochemical Institute, University of Kiel, Kiel, Germany.
Fred ArmbrustUnit for Degradomics of the Protease Web, Biochemical Institute, University of Kiel, Kiel, Germany.
Liana MarengoInstitute for Pathobiochemistry, University Medical Center of the Johannes Gutenberg-University Mainz, Mainz, Germany.
Claus PietrzikInstitute for Pathobiochemistry, University Medical Center of the Johannes Gutenberg-University Mainz, Mainz, Germany. pietrzik@uni-mainz.de.
Christoph Becker-PaulyUnit for Degradomics of the Protease Web, Biochemical Institute, University of Kiel, Kiel, Germany. cbeckerpauly@biochem.uni-kiel.de.ORCID http://orcid.org/0000-0002-5100-9916
Christian-Albrechts-Universität zu Kiel · DEJohannes Gutenberg University Mainz · DE

Funding

Alzheimer Forschung Initiative (DE) 18007Deutsche Forschungsgemeinschaft (DE) 125440785 A15Deutsche Forschungsgemeinschaft (DE) 125440785 A9Deutsche Forschungsgemeinschaft (DE) BE 4086/2-2
6 · The paper itself

Abstract

Alzheimer's Disease (AD) is the sixth-leading cause of death in industrialized countries. Neurotoxic amyloid-β (Aβ) plaques are one of the pathological hallmarks in AD patient brains. Aβ accumulates in the brain upon sequential, proteolytic processing of the amyloid precursor protein (APP) by β- and γ-secretases. However, so far disease-modifying drugs targeting β- and γ-secretase pathways seeking a decrease in the production of toxic Aβ peptides have failed in clinics. It has been demonstrated that the metalloproteinase meprin β acts as an alternative β-secretase, capable of generating truncated Aβ

Indexed as

ADAM10 ProteinAlzheimer DiseaseAmyloid beta-PeptidesHumansMembrane ProteinsMetalloendopeptidasesPresenilin-1ProteolysisSerine EndopeptidasesADAM10 ProteinAmyloid beta-Peptidesmatriptase 2Membrane Proteinsmeprin BMetalloendopeptidasesPresenilin-1Serine EndopeptidasesADAM10Alzheimer’s diseaseAPPMeprin ββ-secretase

Identifiers

PMID31201463
PMCPMC11105663
OpenAlexW2951741361

What Socratic 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 Socratic graph.