Evidence map›Paper›PMID 30787102›Full record

ArticleThe Journal of biological chemistry2019

Létitia Jean, Stephen Brimijoin, David J Vaux

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Aducanumab-Hope or Disappointment for Alzheimer's Disease.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. 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

3 authors at 2 institutions in 2 countries.

Létitia JeanFrom the Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom and.ORCID 0000-0002-6450-7148
Stephen Brimijointhe Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, Minnesota 55905.
David J VauxFrom the Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom and david.vaux@path.ox.ac.uk.ORCID 0000-0002-4901-9795
University of Oxford · GBMayo Clinic · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many neurodegenerative diseases are characterized by amyloid deposition. In Alzheimer's disease (AD), β-amyloid (Aβ) peptides accumulate extracellularly in senile plaques. The AD amyloid cascade hypothesis proposes that Aβ production or reduced clearance leads to toxicity. In contrast, the cholinergic hypothesis argues for a specific pathology of brain cholinergic pathways. However, neither hypothesis in isolation explains the pattern of AD pathogenesis. Evidence suggests that a connection exists between these two scenarios: the synaptic form of human acetylcholinesterase (hAChE-S) associates with plaques in AD brains; among hAChE variants, only hAChE-S enhances Aβ fibrillization

Indexed as

AcetylcholinesteraseAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBrainGPI-Linked ProteinsHumansMiceMice, TransgenicPeptidesProtein DomainsProtein Structure, SecondaryAcetylcholinesteraseACHE protein, humanAmyloid beta-PeptidesGPI-Linked ProteinsPeptidesacetylcholinesterase (AChE)Alzheimer diseaseamyloid-beta (AB)beta-sheet conformationbrainoligomerization domainproteolysisseedingsenile plaquestransgenic mice

Identifiers

PMID30787102
PMCPMC6484111
OpenAlexW2915331042

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.