Evidence map›Paper›PMID 27717375›Full record

ArticleActa neuropathologica communications2016

pGluAβ increases accumulation of Aβ in vivo and exacerbates its toxicity.

Oyinkan Sofola-Adesakin, Mobina Khericha, Inge Snoeren, Leo Tsuda, Linda Partridge

Open access · goldAbstract read
In one paragraph

Article in Acta neuropathologica communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Frontiers in neuroscience · 2022
    Review
  6. Article
  7. Exploring Aβ Proteotoxicity and Therapeutic Candidates UsingInternational journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The structure of the human glutaminyl cyclase-SEN177 complex indicates routes for developing new potent inhibitors as possible agents for the treatment of neurological disorders.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Article
  15. Review
  16. Article
  17. Alzheimer's Disease, Oligomers, and Inflammation.Journal of Alzheimer's disease : JAD · 2018
    Review
  18. Article
  19. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    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

5 authors at 3 institutions in 3 countries.

Oyinkan Sofola-AdesakinInstitute of Healthy Ageing, and G.E.E., University College London, Darwin Building, Gower Street, London, WC1E 6BT, UK.
Mobina KherichaInstitute of Healthy Ageing, and G.E.E., University College London, Darwin Building, Gower Street, London, WC1E 6BT, UK.
Inge SnoerenInstitute of Healthy Ageing, and G.E.E., University College London, Darwin Building, Gower Street, London, WC1E 6BT, UK.
Leo TsudaCenter for Development of Advanced Medicine for Dementia (CAMD), National Center for Geriatrics and Gerontology (NCGG), Obu, Aichi, Japan.
Linda PartridgeInstitute of Healthy Ageing, and G.E.E., University College London, Darwin Building, Gower Street, London, WC1E 6BT, UK. l.partridge@ucl.ac.uk.
University College London · GBMax Planck Institute for Biology of Ageing · DENational Center for Geriatrics and Gerontology · JP

Funding

Wellcome Trust
6 · The paper itself

Abstract

Several species of β-amyloid peptides (Aβ) exist as a result of differential cleavage from amyloid precursor protein (APP) to yield various C-terminal Aβ peptides. Several N-terminal modified Aβ peptides have also been identified in Alzheimer's disease (AD) brains, the most common of which is pyroglutamate-modified Aβ (Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAnimals, Genetically ModifiedDisease Models, AnimalDrosophilaDrosophila ProteinsEyeFemaleJNK Mitogen-Activated Protein KinasesMAP Kinase Signaling SystemMotor ActivityNeprilysinNeuronsPeptide FragmentsProtein StabilityAmyloid beta-Peptidesamyloid beta-protein (1-42)amyloid beta-protein (3-42), pyroglutamyl(3)-Drosophila ProteinsGAL4 protein, DrosophilaJNK Mitogen-Activated Protein KinasesNeprilysinneprilysin 2, DrosophilaPeptide FragmentsTranscription FactorsAlzheimer’s diseaseDrosophilaNeurodegenerationpyroglutamate Abeta

Identifiers

PMID27717375
PMCPMC5055666
OpenAlexW2527711139

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.