Evidence map›Paper›PMID 36151233›Full record

ArticleScientific reports2022

DYRK1A antagonists rescue degeneration and behavioural deficits of in vivo models based on amyloid-β, Tau and DYRK1A neurotoxicity.

Bangfu Zhu, Tom Parsons, Christopher Foley, Yeng Shaw, Travis Dunckley, Christopher Hulme, James J L Hodge

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Sleep regulation inFrontiers in neuroscience · 2026
    Review
  4. Review
  5. Article
  6. 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

7 authors at 3 institutions in 2 countries.

Bangfu ZhuSchool of Physiology, Pharmacology and Neuroscience, Faculty of Life Science, University of Bristol, Biomedical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Tom ParsonsSchool of Physiology, Pharmacology and Neuroscience, Faculty of Life Science, University of Bristol, Biomedical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Christopher FoleyDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, USA.
Yeng ShawDivision of Drug Discovery and Development, Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, AZ, 85721, USA.
Travis DunckleyNeurodegenerative Disease Research Center, Biodesign Institute, Arizona State University, Tempe, AZ, 85281, USA.
Christopher HulmeDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, USA.
James J L HodgeSchool of Physiology, Pharmacology and Neuroscience, Faculty of Life Science, University of Bristol, Biomedical Sciences Building, University Walk, Bristol, BS8 1TD, UK. james.hodge@bristol.ac.uk.
University of Arizona · USUniversity of Bristol · GBArizona State University · US

Funding

DYRK1A Inhibition as a Novel Treatment Approach for Alzheimer's DiseaseR01AG067926 · NIA · UNIVERSITY OF ARIZONA · PI DUNCKLEY, TRAVIS L, HULME, CHRISTOPHER · 2020 to 2024
$3.8M
Biotechnology and Biological Sciences Research Council BB/W000865/1NIA NIH HHS R01 AG067926NIA NIH HHS R01AG067926-01
6 · The paper itself

Abstract

Alzheimer's disease (AD) involves pathological processing of amyloid precursor protein (APP) into amyloid-β and microtubule associated protein Tau (MAPT) into hyperphosphorylated Tau tangles leading to neurodegeneration. Only 5% of AD cases are familial making it difficult to predict who will develop the disease thereby hindering our ability to treat the causes of the disease. A large population who almost certainly will, are those with Down syndrome (DS), who have a 90% lifetime incidence of AD. DS is caused by trisomy of chromosome 21 resulting in three copies of APP and other AD-associated genes, like dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) overexpression. This implies that DYRK1a inhibitors may have therapeutic potential for DS and AD, however It is not clear how overexpression of each of these genes contributes to the pathology of each disease as well as how effective a DYRK1A inhibitor would be at suppressing any of these. To address this knowledge gap, we used Drosophila models with human Tau, human amyloid-β or fly DYRK1A (minibrain (mnb)) neuronal overexpression resulting in photoreceptor neuron degeneration, premature death, decreased locomotion, sleep and memory loss. DYRK1A small molecule Type 1 kinase inhibitors (DYR219 and DYR533) were effective at suppressing these disease relevant phenotypes confirming their therapeutic potential.

Indexed as

Alzheimer DiseaseDown SyndromeNeurotoxicity SyndromesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsDisease Models, AnimalDrosophilaDyrk KinasesHumansPhosphorylationtau ProteinsTyrosineAmyloid beta-PeptidesAmyloid beta-Protein PrecursorDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine Kinasestau ProteinsTyrosine

Identifiers

PMID36151233
PMCPMC9508268
OpenAlexW4297009134

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.