Evidence map›Paper›PMID 34638997›Full record

ArticleInternational journal of molecular sciences2021

Opposing Roles of GSK3α and GSK3β Phosphorylation in Platelet Function and Thrombosis.

Samantha F Moore, Ejaife O Agbani, Andreas Wersäll, Alastair W Poole, Chris M Williams, Xiaojuan Zhao, Yong Li, James L Hutchinson, Roger W Hunter, Ingeborg Hers

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Platelet Activation Pathways Controlling Reversible Integrin αIIbβ3 Activation.TH open : companion journal to thrombosis and haemostasis · 2024
    Article
  6. Article
  7. The Inhibitory Effects ofPreventive nutrition and food science · 2023
    Article
  8. 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

10 authors at 3 institutions in 2 countries.

Samantha F MooreSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Ejaife O AgbaniSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Andreas WersällSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Alastair W PooleSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Chris M WilliamsSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Xiaojuan ZhaoSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Yong LiSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
James L HutchinsonSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Roger W HunterSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Ingeborg HersSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID 0000-0002-6467-5715
University of Bristol · GBNHS Blood and Transplant · GBUniversity of Calgary · CA

Funding

British Heart Foundation FS/14/23/30756British Heart Foundation PG/16/102/32647British Heart Foundation PG/16/3/31833British Heart Foundation PG/16/3/31833, PG/16/21/32083, FS/14/23/30756, RG/15/16/31758British Heart Foundation RG/15/16/31758Medical Research Council MR/R014523/1
6 · The paper itself

Abstract

One of the mechanisms by which PI3 kinase can regulate platelet function is through phosphorylation of downstream substrates, including glycogen synthase kinase-3 (GSK3)α and GSK3β. Platelet activation results in the phosphorylation of an N-terminal serine residue in GSK3α (Ser21) and GSK3β (Ser9), which competitively inhibits substrate phosphorylation. However, the role of phosphorylation of these paralogs is still largely unknown. Here, we employed GSK3α/β phosphorylation-resistant mouse models to explore the role of this inhibitory phosphorylation in regulating platelet activation. Expression of phosphorylation-resistant GSK3α/β reduced thrombin-mediated platelet aggregation, integrin α

Indexed as

AnimalsBlood DonorsBlood PlateletsCells, CulturedDisease Models, AnimalGene Knock-In TechniquesGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansIntegrinsMiceMice, Inbred C57BLMice, TransgenicPhosphatidylinositol 3-KinasesPhosphorylationPlatelet ActivationGlycogen Synthase Kinase 3glycogen synthase kinase 3 alphaGlycogen Synthase Kinase 3 betaGSK3B protein, humanGsk3b protein, mouseIntegrinsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktThrombinAktGSK3integrin activationknock-in mouse modelsp110βphosphorylationPI3 kinaseP-selectin expressionthrombosis

Identifiers

PMID34638997
PMCPMC8508950
OpenAlexW3204658589

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.