Evidence map›Paper›PMID 30597505›Full record

ArticleThrombosis and haemostasis2019

Human Platelet Protein Ubiquitylation and Changes following GPVI Activation.

Amanda J Unsworth, Izabela Bombik, Adan Pinto-Fernandez, Joanna F McGouran, Rebecca Konietzny, René P Zahedi, Steve P Watson, Benedikt M Kessler, Catherine J Pears

Open access · hybridAbstract read
In one paragraph

Article in Thrombosis and haemostasis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Proteomics: A Tool to Study Platelet Function.International journal of molecular sciences · 2021
    Review
  12. The Role of the Proteasome in Platelet Function.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Frontiers in pharmacology · 2020
    Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Amanda J UnsworthDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Izabela BombikDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Adan Pinto-FernandezNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.
Joanna F McGouranNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.
Rebecca KonietznyNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.
René P ZahediJGH Proteomics Centre, Lady Davis Institute, Jewish General Hospital, Montreal, Quebec, Canada.
Steve P WatsonInstitute of Cardiovascular Sciences, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.
Benedikt M KesslerNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.
Catherine J PearsDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
University of Oxford · GBJewish General Hospital · CAUniversity of Birmingham · GB

Funding

British Heart Foundation CH/03/003/15571British Heart Foundation PG/11/121/29308British Heart Foundation PG/14/17/30720
6 · The paper itself

Abstract

Platelet activators stimulate post-translational modification of signalling proteins to change their activity or their molecular interactions leading to signal propagation. One covalent modification is attachment of the small protein ubiquitin to lysine residues in target proteins. Modification by ubiquitin can either target proteins for degradation by the proteasome or act as a scaffold for other proteins. Pharmacological inhibition of deubiquitylases or the proteasome inhibition of platelet activation by collagen, demonstrating a role for ubiquitylation, but relatively few substrates for ubiquitin have been identified and the molecular basis of inhibition is not established. Here, we report the ubiquitome of human platelets and changes in ubiquitylated proteins following stimulation by collagen-related peptide (CRP-XL). Using platelets from six individuals over three independent experiments, we identified 1,634 ubiquitylated peptides derived from 691 proteins, revealing extensive ubiquitylation in resting platelets. Note that 925 of these peptides show an increase of more than twofold following stimulation with CRP-XL. Multiple sites of ubiquitylation were identified on several proteins including Syk, filamin and integrin heterodimer sub-units. This work reveals extensive protein ubiquitylation during activation of human platelets and opens the possibility of novel therapeutic interventions targeting the ubiquitin machinery.

Indexed as

UbiquitinationBlood PlateletsFlow CytometryHumansIntracellular Signaling Peptides and ProteinsLysineMass SpectrometryPlatelet ActivationPlatelet Membrane GlycoproteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProtein-Tyrosine KinasesP-SelectinSignal TransductionUbiquitinIntracellular Signaling Peptides and ProteinsLysinePlatelet Membrane Glycoproteinsplatelet membrane glycoprotein VIProteasome Endopeptidase ComplexProtein-Tyrosine KinasesP-SelectinUbiquitin

Identifiers

PMID30597505
PMCPMC6327716
OpenAlexW2898489609

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.