Evidence map›Paper›PMID 28060719›Full record

ArticleBlood2017

Temporal quantitative phosphoproteomics of ADP stimulation reveals novel central nodes in platelet activation and inhibition.

Florian Beck, Jörg Geiger, Stepan Gambaryan, Fiorella A Solari, Margherita Dell'Aica, Stefan Loroch, Nadine J Mattheij, Igor Mindukshev, Oliver Pötz, Kerstin Jurk and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
8.5field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 139 citations in OpenAlex.

  1. Guideline
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  3. Review
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  8. Review
  9. Article
  10. Suppressed ORAI1-STIM1-dependent CaThe Journal of biological chemistry · 2024
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  11. Article
  12. Chloride Gradient Is Involved in Ammonium Influx in Human Erythrocytes.International journal of molecular sciences · 2024
    Article
  13. Article
  14. Exploring bias in platelet P2YBritish journal of pharmacology · 2024
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. TULA-Family Regulators of Platelet Activation.International journal of molecular sciences · 2022
    Review

7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 4 countries.

Florian BeckLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Jörg GeigerInterdisciplinary Bank of Biomaterials and Data, Würzburg, Germany.
Stepan GambaryanSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Saint Petersburg, Russia.
Fiorella A SolariLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Margherita Dell'AicaLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Stefan LorochLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Nadine J MattheijDepartment of Biochemistry, Cardiovascular Research Institute Maastricht, Maastricht University, The Netherlands.
Igor MindukshevSechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Saint Petersburg, Russia.
Oliver PötzNatural and Medical Sciences Institute at the University of Tübingen, Tübingen, Germany.
Kerstin JurkCenter for Thrombosis and Hemostasis, Universitätsklinikum der Johannes Gutenberg-Universität Mainz, Mainz, Germany.
Julia M BurkhartLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Christian FufezanInstitute for Biology and Biotechnology of Plants, University Münster, Münster, Germany.
Johan W M HeemskerkDepartment of Biochemistry, Cardiovascular Research Institute Maastricht, Maastricht University, The Netherlands.
Ulrich WalterCenter for Thrombosis and Hemostasis, Universitätsklinikum der Johannes Gutenberg-Universität Mainz, Mainz, Germany.
René P ZahediLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Albert SickmannLeibniz-Institut für Analytische Wissenschaften-ISAS-e.V., Dortmund, Germany.
Leibniz Institute for Analytical Sciences - ISAS · DEInstitute of Evolutionary Physiology and Biochemistry · RUJohannes Gutenberg University Mainz · DEMaastricht University · NLNatural and Medical Sciences Institute · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenosine diphosphate (ADP) enhances platelet activation by virtually any other stimulant to complete aggregation. It binds specifically to the G-protein-coupled membrane receptors P2Y1 and P2Y12, stimulating intracellular signaling cascades, leading to integrin αIIbβ3 activation, a process antagonized by endothelial prostacyclin. P2Y12 inhibitors are among the most successful antiplatelet drugs, however, show remarkable variability in efficacy. We reasoned whether a more detailed molecular understanding of ADP-induced protein phosphorylation could identify (1) critical hubs in platelet signaling toward aggregation and (2) novel molecular targets for antiplatelet treatment strategies. We applied quantitative temporal phosphoproteomics to study ADP-mediated signaling at unprecedented molecular resolution. Furthermore, to mimic the antagonistic efficacy of endothelial-derived prostacyclin, we determined how Iloprost reverses ADP-mediated signaling events. We provide temporal profiles of 4797 phosphopeptides, 608 of which showed significant regulation. Regulated proteins are implicated in well-known activating functions such as degranulation and cytoskeletal reorganization, but also in less well-understood pathways, involving ubiquitin ligases and GTPase exchange factors/GTPase-activating proteins (GEF/GAP). Our data demonstrate that ADP-triggered phosphorylation occurs predominantly within the first 10 seconds, with many short rather than sustained changes. For a set of phosphorylation sites (eg, PDE3A

Indexed as

Adenosine DiphosphateBlood PlateletsBlotting, WesternHumansIloprostPhosphorylationPlatelet ActivationPlatelet Aggregation InhibitorsProteomicsSignal TransductionAdenosine DiphosphateIloprostPlatelet Aggregation Inhibitors

Identifiers

PMID28060719
PMCPMC5248936
OpenAlexW2555937343

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.