Evidence map›Paper›PMID 42602438›Full record

ArticleResearch and practice in thrombosis and haemostasis2026

Comparison of variably specific Bruton tyrosine kinase inhibitors on platelet aggregation mediated by Fcγ receptor (FcγR) IIa, glycoprotein VI, and platelet endothelial aggregation receptor (PEAR) 1: implications for Bruton tyrosine kinase inhibitors as antithrombotic therapy.

Thomas Kartika, Lorena Buitrago, Jihong Li, Charlotte Cunningham-Rundles, Barry S Coller

Abstract readComparative Study
In one paragraph

Article in Research and practice in thrombosis and haemostasis, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Thomas KartikaAllen and Frances Adler Laboratory of Blood and Vascular Biology, The Rockefeller University, New York, New York, USA.
Lorena BuitragoAllen and Frances Adler Laboratory of Blood and Vascular Biology, The Rockefeller University, New York, New York, USA.
Jihong LiAllen and Frances Adler Laboratory of Blood and Vascular Biology, The Rockefeller University, New York, New York, USA.
Charlotte Cunningham-RundlesDivisions of Allergy and Immunology and Pediatric Allergy and Immunology, Departments of Medicine and Pediatrics, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Barry S CollerAllen and Frances Adler Laboratory of Blood and Vascular Biology, The Rockefeller University, New York, New York, USA.

Funding

Developing, Demonstrating, and Disseminating Innovative Programs to Achieve Translational SuccessUL1TR001866 · NCATS · ROCKEFELLER UNIVERSITY · PI COLLER, BARRY, KRUEGER, JAMES G · 2016 to 2025
$40.6M
NCATS NIH HHS UL1 TR001866
6 · The paper itself

Abstract

Background: Bruton tyrosine kinase (BTK) inhibitors (BTKi) have been proposed as therapy for thrombosis driven by immune complex activation of platelets via FcγRIIa. Since patients who lack BTK (X-linked agammaglobulinemia [XLA]) do not have excessive bleeding, highly specific BTKi may be antithrombotic without increasing the risk of hemorrhage. Our knowledge of the full range of effects of BTKi on platelet function is incomplete, in particular, the role of BTKi on signaling via platelet endothelial aggregation receptor (PEAR) 1, a receptor linked to thrombotic cardiovascular disease. Objectives: This study assessed the role of BTK in platelet aggregation initiated through Fcγ receptor (FcγR)IIa, glycoprotein (GP)VI, PEAR1, and other receptors. Methods: Platelets of control and patients with XLA were treated with BTKi of varying specificity and analyzed by light transmission aggregometry and immunoblotting. Results: Both nonspecific and highly specific BTKi profoundly inhibited platelet aggregation mediated by FcγRIIa, PEAR1, and GPVI, but not protease-activated receptor 1, the thromboxane receptor, α Conclusion: BTK plays important roles in signaling via FcγRIIa, GPVI, and PEAR1, but clinical studies are required to assess the optimal BTKi for inhibiting thrombotic disorders mediated via these receptors.

Indexed as

Agammaglobulinaemia Tyrosine KinaseBlood PlateletsFibrinolytic AgentsPlatelet AggregationPlatelet Membrane GlycoproteinsProtein Kinase InhibitorsReceptors, Cell SurfaceReceptors, IgGAgammaglobulinemiaGenetic Diseases, X-LinkedHumansSignal TransductionThrombosisTyrosine Kinase InhibitorsAgammaglobulinaemia Tyrosine KinaseBTK protein, humanFc gamma receptor IIAFCGR2A protein, humanFibrinolytic AgentsPEAR1 protein, humanPlatelet Membrane Glycoproteinsplatelet membrane glycoprotein VIProtein Kinase InhibitorsReceptors, Cell SurfaceReceptors, IgGTyrosine Kinase InhibitorsBruton tyrosine kinaseFcγreceptor IIa (FcγRIIa)platelet aggregationplatelet aggregation inhibitorsthrombosis

Identifiers

PMID42602438
PMCPMC13474628

What Socratic holds

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Registered trials

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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 Socratic graph.