Evidence map›Paper›PMID 41506583›Full record

ArticleJournal of thrombosis and haemostasis : JTH2026

Laminin G domains define a critical interface for protein S-mediated factor IXa inhibition.

Rafika Yasmin, Rima Chattopadhyay, Vandana, Narender Kumar, Adrianne Dorsey, Sabyasachi Chatterjee, Sumita Choudhury, Vijaya Satish Pilli, Brenda Temple, Rinku Majumder

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In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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.

Rafika YasminDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Rima ChattopadhyayDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
VandanaDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Narender KumarDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Adrianne DorseyDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Sabyasachi ChatterjeeDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Sumita ChoudhuryDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Vijaya Satish PilliDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
Brenda TempleDepartment of Biochemistry & Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Rinku MajumderDepartment of Interdisciplinary Oncology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA. Electronic address: rmajum@lsuhsc.edu.

Funding

Protein S Regulates Blood Coagulation by Inhibiting Factor IXaR01HL163018 · NHLBI · LSU HEALTH SCIENCES CENTER · PI MAJUMDER, RINKU · 2022 to 2025
$2.2M
NHLBI NIH HHS R01 HL163018
6 · The paper itself

Abstract

backgroundHemostasis is maintained through a delicate balance between procoagulant and anticoagulant mechanisms. Protein S (PS), a multidomain, vitamin K-dependent glycoprotein, contributes to this balance not only as a cofactor for activated protein C and tissue factor pathway inhibitor but also by directly inhibiting activated factor IX (FIXa). However, the structural determinants underlying FIXa inhibition remain unclear.

objectivesThis study aimed to (1) identify the FIXa binding interface on PS and (2) investigate the role of its laminin G (LG) domains in mediating FIXa binding and inhibition.

methodsMolecular docking was used to predict the FIXa binding interface on PS. Fluorescence-based binding assays were performed to determine binding affinities, and functional coagulation assays were conducted to measure inhibitory constants. Finally, site-directed mutagenesis was carried out to generate specific PS mutants.

resultsMolecular docking and in vitro binding assays demonstrated that both the LG1 and LG2 domains interact with FIXa. Quantitative fluorescence-based binding analyses revealed that the LG1+2 tandem domains exhibited the highest affinity for FIXa (K

conclusionThese findings identify the LG domains of PS as essential structural elements for direct FIXa inhibition, independent of its cofactor function. By elucidating this domain-specific mechanism, our work provides a structural framework for the rational design of selective FIXa inhibitors and FIXa-binding peptides as novel antithrombotic strategies.

Indexed as

Factor IXaLamininProtein SBinding SitesBlood CoagulationHumansMolecular Docking SimulationMutagenesis, Site-DirectedMutationProtein BindingProtein DomainsStructure-Activity RelationshipFactor IXaLamininProtein Sfactor IXahemostasislaminin G domainprotein S

Identifiers

PMID41506583
PMCPMC13416700

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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 OpenQuestion graph.