Evidence map›Paper›PMID 39047943›Full record

ArticleJournal of thrombosis and haemostasis : JTH2024

Atomistic characterization of β2-glycoprotein I domain V interaction with anionic membranes.

Hale S Hasdemir, Nicola Pozzi, Emad Tajkhorshid

Abstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2024. 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
–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

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.

  1. βCurrent opinion in immunology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Understanding the structure of βBlood vessels, thrombosis & hemostasis · 2025
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Hale S HasdemirTheoretical and Computational Biophysics Group, NIH Resource for Macromolecular Modeling and Visualization, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA; Center for Biophysics and Computational Biology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA.
Nicola PozziEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri, USA. Electronic address: https://www.twitter.com/LabPozzi.
Emad TajkhorshidTheoretical and Computational Biophysics Group, NIH Resource for Macromolecular Modeling and Visualization, Beckman Institute for Advanced Science and Technology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA; Center for Biophysics and Computational Biology, University of Illinois Urbana-Champaign, Urbana, Illinois, USA; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois, USA. Electronic address: emad@illinois.edu.

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Resource for Macromolecular Modeling and VisualizationR24GM145965 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Emad Tajkhorshid · 2022 to 2026
$6.2M
Toolkit for High-Resolution Structure and Dynamics of Functional LipidsR01GM123455 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H., RIENSTRA, CHAD M · 2016 to 2020
$5.0M
Structural Studies of Beta-2 glycoprotein I in the Antiphospholipid SyndromeR01HL150146 · NHLBI · SAINT LOUIS UNIVERSITY · PI POZZI, NICOLA · 2020 to 2024
$2.0M
NHLBI NIH HHS R01 HL150146NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM123455NIGMS NIH HHS R24 GM145965
6 · The paper itself

Abstract

backgroundInteraction of β

objectivesThis study aimed to elucidate the molecular details of β

methodsWe utilized molecular dynamics simulations to investigate the structural basis of anionic lipid recognition by DV. To corroborate the membrane-binding mode identified in the highly mobile membrane mimetic simulations, we conducted additional simulations using a full membrane model.

resultsThe study identified critical regions in DV, namely the lysine-rich loop and the hydrophobic loop, which are essential for membrane association via electrostatic and hydrophobic interactions, respectively. A novel lysine pair contributing to membrane binding was also discovered, providing new insights into β

conclusionThe study advances our understanding of the molecular interactions between β

Indexed as

Antiphospholipid Syndromebeta 2-Glycoprotein IHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationProtein BindingAnionsBinding SitesCell MembraneHumansLipid BilayersLysineProtein DomainsStatic ElectricityStructure-Activity RelationshipAnionsbeta 2-Glycoprotein ILipid BilayersLysineantiphospholipid syndromebeta 2-Glycoprotein Ibiophysicsmolecular dynamics simulationphospholipids

Identifiers

PMID39047943
PMCPMC11992691

What OpenQuestion holds

Textmetadata
LicenceTDM
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.