Evidence map›Paper›PMID 25185263›Full record

ArticleBlood2014

Carboxyl-terminal-dependent recruitment of nonmuscle myosin II to megakaryocyte contractile ring during polyploidization.

Idinath Badirou, Jiajia Pan, Céline Legrand, Aibing Wang, Larissa Lordier, Siham Boukour, Anita Roy, William Vainchenker, Yunhua Chang

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Research and practice in thrombosis and haemostasis · 2024
    Review
  3. Article
  4. Article
  5. Review
  6. Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018
    Review
  7. Review
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

9 authors at 4 institutions in 2 countries.

Idinath BadirouINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Jiajia PanINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Céline LegrandINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Aibing WangLaboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD.
Larissa LordierINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Siham BoukourINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Anita RoyINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
William VainchenkerINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Yunhua ChangINSERM UMR1009, Institut Gustave Roussy, Villejuif, France; Université Paris-Sud, Unité Mixte de Recherche 1009, Le Kremlin-Bicêtre, France; Institut Gustave Roussy, Unité Mixte de Recherche 1009, Villejuif, France; and.
Université Paris-Sud · FRInserm · FRInstitut Gustave Roussy · FRNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endomitosis is a unique megakaryocyte (MK) differentiation process that is the consequence of a late cytokinesis failure associated with a contractile ring defect. Evidence from in vitro studies has revealed the distinct roles of 2 nonmuscle myosin IIs (NMIIs) on MK endomitosis: only NMII-B (MYH10), but not NMII-A (MYH9), is localized in the MK contractile ring and implicated in mitosis/endomitosis transition. Here, we studied 2 transgenic mouse models in which nonmuscle myosin heavy chain (NMHC) II-A was genetically replaced either by II-B or by a chimeric NMHCII that combined the head domain of II-A with the rod and tail domains of II-B. This study provides in vivo evidence on the specific role of NMII-B on MK polyploidization. It demonstrates that the carboxyl-terminal domain of the heavy chains determines myosin II localization to the MK contractile ring and is responsible for the specific role of NMII-B in MK polyploidization.

Indexed as

AnimalsCell DifferentiationMegakaryocytesMiceMice, TransgenicMitosisMyosin Heavy ChainsNonmuscle Myosin Type IIANonmuscle Myosin Type IIBPolyploidyProtein Structure, TertiaryMyosin Heavy ChainsNonmuscle Myosin Type IIANonmuscle Myosin Type IIBnonmuscle myosin type IIB heavy chain

Identifiers

PMID25185263
PMCPMC4199958
OpenAlexW2006829024

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.