Evidence map›Paper›PMID 29650953›Full record

ArticleNature communications2018

HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis.

Margaux Sevin, Lucia Kubovcakova, Nicolas Pernet, Sébastien Causse, Franck Vitte, Jean Luc Villeval, Catherine Lacout, Marine Cordonnier, Fernando Rodrigues-Lima, Gaétan Chanteloup and 14 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

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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

24 authors at 5 institutions in 3 countries.

Margaux SevinUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
Lucia KubovcakovaDepartment of Biomedicine, Experimental Hematology, University Hospital Basel, Basel, 20 4031, Switzerland.
Nicolas PernetUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
Sébastien CausseUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.ORCID http://orcid.org/0000-0003-3246-3491
Franck VitteCypath, Dijon, 21000, France.
Jean Luc VillevalUniversity Paris XI, UMR 1170, Gustave Roussy, Villejuif, 94800, France.
Catherine LacoutUniversity Paris XI, UMR 1170, Gustave Roussy, Villejuif, 94800, France.
Marine CordonnierUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
Fernando Rodrigues-LimaUniversite Paris Diderot, Sorbonne Paris Cite, Unite BFA, CNRS UMR 8251, 75013, Paris, France.
Gaétan ChanteloupUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
Matthieu MoscaUniversity Paris XI, UMR 1170, Gustave Roussy, Villejuif, 94800, France.
Marie-Lorraine ChrétienHospital University Center (CHU), Dijon, 21000, France.
Jean Noël BastieUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
Sylvain AudiaHospital University Center (CHU), Dijon, 21000, France.
Paul SagotHospital University Center (CHU), Dijon, 21000, France.
Selim RamlaHospital University Center (CHU), Dijon, 21000, France.
Laurent MartinHospital University Center (CHU), Dijon, 21000, France.
Martin GleaveThe Vancouver Prostate Centre, University of British Columbia, Vancouver, BC V6H 3Z6, BC, Canada.
Valérie MezgerCNRS, UMR7216 Épigénétique et Destin Cellulaire, Paris, 75013, Cedex 13, France.
Radek SkodaDepartment of Biomedicine, Experimental Hematology, University Hospital Basel, Basel, 20 4031, Switzerland.
Isabelle PloUniversity Paris XI, UMR 1170, Gustave Roussy, Villejuif, 94800, France.
Carmen GarridoUniversity of Bourgogne Franche-Comté, Dijon, 21000, France.
François GirodonUniversity of Bourgogne Franche-Comté, Dijon, 21000, France. francois.girodon@chu-dijon.fr.
Aurélie de ThonelUniversity of Bourgogne Franche-Comté, Dijon, 21000, France. aurelie.dethonel@univ-paris-diderot.fr.
Inserm · FRMaison des Sciences sociales et des Humanités de Dijon · FRCentre National de la Recherche Scientifique · FRUniversity Hospital of Basel · CHUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein 27 (HSP27/HSPB1) is a stress-inducible chaperone that facilitates cancer development by its proliferative and anti-apoptotic functions. The OGX-427 antisense oligonucleotide against HSP27 has been reported to be beneficial against idiopathic pulmonary fibrosis. Here we show that OGX-427 is effective in two murine models of thrombopoietin- and JAKV617F-induced myelofibrosis. OGX-427 limits disease progression and is associated with a reduction in spleen weight, in megakaryocyte expansion and, for the JAKV617F model, in fibrosis. HSP27 regulates the proliferation of JAK2V617F-positive cells and interacts directly with JAK2/STAT5. We also show that its expression is increased in both CD34

Indexed as

AnimalsBone Marrow CellsBone Marrow TransplantationCell Line, TumorDisease Models, AnimalFemaleHEK293 CellsHSP27 Heat-Shock ProteinsHumansJanus Kinase 2K562 CellsLeukocytesMiceMice, Inbred C57BLMice, TransgenicMolecular Targeted TherapyapatorsenHSP27 Heat-Shock ProteinsHspb2 protein, mouseJak2 protein, mouseJanus Kinase 2OligonucleotidesSTAT5 Transcription FactorThrombopoietin

Identifiers

PMID29650953
PMCPMC5897330
OpenAlexW2796616220

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.