Evidence map›Paper›PMID 32188146›Full record

ArticleCells2020

Interferon- Stimulation Elicited by the Influenza Virus Is Regulated by the Histone Methylase Dot1L through the RIG-I-TRIM25 Signaling Axis.

Laura Marcos-Villar, Estanislao Nistal-Villan, Noelia Zamarreño, Urtzi Garaigorta, Pablo Gastaminza, Amelia Nieto

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

9 citing papers in PubMed, 9 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

6 authors at 3 institutions in 1 country.

Laura Marcos-VillarDepartamento de Biologia Molecular y Celular, Centro Nacional de Biotecnología, C.S.I.C. Darwin 3, Cantoblanco, 28049 Madrid, Spain.
Estanislao Nistal-VillanMicrobiology Section, Dpto. CC, Farmacéuticas y de la Salud, Facultad de Farmacia, Universidad CEU San Pablo, CEU Universities, Boadilla del Monte, 28660 Madrid, Spain.
Noelia ZamarreñoDepartamento de Biologia Molecular y Celular, Centro Nacional de Biotecnología, C.S.I.C. Darwin 3, Cantoblanco, 28049 Madrid, Spain.
Urtzi GaraigortaDepartamento de Biologia Molecular y Celular, Centro Nacional de Biotecnología, C.S.I.C. Darwin 3, Cantoblanco, 28049 Madrid, Spain.
Pablo GastaminzaDepartamento de Biologia Molecular y Celular, Centro Nacional de Biotecnología, C.S.I.C. Darwin 3, Cantoblanco, 28049 Madrid, Spain.
Amelia NietoDepartamento de Biologia Molecular y Celular, Centro Nacional de Biotecnología, C.S.I.C. Darwin 3, Cantoblanco, 28049 Madrid, Spain.
Centro de Investigación Biomédica en Red de Enfermedades Respiratorias · ESCentro Nacional de Biotecnología · ESUniversidad San Pablo CEU · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Influenza virus infection increases the methylation of lysine 79 of histone 3 catalyzed by the Dot1L enzyme. The role of Dot1L against infections was highlighted by an increase of influenza A and vesicular stomatitis virus replication in Dot1L-inhibited cells mediated by a decreased antiviral response. Interferon-beta (IFN-β) reporter assays indicate that Dot1L is involved in the control of retinoic acid-inducible geneI protein (RIG-I) signaling. Accordingly, Dot1L inhibition decreases the IFN-β promoter stimulation and RIG-I- mitochondria-associated viral sensor (RIG-I-MAVS) association upon viral infection. Replication of an influenza A virus lacking NS1 (delNS1), incapable of counteracting the antiviral response, is not affected by Dot1L inhibition. Consequently, RIG-I-MAVS association and nuclear factor-B (NF-κ nuclear translocation, are not affected by the Dot1L inhibition in delNS1 infected cells. Restoration of NS1 expression in

Indexed as

Histone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansImmunity, InnateInfluenza A virusSignal TransductionTranscription FactorsTripartite Motif ProteinsUbiquitin-Protein LigasesViral Nonstructural ProteinsDOT1L protein, humanHistone-Lysine N-MethyltransferaseHistone MethyltransferasesTranscription FactorsTRIM25 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesViral Nonstructural ProteinsDot1L histone methylaseinfluenza virusRIG-I signalingRNA virus infectionTRIM25Type I IFN

Identifiers

PMID32188146
PMCPMC7140698
OpenAlexW3012489296

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.