Evidence map›Paper›PMID 32274761›Full record

ReviewAdvances in experimental medicine and biology2020

SUMO and Cytoplasmic RNA Viruses: From Enemies to Best Friends.

Ahmed El Motiam, Santiago Vidal, Rocío Seoane, Yanis H Bouzaher, José González-Santamaría, Carmen Rivas

Open access · bronzeAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.3field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Frontiers in microbiology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. SUMO: a novel target for anti-coronavirus therapy.Pathogens and global health · 2021
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. 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

6 authors at 4 institutions in 2 countries.

Ahmed El MotiamCentro Singular en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
Santiago VidalCentro Singular en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
Rocío SeoaneCentro Singular en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
Yanis H BouzaherCentro Singular en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
José González-SantamaríaGrupo de Biología Celular y Molecular de Arbovirus, Instituto Conmemorativo Gorgas de Estudios de la Salud, Panamá, Panama.
Carmen RivasCentro Singular en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain. mcarmen.rivas@usc.es.
Instituto de Investigación Sanitaria de Santiago · ESCenter for Research in Molecular Medicine and Chronic Diseases · ESInstituto Conmemorativo Gorgas de Estudios de la Salud · PAUniversidade de Santiago de Compostela · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO is a ubiquitin-like protein that covalently binds to lysine residues of target proteins and regulates many biological processes such as protein subcellular localization or stability, transcription, DNA repair, innate immunity, or antiviral defense. SUMO has a critical role in the signaling pathway governing type I interferon (IFN) production, and among the SUMOylation substrates are many IFN-induced proteins. The overall effect of IFN is increasing global SUMOylation, pointing to SUMO as part of the antiviral stress response. Viral agents have developed different mechanisms to counteract the antiviral activities exerted by SUMO, and some viruses have evolved to exploit the host SUMOylation machinery to modify their own proteins. The exploitation of SUMO has been mainly linked to nuclear replicating viruses due to the predominant nuclear localization of SUMO proteins and enzymes involved in SUMOylation. However, SUMOylation of numerous viral proteins encoded by RNA viruses replicating at the cytoplasm has been lately described. Whether nuclear localization of these viral proteins is required for their SUMOylation is unclear. Here, we summarize the studies on exploitation of SUMOylation by cytoplasmic RNA viruses and discuss about the requirement for nuclear localization of their proteins.

Indexed as

Cell NucleusCytoplasmHumansRNA VirusesSmall Ubiquitin-Related Modifier ProteinsSumoylationViral ProteinsSmall Ubiquitin-Related Modifier ProteinsViral ProteinsInterferonRNA virusesSUMO

Identifiers

PMID32274761
PMCPMC7144409
OpenAlexW3015662008

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.