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MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors

Overview of attention for article published in BMC Biology, May 2012
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Title
MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors
Published in
BMC Biology, May 2012
DOI 10.1186/1741-7007-10-44
Pubmed ID
Authors

Céline Castanier, Naima Zemirli, Alain Portier, Dominique Garcin, Nicolas Bidère, Aimé Vazquez, Damien Arnoult

Abstract

During a viral infection, the intracellular RIG-I-like receptors (RLRs) sense viral RNA and signal through the mitochondrial antiviral signaling adaptor MAVS (also known as IPS-1, Cardif and VISA) whose activation triggers a rapid production of type I interferons (IFN) and of pro-inflammatory cytokines through the transcription factors IRF3/IRF7 and NF-κB, respectively. While MAVS is essential for this signaling and known to operate through the scaffold protein NEMO and the protein kinase TBK1 that phosphorylates IRF3, its mechanism of action and regulation remain unclear.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 121 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 4 3%
United Kingdom 1 <1%
Canada 1 <1%
Austria 1 <1%
Unknown 114 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 42 35%
Researcher 22 18%
Student > Bachelor 13 11%
Student > Master 9 7%
Student > Doctoral Student 5 4%
Other 11 9%
Unknown 19 16%
Readers by discipline Count As %
Agricultural and Biological Sciences 64 53%
Biochemistry, Genetics and Molecular Biology 20 17%
Immunology and Microbiology 10 8%
Chemistry 3 2%
Medicine and Dentistry 3 2%
Other 2 2%
Unknown 19 16%