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Cyclic GMP-AMP Synthase Is a Cytosolic DNA Sensor That Activates the Type I Interferon Pathway
- Lijun Sun, Jiaxi Wu, Fenghe Du, Xiang Chen, Zhijian J. Chen
- Biology, ChemistryScience
- 15 February 2013
Results indicate that cGAS is a cytosolic DNA sensor that induces interferons by producing the second messenger cGAMP, which belongs to the nucleotidyltransferase family.
TAK1 is a ubiquitin-dependent kinase of MKK and IKK
The purification and identification of TRIKA2, which is composed of TAK1, TAB1 and TAB2, a protein kinase complex previously implicated in IKK activation through an unknown mechanism, indicate that ubiquitination has an important regulatory role in stress response pathways, including those of IKK and JNK.
TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
It is demonstrated that TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic Rig-I signalling pathway to elicit host antiviral innate immunity.
RNA Polymerase III Detects Cytosolic DNA and Induces Type I Interferons through the RIG-I Pathway
Identification and Characterization of MAVS, a Mitochondrial Antiviral Signaling Protein that Activates NF-κB and IRF3
Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation
A common signaling mechanism used by all three types of innate immune receptor-adaptor protein pairs to activate IRF3 and generate IFNs is reported, which is important because cells must regulate their IFN production carefully to avoid inflammation and autoimmunity.
Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO.
Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain
STING Specifies IRF3 Phosphorylation by TBK1 in the Cytosolic DNA Signaling Pathway
STING is shown to stimulate phosphorylation of IRF3 by the kinase TBK1 (TANK-binding kinase 1) in an in vitro reconstitution system, suggesting that STING functions as a scaffold protein to specify and promote the phosphorylated of IRf3 by TBk1.
Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity.
- Xiao-Dong Li, Lijun Sun, R. Seth, Gabriel Pineda, Zhijian J. Chen
- BiologyProceedings of the National Academy of Sciences…
- 6 December 2005
An example of host-pathogen interaction in which the virus evades innate immunity by dislodging a pivotal antiviral protein from the mitochondria is provided and blocking the cleavage of MAVS by NS3/4A is suggested to be applied to the prevention and treatment of HCV.