NLRX1 is a regulator of mitochondrial antiviral immunity

By C. Moore, D. Bergstralh, J. Duncan, Y. Lei, T. Morrison, A. Zimmermann, M. Accavitti-Loper, V. Madden, Lijun Sun, Z. Ye and 4 more. Nature, 2008

605 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/cd070b0beb7c801e4ba80cc18ae4db2919cfd609

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. Shizuo Akira
2. O. Takeuchi
3. Taro Kawai
4. J. Tschopp
5. Himanshu Kumar
6. G. Núñez
7. R. Medzhitov
8. M. Gale

In Molecular Biology

1. Shizuo Akira
2. J. Tschopp
3. Taro Kawai
4. O. Takeuchi
5. G. Núñez
6. L. Franchi
7. Fabio Martinon
8. Annick Mayor

Citations in the corpus

• RNA recognition and signal transduction by RIG‐I‐like receptors (2009, background): “Interestingly, a member of NLR family protein, NLRX1, has also been identified as a negative regulator of RLR-mediated antiviral signal (102).”
• The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. (2008, positive): “Various studies suggest that virus-triggered type I IFN signaling pathways are also positively regulated by TRIM25mediated ubiquitation of RIG-I (Gack et al., 2007) or negatively regulated by a divergent groups of cellular or viral proteins, such as A20 (Lin et al., 2006b), DUBA (Kayagaki et al., 20”
• Type I interferon inhibits interleukin-1 production and inflammasome activation. (2011, positive): “In addition, A20, NLRX1, PIN1, DUBA, and Triad3A deregulate RIG-I-mediated signaling by inhibiting MAVS, IRF3, and TRAF3 (Kayagaki et al., 2007; Lin et al., 2006; Moore et al., 2008; Nakhaei et al., 2009b; Saitoh et al., 2006).”
• The NLRP3 Inflammasome Mediates in vivo Innate Immunity to Influenza A Virus through Recognition of Viral RNA (2009, background): “One report identifies endogenous NLRX1 as an inhibitor of the RIG-I and MDA-5 pathway through interactions with the essential mitochondrial antiviral signaling adaptor (MAVS) (Moore et al., 2008).”
• Pattern recognition receptors and inflammation. (2010, background): “NLRX1 (also known as NOD9), an NLR family member, is localized on the mitochondrial membrane and acts as an inhibitor of IPS-1 signaling (Moore et al., 2008).”
• The inflammasomes: guardians of the body. (2009, background): “One study suggested that NOD5/NLRX1 interacts and negatively regulates the antiviral pathway involving the CARD-containing adapter MAVS/CARDIF/IPS-1/VISA (36), whereas another study proposed that NLRX1 promotes the production of reactive oxygen species (ROS) (37).”
• The inflammasomes. (2010, neutral): “…the mitochondrial matrix, or, alternatively, as recruited to the outer mitochondrial membrane, and propose functions in either suppressing MAVS-dependent antiviral pathways or promoting the generation of reactive oxygen species (ROS) (Arnoult et al., 2009; Moore et al., 2008; Tattoli et al., 2008).”
• MicroRNA-146a Feedback Inhibits RIG-I-Dependent Type I IFN Production in Macrophages by Targeting TRAF6, IRAK1, and IRAK21 (2009, background): “identified to inhibit RIG-I-dependent type I IFN production, which may help host to avoid immune disorders mediated by uncontrolled or excessive production of type I IFN (12, 13).”
• Peroxisomes are signaling platforms for antiviral innate immunity (2010, neutral): “Notably, overexpression of NLRX1, a negative regulator that is uniquely located on mitochondria (Figure S5B) (Moore et al., 2008) did not interfere with MAVS-Pex signaling, but did inhibit signaling by MAVS-WT (Figure S5A).”
• Function of Nod‐like receptors in microbial recognition and host defense (2009, background): “An additional subfamily, NLRX, characterized by the presence of an N-terminal domain without significant homology to any known domains and by its localization to the mitochondria, has been recognized (20, 21).”
• Pathogen Recognition by the Innate Immune System (2011, background): “NLRX1 interacts with IPS-1 at the outer membrane and inhibits IPS-1-mediated antiviral responses [68].”