5'-Triphosphate RNA Is the Ligand for RIG-I

By V. Hornung, J. Ellegast, Sarah Kim, K. Brzózka, A. Jung, H. Kato, Hendrik Poeck, Shizuo Akira, K. Conzelmann, M. Schlee and 2 more. 2006

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Citations in the corpus

Highly efficient reprogramming to pluripotency and directed differentiation of human cells using synthetic modified mRNA (2010, background): “Cel It is known that exogenous single-stranded RNA (ssRNA) activates antiviral defenses in mammalian cells through interferonand NF-kB-dependent pathways (Diebold et al., 2004; Hornung et al., 2006; Kawai and Akira, 2007; Pichlmair et al., 2006; Uematsu and Akira, 2007).”
Structural insights into RNA recognition by RIG-I (2011, unknown): “It is generally accepted that RIG-I can be activated by 5’triphosphate (5’ppp) ssRNA or dsRNA (Hornung et al., 2006; Kato et al., 2006; Lu et al., 2010; Pichlmair et al., 2006; Wang et al., 2010b).”
Pathogen Recognition by the Innate Immune System (2011, background): “It was thought that single-stranded RNAs bearing a 5′ triphosphate were the only essential component for this recognition [50, 51]; however, recent studies suggest that, during the enzymatic synthesis of RNA, a secondary structure for double stranded RNA is generated, which acts as a RIG-I ligand [5”
NLRP3 (NALP3/CIAS1/Cryopyrin) mediates key innate and healing responses to influenza A virus via the regulation of caspase-1 (2009, unknown): “The ssRNA influenza virus genome has been shown to activate the TLR7 and RIG-I pathways in APCs such as macrophages and dendritic cells (Diebold et al., 2004; Pichlmair et al., 2006).”
MAVS Forms Functional Prion-Like Aggregates To Activate and Propagate Antiviral Innate Immune Response (2011, unknown): “RIG-I also contains a C-terminal regulatory domain (RD) that binds to viral RNA harboring 50-triphosphate (50-pppRNA) (Hornung et al., 2006; Pichlmair et al., 2006).”
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 (2015, unknown): “They recognize RNA species harboring 5′-triphosphate or diphosphate ends and/or double-stranded features (dsRNA) [3–7] that are physiologically absent from the cytosol (see [2] for review).”
ADAR1 Limits RIG-I RNA Detection and Suppresses IFN Production Responding to Viral and Endogenous RNAs (2014, background): “The viral RNA usually forms long, double-stranded hairpin structures and may carry 59-triphosphate that can be detected by retinoic acid–inducible gene I (RIG-I)–like receptors (RLRs) (30).”
RIG-I uses an ATPase-powered translocation-throttling mechanism for kinetic proofreading of RNAs and oligomerization (2018, background): “many viral RNA genomes and replication intermediates (Hornung et al., 2006; Rehwinkel et al., 2010; Schlee et al., 2009).”