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Interactions between Viperin, IRAK1 andTRAF6 couple innate immune signaling to antiviral ribonucleotide synthesis

https://doi.org/10.1101/318840
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/hep.24542openalex-snapshot
The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A
inferredcites →https://doi.org/10.1002/jcp.1040970311openalex-snapshot
Methionine metabolism in BHK cells: Preliminary characterization of the physiological effects of cycloleucine, an inhibitor of S‐adenosylmethionine biosynthesis
inferredcites →https://doi.org/10.1016/0006-291x(79)91866-7openalex-snapshot
Sinefungin, a potent inhibitor of S-adenosylmethionine: Protein O-methyltransferase
inferredcites →https://doi.org/10.1016/0092-8674(95)90407-7openalex-snapshot
Heterotrimeric C proteins: Organizers of transmembrane signals
inferredcites →https://doi.org/10.1016/j.bbrc.2009.12.070openalex-snapshot
Structural characterization reveals that viperin is a radical S-adenosyl-l-methionine (SAM) enzyme
inferredcites →https://doi.org/10.1016/j.bioorg.2004.06.001openalex-snapshot
S-Adenosylmethionine radical enzymes
inferredcites →https://doi.org/10.1016/j.bpc.2010.02.004openalex-snapshot
Protein kinetic stability
inferredcites →https://doi.org/10.1016/j.chom.2007.06.009openalex-snapshot
The Interferon-Inducible Protein Viperin Inhibits Influenza Virus Release by Perturbing Lipid Rafts
inferredcites →https://doi.org/10.1016/j.chom.2011.11.004openalex-snapshot
Viperin: A Multifunctional, Interferon-Inducible Protein that Regulates Virus Replication
inferredcites →https://doi.org/10.1016/j.immuni.2006.08.009openalex-snapshot
Type I Inteferon Gene Induction by the Interferon Regulatory Factor Family of Transcription Factors
inferredcites →https://doi.org/10.1016/j.immuni.2010.03.012openalex-snapshot
Intracellular Toll-like Receptors
inferredcites →https://doi.org/10.1016/j.immuni.2011.03.010openalex-snapshot
Antiviral Protein Viperin Promotes Toll-like Receptor 7- and Toll-like Receptor 9-Mediated Type I Interferon Production in Plasmacytoid Dendritic Cells
inferredcites →https://doi.org/10.1016/j.immuni.2011.03.012openalex-snapshot
Viperin Links Lipid Bodies to Immune Defense
inferredcites →https://doi.org/10.1016/j.jmb.2013.10.019openalex-snapshot
The Role of Viperin in the Innate Antiviral Response
inferredcites →https://doi.org/10.1016/j.molcel.2009.11.022openalex-snapshot
Optimizing Protein Stability In Vivo
inferredcites →https://doi.org/10.1016/j.virol.2017.10.012openalex-snapshot
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication
inferredcites →https://doi.org/10.1016/s0021-9258(18)83275-6openalex-snapshot
The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
inferredcites →https://doi.org/10.1021/bi101023copenalex-snapshot
Biotin Synthase Exhibits Burst Kinetics and Multiple Turnovers in the Absence of Inhibition by Products and Product-Related Biomolecules
inferredcites →https://doi.org/10.1021/cb5004674openalex-snapshot
Recent Advances in Radical SAM Enzymology: New Structures and Mechanisms
inferredcites →https://doi.org/10.1021/cr4004709openalex-snapshot
RadicalS-Adenosylmethionine Enzymes
inferredcites →https://doi.org/10.1021/cr9002616openalex-snapshot
Structural Insights into Radical Generation by the Radical SAM Superfamily
inferredcites →https://doi.org/10.1038/cr.2016.40openalex-snapshot
Ubiquitin signaling in immune responses
inferredcites →https://doi.org/10.1038/nature00888openalex-snapshot
Distinct molecular mechanism for initiating TRAF6 signalling
inferredcites →https://doi.org/10.1038/nature07959openalex-snapshot
Ubiquitylation in innate and adaptive immunity
inferredcites →https://doi.org/10.1038/s41586-018-0238-4openalex-snapshot
A naturally occurring antiviral ribonucleotide encoded by the human genome
inferredcites →https://doi.org/10.1042/bj20071365openalex-snapshot
The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1
inferredcites →https://doi.org/10.1073/pnas.011593298openalex-snapshot
Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus
inferredcites →https://doi.org/10.1073/pnas.0406933101openalex-snapshot
Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling
inferredcites →https://doi.org/10.1073/pnas.0911679106openalex-snapshot
The antiviral protein, viperin, localizes to lipid droplets via its N-terminal amphipathic α-helix
inferredcites →https://doi.org/10.1073/pnas.1705402114openalex-snapshot
Structural studies of viperin, an antiviral radical SAM enzyme
inferredcites →https://doi.org/10.1073/pnas.1714386114openalex-snapshot
Crystal structure of human IRAK1
inferredcites →https://doi.org/10.1073/pnas.1721788115openalex-snapshot
Mechanism of ubiquitin transfer promoted by TRAF6
inferredcites →https://doi.org/10.1074/jbc.272.7.3871openalex-snapshot
RGS Proteins and Signaling by Heterotrimeric G Proteins
inferredcites →https://doi.org/10.1074/jbc.m116.751040openalex-snapshot
Does Viperin Function as a Radical S-Adenosyl-l-methionine-dependent Enzyme in Regulating Farnesylpyrophosphate Synthase Expression and Activity?
inferredcites →https://doi.org/10.1074/jbc.m807261200openalex-snapshot
The N-terminal Amphipathic α-Helix of Viperin Mediates Localization to the Cytosolic Face of the Endoplasmic Reticulum and Inhibits Protein Secretion
inferredcites →https://doi.org/10.1080/10409230701829169openalex-snapshot
The Radical SAM Superfamily
inferredcites →https://doi.org/10.1089/jir.2010.0127openalex-snapshot
The Interferon Inducible Gene: Viperin
inferredcites →https://doi.org/10.1099/vir.0.033860-0openalex-snapshot
Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein hVAP-33
inferredcites →https://doi.org/10.1111/cmi.12241openalex-snapshot
Viperin is an iron-sulfur protein that inhibits genome synthesis of tick-borne encephalitis virus via radical SAM domain activity
inferredcites →https://doi.org/10.1126/science.1202007openalex-snapshot
Human Cytomegalovirus Directly Induces the Antiviral Protein Viperin to Enhance Infectivity
inferredcites →https://doi.org/10.1128/jvi.01751-17openalex-snapshot
Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles
inferredcites →https://doi.org/10.1128/jvi.02054-17openalex-snapshot
Viperin Restricts Zika Virus and Tick-Borne Encephalitis Virus Replication by Targeting NS3 for Proteasomal Degradation
inferredcites →https://doi.org/10.1128/mcb.02098-07openalex-snapshot
Lys63-Linked Polyubiquitination of IRAK-1 Is Required for Interleukin-1 Receptor- and Toll-Like Receptor-Mediated NF-κB Activation
inferredcites →https://doi.org/10.1146/annurev-biochem-060713-035504openalex-snapshot
Radical S-Adenosylmethionine Enzymes in Human Health and Disease
inferredcites →https://doi.org/10.1146/annurev-immunol-032713-120156openalex-snapshot
Innate Immune Sensing and Signaling of Cytosolic Nucleic Acids
inferredcites →https://doi.org/10.1182/blood-2012-01-407395openalex-snapshot
HIV-1 infection of human macrophages directly induces viperin which inhibits viral production
inferredcites →https://doi.org/10.1371/journal.pntd.0002178openalex-snapshot
Viperin Is Induced following Dengue Virus Type-2 (DENV-2) Infection and Has Anti-viral Actions Requiring the C-terminal End of Viperin
inferredcites →https://doi.org/10.1371/journal.pone.0031797openalex-snapshot
The Presence of the Iron-Sulfur Motif Is Important for the Conformational Stability of the Antiviral Protein, Viperin

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1101/493098openalex-snapshot
Viperin binds STING and enhances the type-I interferon response following dsDNA detection
inferred← citeshttps://doi.org/10.1101/824458openalex-snapshot
The Interaction of Viperin with Hepatitis C Virus Non-Structural Protein 5A Inhibits the Catalytic Activity of Viperin
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