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The Interaction of Viperin with Hepatitis C Virus Non-Structural Protein 5A Inhibits the Catalytic Activity of Viperin

https://doi.org/10.1101/824458
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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/jmv.25595openalex-snapshot
Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein
inferredcites →https://doi.org/10.1007/bf02256065openalex-snapshot
The Nonstructural NS5A Protein of Hepatitis C Virus: An Expanding, Multifunctional Role in Enhancing Hepatitis C Virus Pathogenesis
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.cbpa.2004.08.001openalex-snapshot
Structure and function of radical SAM enzymes
inferredcites →https://doi.org/10.1016/j.chroma.2016.04.006openalex-snapshot
Benzoyl chloride derivatization with liquid chromatography–mass spectrometry for targeted metabolomics of neurochemicals in biological samples
inferredcites →https://doi.org/10.1016/j.febslet.2010.02.041openalex-snapshot
The antiviral protein viperin is a radical SAM enzyme
inferredcites →https://doi.org/10.1016/j.virol.2018.07.014openalex-snapshot
Toll-like receptor agonist R848 blocks Zika virus replication by inducing the antiviral protein viperin
inferredcites →https://doi.org/10.1021/cr4004709openalex-snapshot
RadicalS-Adenosylmethionine Enzymes
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/10.1038/s41598-017-04138-1openalex-snapshot
Viperin is an important host restriction factor in control of Zika virus infection
inferredcites →https://doi.org/10.1073/pnas.1705402114openalex-snapshot
Structural studies of viperin, an antiviral radical SAM enzyme
inferredcites →https://doi.org/10.1074/jbc.m109.038877openalex-snapshot
The Hepatitis C Virus Non-structural NS5A Protein Impairs Both the Innate and Adaptive Hepatic Immune Response in Vivo
inferredcites →https://doi.org/10.1074/jbc.m111392200openalex-snapshot
Hepatitis C Virus (HCV) NS5A Binds RNA-dependent RNA Polymerase (RdRP) NS5B and Modulates RNA-dependent RNA Polymerase Activity
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.m201191200openalex-snapshot
Vesicle-associated Membrane Protein-associated Protein-A (VAP-A) Interacts with the Oxysterol-binding Protein to Modify Export from the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1074/jbc.ra119.007719openalex-snapshot
Viperin interacts with the kinase IRAK1 and the E3 ubiquitin ligase TRAF6, coupling innate immune signaling to antiviral ribonucleotide synthesis
inferredcites →https://doi.org/10.1080/10409230701829169openalex-snapshot
The Radical SAM Superfamily
inferredcites →https://doi.org/10.1089/dna.2018.4328openalex-snapshot
The Role of Viperin in Antiflavivirus Responses
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/10.1101/318840openalex-snapshot
Interactions between Viperin, IRAK1 andTRAF6 couple innate immune signaling to antiviral ribonucleotide synthesis
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/10.1128/jvi.00616-10openalex-snapshot
All Three Domains of the Hepatitis C Virus Nonstructural NS5A Protein Contribute to RNA Binding
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/jvi.02113-07openalex-snapshot
Identification of Three Interferon-Inducible Cellular Enzymes That Inhibit the Replication of Hepatitis C Virus
inferredcites →https://doi.org/10.1128/jvi.02199-09openalex-snapshot
Identification of Five Interferon-Induced Cellular Proteins That Inhibit West Nile Virus and Dengue Virus Infections
inferredcites →https://doi.org/10.1128/jvi.78.6.2738-2748.2004openalex-snapshot
Effect of Interaction between Hepatitis C Virus NS5A and NS5B on Hepatitis C Virus RNA Replication with the Hepatitis C Virus Replicon
inferredcites →https://doi.org/10.1128/mcb.18.9.5208openalex-snapshot
Control of PKR Protein Kinase by Hepatitis C Virus Nonstructural 5A Protein: Molecular Mechanisms of Kinase Regulation
inferredcites →https://doi.org/10.1146/annurev-biochem-060713-035504openalex-snapshot
Radical S-Adenosylmethionine Enzymes in Human Health and Disease
inferredcites →https://doi.org/10.1371/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
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