Hepatitis C virus NS5A protein interacts with 2',5'-oligoadenylate synthetase and inhibits antiviral activity of IFN in an IFN sensitivity-determining region-independent manner (Q24319540)

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English	Hepatitis C virus NS5A protein interacts with 2',5'-oligoadenylate synthetase and inhibits antiviral activity of IFN in an IFN sensitivity-determining region-independent manner	scientific article

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scholarly article

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Hepatitis C virus NS5A protein interacts with 2',5'-oligoadenylate synthetase and inhibits antiviral activity of IFN in an IFN sensitivity-determining region-independent manner (English)

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2'-5' oligoadenylate synthetase 1A

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GOA release 2020-03-11

Hepatitis C virus

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based on heuristic

inferred from title

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author name string

Takashi Taguchi

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Motoko Nagano-Fujii

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Masato Akutsu

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Hiroyasu Kadoya

4

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Shinji Ohgimoto

5

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Satoshi Ishido

6

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Hak Hotta

7

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language of work or name

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publication date

April 2004

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Journal of General Virology

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85

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Pt 4

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959-69

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Effect of interferon treatment on serum 2',5'-oligoadenylate synthetase levels in hepatitis C-infected patients

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Hepatitis C virus genotypes and risk of hepatocellular carcinoma in cirrhosis: a prospective study

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Characterization of the effects of hepatitis C virus nonstructural 5A protein expression in human cell lines and on interferon-sensitive virus replication

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Production of two phosphoproteins from the NS5A region of the hepatitis C viral genome.

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Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein

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Cell growth regulatory and antiviral effects of the P69 isozyme of 2-5 (A) synthetase

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Cleavage of hepatitis C virus nonstructural protein 5A by a caspase-like protease(s) in mammalian cells

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Ser(2194) is a highly conserved major phosphorylation site of the hepatitis C virus nonstructural protein NS5A.

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The hepatitis C virus core protein interacts with NS5A and activates its caspase-mediated proteolytic cleavage

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Hepatitis C virus NS5A colocalizes with the core protein on lipid droplets and interacts with apolipoproteins

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An altered cellular response to interferon and up-regulation of interleukin-8 induced by the hepatitis C viral protein NS5A uncovered by microarray analysis

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Classification, nomenclature, and database development for hepatitis C virus (HCV) and related viruses: proposals for standardization. International Committee on Virus Taxonomy

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Nuclear localization and intramolecular cleavage of N-terminally deleted NS5A protein of hepatitis C virus

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Evidence for a deficiency of interferon response in mononuclear cells from hepatitis C viremic patients

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Characterization of the nuclear localization signal and subcellular distribution of hepatitis C virus nonstructural protein NS5A.

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Activation and evasion of the antiviral 2'-5' oligoadenylate synthetase/ribonuclease L pathway by hepatitis C virus mRNA.

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Expression of hepatitis C virus NS5A natural mutants in a hepatocytic cell line inhibits the antiviral effect of interferon in a PKR-independent manner

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Mutations in the nonstructural protein 5A gene and response to interferon in patients with chronic hepatitis C virus 1b infection

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Interferon alfa-2b alone or in combination with ribavirin as initial treatment for chronic hepatitis C. Hepatitis Interventional Therapy Group

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Hepatitis C virus infection

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Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321

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An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A

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Hepatitis C virus (HCV) NS5A binds RNA-dependent RNA polymerase (RdRP) NS5B and modulates RNA-dependent RNA polymerase activity

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Effects of specific mutations in active site motifs of 2',5'-oligoadenylate synthetase on enzymatic activity

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Sequence analysis of the NS5A protein of European hepatitis C virus 1b isolates and relation to interferon sensitivity.

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The NS5A protein of hepatitis C virus partially inhibits the antiviral activity of interferon

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10.1099/VIR.0.19513-0

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