Results 11 to 20 of about 3,421,850 (195)

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein [PDF]

open access: yesJournal of Biological Chemistry, 2005
Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) has been shown to antagonize numerous cellular pathways, including the antiviral interferon-α response.
Hargittai, M.R.S.   +7 more
core   +5 more sources

The hepatitis C viral nonstructural protein 5A stabilizes growth-regulatory human transcripts. [PDF]

open access: yesNucleic Acids Res, 2018
Numerous mammalian proto-oncogene and other growth-regulatory transcripts are upregulated in malignancy due to abnormal mRNA stabilization. In hepatoma cells expressing a hepatitis C virus (HCV) subgenomic replicon, we found that the viral nonstructural ...
Guo L   +8 more
europepmc   +3 more sources

Phosphorylation of Nonstructural 5A Protein of Hepatitis C Virus: HCV Group-Specific Hyperphosphorylation [PDF]

open access: yesVirology, 1999
We previously showed that two proteins with molecular weights of 56 and 58 kDa are produced from nonstructural protein 5A (NS5A) derived from hepatitis C virus (HCV)-1b genotype.
Asabe, Shin-ichi   +7 more
core   +3 more sources

Nonstructural protein 5A of hepatitis C virus inhibits the function of karyopherin beta 3 [PDF]

open access: yesJournal of Virology, 2019
It has been suggested that nonstructural protein 5A (NS5A) of hepatitis C virus (HCV) plays a role in the incapacitation of interferon by inactivation of RNA-dependent protein kinase PKR.
Hahm, B   +8 more
core   +4 more sources

Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation.

open access: yesPLoS ONE, 2013
Hepatitis C virus (HCV) is highly dependent on cellular factors for its own propagation. By employing tandem affinity purification method, we identified pyruvate carboxylase (PC) as a cellular partner for NS5A protein. NS5A interacted with PC through the
Seung-Ae Yim   +3 more
doaj   +4 more sources

Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A. [PDF]

open access: yesJournal of Biological Chemistry, 2004
International audienceHepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a membrane-associated, essential component of the viral replication complex.
Brass, V.   +8 more
core   +7 more sources

Variability of the nonstructural 5A protein of hepatitis C virus type 3a isolates and relation to interferon sensitivity. [PDF]

open access: yesThe Journal of Infectious Diseases, 2002
International audienceThe nonstructural 5A (NS5A) protein of hepatitis C virus (HCV) genotype 1 is thought to interact with several cellular proteins, including the double-stranded RNA-dependent protein kinase (PKR) induced by interferon (IFN).
Capron, D.   +9 more
core   +5 more sources

PACSIN2 Interacts with Nonstructural Protein 5A and Regulates Hepatitis C Virus Assembly. [PDF]

open access: yesJ Virol, 2020
PACSIN2 is a lipid-binding protein that triggers the tubulation of the phosphatidic acid-containing membranes. The functional involvement of PACSIN2 in the virus life cycle has not yet been demonstrated. We showed that phosphorylation of PACSIN2 displayed a negative effect on NS5A and core interaction. The most significant finding is that NS5A prevents
Nguyen LP   +4 more
europepmc   +4 more sources

Essential role of domain III of nonstructural protein 5A for hepatitis C virus infectious particle assembly.

open access: yesPLoS Pathogens, 2008
Persistent infection with the hepatitis C virus (HCV) is a major risk factor for the development of liver cirrhosis and hepatocellular carcinoma. With an estimated about 3% of the world population infected with this virus, the lack of a prophylactic ...
Nicole Appel   +8 more
doaj   +4 more sources

The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A [PDF]

open access: yesHepatology, 2011
The interferon-stimulated gene, viperin, has been shown to have antiviral activity against hepatitis C virus (HCV) in the context of the HCVreplicon, although the molecular mechanisms responsible are not well understood. Here, we demonstrate that viperin
Yip, L.   +19 more
core   +4 more sources

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