HCV NS5A: A Multifunctional Regulator of Cellular Pathways and Virus Replication

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• Publication year

  2006

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  Biology, Medicine

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  Semantic Scholar

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• No concepts are published for this paper.

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• Robust hepatitis C virus infection in vitro.

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• Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication.

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• Hepatitis C Virus Nonstructural Protein 5A (NS5A) Is an RNA-binding Protein*

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• HCV NS5A abrogates p53 protein function by interfering with p53-DNA binding.

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• Reduction of Hepatitis C Virus NS5A Hyperphosphorylation by Selective Inhibition of Cellular Kinases Activates Viral RNA Replication in Cell Culture

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• Dominant negative effect of wild-type NS5A on NS5A-adapted subgenomic hepatitis C virus RNA replicon.

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• The NS5A Protein of Hepatitis C Virus Is a Zinc Metalloprotein*

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• HCV core, NS3, NS5A and NS5B proteins modulate cell proliferation independently from p53 expression in hepatocarcinoma cell lines

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• Interactions between Viral Nonstructural Proteins and Host Protein hVAP-33 Mediate the Formation of Hepatitis C Virus RNA Replication Complex on Lipid Raft

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• High-Throughput Screening of the Yeast Kinome: Identification of Human Serine/Threonine Protein Kinases That Phosphorylate the Hepatitis C Virus NS5A Protein

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• Proteomic approach identifies HSP27 as an interacting partner of the hepatitis C virus NS5A protein.

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• Calcium-Dependent Calpain Proteases Are Implicated in Processing of the Hepatitis C Virus NS5A Protein

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• Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication.

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• Effect of Interaction between Hepatitis C Virus NS5A and NS5B on Hepatitis C Virus RNA Replication with the Hepatitis C Virus Replicon

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• Insertion of Green Fluorescent Protein into Nonstructural Protein 5A Allows Direct Visualization of Functional Hepatitis C Virus Replication Complexes

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• Hepatitis C virus NS5A mediated STAT3 activation requires co-operation of Jak1 kinase.

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• Hepatitis C virus NS5A‐regulated gene expression and signaling revealed via microarray and comparative promoter analyses

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• Structure and Function of the Membrane Anchor Domain of Hepatitis C Virus Nonstructural Protein 5A*

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• The Hepatitis C Virus NS5A Protein Activates a Phosphoinositide 3-Kinase-dependent Survival Signaling Cascade*

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• Modulation of interferon expression by hepatitis C virus NS5A protein and human homeodomain protein PTX1.

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• Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.

  2003cited by this paper
• The Hepatitis C Virus Non-structural NS5A Protein Inhibits Activating Protein–1 Function by Perturbing Ras-ERK Pathway Signaling*

  2003cited by this paper
• The regulation of hepatitis C virus (HCV) internal ribosome-entry site-mediated translation by HCV replicons and nonstructural proteins.

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• Amphipathic Helix-Dependent Localization of NS5A Mediates Hepatitis C Virus RNA Replication

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• Hepatitis C Virus NS5A and Subgenomic Replicon Activate NF-κB via Tyrosine Phosphorylation of IκBα and Its Degradation by Calpain Protease*

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• Hepatitis C virus nonstructural protein 5A inhibits tumor necrosis factor-alpha-mediated apoptosis in Huh7 cells.

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• Suppression of the ERK1/2 signaling pathway from HCV NS5A protein expressed by herpes simplex recombinant viruses

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• Hepatitis C Virus NS5A Protein Modulates c-Jun N-terminal Kinase through Interaction with Tumor Necrosis Factor Receptor-associated Factor 2*

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• Hepatitis C virus NS5A as a potential viral Bcl‐2 homologue interacts with Bax and inhibits apoptosis in hepatocellular carcinoma

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• Alpha Interferon Induces Distinct Translational Control Programs To Suppress Hepatitis C Virus RNA Replication

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• Endoplasmic reticulum (ER) stress: hepatitis C virus induces an ER-nucleus signal transduction pathway and activates NF-kappaB and STAT-3.

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• HCV NS5A interacts with p53 and inhibits p53-mediated apoptosis

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

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• To Interfere and to Anti-interfere: The Interplay Between Hepatitis C Virus and Interferon

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• An Amino-terminal Amphipathic α-Helix Mediates Membrane Association of the Hepatitis C Virus Nonstructural Protein 5A*

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• Hepatitis C virus NS5A protein binds TBP and p53, inhibiting their DNA binding and p53 interactions with TBP and ERCC3.

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• Mutations that permit efficient replication of hepatitis C virus RNA in Huh-7 cells prevent productive replication in chimpanzees

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• Subversion of Cell Signaling Pathways by Hepatitis C Virus Nonstructural 5A Protein via Interaction with Grb2 and P85 Phosphatidylinositol 3-Kinase

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• Hepatitis C virus NS5A protein impairs TNF-mediated hepatic apoptosis, but not by an anti-FAS antibody, in transgenic mice.

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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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• Nonstructural 5A Protein of Hepatitis C Virus Modulates Tumor Necrosis Factor α-stimulated Nuclear Factor κB Activation*

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• How hepatitis C virus counteracts the interferon response: the jury is still out on NS5A.

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• Modulation of Cell Growth by the Hepatitis C Virus Nonstructural Protein NS5A*

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• Regulation of mRNA Translation and Cellular Signaling by Hepatitis C Virus Nonstructural Protein NS5A

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• Characterization of Cell Lines Carrying Self-Replicating Hepatitis C Virus RNAs

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• Hepatitis C Virus NS5A Physically Associates with p53 and Regulates p21/waf1 Gene Expression in a p53-Dependent Manner

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• Human hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-κB

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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 Protein Modulates Transcription through a Novel Cellular Transcription Factor SRCAP*

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• Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties.

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

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• Nonstructural Protein 5A of Hepatitis C Virus Inhibits the Function of Karyopherin β3

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• Hepatitis C virus NS5A protein protects against TNF-α mediated apoptotic cell death

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

  2000cited by this paper
• Cleavage of hepatitis C virus nonstructural protein 5A by a caspase-like protease(s) in mammalian cells.

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• Hepatitis C virus NS5A protein modulates cell cycle regulatory genes and promotes cell growth.

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• Hepatitis C virus RNA polymerase and NS5A complex with a SNARE-like protein.

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• Hepatitis C virus NS5A protein is phosphorylated by casein kinase II.

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• The hepatitis C virus NS2 protein generated by NS2-3 autocleavage is required for NS5A phosphorylation.

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• Phosphorylation of nonstructural 5A protein of hepatitis C virus: HCV group-specific hyperphosphorylation.

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• NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signaling.

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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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• Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B

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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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• Hyperphosphorylation of the Hepatitis C Virus NS5A Protein Requires an Active NS3 Protease, NS4A, NS4B, and NS5A Encoded on the Same Polyprotein

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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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• The amino terminal deletion mutants of hepatitis C virus nonstructural protein NS5A function as transcriptional activators in yeast.

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• Hepatitis C virus nonstructural region 5A protein is a potent transcriptional activator.

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

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