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

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

http://www.wikidata.org/entity/Q24561987

about

The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5A Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication.Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90 A single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication Hepatitis C virus NS5A inhibits mixed lineage kinase 3 to block apoptosis Nonstructural 5A protein of hepatitis C virus interacts with pyruvate carboxylase and modulates viral propagation Cellular cofactors affecting hepatitis C virus infection and replication Polo-like kinase 1 is involved in hepatitis C virus replication by hyperphosphorylating NS5A Human VAP-C negatively regulates hepatitis C virus propagation Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B Lipid droplet-binding protein TIP47 regulates hepatitis C Virus RNA replication through interaction with the viral NS5A protein Hepatitis C virus proteins The yin and yang of hepatitis C: synthesis and decay of hepatitis C virus RNA Autophagy in hepatitis C virus-host interactions: potential roles and therapeutic targets for liver-associated diseases The modulation of apoptosis by oncogenic viruses Spatiotemporal analysis of hepatitis C virus infection Activation of the N-Ras-PI3K-Akt-mTOR pathway by hepatitis C virus: control of cell survival and viral replication.Quantitative Analysis of the Hepatitis C Virus Replication Complex Molecular virology of hepatitis C virus (HCV): 2006 update Replication of Hepatitis C Virus (HCV) RNA in Mouse Embryonic Fibroblasts: Protein Kinase R (PKR)-Dependent and PKR-Independent Mechanisms for Controlling HCV RNA Replication and Mediating Interferon Activities The Isoform of Protein Kinase CKI Is Responsible for Hepatitis C Virus NS5A Hyperphosphorylation Conserved Determinants for Membrane Association of Nonstructural Protein 5A from Hepatitis C Virus and Related Viruses Identification of Determinants Involved in Initiation of Hepatitis C Virus RNA Synthesis by Using Intergenotypic Replicase Chimeras Allelic Variation in the Hepatitis C Virus NS4B Protein Dramatically Influences RNA Replication The C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral Replication Studying Hepatitis C Virus: Making the Best of a Bad Virus Nuclear factors are involved in hepatitis C virus RNA replication Human Apolipoprotein E Is Required for Infectivity and Production of Hepatitis C Virus in Cell Culture Cell Culture Adaptation of Hepatitis C Virus and In Vivo Viability of an Adapted Variant Visualization of Double-Stranded RNA in Cells Supporting Hepatitis C Virus RNA Replication Regulation of Hepatitis C Virion Production via Phosphorylation of the NS5A Protein The FUSE Binding Protein Is a Cellular Factor Required for Efficient Replication of Hepatitis C Virus Cyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In Vitro Characterization of a Peptide Domain within the GB Virus C NS5A Phosphoprotein that Inhibits HIV Replication Interaction of Hepatitis C Virus Nonstructural Protein 5A with Core Protein Is Critical for the Production of Infectious Virus Particles Production of Infectious Genotype 1b Virus Particles in Cell Culture and Impairment by Replication Enhancing Mutations Critical Role of Cyclophilin A and Its Prolyl-Peptidyl Isomerase Activity in the Structure and Function of the Hepatitis C Virus Replication Complex Hepatitis C virus NS4B carboxy terminal domain is a membrane binding domain Role of Oxysterol Binding Protein in Hepatitis C Virus infection

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

http://www.wikidata.org/entity/Q24561987

description

2004 nî lūn-bûn

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2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի օգոստոսին հրատարակված գիտական հոդված

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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name

Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Proceedings of the National Academy of Sciences of the United States of America

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Phosphorylation of hepatitis C ...... ions and viral RNA replication

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Charles M Rice

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Stephen P Goff

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P2860

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

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

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

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

Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft

Modulation of hepatitis C virus NS5A hyperphosphorylation by nonstructural proteins NS3, NS4A, and NS4B

Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.

Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyprotein

Mutations in Hepatitis C Virus RNAs Conferring Cell Culture Adaptation

Enhancement of hepatitis C virus RNA replication by cell culture-adaptive mutations.

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Matthew J. Evans

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phosphorylation

Hepatitis C virus

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516513

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