Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein. - Wikidata - wikimedia - TriplyDB

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

http://www.wikidata.org/entity/Q38321693

about

The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5A Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5A Hepatitis C virus proteins Human Choline Kinase-α Promotes Hepatitis C Virus RNA Replication through Modulation of Membranous Viral Replication Complex Formation 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 Analysis of Hepatitis C Virus Superinfection Exclusion by Using Novel Fluorochrome Gene-Tagged Viral Genomes Identification of Determinants Involved in Initiation of Hepatitis C Virus RNA Synthesis by Using Intergenotypic Replicase Chimeras Studying Hepatitis C Virus: Making the Best of a Bad Virus 3' RNA Elements in Hepatitis C Virus Replication: Kissing Partners and Long Poly(U)Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein Single Strand Binding Proteins Increase the Processivity of DNA Unwinding by the Hepatitis C Virus Helicase 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 A virocidal amphipathic -helical peptide that inhibits hepatitis C virus infection in vitro Interaction of Hepatitis C Virus Nonstructural Protein 5A with Core Protein Is Critical for the Production of Infectious Virus Particles Hepatitis C Virus NS5B Polymerase Exhibits Distinct Nucleotide Requirements for Initiation and Elongation Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B The Hepatitis C Virus NS5A Stimulates NS5B During In Vitro RNA Synthesis in a Template Specific Manner Essential Role of Cyclophilin A for Hepatitis C Virus Replication and Virus Production and Possible Link to Polyprotein Cleavage Kinetics Identification of Hepatitis C Virus NS5A Inhibitors Endocytic Rab proteins are required for hepatitis C virus replication complex formation The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors Metabolism of phosphatidylinositol 4-kinase IIIα-dependent PI4P Is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activity A quantitative high-resolution genetic profile rapidly identifies sequence determinants of hepatitis C viral fitness and drug sensitivity HCV core residues critical for infectivity are also involved in core-NS5A complex formation Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation Hepatitis C virus NS5A protein blocks epidermal growth factor receptor degradation via a proline motif- dependent interaction Both Cyclophilin Inhibitors and Direct-Acting Antivirals Prevent PKR Activation in HCV-Infected Cells.Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins Involvement of hepatitis C virus NS5A hyperphosphorylation mediated by casein kinase I-α in infectious virus production.RNA polymerase activity and specific RNA structure are required for efficient HCV replication in cultured cells.Inhibition of hepatitis C virus replication by single-stranded RNA structural mimics.Small molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Discovery of a hepatitis C target and its pharmacological inhibitors by microfluidic affinity analysis.

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P2860

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

http://www.wikidata.org/entity/Q38321693

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2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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name

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

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type

label

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

@en

prefLabel

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

@en

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P1433

Journal of Biological Chemistry

P1476

Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.

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P2093

Jamie J Arnold

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Jungwook Hwang

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Kevin D Raney

http://www.w3.org/2001/XMLSchema#string

Luyun Huang

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Michele R S Hargittai

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Suresh D Sharma

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Yingfeng Chen

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P2860

The apoptosis-promoting factor TIA-1 is a regulator of alternative pre-mRNA splicing

Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex

Domains on the hepatitis C virus internal ribosome entry site for 40s subunit binding

3' nontranslated RNA signals required for replication of hepatitis C virus RNA

A cis-acting replication element in the sequence encoding the NS5B RNA-dependent RNA polymerase is required for hepatitis C virus RNA replication

Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein

Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.

Sequences in the 5' nontranslated region of hepatitis C virus required for RNA replication.

The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.

Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication.

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36417-36428

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10.1074/JBC.M508175200

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43

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280

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Craig E. Cameron

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2005-08-25T00:00:00Z

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16126720

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P921

Hepatitis C virus