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

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

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

http://www.wikidata.org/entity/Q27472668

about

The DNA damage sensors ataxia-telangiectasia mutated kinase and checkpoint kinase 2 are required for hepatitis C virus RNA replication Ddx42p--a human DEAD box protein with RNA chaperone activities.Hepatitis C virus proteins SF1 and SF2 helicases: family matters Choosing between DNA and RNA: the polymer specificity of RNA helicase NPH-II DEAD-box helicases as integrators of RNA, nucleotide and protein binding RNA helicase proteins as chaperones and remodelers Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase Structure of the Dengue Virus Helicase/Nucleoside Triphosphatase Catalytic Domain at a Resolution of 2.4 A Hepatitis C virus subgenomic replicon requires an active NS3 RNA helicase.A promoter activity is present in the DNA sequence corresponding to the hepatitis C virus 5' UTR Hepatitis C Virus NS3 ATPases/Helicases from Different Genotypes Exhibit Variations in Enzymatic Properties Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP 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 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 The Two-component NS2B-NS3 Proteinase Represses DNA Unwinding Activity of the West Nile Virus NS3 Helicase Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro Hepatitis C Viral NS3-4A Protease Activity Is Enhanced by the NS3 Helicase Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 Helicase NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations The NS4A Protein of Hepatitis C Virus Promotes RNA-Coupled ATP Hydrolysis by the NS3 Helicase Helicase inhibitors as specifically targeted antiviral therapy for hepatitis C Investigation of Translocation, DNA Unwinding, and Protein Displacement by NS3h, the Helicase Domain from the Hepatitis C Virus Helicase Visualizing ATP-Dependent RNA Translocation by the NS3 Helicase from HCV RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex Prp43p is a DEAH-box spliceosome disassembly factor essential for ribosome biogenesis Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome.The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis.Overexpression of a DEAD box/RNA helicase protein, rck/p54, in human hepatocytes from patients with hepatitis C virus-related chronic hepatitis and its implication in hepatocellular carcinogenesis Unravelling hepatitis C virus replication from genome to function Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2.Statistical linkage analysis of substitutions in patient-derived sequences of genotype 1a hepatitis C virus nonstructural protein 3 exposes targets for immunogen design Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.Rad51 Interacts with Non-structural 3 Protein of Hepatitis C Virus and Regulates Viral Production The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.

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

http://www.wikidata.org/entity/Q27472668

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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name

The hepatitis C viral NS3 prot ...... ofactor enhanced RNA unwinding

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The hepatitis C viral NS3 prot ...... ofactor enhanced RNA unwinding

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The hepatitis C viral NS3 prot ...... ofactor enhanced RNA unwinding

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

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The EMBO Journal

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The hepatitis C viral NS3 prot ...... factor enhanced RNA unwinding.

@en

P2093

Anna Marie Pyle

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

Paul J Planet

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

Phillip S Pang

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

P2860

Nuclear localization of the NS3 protein of hepatitis C virus and factors affecting the localization

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Subcellular localization, stability, and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines.

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

Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing

Pestivirus NS3 (p80) protein possesses RNA helicase activity

Hepatitis C virus nonstructural protein NS3 transforms NIH 3T3 cells

Complex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation

The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)

Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells

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1168-1176

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scholarly article

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10.1093/EMBOJ/21.5.1168

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5

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21

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Eckhard Jankowsky

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2002-03-01T00:00:00Z

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11493772

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11867545

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125889

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