Helicase from hepatitis C virus, energetics of DNA binding. - Wikidata - wikimedia - TriplyDB

Helicase from hepatitis C virus, energetics of DNA binding.

Helicase from hepatitis C virus, energetics of DNA binding.

http://www.wikidata.org/entity/Q43038035

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Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains Hepatitis C Virus NS3 ATPases/Helicases from Different Genotypes Exhibit Variations in Enzymatic Properties RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP Single Strand Binding Proteins Increase the Processivity of DNA Unwinding by the Hepatitis C Virus Helicase Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 Helicase Fuel Specificity of the Hepatitis C Virus NS3 Helicase Interaction of CheY with the C-Terminal Peptide of CheZ Biochemical Characterization of a Mycobacteriophage Derived DnaB Ortholog Reveals New Insight into the Evolutionary Origin of DnaB Helicases Double-stranded DNA-induced localized unfolding of HCV NS3 helicase subdomain 2.Model-based global analysis of heterogeneous experimental data using gfit.The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target Analysis of heterogeneous interactions Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA.Identification and analysis of hepatitis C virus NS3 helicase inhibitors using nucleic acid binding assays The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target Helicases as antiviral drug targets.Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis.Helicase processivity and not the unwinding velocity exhibits universal increase with force.Understanding helicases as a means of virus control.Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action.Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding.Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus.Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro.Comparison of structural architecture of HCV NS3 genotype 1 versus Pakistani genotype 3a.Synthesis and biological activity of 1H-benzotriazole and 1H-benzimidazole analogues--inhibitors of the NTpase/helicase of HCV and of some related Flaviviridae.Unwinding initiation by the viral RNA helicase NPH-II.Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.Two-state model for helicase translocation and unwinding of nucleic acids.A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase.ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase.The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity.Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha.Allostery in the dengue virus NS3 helicase: Insights into the NTPase cycle from molecular simulations.

P2860

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P2860

Helicase from hepatitis C virus, energetics of DNA binding.

http://www.wikidata.org/entity/Q43038035

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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name

Helicase from hepatitis C virus, energetics of DNA binding.

@en

Helicase from hepatitis C virus, energetics of DNA binding.

@nl

type

label

Helicase from hepatitis C virus, energetics of DNA binding.

@en

Helicase from hepatitis C virus, energetics of DNA binding.

@nl

prefLabel

Helicase from hepatitis C virus, energetics of DNA binding.

@en

Helicase from hepatitis C virus, energetics of DNA binding.

@nl

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P1433

Journal of Biological Chemistry

P1476

Helicase from hepatitis C virus, energetics of DNA binding.

@en

P2093

Mikhail K Levin

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

Smita S Patel

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P2860

Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3' nontranslated region are essential for virus replication in vivo

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

Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism

Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA

Calculation of protein extinction coefficients from amino acid sequence data

Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis.

Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A

C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity

P304

29377-29385

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scholarly article

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10.1074/JBC.M112315200

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P433

33

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P478

277

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2002-05-28T00:00:00Z

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12034714

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