RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP - Test2 - elhamkhani - TriplyDB

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

http://www.wikidata.org/entity/Q27477448

about

Identification of GBV-D, a novel GB-like flavivirus from old world frugivorous bats (Pteropus giganteus) in Bangladesh A polypeptide-DNA hybrid with selective linking capability applied to single molecule nano-mechanical measurements using optical tweezers Involvement of creatine kinase B in hepatitis C virus genome replication through interaction with the viral NS4A protein Hepatitis C virus proteins RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling RNA helicases at work: binding and rearranging Phosphate and R2D2 restrict the substrate specificity of Dicer-2, an ATP-driven ribonuclease Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase Multicolor super-resolution imaging with photo-switchable fluorescent probes Real-time observation of bacteriophage T4 gp41 helicase reveals an unwinding mechanism In silico investigation of conformational motions in superfamily 2 helicase proteins Structure-Based Mutational Analysis of the NS3 Helicase from Dengue Virus Role of Divalent Metal Cations in ATP Hydrolysis Catalyzed by the Hepatitis C Virus NS3 Helicase: Magnesium Provides a Bridge for ATP to Fuel Unwinding Studying Hepatitis C Virus: Making the Best of a Bad Virus NS3 helicase actively separates RNA strands and senses sequence barriers ahead of the opening fork NS3 Peptide, a Novel Potent Hepatitis C Virus NS3 Helicase Inhibitor: Its Mechanism of Action and Antiviral Activity in the Replicon System Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro 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 Fuel Specificity of the Hepatitis C Virus NS3 Helicase Helicase inhibitors as specifically targeted antiviral therapy for hepatitis C RNA Unwinding by NS3 Helicase: A Statistical Approach Hepatitis C: recent successes and continuing challenges in the development of improved treatment modalities Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism.Investigation of Translocation, DNA Unwinding, and Protein Displacement by NS3h, the Helicase Domain from the Hepatitis C Virus Helicase Structural basis for DNA duplex separation by a superfamily-2 helicase A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility Domain-level rocking motion within a polymerase that translocates on single-stranded nucleic acid Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme High-resolution optical tweezers for single-molecule manipulation.Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I.Impediment of E. coli UvrD by DNA-destabilizing force reveals a strained-inchworm mechanism of DNA unwinding In the absence of writhe, DNA relieves torsional stress with localized, sequence-dependent structural failure to preserve B-form Visualizing helicases unwinding DNA at the single molecule level Tracing entire operation cycles of molecular motor hepatitis C virus helicase in structurally resolved dynamical simulations.High-resolution, single-molecule measurements of biomolecular motion.Mechanism of strand displacement synthesis by DNA replicative polymerases Direct imaging of single UvrD helicase dynamics on long single-stranded DNA DNA Y structure: a versatile, multidimensional single molecule assay.

P2860

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P2860

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

http://www.wikidata.org/entity/Q27477448

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2006 թվականի հունվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@ast

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@en

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@nl

type

label

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@ast

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@en

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@nl

prefLabel

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@ast

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

@en

RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

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RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP

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P2093

Anna Marie Pyle

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

Ignacio Tinoco

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

Rudolf K Beran

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

Sophie Dumont

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

Victor Serebrov

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

Wei Cheng

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

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.

Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins

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

Structure of the hepatitis C virus RNA helicase domain

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

Entropic elasticity of lambda-phage DNA

Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks

Single-molecule assay reveals strand switching and enhanced processivity of UvrD

Forward and reverse motion of single RecBCD molecules on DNA.

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10.1038/NATURE04331

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7072

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439

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Carlos Bustamante

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2006-01-05T00:00:00Z

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1029960143

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1560093

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