Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity - Wikidata - thesis-toulmin - TriplyDB

Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity

Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity

http://www.wikidata.org/entity/Q33966563

about

Mechanisms of virus assembly Preparation by alkaline treatment and detailed characterisation of empty hepatitis B virus core particles for vaccine and gene therapy applications.Assembly-Directed Antivirals Differentially Bind Quasiequivalent Pockets to Modify Hepatitis B Virus Capsid Tertiary and Quaternary Structure Importin β Can Bind Hepatitis B Virus Core Protein and Empty Core-Like Particles and Induce Structural Changes Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA lattice Secretion of genome-free hepatitis B virus--single strand blocking model for virion morphogenesis of para-retrovirus.Viral double-strand RNA-binding proteins can enhance innate immune signaling by toll-like Receptor 3.Pathways for virus assembly around nucleic acids.A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro.A theoretical study of SRPK interaction with the flexible domains of hepatitis B capsids.A simple and general method for determining the protein and nucleic acid content of viruses by UV absorbance The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation.Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators.Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.Replication-competent infectious hepatitis B virus vectors carrying substantially sized transgenes by redesigned viral polymerase translation.Thermodynamic basis for the genome to capsid charge relationship in viral encapsidation.A theoretical model for the dynamic structure of hepatitis B nucleocapsid Whole-Chain Tick Saliva Proteins Presented on Hepatitis B Virus Capsid-Like Particles Induce High-Titered Antibodies with Neutralizing Potential Self-assembly of viral capsid protein and RNA molecules of different sizes: requirement for a specific high protein/RNA mass ratio.The Role of Packaging Sites in Efficient and Specific Virus Assembly Hepatitis B virus nucleocapsid but not free core antigen controls viral clearance in mice.Density functional theory for encapsidated polyelectrolytes: a comparison with Monte Carlo simulation.A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.Carbonyl J acid derivatives block protein priming of hepadnaviral P protein and DNA-dependent DNA synthesis activity of hepadnaviral nucleocapsids.Isothiafludine, a novel non-nucleoside compound, inhibits hepatitis B virus replication through blocking pregenomic RNA encapsidation.Hepatitis B Virus Core Protein Phosphorylation Sites Affect Capsid Stability and Transient Exposure of the C-terminal Domain.In vitro quantification of the relative packaging efficiencies of single-stranded RNA molecules by viral capsid protein.Cyclin-dependent kinase 2 phosphorylates s/t-p sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids.Hepatitis B Virus Capsids Have Diverse Structural Responses to Small-Molecule Ligands Bound to the Heteroaryldihydropyrimidine Pocket To build a virus on a nucleic acid substrate.Viral genome structures are optimal for capsid assembly HBV polymerase overexpression due to large core gene deletion enhances hepatoma cell growth by binding inhibition of microRNA-100.Structural insights into the coupling of virion assembly and rotavirus replication.Virus assembly, allostery and antivirals Hepatitis B core-based virus-like particles to present heterologous epitopes.Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.PGC1α Transcriptional Adaptor Function Governs Hepatitis B Virus Replication by Controlling HBcAg/p21 Protein-Mediated Capsid Formation.SplitCore: an exceptionally versatile viral nanoparticle for native whole protein display regardless of 3D structure.A Role for the Host DNA Damage Response in Hepatitis B Virus cccDNA Formation-and Beyond?

P2860

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P2860

Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity

http://www.wikidata.org/entity/Q33966563

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Full-length hepatitis B virus ...... y high levels of cooperativity

@ast

Full-length hepatitis B virus ...... y high levels of cooperativity

@en

type

label

Full-length hepatitis B virus ...... y high levels of cooperativity

@ast

Full-length hepatitis B virus ...... y high levels of cooperativity

@en

prefLabel

Full-length hepatitis B virus ...... y high levels of cooperativity

@ast

Full-length hepatitis B virus ...... y high levels of cooperativity

@en

P1433

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P1476

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P2093

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P2860

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P1433

Journal of Virology

P1476

Full-length hepatitis B virus ...... y high levels of cooperativity

@en

P2093

Daniel D Loeb

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

J Zachary Porterfield

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

Mary Savari Dhason

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

Stephen J Stray

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

P2860

Hepatitis B virus replication

Processive phosphorylation of alternative splicing factor/splicing factor 2

Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein

Sequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses

The crystal structure of the human hepatitis B virus capsid

How to measure and predict the molar absorption coefficient of a protein

Validity of nucleic acid purities monitored by 260nm/280nm absorbance ratios

Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids

A bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesis

Hepatitis B virus infection--natural history and clinical consequences

P304

7174-7184

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scholarly article

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10.1128/JVI.00586-10

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14

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84

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2010-04-28T00:00:00Z

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20427522

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2898219

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