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

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

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

http://www.wikidata.org/entity/Q28475989

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Virus strategies for passing the nuclear envelope barrier Preparation by alkaline treatment and detailed characterisation of empty hepatitis B virus core particles for vaccine and gene therapy applications.Molecular biology of hepatitis B virus infection Nuclear export and import of human hepatitis B virus capsid protein and particles Importin β Can Bind Hepatitis B Virus Core Protein and Empty Core-Like Particles and Induce Structural Changes Hepatitis B virus molecular biology and pathogenesis Generation of covalently closed circular DNA of hepatitis B viruses via intracellular recycling is regulated in a virus specific manner.Review of hepatocellular carcinoma: Epidemiology, etiology, and carcinogenesis Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity Viral double-strand RNA-binding proteins can enhance innate immune signaling by toll-like Receptor 3.Coexistence of hepatitis B virus quasispecies enhances viral replication and the ability to induce host antibody and cellular immune responses.A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro.Control of hepatitis B virus replication by interferons and Toll-like receptor signaling pathways Subunit exchange rates in Hepatitis B virus capsids are geometry- and temperature-dependent.Potent inhibition of late stages of hepadnavirus replication by a modified cell penetrating peptide Parvovirus particles and movement in the cellular cytoplasm and effects of the cytoskeleton.Hepatitis B and C virus hepatocarcinogenesis: lessons learned and future challenges.A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore.Hepatitis B Virus Core Protein Phosphorylation Sites Affect Capsid Stability and Transient Exposure of the C-terminal Domain.Cyclin-dependent kinase 2 phosphorylates s/t-p sites in the hepadnavirus core protein C-terminal domain and is incorporated into viral capsids.Viral subversion of the nuclear pore complex.Maturation-associated destabilization of hepatitis B virus nucleocapsid.Nuclear Import of Hepatitis B Virus Capsids and Genome.Implications of the nucleocapsid and the microenvironment in retroviral reverse transcription.Viruses challenge selectivity barrier of nuclear pores Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Intracytoplasmic Transport of Hepatitis B Virus Capsids.Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in the nuclear basket Identification and characterization of a novel bipartite nuclear localization signal in the hepatitis B virus polymerase Coexpression network analysis in chronic hepatitis B and C hepatic lesions reveals distinct patterns of disease progression to hepatocellular carcinoma.Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded.Hepatitis B virus: virology, molecular biology, life cycle and intrahepatic spread.Spatiotemporal dynamics of HSV genome nuclear entry and compaction state transitions using bioorthogonal chemistry and super-resolution microscopy.The diverse functions of the hepatitis B core/capsid protein (HBc) in the viral life cycle: Implications for the development of HBc-targeting antivirals.Hepatitis B virus core protein allosteric modulators can distort and disrupt intact capsids.

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P2860

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

http://www.wikidata.org/entity/Q28475989

description

2009 nî lūn-bûn

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2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի օգոստոսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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type

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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prefLabel

Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

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JOURNAL.PPAT.1000563

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Nuclear entry of hepatitis B v ...... clear reassociation to capsids

@en

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Andreas Bischof

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

Birgit Rabe

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

Christian Cazenave

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

Michael Foss

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

Michael Kann

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

Michel Castroviejo

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

Mildred Delaleau

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

Paul Pumpens

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

P2860

Nuclear envelope permeability

Detection of specific sequences among DNA fragments separated by gel electrophoresis

The crystal structure of the human hepatitis B virus capsid

Hepatitis B virus nucleocapsid particles do not cross the hepatocyte nuclear membrane in transgenic mice

Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein.

A structural model for maturation of the hepatitis B virus core

Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry.

A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assembly

Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm

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e1000563

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scholarly article

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4103958

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10.1371/JOURNAL.PPAT.1000563

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8

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5

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Irina Sominskaya

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2009-08-28T00:00:00Z

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26774095

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19714236

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2727048

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