Phosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs.
about
Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core proteinNuclear import and export of influenza virus nucleoprotein.Nuclear export and import of human hepatitis B virus capsid protein and particlesImportin β Can Bind Hepatitis B Virus Core Protein and Empty Core-Like Particles and Induce Structural ChangesNucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assemblyNuclear targeting of the cauliflower mosaic virus coat proteinPhosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase.Phosphorylation status of the parvovirus minute virus of mice particle: mapping and biological relevance of the major phosphorylation sites.Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically.Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativityPhosphoacceptors threonine 162 and serines 170 and 178 within the carboxyl-terminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication.A kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro.Phosphorylation state-dependent interactions of hepadnavirus core protein with host factorsC-terminal substitution of HBV core proteins with those from DHBV reveals that arginine-rich 167RRRSQSPRR175 domain is critical for HBV replication.Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.Hepatitis B viral core protein disrupts human host gene expression by binding to promoter regions.Sulfamoylbenzamide derivatives inhibit the assembly of hepatitis B virus nucleocapsids.Regulation of multiple stages of hepadnavirus replication by the carboxyl-terminal domain of viral core protein in trans.HBV life cycle: entry and morphogenesis.Role of peroxisome proliferator-activated receptor gamma coactivator 1alpha in AKT/PKB-mediated inhibition of hepatitis B virus biosynthesis.A theoretical model for the dynamic structure of hepatitis B nucleocapsidAutophagy required for hepatitis B virus replication in transgenic mice.Regulation of hepadnavirus reverse transcription by dynamic nucleocapsid phosphorylation.n-Butyrate, a cell cycle blocker, inhibits early amplification of duck hepatitis B virus covalently closed circular DNA after in vitro infection of duck hepatocytesA hydrophobic heptad repeat of the core protein of woodchuck hepatitis virus is required for capsid assembly.Tumor necrosis factor activates a conserved innate antiviral response to hepatitis B virus that destabilizes nucleocapsids and reduces nuclear viral DNA.Alteration of Mature Nucleocapsid and Enhancement of Covalently Closed Circular DNA Formation by Hepatitis B Virus Core Mutants Defective in Complete-Virion Formation.Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration.Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex.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.Electrostatic regulation of genome packaging in human hepatitis B virus.HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acidsPhosphorylation meets nuclear import: a review.Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Capsid Phosphorylation State and Hepadnavirus Virion SecretionExposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173).Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments.
P2860
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P2860
Phosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@ast
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@en
type
label
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@ast
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@en
prefLabel
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@ast
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@en
P2860
P1433
P1476
Phosphorylation and nuclear lo ...... e three repeated SPRRR motifs.
@en
P2860
P304
P407
P577
1995-02-01T00:00:00Z