Testing the balanced electrostatic interaction hypothesis of hepatitis B virus DNA synthesis by using an in vivo charge rebalance approach
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3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core ProteinNuclear export and import of human hepatitis B virus capsid protein and particlesNucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically.Secretion of genome-free hepatitis B virus--single strand blocking model for virion morphogenesis of para-retrovirus.A simple and general method for determining the protein and nucleic acid content of viruses by UV absorbanceC-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.Replication-competent infectious hepatitis B virus vectors carrying substantially sized transgenes by redesigned viral polymerase translation.Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging.Identification of a novel antimicrobial peptide from human hepatitis B virus core protein arginine-rich domain (ARD)MicroRNA-130a can inhibit hepatitis B virus replication via targeting PGC1α and PPARγA theoretical model for the dynamic structure of hepatitis B nucleocapsidThe Dual Role of an ESCRT-0 Component HGS in HBV Transcription and Naked Capsid Secretion.A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.MicroRNA miR-204 and miR-1236 inhibit hepatitis B virus replication via two different mechanisms.HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acidsCore protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Cell-Free Hepatitis B Virus Capsid Assembly Dependent on the Core Protein C-Terminal Domain and Regulated by PhosphorylationSerum viral duplex-linear DNA proportion increases with the progression of liver disease in patients infected with HBV.The Structural Biology of Hepatitis B Virus: Form and Function.The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication.A molecular thermodynamic model for the stability of hepatitis B capsids.PRMT5: A novel regulator of Hepatitis B virus replication and an arginine methylase of HBV core.Common and Distinct Capsid and Surface Protein Requirements for Secretion of Complete and Genome-free Hepatitis B Virions.Post-translational Modification Control of HBV Biological Processes
P2860
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P2860
Testing the balanced electrostatic interaction hypothesis of hepatitis B virus DNA synthesis by using an in vivo charge rebalance approach
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Testing the balanced electrost ...... vivo charge rebalance approach
@ast
Testing the balanced electrost ...... vivo charge rebalance approach
@en
type
label
Testing the balanced electrost ...... vivo charge rebalance approach
@ast
Testing the balanced electrost ...... vivo charge rebalance approach
@en
prefLabel
Testing the balanced electrost ...... vivo charge rebalance approach
@ast
Testing the balanced electrost ...... vivo charge rebalance approach
@en
P2093
P2860
P356
P1433
P1476
Testing the balanced electrost ...... vivo charge rebalance approach
@en
P2093
Chiaho Shih
Ching-Shu Suen
Fan-Mei Tang
Jyuan-Yuan Huang
Pong Kian Chua
P2860
P304
P356
10.1128/JVI.01666-09
P577
2009-12-16T00:00:00Z