Proteolytic processing of foamy virus Gag and Pol proteins.
about
Determination of the relative amounts of Gag and Pol proteins in foamy virus particlesFoamy virus biology and its application for vector developmentFoamy virus budding and releaseA unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsidFoamy Virus Protein-Nucleic Acid Interactions during Particle MorphogenesisOrchestrating the Selection and Packaging of Genomic RNA by Retroviruses: An Ensemble of Viral and Host FactorsNon-simian foamy viruses: molecular virology, tropism and prevalence and zoonotic/interspecies transmissionAn N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivityA comparative analysis of the foamy and ortho virus capsid structures reveals an ancient domain duplication.Early reverse transcription is essential for productive foamy virus infection.A nuclear export signal within the structural Gag protein is required for prototype foamy virus replicationStructure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.Genetic characterization of simian foamy viruses infecting humans.Restriction of foamy viruses by primate Trim5alphaAmino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding.Role of the C terminus of foamy virus Gag in RNA packaging and Pol expressionComparative studies on retroviral proteases: substrate specificity.Prototype foamy virus protease activity is essential for intraparticle reverse transcription initiation but not absolutely required for uncoating upon host cell entry.The multifaceted poliovirus 2A protease: regulation of gene expression by picornavirus proteases.AZT-resistant foamy virus.Correct capsid assembly mediated by a conserved YXXLGL motif in prototype foamy virus Gag is essential for infectivity and reverse transcription of the viral genome.N-terminal Gag domain required for foamy virus particle assembly and export.RNA and protein requirements for incorporation of the Pol protein into foamy virus particlesDistinct Particle Morphologies Revealed through Comparative Parallel Analyses of Retrovirus-Like Particles.Basic residues in the foamy virus Gag protein.Protease-dependent uncoating of a complex retrovirus.Role of the foamy virus Pol cleavage site in viral replication.
P2860
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P2860
Proteolytic processing of foamy virus Gag and Pol proteins.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Proteolytic processing of foamy virus Gag and Pol proteins.
@ast
Proteolytic processing of foamy virus Gag and Pol proteins.
@en
type
label
Proteolytic processing of foamy virus Gag and Pol proteins.
@ast
Proteolytic processing of foamy virus Gag and Pol proteins.
@en
prefLabel
Proteolytic processing of foamy virus Gag and Pol proteins.
@ast
Proteolytic processing of foamy virus Gag and Pol proteins.
@en
P1476
Proteolytic processing of foamy virus Gag and Pol proteins.
@en
P2093
K I Pfrepper
R M Flügel
P577
2003-01-01T00:00:00Z