Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.
about
Foamy virus assembly with emphasis on pol encapsidationFoamy Virus Protein-Nucleic Acid Interactions during Particle MorphogenesisEvidence that the human foamy virus genome is DNANon-simian foamy viruses: molecular virology, tropism and prevalence and zoonotic/interspecies transmissionFoamy viruses are unconventional retrovirusesThe roles of Pol and Env in the assembly pathway of human foamy virus.Proteolytic processing and assembly of gag and gag-pol proteins of TED, a baculovirus-associated retrotransposon of the gypsy family.Proteolytic activity, the carboxy terminus of Gag, and the primer binding site are not required for Pol incorporation into foamy virus particles.Mutation of the catalytic domain of the foamy virus reverse transcriptase leads to loss of processivity and infectivity.Foamy retrovirus integrase contains a Pol dimerization domain required for protease activation.Efficient transient genetic manipulation in vitro and in vivo by prototype foamy virus-mediated nonviral RNA transferExpression and maturation of human foamy virus Gag precursor polypeptides.Characterization of the genome of feline foamy virus and its proteins shows distinct features different from those of primate spumavirusesAmino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.Foamy virus reverse transcriptase is expressed independently from the Gag protein.The foamy virus Gag proteins: what makes them different?Comparative studies on retroviral proteases: substrate specificity.Orthoretroviral-like prototype foamy virus Gag-Pol expression is compatible with viral replication.Prototype foamy virus protease activity is essential for intraparticle reverse transcription initiation but not absolutely required for uncoating upon host cell entry.Molecular characterization of proteolytic processing of the Gag proteins of human spumavirusCharacterization of a cis-acting sequence in the Pol region required to transfer human foamy virus vectors.Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease.A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity.Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain.Foamy virus particle formation.An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivityThe human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein.The carboxyl terminus of the human foamy virus Gag protein contains separable nucleic acid binding and nuclear transport domainsNuclear targeting of incoming human foamy virus Gag proteins involves a centriolar step.Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle.N-terminal Gag domain required for foamy virus particle assembly and export.Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assemblyFoamy virus Gag p71-p68 cleavage is required for template switch of the reverse transcriptase.The prototype foamy virus protease is active independently of the integrase domain.Protease-dependent uncoating of a complex retrovirus.Role of the foamy virus Pol cleavage site in viral replication.
P2860
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P2860
Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Active foamy virus proteinase ...... ormation of a Pol polyprotein.
@en
type
label
Active foamy virus proteinase ...... ormation of a Pol polyprotein.
@en
prefLabel
Active foamy virus proteinase ...... ormation of a Pol polyprotein.
@en
P2093
P2860
P1433
P1476
Active foamy virus proteinase ...... ormation of a Pol polyprotein.
@en
P2093
Kräusslich HG
Zentgraf H
P2860
P304
P407
P577
1995-11-01T00:00:00Z