The prototype foamy virus protease is active independently of the integrase domain.
about
Evolution of foamy viruses: the most ancient of all retrovirusesFoamy virus assembly with emphasis on pol encapsidationMutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding.Prototype foamy virus protease activity is essential for intraparticle reverse transcription initiation but not absolutely required for uncoating upon host cell entry.Expression of prototype foamy virus pol as a Gag-Pol fusion protein does not change the timing of reverse transcription.Foamy virus Gag p71-p68 cleavage is required for template switch of the reverse transcriptase.Structural requirements for enzymatic activities of foamy virus protease-reverse transcriptase.
P2860
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P2860
The prototype foamy virus protease is active independently of the integrase domain.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The prototype foamy virus protease is active independently of the integrase domain.
@en
The prototype foamy virus protease is active independently of the integrase domain.
@nl
type
label
The prototype foamy virus protease is active independently of the integrase domain.
@en
The prototype foamy virus protease is active independently of the integrase domain.
@nl
prefLabel
The prototype foamy virus protease is active independently of the integrase domain.
@en
The prototype foamy virus protease is active independently of the integrase domain.
@nl
P2093
P2860
P356
P1433
P1476
The prototype foamy virus protease is active independently of the integrase domain.
@en
P2093
Axel Rethwilm
Birgitta M Wöhrl
Maximilian J Hartl
Ralf Spannaus
P2860
P2888
P356
10.1186/1742-4690-9-41
P50
P577
2012-05-10T00:00:00Z
P5875
P6179
1030302413