A HIV-1 minimal gag protein is superior to nucleocapsid at in vitro annealing and exhibits multimerization-induced inhibition of reverse transcription.
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Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteinsFundamental differences between the nucleic acid chaperone activities of HIV-1 nucleocapsid protein and Gag or Gag-derived proteins: biological implicationsMatrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding.Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription.Nucleic acid chaperone activity of retroviral Gag proteinsRole of HIV-1 nucleocapsid protein in HIV-1 reverse transcription.Diverse interactions of retroviral Gag proteins with RNAs.HIV-1 nucleocapsid proteins as molecular chaperones for tetramolecular antiparallel G-quadruplex formation.Formation of the tRNALys packaging complex in HIV-1.HIV-1 Exploits a Dynamic Multi-aminoacyl-tRNA Synthetase Complex To Enhance Viral Replication.New Structure Sheds Light on Selective HIV-1 Genomic RNA Packaging.Molecular mimicry of human tRNALys anti-codon domain by HIV-1 RNA genome facilitates tRNA primer annealing
P2860
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P2860
A HIV-1 minimal gag protein is superior to nucleocapsid at in vitro annealing and exhibits multimerization-induced inhibition of reverse transcription.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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name
A HIV-1 minimal gag protein is ...... tion of reverse transcription.
@en
type
label
A HIV-1 minimal gag protein is ...... tion of reverse transcription.
@en
prefLabel
A HIV-1 minimal gag protein is ...... tion of reverse transcription.
@en
P2093
P2860
P356
P1476
A HIV-1 minimal gag protein is ...... tion of reverse transcription.
@en
P2093
Ariel Roldan
Chen Liang
Mark A Wainberg
Otis U Warren
Rodney S Russell
P2860
P304
17488-17496
P356
10.1074/JBC.M501310200
P407
P577
2005-02-24T00:00:00Z