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Envelope surface glycoprotein gp120
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env
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Tandem affinity purification and mass spectrometry analysis identify DEAD (Asp-Glu-Ala-Asp) box helicase 1 (DDX1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Gag-Pol
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gag-pol
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Tandem affinity purification and mass spectrometry analysis identify DEAD (Asp-Glu-Ala-Asp) box helicase 1 (DDX1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Nef
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nef
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Tandem affinity purification and mass spectrometry analysis identify DEAD (Asp-Glu-Ala-Asp) box helicase 1 (DDX1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Pr55(Gag)
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gag
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Tandem affinity purification and mass spectrometry analysis identify DEAD (Asp-Glu-Ala-Asp) box helicase 1 (DDX1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Rev
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rev
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Overexpression of DDX1 can compensate for the inhibitory effect of HIV-1 Tat mutant Nullbasic on HIV-1 Rev function |
PubMed
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rev
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HIV-1 Tat mutant Nullbasic can compete with HIV-1 Rev for binding to DDX1 and the interaction of Nullbasic with DDX1 is not through Tat's basic domain |
PubMed
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rev
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DDX1 co-localizes with HIV-1 Rev in the nucleolus. DDX1 interacts with DDX3 or DDX5 and synergistically enhances the Rev function |
PubMed
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rev
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The RNA helicase DDX1 interacts with HIV-1 Rev through yeast two-hybrid screening and co-immunoprecipitation assays, and DDX1 is required for proper subcellular localization of Rev |
PubMed
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rev
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DDX1 interacts with HIV-1 Rev and promotes oligomerization of Rev on the RRE. The location of the DDX1 binding region in Rev is amino acids 10 to 24 |
PubMed
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rev
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HIV-1 Rev interacting protein, DEAD (Asp-Glu-Ala-Asp) box polypeptide 1 (DDX1), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with DDX1 is increased by RRE |
PubMed
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rev
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The HIV-1 Rev V16D, I55N, and V16D/I55N mutants abolish the interaction between Rev and DDX1 |
PubMed
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rev
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Overexpression of exogenous DDX1 significantly alters both Rev sub-cellular localization from cytoplasmic to nuclear predominance and concomitantly increases HIV-1 viral production in human astrocytes |
PubMed
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rev
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Endogenous DDX1 expression in human astrocytes leads to a shift of Rev sub-cellular distribution dominance from nuclear and/or nucleolar to cytoplasmic |
PubMed
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rev
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DDX1 is capable of binding to HIV-1 RRE RNA in vivo, suggesting an interaction with HIV-1 Rev, however DDX1 alone cannot rescue HIV-1 virion production from a Rev-negative provirus in the absence of Rev |
PubMed
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Tat
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tat
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DEAD (Asp-Glu-Ala-Asp) box helicase 1 (DDX1) is identified to interact with HIV-1 Tat mutant Nullbasic in HeLa cells by LC MS/MS |
PubMed
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tat
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HIV-1 Tat mutant Nullbasic can compete with HIV-1 Rev for binding to DDX1 and the interaction of Nullbasic with DDX1 is not through Tat's basic domain |
PubMed
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tat
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HIV-1 Tat mutant Nullbasic significantly enhances the level of DDX1 in the cytoplasm compared with in its absence |
PubMed
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tat
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Overexpression of DDX1 can compensate for the inhibitory effect of HIV-1 Tat mutant Nullbasic on HIV-1 Rev function |
PubMed
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capsid
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gag
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Coexpression of HIV-1 Rev with DDX1 greatly downregulate the expression of HIV-1 CA in HeLa cells |
PubMed
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