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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 X-linked DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 (DDX3X), 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 X-linked DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 (DDX3X), 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 X-linked DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 (DDX3X), 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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Cellular biotinylated DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked (DDX3X) protein is incorporated into HIV-1 Gag virus-like particles |
PubMed
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gag
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Tandem affinity purification and mass spectrometry analysis identify X-linked DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 (DDX3X), 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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HIV-1 Rev function is inhibited by DDX3X expression in astrocytes |
PubMed
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rev
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Computational molecular docking, alanine scanning, clustering, and evolutionary analysis reveal the interaction of DDX3 with HIV-1 Rev-CRM1-RanGTP complex |
PubMed
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rev
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Coexpression of HIV-1 Rev with DDX3 greatly upregulate the expression of HIV-1 CA in HeLa cells |
PubMed
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rev
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DDX3 interacts with DDX1 or DDX5 and synergistically enhances the Rev function |
PubMed
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rev
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DDX3 interacts with HIV-1 Rev and enhances the Rev function. DDX3 co-localizes with Rev in both nucleolus and cytoplasm |
PubMed
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rev
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Translation of HIV-1 early regulatory proteins Tat and Rev is impaired in DDX3-depleted cells. The RNA helicase activity of DDX3 is required for its function in HIV-1 mRNA translation via 5'UTRs |
PubMed
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rev
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As part of the HIV-1 Rev-RRE/CRM1 pathway, DDX3, an RNA-dependent ATPase/helicase, locates to nuclear pores and binds CRM1 in order to export Rev and unspliced/partially spliced HIV-1 transcripts to the cytoplasm |
PubMed
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rev
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HIV-1 Rev interacting protein, DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 X-linked (DDX3X), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with DDX3X is increased by RRE |
PubMed
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Tat
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tat
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DEAD (Asp-Glu-Ala-Asp) box helicase 3, X-linked (DDX3) 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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DDX3 enhances the HIV-1 Tat-induced transcription and co-localizes with Tat in cytoplasmic foci in 293FT cells |
PubMed
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tat
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Translation of HIV-1 early regulatory proteins Tat and Rev is impaired in DDX3-depleted cells. The RNA helicase activity of DDX3 is required for its function in HIV-1 mRNA translation via 5'UTRs |
PubMed
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tat
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HIV-1 Tat co-localizes with DDX3 in cytoplasmic stress granules under stree conditions |
PubMed
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tat
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HIV-1 Tat binds DDX3 in vitro and in vivo. The C-terminal region (residues 536-661) of DDX3 is responsible for Tat binding |
PubMed
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capsid
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gag
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Coexpression of HIV-1 Rev with DDX3 greatly upregulate the expression of HIV-1 CA in HeLa cells |
PubMed
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