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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 GTP binding protein RAN (RanGTP), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
|
Gag-Pol
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gag-pol
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Tandem affinity purification and mass spectrometry analysis identify GTP binding protein RAN (RanGTP), 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
|
nef
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Tandem affinity purification and mass spectrometry analysis identify GTP binding protein RAN (RanGTP), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
|
Pr55(Gag)
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gag
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Tandem affinity purification and mass spectrometry analysis identify GTP binding protein RAN (RanGTP), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
|
gag
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Ran terminates the nuclear import of the Matrix protein of HIV-1 Gag by directly binding to karyopherin beta and disassembling the import complex |
PubMed
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|
Rev
|
rev
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the GTP bound form of Ran (RanGTP) binds to a preformed Rev-CRM1 (exportin 1) complex to mediate nuclear export of HIV-1 mRNA |
PubMed
|
|
rev
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A dimeric CRM1-RanGTP complex binds a Rev-RRE complex to export the Rev-RRE complex from the nuclear to the cytoplasm in cells |
PubMed
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|
rev
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HIV-1 Rev interacting protein, RAN, is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells |
PubMed
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rev
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Rev-Rev interactions (multimerization) are enhanced by RanGTP |
PubMed
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|
rev
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binding of the GTP bound form of Ran (RanGTP) to a preformed Rev-CRM1 complex is linked to an interaction of RanGTP with the nuclear export signal (NES) of Rev (amino acids 75-83) |
PubMed
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Tat
|
tat
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Interaction of HIV-1 Tat with RAN in T-cells is identified by a proteomic strategy based on affinity chromatography |
PubMed
|
|
capsid
|
gag
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RanGTP inhibits the ability of TNPO3 to stimulate the uncoating of HIV-1 CA cores |
PubMed
|
|
integrase
|
gag-pol
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The binding between HIV-1 IN and TNPO3 is inhibited by RanGTP in a dose-dependent manner, leading to a TNPO3-RanGTP complex formation |
PubMed
|
|
matrix
|
gag
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Ran terminates the nuclear import of HIV-1 Matrix by directly binding to karyopherin beta and disassembling the import complex |
PubMed
|