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Pr55(Gag)
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gag
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Human CRM1 exports gag mRNA to the cytoplasm more efficiently than rat CRM1 in rat cells, leading to efficient processing of Gag proteins and particle formation |
PubMed
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gag
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Mouse-human CRM1 chimera analysis reveals that the amino-acid residues 146-444 of human CRM1 are important for increased HIV-1 titers in mouse cells. Three residues P411/M412/F414 are critical for human CRM1 function |
PubMed
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gag
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Human CRM1 increases HIV-1 Gag production in mouse cells. Human CRM1 and SRp40 increase the amount of unspliced HIV-1 RNA and have a more-than-additive effect on HIV-1 titers in mouse cells |
PubMed
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gag
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Human CRM1 enhances HIV-1 MA-dependent Gag membrane targeting in mouse cells |
PubMed
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gag
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Expression of CRM1 enhances Gag production 10-15 fold in rat macrophages, but only marginally in rat T cells. Expression of both CRM1 and CycT1 factors synergistically enhances Gag production to levels approximately 10-40% of those detected in human cells |
PubMed
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gag
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HIV-1 Matrix contains a nuclear export signal (amino acids 15-32) which is recognized by exportin 1 (CRM1; XPO1) and is important for nucleocytoplasmic shuttling of HIV-1 Gag and genomic RNA to the cytoplasm by exportin 1 |
PubMed
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Rev
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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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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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Co-immunoprecipitation analysis demonstrates that endogenous RBM14 associates with HIV-1 Rev, XPO1, and p54NRB in cells |
PubMed
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rev
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The CRM1 dimer interface, including residues T346, P411, M412, F414, R474, E478, and H481, facilitates cooperative assembly with the Rev-RRE complex |
PubMed
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rev
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CRM1-mediated nuclear export of Rev involves interactions of CRM1 with RanGTP, RanBP1 and RanGEF |
PubMed
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rev
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CRM1 interacts with the nuclear export signal of Rev and acts as a bridge between Rev and nuclear pore proteins |
PubMed
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rev
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Nuclear export of Rev is dependent on its activation domain which encodes a nuclear export signal (amino acids 75-83) |
PubMed
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rev
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The addition of a second NES to HIV-1 Rev or a second RRE to Rev-dependent transcripts rescues HIV-1 virion production in murine cells independently of human CRM1 |
PubMed
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rev
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HIV-1 Rev co-localizes with CRM1 at the HIV-1 transcription site in the nucleus |
PubMed
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rev
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Human CRM1 rescues RRE/Rev-dependent HIV-1 virion production in mouse cells |
PubMed
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rev
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Rev recruitment of CRM1 to HIV-1 mRNA is sufficient to mediate nuclear export of incompletely spliced HIV-1 mRNA |
PubMed
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rev
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Ratjadone A (myxobacterial metabolite) interacts with CRM1 to inhibit the Rev-dependent HIV-1 RNA nuclear export |
PubMed
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rev
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Eukaryotic initiation factor 5A (eIF-5A) mediates the binding of CRM1 to Rev |
PubMed
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rev
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Interaction of CRM1 with nucleoporins Nup42 and Nup159 results in the release of Rev from CRM1 |
PubMed
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rev
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During Rev-mediated nuclear export of HIV-1 mRNA, Rev interacts directly with the nucleocytoplasmic mRNA-transport system |
PubMed
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rev
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Excess CRM1 may downregulate Rev-mediated RNA export by sequestering Rev to a subnucleolar structure |
PubMed
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rev
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Nuclear retention and co-localization of Rev and CRM1 is caused by down-modulation of GAP-associated tyrosine phosphoprotein p62 (Sam68), suggesting Sam68 is directly involved in the CRM1-mediated Rev nuclear export pathway |
PubMed
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rev
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HIV-1 Rev interacting protein, exportin 1 (XPO1), 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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The HEAT repeat helix 9A domain (residues 402-423) of CRM1 serves as an effective cofactor for HIV-1 Rev function in higher primates |
PubMed
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rev
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Three specific domains (residues 89-123, 405-593, and 594-670) of NF90 promote Rev-RRE mediated nuclear export of Gag mRNA, which is dependent on CRM1 function |
PubMed
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rev
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HIV-1 Rev/CRM1 export complexes are observed in nucleoli by cotransfection with CFP/YFP pairs of the proteins on a large three-dimensional set of fixed cells, with Rev/CRM1 colocalization in nucleoli decreasing exponentially after addition of leptomycin B |
PubMed
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rev
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Studies suggest Rev is necessary and sufficient for the accumulation of incompletely spliced HIV RNAs at nuclear pores while CRM1 is required for translocation across the nuclear pore complex |
PubMed
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rev
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Rev-Rev interactions (multimerization) are enhanced by CRM1 |
PubMed
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rev
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The C-terminal region of Rev (amino acids 86-116) plays a role in enhancing the interaction of Rev with CRM1 |
PubMed
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rev
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CRM1 is involved in the binding of Rev to yeast Rip1 and hRip/Rab, which is involved in Rev-mediated nuclear export of HIV-1 mRNA |
PubMed
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rev
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CRM1 interacts with FG-repeat-containing nuclear pore proteins during nuclear export of Rev |
PubMed
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Tat
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tat
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Exportin 1 (XPO1, CRM1 homolog) 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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Interaction of HIV-1 Tat with XPO1 in T-cells is identified by a proteomic strategy based on affinity chromatography |
PubMed
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Vpr
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vpr
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Nuclear export of HIV-1 Vpr by exportin-1 is required for efficient HIV replication in tissue macrophages and is important for Vpr incorporation into virions |
PubMed
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vpr
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HIV-1 Vpr contains a nuclear export signal within amino acids 1-71 that is sensitive to Leptomycin B, suggesting it is recognized by CRM1 (exportin 1) |
PubMed
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Vpu
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vpu
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HIV-1 Vpu is identified to have a physical interaction with exportin 1 (XPO1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses |
PubMed
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capsid
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gag
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Human CRM1 and SRp40 have a more-than-additive effect on HIV-1 CA production in mouse cells |
PubMed
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matrix
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gag
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Human CRM1 enhances HIV-1 MA-dependent Gag membrane targeting in mouse cells |
PubMed
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gag
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HIV-1 Matrix contains a nuclear export signal (amino acids 15-32) which is recognized by exportin 1 (CRM1; XPO1) and is important for nucleocytoplasmic shuttling of HIV-1 Gag and genomic RNA to the cytoplasm by exportin 1 |
PubMed
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