2010
DOI: 10.4161/nucl.11300
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Nucleocytoplasmic shuttling of HIV-1 integrase is controlled by the viral Rev protein

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Cited by 11 publications
(14 citation statements)
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“…As shown in Figure 1B and C, these two peptides failed to promote dissociation of the IN-TNPO3 complex, indicating that different domains mediate the interaction of IN with these two nuclearimport receptors. The results in Figure 1 also show that neither peptide had any effect on the interaction between Rev and IN, shown by us previously to occur in virus-infected cells [40][41][42][43][44] and indicating specificity of function.…”
Section: Introductionmentioning
confidence: 49%
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“…As shown in Figure 1B and C, these two peptides failed to promote dissociation of the IN-TNPO3 complex, indicating that different domains mediate the interaction of IN with these two nuclearimport receptors. The results in Figure 1 also show that neither peptide had any effect on the interaction between Rev and IN, shown by us previously to occur in virus-infected cells [40][41][42][43][44] and indicating specificity of function.…”
Section: Introductionmentioning
confidence: 49%
“…7A). Interestingly, the Rev protein which, similar to the Rev-derived peptides, has been shown to block nuclear import of IN, 42 prevented interaction of IN with both receptors. The disruption of the IN-TNPO3 complex by the Rev derived and IN-1 peptides is not necessarily due to direct masking of the TNPO3 binding sites.…”
Section: Discussionmentioning
confidence: 99%
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