RNA aptamers selected to bind human immunodeficiency virus type 1 Rev in vitro are Rev responsive in vivo

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Restriction of human immunodeficiency virus type 1 Rev function in murine A9 cells involves the Rev C-terminal domain.

The human immunodeficiency virus type 1 (HIV-1) Rev and human T-cell leukemia virus type 1 (HTLV-1) Rex proteins are essential for the expression of viral structural proteins and productive infection. Both contain a nuclear export signal (NES) in their C-terminal domain and a nuclear localization signal (NLS) in their N-terminal domain. The NES and NLS are necessary for shuttling between nucleu...

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Phenotypic analysis of human immunodeficiency virus type 1 Rev trimerization-interface mutants in human cells.

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The human immunodeficiency virus type 1 Rev protein and the Rev-responsive element counteract the effect of an inhibitory 5' splice site in a 3' untranslated region.

A 5' splice site located in a 3' untranslated region (3'UTR) has been shown previously to inhibit gene expression. Natural examples of inhibitory 5' splice sites have been identified in the late 3'UTRs of papillomaviruses and are thought to inhibit viral late gene expression at early stages of the viral life cycle. In this study, we demonstrate that the interaction of the human immunodeficiency...

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Conserved functional organization of the human immunodeficiency virus type 1 and visna virus Rev proteins.

Visna virus encodes a posttranscriptional regulatory protein that is functionally analogous to the Rev trans activator of human immunodeficiency virus type 1. Here, we demonstrate that the known functional organization of the human immunodeficiency virus type 1 Rev trans activator is shared by the distantly related visna virus Rev protein. In particular, both Rev proteins contain an N-terminal ...

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Phosphorylation of the rev gene product of human immunodeficiency virus type 1.

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ژورنال

عنوان ژورنال: Journal of Virology

سال: 1996

ISSN: 0022-538X,1098-5514

DOI: 10.1128/jvi.70.1.179-187.1996