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Sheila M. Green

Researcher at Laboratory of Molecular Biology

Publications -  12
Citations -  2185

Sheila M. Green is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: RNA & Binding site. The author has an hindex of 10, co-authored 12 publications receiving 2142 citations. Previous affiliations of Sheila M. Green include Medical Research Council.

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Human immunodeficiency virus 1 tat protein binds trans-activation-responsive region (TAR) RNA in vitro

TL;DR: Tat, the trans-activator protein for human immunodeficiency virus 1 (HIV-1), has been expressed in Escherichia coli from synthetic genes and binds specifically to HIV-1 trans-activation-responsive region (TAR) RNA in gel-retardation, filter-binding, and immunoprecipitation assays.
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HIV-1 tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure.

TL;DR: There is a direct correlation between the ability of tat to bind to TAR RNA and to activate HIV transcription, and Viral LTRs carrying TAR sequences encoding any of the mutations known to produce transcripts which bind tat weakly, are not stimulated efficiently by tat in vivo.
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HIV-1 regulator of virion expression (Rev) protein binds to an RNA stem-loop structure located within the Rev response element region

TL;DR: A approximately 33 nucleotide fragment is protected from ribonuclease T1 digestion by the binding of Rev to RRE RNA, suggesting that Rev binds with high affinity to only a restricted region of the RRE.
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High affinity binding of TAR RNA by the human immunodeficiency virus type-1 tat protein requires base-pairs in the RNA stem and amino acid residues flanking the basic region.

TL;DR: The binding site for tat protein on TAR RNA has been defined in quantitative terms using an extensive series of mutations and the binding of a series of peptides spanning the basic "arginine-rich" sequence of tat was examined using both filter-binding and gel mobility shift assays.
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A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression

TL;DR: The data suggest that the RRE acts as a "molecular rheostat" designed to detect rev levels during the early stages of the HIV growth cycle, with the longest truncations producing the greatest losses of activity.