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Characterization of the Interaction between the Acidic Activation Domain of VP16 and the RNA Polymerase II Initiation Factor TFIIB

Data up to Jan 2025

Published1996
Citations25
References72

Total Citations Per Year

Abstract

References (72)

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Proline-rich activator CTF1 targets the TFIIB assembly step during transcriptional activation.

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Initiation of transcription by RNA polymerase II is limited by melting of the promoter DNA in the region immediately upstream of the initiation site.

1994 • 110 citations

Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription.

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The acidic activation domain of the Epstein-Barr virus transcription factor R interacts in vitro with both TBP and TFIIB and is cell-specifically potentiated by a proline-rich region.

1993 • 47 citations

The ability to associate with activation domains in vitro is not required for the TATA box-binding protein to support activated transcription in vivo.

1995 • 39 citations

Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB.

1993 • 32 citations

Promoter-dependent Photocross-linking of the Acidic Transcriptional Activator E2F-1 to the TATA-binding Protein

1995 • 30 citations

Transcriptional activation by the acidic domain of Vmw65 requires the integrity of the domain and involves additional determinants distinct from those necessary for TFIIB binding.

1993 • 28 citations

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Characterization of the Interaction between the Acidic Activation Domain of VP16 and the… (1996) – Nucleic Acids Research | Metascience Observatory Explorer