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Article

Critical structural elements of the VP16 transcriptional activation domain.

Science (New York, N.Y.) - 4 Jan 1991

Cress W D, Triezenberg S J

Abstract excerpt

Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component...

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Source

Identifiers

PMID: 1846049
DOI: 10.1126/science.1846049

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Critical structural elements of the VP16 transcriptional activation domain.PMID 1846049Read ↗

Mutational analysis of a transcriptional activation region of the VP16 protein of herpes simplex virus.Semantic proximity Read ↗

Defective transcriptional activation by diverse VP16 mutants associated with a common inability to form open promoter complexes.Semantic proximity Read ↗

Transcriptional activation by DNA-binding derivatives of HSV-1 VP16 that lack the carboxyl-terminal acidic activation domain.Semantic proximity Read ↗

Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites.Semantic proximity Read ↗

Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB.Semantic proximity Read ↗

Structure of the VP16 transactivator target in the Mediator.Semantic proximity Read ↗

VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection.Semantic proximity Read ↗

Amino acid substitutions in the herpes simplex virus transactivator VP16 uncouple direct protein-protein interaction and DNA binding from complex assembly and transactivation.Semantic proximity Read ↗

Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 produces a phenotype similar to that of the in1814 linker insertion mutation.Semantic proximity Read ↗

The herpes simplex virus trans-activator VP16 recognizes the Oct-1 homeo domain: evidence for a homeo domain recognition subdomain.Semantic proximity Read ↗

Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements.Semantic proximity Read ↗

The C terminus of AvrXa10 can be replaced by the transcriptional activation domain of VP16 from the herpes simplex virus.Semantic proximity Read ↗

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