Resveratrol suppresses nuclear factor-kappaB in herpes simplex virus infected cells.
Animals; Antiviral Agents/*pharmacology; Cell Nucleus/chemistry; Cercopithecus aethiops; Cytoplasm/chemistry; DNA; Electrophoretic Mobility Shift Assay; Fluorescence; Herpesvirus 1; Herpesvirus 2; Human/drug effects/genetics/*growth & development; Human/drug effects/genetics/*physiology; I-kappa B Proteins/metabolism; Messenger/biosynthesis; Microscopy; NF-kappa B/*metabolism; NF-KappaB Inhibitor alpha; Polymerase Chain Reaction; Resveratrol; Reverse Transcriptase Polymerase Chain Reaction; RNA; Stilbenes/*pharmacology; Transcription Factor RelA/metabolism; Vero Cells; Viral/biosynthesis; Virus Replication/*drug effects
Resveratrol inhibits herpes simplex virus (HSV) replication by an unknown mechanism. Previously it was suggested that this inhibition may be mediated through a cellular factor essential for HSV replication [Docherty, J.J., Fu, M.M., Stiffler, B.S., Limperos, R.J., Pokabla, C.M., DeLucia, A.L., 1999. Resveratrol inhibition of herpes simplex virus replication. Antivir. Res. 43,
Faith Seth A; Sweet Thomas J; Bailey Erin; Booth Tristan; Docherty John J
Antiviral research
2006
2006-12
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1016/j.antiviral.2006.06.011" target="_blank" rel="noreferrer noopener">10.1016/j.antiviral.2006.06.011</a>
Binding of sequence-specific proteins to the 3'-untranslated region of vasoactive intestinal peptide mRNA.
Animals; Anterior/*metabolism; Base Sequence; Binding; Competitive; Cytoplasm/chemistry; Gene Expression Regulation; Genomic Library; Male; Messenger/*metabolism; Molecular Sequence Data; Pituitary Gland; Post-Transcriptional; Protein Binding; Proto-Oncogene Proteins c-fos/genetics; Rats; RNA; RNA Processing; RNA-Binding Proteins/*metabolism; RNA/metabolism; Sprague-Dawley; Subcellular Fractions; Tissue Distribution; Vasoactive Intestinal Peptide/*genetics
Multimeric AUUUA elements in an AU-rich 3'-untranslated region (3'-UTR) have been shown to confer message instability to numerous ephemeral transcripts through the formation of RNA-protein complexes. We show here that the 3'-UTR of VIP mRNA, which contains 3 AUUUA motifs in an AU-rich context, forms specific complexes with cytoplasmic proteins in a concentration-dependent, tissue-specific manner. We also demonstrate that an AU-rich segment of c-fos mRNA can successfully compete with VIP mRNA for binding with cytoplasmic proteins. These studies provide the first evidence for a mechanism by which VIP is post-transcriptionally regulated through specific sequences in its 3'-UTR.
Wolford J K; Signs S A
Biochemical and biophysical research communications
1995
1995-06
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1006/bbrc.1995.1885" target="_blank" rel="noreferrer noopener">10.1006/bbrc.1995.1885</a>