ds-Oligonucleotide-peptide conjugates featuring peptides from the leucine-zipper region of Fos as switchable receptors for the oncoprotein Jun.
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منابع مشابه
New developments in the
The stability of oligodeoxynucleotides to trifluoroacetic acid is studied. Pyrimidine oligonucleotides were stable in the conditions used for the removal of tbutyl groups. Oligonucleotide-3’-peptide conjugates carrying pyrimidine oligonucleotides are prepared stepwise using peptide-supports and Fmoc, t-butyl strategy. Using this strategy we have prepared an oligonucleotide-peptide conjugate con...
متن کاملMechanism of specificity in the Fos-Jun oncoprotein heterodimer.
Fos and Jun, the protein products of the nuclear proto-oncogenes c-fos and c-jun, associate preferentially to form a heterodimer that binds to DNA and modulates transcription of a wide variety of genes in response to mitogenic stimuli. Both Fos and Jun contain a single leucine zipper region. Previous studies have shown that the leucine zippers of Fos and Jun are necessary and sufficient to medi...
متن کاملA Fluorescence Assay for Leucine Zipper Dimerization: Avoiding Unintended Consequences of Fluorophore Attachment
Formation of R-helical coiled-coil dimers represents one of the simplest examples of a specific protein-protein interaction. This dimerization mode is commonly observed among transcription regulator proteins, where the process is referred to as leucine zipper formation. Inhibitors of leucine zipper dimerization would allow one to control gene expression. As a first step toward identifying such ...
متن کاملNoncovalent multivalent assembly of jun peptides on a leucine zipper dendrimer displaying fos peptides.
[reaction: see text] The synthesis and characterization of a new leucine-zipper dendrimer (LZD) is reported that displays four copies of the peptide corresponding to the coiled-coiled dimerization domain of Fos. Circular dichroism spectroscopy, fluorescence titration, and sedimentation equilibrium experiments demonstrate that Fos-LZD can noncovalently assemble four copies of the peptide corresp...
متن کاملPreferential heterodimer formation by isolated leucine zippers from fos and jun.
The products of the nuclear oncogenes fos and jun are known to form heterodimers that bind to DNA and modulate transcription. Both proteins contain a leucine zipper that is important for heterodimer formation. Peptides corresponding to these leucine zippers were synthesized. When mixed, these peptides preferentially form heterodimers over homodimers by at least 1000-fold. Both homodimers and th...
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ورودعنوان ژورنال:
- Chembiochem : a European journal of chemical biology
دوره 8 10 شماره
صفحات -
تاریخ انتشار 2007