C
Cory Abate
Researcher at Roche Institute of Molecular Biology
Publications - 15
Citations - 3435
Cory Abate is an academic researcher from Roche Institute of Molecular Biology. The author has contributed to research in topics: Binding site & Leucine zipper. The author has an hindex of 14, co-authored 15 publications receiving 3411 citations.
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Journal ArticleDOI
Redox regulation of fos and jun DNA-binding activity in vitro
TL;DR: DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation of a single conserved cysteine residue in the DNA-binding domains of the two proteins, suggesting that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism.
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Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding Domains
TL;DR: The data suggest that Fos and Jun dimerize via a parallel interaction of helical domains containing a heptad repeat ofLeucine residues (the leucine zipper).
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Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
TL;DR: Evidence is provided that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kDa ribosomal S6 kinase (RSK and MAP kinase), contribute to the serum-induced phosphorylation of c-Fos.
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Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly.
TL;DR: UV-crosslinking studies demonstrated that Fos and Jun contact DNA directly and that both proteins interacted equivalently with either strand of the AP-1-binding site, suggesting efficient DNA binding of wbJun and wbFos-wbJun complexes required an additional activity present in nuclear extracts.
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Altered protein conformation on DNA binding by fos and jun
L Patel,Cory Abate,Tom Curran +2 more
TL;DR: Assessment systems using fluorescence spectroscopy and circular dichroism to monitor dimerization and DNA binding directly indicate that the interaction of Fos and Jun with DNA results in an altered conformation of the protein dimers and an increased α-helical content.