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Briefings in Functional Genomics and Proteomics Advance Access originally published online on July 28, 2006
Briefings in Functional Genomics and Proteomics 2006 5(3):209-221; doi:10.1093/bfgp/ell028
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© Oxford University Press, 2006, All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Special Issue Papers

Histone acetylation in gene regulation

Loredana Verdone, Eleonora Agricola, Micaela Caserta and Ernesto Di Mauro

Corresponding author. Ernesto Di Mauro, Dipartimento di Genetica e Biologia Molecolare, Università ‘La Sapienza’, P.le Aldo Moro 5, 00185, Rome, Italy. Tel: ++39–06–49912096; Fax: ++39–06–49912500; E-mail: ernesto.dimauro{at}uniroma1.it

Genetic information is packaged in the highly dynamic nucleoprotein structure called chromatin. Many biological processes are regulated via post-translational modifications of key proteins. Acetylation of lysine residues at the N-terminal histone tails is one of the most studied covalent modifications influencing gene regulation in eukaryotic cells.

This review focuses on the role of enzymes involved in controlling both histone and non-histone proteins acetylation levels in the cell, with particular emphasis on their effects on cancer.

Keywords: nucleosomes, gene expression, acetylation, deacetylation, cancer


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