Histone acetylation in gene regulation
L Verdone, E Agricola, M Caserta… - Briefings in Functional …, 2006 - academic.oup.com
L Verdone, E Agricola, M Caserta, E Di Mauro
Briefings in Functional Genomics, 2006•academic.oup.comGenetic 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.
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.
Abstract
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.
Oxford University Press以上显示的是最相近的搜索结果。 查看全部搜索结果