Genome Biology
|
Viewing options:Associated material:Related literature:- Articles citing this article
- Other articles by authors
- Related articles/pages
Tools:Post to:
|
ReviewThe diversity of acetylated proteinsBogdan Polevoda and Fred Sherman  Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA  author email corresponding author email
Genome Biology 2002,
3:reviews0006.1-0006.6doi:10.1186/gb-2002-3-5-reviews0006
Subject areas: Biochemistry and structural biology, Molecular biology, Genetics, Cell biology Abstract
Acetylation of proteins, either on various amino-terminal residues or on the ε-amino group of lysine residues, is catalyzed by a wide range of acetyltransferases. Amino-terminal acetylation occurs on the bulk of eukaryotic proteins and on regulatory peptides, whereas lysine acetylation occurs at different positions on a variety of proteins, including histones, transcription factors, nuclear import factors, and α-tubulin. | 
on Google Scholar
