Premium
Targeting Reversible Lysine Modifications
Author(s) -
Cole Philip
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.107.3
Subject(s) - lysine , semisynthesis , demethylation , acylation , succinylation , methylation , function (biology) , chemistry , bromodomain , posttranslational modification , sumo protein , biochemistry , computational biology , microbiology and biotechnology , biology , epigenetics , gene expression , amino acid , dna methylation , gene , ubiquitin , enzyme , catalysis
Reversible protein lysine modifications including acylation and methylation have been recognized as critical to the regulation of cell growth, differentiation, and gene expression. However, many aspects of their function are poorly understood. We will discuss several chemical approaches that our lab is taking to the functional analysis of lysine acylation and demethylation including inhibitor design strategies and protein semisynthesis. In combination with enzymologic, biophysical, and cellular strategies, these chemical approaches have offered new insights into the roles of lysine post‐ translational modifications in normal and disease states.