| Literature DB >> 26656971 |
Tao Peng1, Emmanuelle Thinon2, Howard C Hang3.
Abstract
Protein fatty-acylation in eukaryotes has been associated with many fundamental biological processes. However, the diversity, abundance and regulatory mechanisms of protein fatty-acylation in vivo remain to be explored. Herein, we review the proteomic analysis of fatty-acylated proteins, with a focus on N-myristoylation and S-palmitoylation. We then highlight major challenges and emerging methods for direct site identification, quantitation, and lipid structure characterization to understand the functions and regulatory mechanisms of fatty-acylated proteins in physiology and disease.Entities:
Mesh:
Substances:
Year: 2015 PMID: 26656971 PMCID: PMC4731282 DOI: 10.1016/j.cbpa.2015.11.008
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN: 1367-5931 Impact factor: 8.822