Post-Translational Modification of Proteins in Toxicological Research: Focus on Lysine Acylation
Toxicological Research
;
: 81-86, 2013.
Article
in English
| WPRIM
| ID: wpr-59645
ABSTRACT
Toxicoproteomics integrates the proteomic knowledge into toxicology by enabling protein quantification in biofluids and tissues, thus taking toxicological research to the next level. Post-translational modification (PTM) alters the three-dimensional (3D) structure of proteins by covalently binding small molecules to them and therefore represents a major protein function diversification mechanism. Because of the crucial roles PTM plays in biological systems, the identification of novel PTMs and study of the role of PTMs are gaining much attention in proteomics research. Of the 300 known PTMs, protein acylation, including lysine formylation, acetylation, propionylation, butyrylation, malonylation, succinylation, and crotonylation, regulates the crucial functions of many eukaryotic proteins involved in cellular metabolism, cell cycle, aging, growth, angiogenesis, and cancer. Here, I reviewed recent studies regarding novel types of lysine acylation, their biological functions, and their applicationsin toxicoproteomics research.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Acetylation
/
Toxicology
/
Aging
/
Acylation
/
Proteins
/
Cell Cycle
/
Protein Processing, Post-Translational
/
Proteomics
/
Lysine
Language:
English
Journal:
Toxicological Research
Year:
2013
Type:
Article
Similar
MEDLINE
...
LILACS
LIS