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Post-translational Modifications of proteins

Post-translational modifications: Key regulators of development, cell division, and disease

Fifteen of the twenty canonical amino acids can be chemically modified in vivo, either by enzymes or small molecules, after they have been incorporated into a protein sequence. To date, more then 300 different modifications have been described – relating to nearly every aspect of biology. PTMs serve to alter many aspects of a protein's function including: where it resides in the cell, what it interacts with, how long it remains functional, and the extent of its activity. Nearly every day systems-wide proteomics studies are uncovering new PTMs associated with specific diseases or cell states although the function of most modifications remains a mystery.

In the Fuchs lab we are working to: 1) develop methodology to probe the function of PTMs, and 2) understand the role of PTMs in regulating processes. Currently, we have a particular interest in PTMs of histone proteins and their roles in regulating transcription and other DNA-templated processes.