| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871051 | FEBS Letters | 2013 | 11 Pages |
Abstract
Post-translational modifications (PTMs) occur on nearly all proteins. Many domains within proteins are modified on multiple amino acid sidechains by diverse enzymes to create a myriad of possible protein species. How these combinations of PTMs lead to distinct biological outcomes is only beginning to be understood. This manuscript highlights several examples of combinatorial PTMs in proteins, and describes recent technological developments, which are driving our ability to understand how PTM patterns may “code” for biological outcomes.
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Authors
Adam P. Lothrop, Matthew P. Torres, Stephen M. Fuchs,