| Title : Peptidase substrates via global peptide profiling - Tagore_2009_Nat.Chem.Biol_5_23 |
| Author(s) : Tagore DM , Nolte WM , Neveu JM , Rangel R , Guzman-Rojas L , Pasqualini R , Arap W , Lane WS , Saghatelian A |
| Ref : Nat Chemical Biology , 5 :23 , 2009 |
|
Abstract :
Peptide metabolism is a complex process that involves many proteins working in concert. Mass spectrometry-based global peptide profiling of mice lacking dipeptidyl peptidase 4 (DPP4) identified endogenous DPP4 substrates and revealed an unrecognized pathway during proline peptide catabolism that interlinks aminopeptidase and DPP4 activities. Together, these studies elucidate specific aspects of DPP4-regulated metabolism and, more generally, highlight the utility of global peptide profiling for studying peptide metabolism in vivo. |
| PubMedSearch : Tagore_2009_Nat.Chem.Biol_5_23 |
| PubMedID: 19011639 |
Tagore DM, Nolte WM, Neveu JM, Rangel R, Guzman-Rojas L, Pasqualini R, Arap W, Lane WS, Saghatelian A (2009)
Peptidase substrates via global peptide profiling
Nat Chemical Biology
5 :23
Tagore DM, Nolte WM, Neveu JM, Rangel R, Guzman-Rojas L, Pasqualini R, Arap W, Lane WS, Saghatelian A (2009)
Nat Chemical Biology
5 :23