Methods for the proteomic identification of protease substrates.
Curr Opin Chem Biol
; 13(5-6): 503-9, 2009 Dec.
Article
en En
| MEDLINE
| ID: mdl-19729334
ABSTRACT
Proteolysis is a key regulatory post-translational modification in diverse cellular processes including programed cell death, immune function, and development. Tracking proteolytic events has become a focus of researchers assessing the downstream consequences of protease activation. In this review we summarize unbiased methods for identifying protease substrates and tracking the extent of cleavage, a field termed 'degradomics'. These include one-dimensional and two-dimensional gel-based methods for identifying protease substrates, N-terminal peptide identification methods for simultaneously identifying substrates and cleavage sites, and approaches for the quantitation of cleavage events during endogenous proteolysis. Individual methods have identified more than 300 caspase-cleaved targets during apoptosis suggesting broad future applications for these technologies.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Péptido Hidrolasas
/
Proteómica
Tipo de estudio:
Diagnostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Curr Opin Chem Biol
Asunto de la revista:
BIOQUIMICA
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos