Accurate annotation of peptide modifications through unrestrictive database search.
J Proteome Res
; 7(1): 170-81, 2008 Jan.
Article
en En
| MEDLINE
| ID: mdl-18034453
ABSTRACT
Proteins are extensively modified after translation due to cellular regulation, signal transduction, or chemical damage. Peptide tandem mass spectrometry can discover post-translational modifications, as well as sequence polymorphisms. Recent efforts have studied modifications at the proteomic scale. In this context, it becomes crucial to assess the accuracy of modification discovery. We discuss methods to quantify the false discovery rate from a search and demonstrate how several features can be used to distinguish valid modifications from search artifacts. We present a tool, PTMFinder, which implements these methods. We summarize the corpus of post-translational modifications identified on large data sets. Thousands of known and novel modification sites are identified, including site-specific modifications conserved over vast evolutionary distances.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Programas Informáticos
/
Proteínas
/
Procesamiento Proteico-Postraduccional
/
Almacenamiento y Recuperación de la Información
/
Bases de Datos de Proteínas
Idioma:
En
Revista:
J Proteome Res
Asunto de la revista:
BIOQUIMICA
Año:
2008
Tipo del documento:
Article
País de afiliación:
Estados Unidos