Cargando…
Serine is a new target residue for endogenous ADP-ribosylation on histones
ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have...
Autores principales: | Leidecker, Orsolya, Bonfiglio, Juan José, Colby, Thomas, Zhang, Qi, Atanassov, Ilian, Zaja, Roko, Palazzo, Luca, Stockum, Anna, Ahel, Ivan, Matic, Ivan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5113755/ https://www.ncbi.nlm.nih.gov/pubmed/27723750 http://dx.doi.org/10.1038/nchembio.2180 |
Ejemplares similares
-
Serine ADP-Ribosylation Depends on HPF1
por: Bonfiglio, Juan José, et al.
Publicado: (2017) -
Serine is the major residue for ADP-ribosylation upon DNA damage
por: Palazzo, Luca, et al.
Publicado: (2018) -
Interplay of Histone Marks with Serine ADP-Ribosylation
por: Bartlett, Edward, et al.
Publicado: (2018) -
Serine ADP-ribosylation reversal by the hydrolase ARH3
por: Fontana, Pietro, et al.
Publicado: (2017) -
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
por: Bonfiglio, Juan J., et al.
Publicado: (2017)