Measurement of acetylation turnover at distinct lysines in human histones identifies long-lived acetylation sites

Histone acetylation has long been determined as a highly dynamic modification associated with open chromatin and transcriptional activation. Here we develop a metabolic labeling scheme using stable isotopes to study the kinetics of acetylation turnover at 19 distinct lysines on histones H3, H4, and...

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Detalles Bibliográficos
Autores principales: Zheng, Yupeng, Thomas, Paul M., Kelleher, Neil L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3929392/
https://www.ncbi.nlm.nih.gov/pubmed/23892279
http://dx.doi.org/10.1038/ncomms3203

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3929392/
https://www.ncbi.nlm.nih.gov/pubmed/23892279
http://dx.doi.org/10.1038/ncomms3203

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