Cargando…
Phosphorylation of histone H3(T118) alters nucleosome dynamics and remodeling
Nucleosomes, the fundamental units of chromatin structure, are regulators and barriers to transcription, replication and repair. Post-translational modifications (PTMs) of the histone proteins within nucleosomes regulate these DNA processes. Histone H3(T118) is a site of phosphorylation [H3(T118ph)]...
Autores principales: | North, Justin A., Javaid, Sarah, Ferdinand, Michelle B., Chatterjee, Nilanjana, Picking, Jonathan W., Shoffner, Matthew, Nakkula, Robin J., Bartholomew, Blaine, Ottesen, Jennifer J., Fishel, Richard, Poirier, Michael G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159469/ https://www.ncbi.nlm.nih.gov/pubmed/21576235 http://dx.doi.org/10.1093/nar/gkr304 |
Ejemplares similares
-
Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure
por: North, Justin A., et al.
Publicado: (2014) -
Regulation of the nucleosome unwrapping rate controls DNA accessibility
por: North, Justin A., et al.
Publicado: (2012) -
Extranucleosomal DNA enhances the activity of the LSD1/CoREST histone demethylase complex
por: Kim, Sang-Ah, et al.
Publicado: (2015) -
Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms
por: Chatterjee, Nilanjana, et al.
Publicado: (2011) -
Dynamic unwrapping of nucleosomes by HsRAD51 that includes sliding and rotational motion of histone octamers
por: Senavirathne, Gayan, et al.
Publicado: (2017)