Histone deacetylase 10 structure and molecular function as a polyamine deacetylase
Polyamines bind to nucleic acids and their function is regulated by reversible acetylation. Here, the authors show that histone deacetylase 10 is a polyamine deacetylase and present its crystal structure with a bound polyamine transition state analogue inhibitor.
Guardado en:
Autores principales: | Yang Hai, Stephen A. Shinsky, Nicholas J. Porter, David W. Christianson |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/a275abbed63b43529d75e158a00c61cf |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural Characterization of the SMRT Corepressor Interacting with Histone Deacetylase 7
por: Danielle C. Desravines, et al.
Publicado: (2017) -
Antitheilerial Activity of the Anticancer Histone Deacetylase Inhibitors
por: Madhumanti Barman, et al.
Publicado: (2021) -
Hypothalamic leptin action is mediated by histone deacetylase 5
por: Dhiraj G. Kabra, et al.
Publicado: (2016) -
Histone deacetylase complexes promote trinucleotide repeat expansions.
por: Kim Debacker, et al.
Publicado: (2012) -
Histone deacetylase inhibitors (HDACIs): multitargeted anticancer agents
por: Ververis K, et al.
Publicado: (2013)