Cargando…
Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions
BACKGROUND: Histone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized “reader” domains. Despite efforts to elucidate reader domain–PTM interactions, the influence of neighboring PT...
Autores principales: | Shanle, Erin K., Shinsky, Stephen A., Bridgers, Joseph B., Bae, Narkhyun, Sagum, Cari, Krajewski, Krzysztof, Rothbart, Scott B., Bedford, Mark T., Strahl, Brian D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5348760/ https://www.ncbi.nlm.nih.gov/pubmed/28293301 http://dx.doi.org/10.1186/s13072-017-0117-5 |
Ejemplares similares
-
The histone and non-histone methyllysine reader activities of the UHRF1 tandem Tudor domain are dispensable for the propagation of aberrant DNA methylation patterning in cancer cells
por: Vaughan, Robert M., et al.
Publicado: (2020) -
The Taf14 YEATS domain is a reader of histone crotonylation
por: Andrews, Forest H., et al.
Publicado: (2016) -
Tudor-domain protein PHF20L1 reads lysine methylated retinoblastoma tumour suppressor protein
por: Carr, Simon M, et al.
Publicado: (2017) -
Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions
por: Jain, Kanishk, et al.
Publicado: (2020) -
Binding specificity and function of the SWI/SNF subunit SMARCA4 bromodomain interaction with acetylated histone H3K14
por: Enríquez, Paul, et al.
Publicado: (2021)