How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
By Sean D. Taverna, Haitao Li, Alexander J. Ruthenburg, C. D. Allis, Dinshaw J. Patel. Nature Structural &Molecular Biology, 2007
1,497 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/f27ade16fec02cf42ca94e72083848ac889ef7dc
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In Molecular Biology
- Matthias Mann
- Tony Kouzarides
- Jesper V. Olsen
- D. Reinberg
- M. Dawson
- M. Vermeulen
- P. Voigt
- Brian D. Strahl
Citations in the corpus
- Nucleosome-Interacting Proteins Regulated by DNA and Histone Methylation (2010, background): “Such effector molecules use a range of different recognition domains such as methyl-CpG-binding domains (MBD), zinc fingers (ZnF), chromo-domains, or plant homeodomains (PHD) in order to establish and orchestrate biological events (Sasai and Defossez, 2009; Taverna et al., 2007).”
- Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. (2010, background): “A number of these ‘‘chromatin readers’’ for various histone methyl lysine sites have already been identified and characterized (Kouzarides, 2007; Shilatifard, 2006; Taverna et al., 2007), but this list is unlikely to be exhaustive.”
- A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO. (2017, background): “This value is in the range of binding affinities exhibited by the majority of epigenetic readers (Andrews et al., 2016; Musselman et al., 2012; Taverna et al., 2007).”