The SANT domain: a unique histone-tail-binding module?
By Laurie A. Boyer, R. Latek, C. Peterson. 2004
423 citations recorded by the source corpus.
Subfields: Molecular Biology
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In Molecular Biology
- Yang Shi
- Cedric R Clapier
- Katja Machemer
- Edward L. Braun
- F. Lan
- Erich Grotewold
- Dirk Schübeler
- B. Cairns
Citations in the corpus
- Impact of cytosine methylation on DNA binding specificities of human transcription factors (2017, background): “As described previously (26), a relatively low rate of success was observed for C2H2 zinc finger proteins, SMAD proteins, and SANT/Myb proteins, likely because of the very long recognitionmotifs of some C2H2 proteins, the fact that SMAD proteins act as obligate heterotrimers, and the misclassificati”
- Regulation of LSD1 histone demethylase activity by its associated factors. (2005, background): “The SANT domain is a conserved protein motif found in a number of chromatin and transcriptional regulators (Aasland et al., 1996; Boyer et al., 2004; de la Cruz et al., 2005), including CoREST, which contains two copies located at the middle and the C-terminal regions (Andres et al.”
- The world of protein acetylation. (2016, background): “A histone in a hypoacetylated state promotes binding of SANT-domain containing enzymes, mainly found in transcriptional corepressors [238].”
- The biology of chromatin remodeling complexes. (2009, background): “Instead, the SANT domains bind unmodified histone tails (11, 28, 29).”
- Evolutionary and comparative analysis of MYB and bHLH plant transcription factors. (2011, background): “Instead, SANT domain proteins often recognize histone tails (Boyer et al., 2002, 2004).”