Structural basis for DAXX interaction with ATRX
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Drug Discovery,Biochemistry,Biotechnology
Link
http://link.springer.com/article/10.1007/s13238-017-0462-y/fulltext.html
Reference14 articles.
1. Clynes D, Higgs DR, Gibbons RJ (2013) The chromatin remodeller ATRX: a repeat offender in human disease. Trends Biochem Sci 38:461–466
2. Dyer MA, Qadeer, Z.A., Valle-Garcia, D., and Bernstein E (2017) ATRX and DAXX: Mechanisms and Mutations. Cold Spring Harb Perspect Med 7.
3. Elsasser SJ, Huang H, Lewis PW, Chin JW, Allis CD, Patel DJ (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature 491:560–565
4. Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP (2010) Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. Structure 18:1642–1653
5. Goldberg AD, Banaszynski LA, Noh KM, Lewis PW, Elsaesser SJ, Stadler S, Dewell S, Law M, Guo X, Li X et al (2010) Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 140:678–691
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