Histone H2A-Bbd type 1

[1]. Viola Sansoni, et al. The histone variant H2A.Bbd is enriched at sites of DNA synthesis. Nucleic Acids Res. 2014 Jun;42(10):6405-20. [Content Brief]

[2]. Yunhe Bao, et al. Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA. EMBO J. 2004 Aug 18;23(16):3314-24. [Content Brief]

[3]. Cécile-Marie Doyen, et al. Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. EMBO J. 2006 Sep 20;25(18):4234-44. [Content Brief]

[4]. Rodrigo González-Romero, et al. Quickly evolving histones, nucleosome stability and chromatin folding: all about histone H2A.Bbd. Gene. 2008 Apr 30;413(1-2):1-7. [Content Brief]

[5]. Michael Y Tolstorukov, et al. Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells. Mol Cell. 2012 Aug 24;47(4):596-607. [Content Brief]

[6]. Yasuhiro Arimura, et al. Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin. Sci Rep. 2013 Dec 16;3:3510. [Content Brief]

[7]. Mitsuru Okuwaki, et al. Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I. Mol Cell Biol. 2005 Dec;25(23):10639-51. [Content Brief]

[8]. Hervé Menoni, et al. ATP-dependent chromatin remodeling is required for base excision repair in conventional but not in variant H2A.Bbd nucleosomes. Mol Cell Biol. 2007 Sep;27(17):5949-56. [Content Brief]

[9]. José María Eirín-López, et al. H2A.Bbd: a quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way. FASEB J. 2008 Jan;22(1):316-26. [Content Brief]