Male-specific lethal 3 homolog

[1]. Daesung Kim, et al. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. [Content Brief]

[2]. Jan Kadlec, et al. Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol. 2011 Feb;18(2):142-9. [Content Brief]

[3]. Sascha Mendjan, et al. Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol Cell. 2006 Mar 17;21(6):811-23. [Content Brief]

[4]. Jing Huang, et al. Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex. Cell Res. 2012 Jun;22(6):1078-81. [Content Brief]

[5]. M Felicia Basilicata, et al. De novo mutations in MSL3 cause an X-linked syndrome marked by impaired histone H4 lysine 16 acetylation. Nat Genet. 2018 Oct;50(10):1442-1451. [Content Brief]

[6]. Edwin R Smith, et al. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol. 2005 Nov;25(21):9175-88. [Content Brief]

[7]. Yong Cai, et al. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. [Content Brief]

[8]. Stanley A Moore, et al. Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4. J Biol Chem. 2010 Dec 24;285(52):40879-90. [Content Brief]