HHF1/YBR009C Literature Guide Help

Other names published for HHF1: YBR009C

HHF1 - Protein/Nucleic Acid Structure (17)

ReferenceOther Genes Addressed
Chavez MS, et al.  (2012) The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability. Epigenetics Chromatin 5(1):5
Genereaux J, et al.  (2012) Genetic evidence links the ASTRA protein chaperone component Tti2 to the SAGA transcription factor Tra1. Genetics 191(3):765-80
Yang H, et al.  (2012) Saccharomyces Cerevisiae MHF Complex Structurally Resembles the Histones (H3-H4)(2) Heterotetramer and Functions as a Heterotetramer. Structure 20(2):364-70
Armache KJ, et al.  (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution. Science 334(6058):977-82
Arnold KM, et al.  (2011) Processing Mechanism and Substrate Selectivity of the Core NuA4 Histone Acetyltransferase Complex. Biochemistry 50(5):727-37
Su D, et al.  (2011) Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. J Biol Chem 286(18):15625-9
Xiao H, et al.  (2011) Nonhistone Scm3 Binds to AT-Rich DNA to Organize Atypical Centromeric Nucleosome of Budding Yeast. Mol Cell 43(3):369-80
Xu F, et al.  (2010) Long-range effects of histone point mutations on DNA remodeling revealed from computational analyses of SIN-mutant nucleosome structures. Nucleic Acids Res 38(20):6872-82
Milani P, et al.  (2009) Nucleosome positioning by genomic excluding-energy barriers. Proc Natl Acad Sci U S A 106(52):22257-62
Andrews AJ, et al.  (2008) A thermodynamic model for nap1-histone interactions. J Biol Chem 283(47):32412-8
Blackwell JS Jr, et al.  (2007) Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import. J Biol Chem 282(28):20142-50
Ramaswamy A and Ioshikhes I  (2007) Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone. BMC Struct Biol 7():76
Fry CJ, et al.  (2006) The LRS and SIN domains: two structurally equivalent but functionally distinct nucleosomal surfaces required for transcriptional silencing. Mol Cell Biol 26(23):9045-59
Silverman BD  (2005) The hydrophobicity of the H3 histone fold differs from the hydrophobicity of the other three folds. J Mol Evol 60(3):354-64
Ye J, et al.  (2005) Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly. Mol Cell 18(1):123-30
Zhang L, et al.  (2003) Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112(2):77-86
Bang E, et al.  (2001) Solution structures of the N-terminal domain of histone H4. J Pept Res 58(5):389-98