HTZ1/YOL012C Literature Guide Help

Other names published for HTZ1: HTA3, H2A.F/Z, H2AZ, YOL012C

HTZ1 - Non-Fungal Related Genes/Proteins (24)

ReferenceOther Genes Addressed
Fernandez MA, et al.  (2012) Identification of a core set of signature cell cycle genes whose relative order of time to peak expression is conserved across species. Nucleic Acids Res 40(7):2823-32
Wratting D, et al.  (2012) A conserved function for the H2A.Z C terminus. J Biol Chem 287(23):19148-57
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
Jensen K, et al.  (2011) Histone H2A.Z acid patch residues required for deposition and function. Mol Genet Genomics 285(4):287-96
Kawano A, et al.  (2011) Global analysis for functional residues of histone variant Htz1 using the comprehensive point mutant library. Genes Cells 16(5):590-607
Wang AY, et al.  (2011) Key functional regions in the histone variant H2A.Z C-terminal docking domain. Mol Cell Biol 31(18):3871-84
On T, et al.  (2010) The evolutionary landscape of the chromatin modification machinery reveals lineage specific gains, expansions, and losses. Proteins 78(9):2075-89
Tirosh I, et al.  (2010) Chromatin regulators as capacitors of interspecies variations in gene expression. Mol Syst Biol 6():435
Clapier CR and Cairns BR  (2009) The biology of chromatin remodeling complexes. Annu Rev Biochem 78():273-304
Cui F and Zhurkin VB  (2009) Distinctive sequence patterns in metazoan and yeast nucleosomes: implications for linker histone binding to AT-rich and methylated DNA. Nucleic Acids Res 37(9):2818-29
Tolstorukov MY, et al.  (2009) Comparative analysis of H2A.Z nucleosome organization in the human and yeast genomes. Genome Res 19(6):967-77
Rong YS  (2008) Loss of the Histone Variant H2A.Z Restores Capping to Checkpoint-Defective Telomeres in Drosophila. Genetics 180(4):1869-75
Zlatanova J and Thakar A  (2008) H2A.Z: view from the top. Structure 16(2):166-79
Gevry N, et al.  (2007) p21 transcription is regulated by differential localization of histone H2A.Z. Genes Dev 21(15):1869-81
Sarcinella E, et al.  (2007) Monoubiquitylation of H2A.Z Distinguishes Its Association with Euchromatin or Facultative Heterochromatin. Mol Cell Biol 27(18):6457-68
Carroll CW and Straight AF  (2006) Centromere formation: from epigenetics to self-assembly. Trends Cell Biol 16(2):70-8
Guillemette B and Gaudreau L  (2006) Reuniting the contrasting functions of H2A.Z. Biochem Cell Biol 84(4):528-35
Wu WH, et al.  (2005) Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat Struct Mol Biol 12(12):1064-71
Redon C, et al.  (2002) Histone H2A variants H2AX and H2AZ. Curr Opin Genet Dev 12(2):162-9
Green GR  (2001) Phosphorylation of histone variant regions in chromatin: unlocking the linker? Biochem Cell Biol 79(3):275-87
Jackson JD and Gorovsky MA  (2000) Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res 28(19):3811-6
Santisteban MS, et al.  (2000) Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes. Cell 103(3):411-22
Jackson JD, et al.  (1996) A likely histone H2A.F/Z variant in Saccharomyces cerevisiae. Trends Biochem Sci 21(12):466-7
Liu X, et al.  (1996) Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae. Mol Cell Biol 16(6):2878-87