Primary Literature
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- Oberbeckmann E, et al. (2024) In vitro reconstitution of chromatin domains shows a role for nucleosome positioning in 3D genome organization. Nat Genet. PMID: 38291333
- Attar N, et al. (2020) The histone H3-H4 tetramer is a copper reductase enzyme. Science 369(6499):59-64 PMID: 32631887
- Knutson BA, et al. (2020) Molecular Topology of RNA Polymerase I Upstream Activation Factor. Mol Cell Biol 40(13) PMID: 32253346
- Birgit Meldal and Sandra Orchard (2018) Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity.
- Brahma S, et al. (2017) INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers. Nat Commun 8:15616 PMID: 28604691
- Gallego LD, et al. (2016) Structural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1. Proc Natl Acad Sci U S A 113(38):10553-8 PMID: 27601672
- Smolle M, et al. (2012) Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange. Nat Struct Mol Biol 19(9):884-92 PMID: 22922743
- Chatterjee N, et al. (2011) Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms. Nucleic Acids Res 39(19):8378-91 PMID: 21749977
- Gardner JM, et al. (2011) Targeting of the SUN protein Mps3 to the inner nuclear membrane by the histone variant H2A.Z. J Cell Biol 193(3):489-507 PMID: 21518795
- 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 PMID: 21791612
- Luk E, et al. (2010) Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome. Cell 143(5):725-36 PMID: 21111233
- Hansen DF, et al. (2009) Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy. J Mol Biol 387(1):1-9 PMID: 19385041
- Johnson A, et al. (2009) Reconstitution of heterochromatin-dependent transcriptional gene silencing. Mol Cell 35(6):769-81 PMID: 19782027
- Altaf M, et al. (2007) Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin. Mol Cell 28(6):1002-14 PMID: 18158898
- Kim HJ, et al. (2007) Histone chaperones regulate histone exchange during transcription. EMBO J 26(21):4467-74 PMID: 17914459
- Luk E, et al. (2007) Chz1, a nuclear chaperone for histone H2AZ. Mol Cell 25(3):357-68 PMID: 17289584
- Park YJ, et al. (2005) Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding. J Biol Chem 280(3):1817-25 PMID: 15516689
- 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 PMID: 16299513
- Zhang H, et al. (2005) Genome-wide dynamics of Htz1, a histone H2A variant that poises repressed/basal promoters for activation through histone loss. Cell 123(2):219-31 PMID: 16239141
- Mizuguchi G, et al. (2004) ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303(5656):343-8 PMID: 14645854
- Mosammaparast N, et al. (2002) Pathways mediating the nuclear import of histones H3 and H4 in yeast. J Biol Chem 277(1):862-8 PMID: 11694505
- Sharp JA, et al. (2001) Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr Biol 11(7):463-73 PMID: 11412995
- 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 PMID: 11000274
- Kurumizaka H and Wolffe AP (1997) Sin mutations of histone H3: influence on nucleosome core structure and function. Mol Cell Biol 17(12):6953-69 PMID: 9372928