The many faces of histone lysine methylation.
By M. Lachner, T. Jenuwein. Current Opinion in Cell Biology, 2002
871 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/8004f0b459c4e4bc3ae5c0ae20942a43a84fc3e7
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In Molecular Biology
- Ryuji Hamamoto
- Yusuke Nakamura
- Yi Zhang
- N. Dohmae
- S. Khorasanizadeh
- C. D. Allis
- D. Reinberg
- Yang Shi
Citations in the corpus
- Epigenetic regulation in psychiatric disorders (2007, background): “In contrast to acetylation, histone methylation can correlate with either gene activation or repression, depending on the residue undergoing methylatio”
- Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. (2006, background): “Histone methylation has been implicated in multiple biological processes including heterochromatin formation, X-inactivation, genomic imprinting, and silencing of homeotic genes (Kouzarides, 2002; Lachner and Jenuwein, 2002; Margueron et al., 2005; Martin and Zhang, 2005).”
- G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis (2006, background): “Once H3(K9) is deacetylated, G9a may then instigate di-and tri-methylation of Lys 9, either directly 17 or through the recruitment or activation of other histone methylases 18 .”
- Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. (2005, background): “For example, lysine methylation on histone H3 or H4 is involved in a variety of biological processes including transcriptional regulation, DNA elimination, DNA methylation, heterochromatin formation, and X-chromosome inactivation (Lachner and Jenuwein 2002; Lachner et al. 2003; Cao and Zhang 2004a).”
- A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. (2004, methodology): “…fusion proteins were incubated with in vitro translated myc3-tagged HP1 isoforms (HP1 , amino acids 5–191; HP1 , amino acids 5–185; HP1 , amino acids 5–173; Lachner et al. 2001) in IP buffer (50 mM Tris-HCl at pH 7.5, 500 mM NaCl, 1 mM EDTA, 0.5% NP-40, 10% glycerol, proteinase inhibitor cocktail).”
- Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. (2003, background): “Several SET-domain histone lysine methyltransferases have been identified (Zhang and Reinberg 2001; Lachner and Jenuwein 2002): They methylate various lysine residues located at the flexible N termini of histones H3 and H4.”
- The SET-domain protein superfamily: protein lysine methyltransferases (2005, background): “Adapted from [54-56]; additional references listed in the table are those not cited in these reviews.”
- Histone lysine methyltransferase SETD8 promotes carcinogenesis by deregulating PCNA expression. (2012, methodology): “293T cells were transfected with FLAG-PCNA (WT) or FLAG-PCNA (K248A) andHA-SETD8 (1-352) expression vectors.”
- Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. (2003, positive): “To The organization of DNA into heterochromatin contributes to nuclear organization, chromosome structure, directly target Rb, we exploited stable RNA interference (RNAi) technology to specifically knock down p16 and gene silencing (Dillon and Festenstein, 2002; Lachner and Jenuwein, 2002).”
- SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells (2004, background): “7 ), is considered to be critical for transcriptional regulatio”
- Regulation of histone methylation by demethylimination and demethylation (2007, background): “intermediate (1), which is hydrolysed to form formaldehyde by a non-enzymatic process (2).”
- Gene silencing in cancer by histone H3 lysine 27 trimethylation independent of promoter DNA methylation (2008, background): “Trimethylation at H3K27 (H3K27triM) is a distinct histone modification involved in regulation of homeotic (Hox) gene expression and in early steps of X-chromosome inactivation in wome”
- Binary switches and modification cassettes in histone biology and beyond (2003, background): “Histone modifications can be highly reversible, such as histone (lysine) acetylation and histone (serine and threonine) phosphorylation, or more stable, such as histone (lysine and arginine) methylatio”
- Regulation of LSD1 histone demethylase activity by its associated factors. (2005, background): “Thus, methylation represents a critical posttranslational modification of histones that impacts chromatin structure and gene transcription (Bannister et al., 2002; Lachner and Jenuwein, 2002; Zhang and Reinberg, 2001).”
- Histone and chromatin cross-talk. (2003, neutral): “[1–5]).”