Histone methylation in transcriptional control.

By Tony Kouzarides. Current Opinion in Genetics and Development, 2002

966 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/76155af4bd1254ec038e9fb3da0e137ff095080b

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Citations in the corpus

Genome-wide map of nucleosome acetylation and methylation in yeast. (2005, neutral): “Nucleosomes are thus critical to the organization and maintenance of genetic material, and their position and modification state can profoundly influence genetic activities such as regulation of gene expression (Kouzarides, 2002; Narlikar et al., 2002).”
Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. (2005, neutral): “While histone acetylation has been actively investigated for a number of years, the effects of histone methylation have only been appreciated more recently (Kouzarides, 2002; Lachner and Jenuwein, 2002).”
Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells (2008, background): “SMYD3 contains an amino acid sequence termed SET-N region between codons 5 and 27, which is conserved in SET domain proteins (Kouzarides, 2002; Lachner and Jenuwein, 2002; Marmorstein, 2003).”
Human SWI/SNF-Associated PRMT5 Methylates Histone H3 Arginine 8 and Negatively Regulates Expression of ST7 and NM23 Tumor Suppressor Genes (2004, background): “PRMTs can be divided into type I PRMTs, which catalyze monomethylation and asymmetric dimethylation of arginine residues, and type II PRMTs, which catalyze the formation of monomethylated and symmetrically dimethylated arginines (57).”
The PR/SET Domain Zinc Finger Protein Prdm4 Regulates Gene Expression in Embryonic Stem Cells but Plays a Nonessential Role in the Developing Mouse Embryo (2013, background): “The evolutionarily conserved PR/SET domain is 20 to 30% identical to the SET domain found in numerous histone lysine methyltransferases (HMTs) that modify nucleosome structure (18, 19).”
Histone and chromatin cross-talk. (2003, neutral): “[1–5]).”
The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. (2004, background): “On the other hand, most histone methylases seem to modify only a defined arginine or lysine residue (Zhang and Reinberg 2001; Kouzarides 2002).”
Posttranslational Protein Modification in Archaea (2005, background): “Given the modulation of eucaryal histone function that results from methylation (59, 238), it is likely that methylation of archaeal Sul7 proteins also affects their behavior.”
Mechanisms and Functions of Long Non-Coding RNAs at Multiple Regulatory Levels (2019, background): “Histone methylation has complex functions; for example, H3K4, H3K36, and H3K79 promote gene transcription, whereas H3K9, H3K27, and H4K20 inhibit gene transcription [20,25].”
Enhanced expression of EHMT2 is involved in the proliferation of cancer cells through negative regulation of SIAH1. (2011, background): “Histone lysine methylation is considered to regulate the transcription positively or negatively depending on the methylation sites and the methylation status [1].”
Coordinated histone modifications mediated by a CtBP co-repressor complex (2003, methodology): “We next analysed the CtBP complex for HMT activity, which has recently been shown to be involved in transcriptional repressio”