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January 2017

Volume 16Issue 1p1-145
Open Access
On the cover: Isocitrate dehydrogenase 1 (IDH1) mutation is observed in nearly all secondary glioblastomas and suppresses the biochemical ability of IDH1 to convert isocitrate into α-Ketoglutarate (α-KG) by further converting α-KG into 2-hydroxyglutarate (2-HG). As a result, the 2-HG oncometabolite accumulates at high levels in IDH1 mutant tumors and inhibits α-KG-dependent histone and DNA demethylases, affecting epigenetic regulation and associated gene expression. Using targeted mass spectrometry the article by Doll et al. (This Issue) reports the quantification of significant histone methylation (Me), acetylation (Ac), and butyrylation (Bu) site occupancy changes related to IDH1 mutation in a cellular model of secondary glioblastoma. For more details, see the article by Sophia Doll et al., pages 39–56....
On the cover: Isocitrate dehydrogenase 1 (IDH1) mutation is observed in nearly all secondary glioblastomas and suppresses the biochemical ability of IDH1 to convert isocitrate into α-Ketoglutarate (α-KG) by further converting α-KG into 2-hydroxyglutarate (2-HG). As a result, the 2-HG oncometabolite accumulates at high levels in IDH1 mutant tumors and inhibits α-KG-dependent histone and DNA demethylases, affecting epigenetic regulation and associated gene expression. Using targeted mass spectrometry the article by Doll et al. (This Issue) reports the quantification of significant histone methylation (Me), acetylation (Ac), and butyrylation (Bu) site occupancy changes related to IDH1 mutation in a cellular model of secondary glioblastoma. For more details, see the article by Sophia Doll et al., pages 39–56.

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