Histone H2A Ubiquitination Inhibits the Enzymatic Activity of H3 Lysine 36 Methyltransferases

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Dense Chromatin Activates Polycomb Repressive Complex 2 to Regulate H3 Lysine 27 Methylation

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The Structure of NSD1 Reveals an Autoregulatory Mechanism Underlying Histone H3K36 Methylation

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H3K36 Methylation Antagonizes PRC2-mediated H3K27 Methylation

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NSD2 Links Dimethylation of Histone H3 at Lysine 36 to Oncogenic Programming

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Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function

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A Vertebrate Polycomb Response Element Governs Segmentation of the Posterior Hindbrain

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A systematic evaluation of the compatibility of histones containing methyl-lysine analogues with biochemical reactions

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Heterogeneous Nuclear Ribonucleoprotein L Is a Subunit of Human KMT3a/Set2 Complex Required for H3 Lys-36 Trimethylation Activityin Vivo

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The Target of the NSD Family of Histone Lysine Methyltransferases Depends on the Nature of the Substrate

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Genome-Wide uH2A Localization Analysis Highlights Bmi1-Dependent Deposition of the Mark at Repressed Genes

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Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation

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dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing

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Histone H2A Monoubiquitination Represses Transcription by Inhibiting RNA Polymerase II Transcriptional Elongation

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Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation

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