Michiel Vermeulen

TL;DR: High-resolution mass spectrometry–based proteomics was applied to investigate the proteome and phosphoproteome of the human cell cycle on a global scale and quantified 6027 proteins and 20,443 unique phosphorylation sites and their dynamics, finding that nuclear proteins and proteins involved in regulating metabolic processes have high phosphorylated site occupancy in mitosis, suggesting that these proteins may be inactivated by phosphorylate in mitotic cells.

TL;DR: Oxidized derivatives of mC recruit distinct transcription regulators as well as a large number of DNA repair proteins in mouse ES cells, implicating the DNA damage response as a major player in active DNA demethylation.

TL;DR: Experiments reveal crosstalk between histone modifications and the transcription factor TFIID, which has important implications for regulation of RNA polymerase II-mediated transcription in higher eukaryotes.

TL;DR: The authors' data reveal a highly adapted interplay between chromatin marks and their associated protein complexes, and reading specific trimethyl-lysine sites by specialized complexes appears to be a widespread mechanism to mediate gene expression.

TL;DR: This work uses nucleosomes methylated on DNA and on histone H3 in an affinity assay and a proteomic analysis to identify "crosstalk" between these two distinct classes of modification, establishing SILAC nucleosome affinity purifications (SNAP) as a tool for studying the dynamics between different chromatin modifications.