A5115075508- Epigenetics and DNA Methylation
- Renal and related cancers
- Genetic Syndromes and Imprinting
- Ubiquitin and proteasome pathways
- Genomics and Chromatin Dynamics
- Protein Degradation and Inhibitors
- RNA Research and Splicing
- DNA and Nucleic Acid Chemistry
- Histone Deacetylase Inhibitors Research
EpiCypher (United States)
2024-2025
Abstract Polycomb group proteins maintain gene expression patterns established during early development, with Repressive Complex 2 (PRC2) methyltransferase a key regulator of cell differentiation, identity and plasticity. Consequently, extensive somatic mutations in PRC2, including gain- or loss- function (GOF LOF), are observed human cancers. The regulation chromatin structure by PRC2 is critically dependent on its EZH2 (Enhancer Zeste Homolog 2) subunit, which catalyzes the methylation...
Chromatin is more than a simple genome packaging system, and instead locally distinguished by histone post-translational modifications (PTMs) that can directly change nucleosome structure / or be ″read″ chromatin-associated proteins to mediate downstream events. An accurate understanding of PTM binding preference vital explain normal function pathogenesis, has revealed multiple therapeutic opportunities. Such studies most often use peptides, even though these cannot represent the full...
Histone post-translational modifications (PTMs) often serve as distinct recognition sites for the recruitment of chromatin-associated proteins (CAPs) epigenome regulation. While CAP-PTM interactions have been extensively studied using histone peptides, this cannot consider regulatory potential multi-site binding on intact nucleosomes. To overcome limitation, we applied Nucleosome Mass Spectrometry (Nuc-MS), a native Top-Down MS approach that enables controlled disassembly CAP:nucleosome...
ABSTRACT The cat eye syndrome chromosome region candidate 2 (CECR2) protein is an epigenetic regulator involved in chromatin remodeling and transcriptional control. CECR2 bromodomain (CECR2-BRD) plays a pivotal role directing the activity of through its capacity to recognize bind acetylated lysine residues on histone proteins. This study elucidates binding specificity structural mechanisms CECR2-BRD interactions with both non-histone ligands, employing techniques such as isothermal titration...