Matthew R. Marunde

This study shows that PBRM1 in PBAF is essential for EMT and metastasis in breast cancer by enabling promoter targeting and DNA accessibility for TGFβ1-inducible genes.

The paper shows that different binding modes to the nucleosome acidic patch lead to distinct cellular outcomes, with overexpression of Dot5 and camelid antibodies causing growth, DNA repair, and heterochromatin defects.

This study shows that BRD4's tandem bromodomains cooperatively bind poly-acetylated nucleosomes, enhancing chromatin engagement and influencing breast cancer phenotypes.

This study investigates how the conserved SBD of EZH2 regulates PRC2 activity, showing its necessity for histone methylation and cancer cell proliferation.

This paper introduces Nuc-MS, a method to directly analyze chromatin reader-nucleosome interactions by disassembling complexes and identifying histone proteoforms involved in binding.

The paper provides a detailed CUT&RUN protocol for high-resolution epigenomic profiling, including best practices and controls for efficient target profiling.

The paper identifies H3 serine 28 phosphorylation as a mechanism driving chromatin derepression and immune cell fate transitions by disrupting repressive chromatin domains.

The paper investigates how nucleosome context influences chromatin reader binding preferences using biochemical and genomic approaches, revealing that multivalent engagement often has regulatory effects beyond simple additivity.

This study shows PHRF1's PHD finger binds histone H3 N-terminal region, regulates transcription and RNA splicing, and is essential for DNA damage response.

The paper identifies KDM4 demethylase inhibition as a therapeutic strategy for lymphoma and other cancers by rewiring heterochromatin and inducing DNA damage.

This paper investigates the binding specificity of CECR2-BRD to acetylated histone and non-histone ligands, revealing distinct binding modes and functional roles in chromatin regulation and inflammation.

The paper shows that histone reader domains interact with PTMs in a nucleosome-dependent manner, necessitating a refinement of the histone code concept to the nucleosome level.

The paper reports the cryo-EM structure of the yeast NuA4 complex hub and describes its interaction with HAT and TINTIN modules for nucleosome recognition.

The paper investigates the substrate preferences and functional consequences of Type I and II PRMTs by inhibiting them in A549 cells and analyzing proteomic and transcriptomic changes.