Los miembros de la RSEQ: Carla Casadevall, Nicoletta Liguori y Carlos Moreno Yruela consiguen una ERC Starting Grant en la convocatoria 2025.

Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

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Histone deacetylase (HDAC) enzymes are epigenetic regulators that affect diverse protein function by removing acyl groups from lysine side chains throughout the proteome. The most recently discovered ...

Roughly 6,000 readers answered our poll, with many declaring that Bluesky was nicer, kinder and less antagonistic to science than X.

Specialized magnetic beads that bind target proteins to a cryogenic electron microscopy grid make it possible to study the structure of protein complexes from dilute samples.

Histone deacetylase (HDAC) enzymes are epigenetic regulators that affect diverse protein function by removing acyl groups from lysine side chains throughout the proteome. The most recently discovered ...

A free interactive resource for viewing predicted AlphaFold multimer structures for protein pairs in biological pathways.

A PhD position is available in the group of Prof. Dr. Nina Hartrampf at the Department of Chemistry, University of Zurich (Switzerland), in collaboration with the company Novo Nordisk in Måløv, Denmar...

The dysregulated post-translational modification of proteins is an established hallmark of human disease. Through Zn2+-dependent hydrolysis of acyl-lysine modifications, histone deacetylases (HDACs) a...

Using a combination of antibody- and LC–MS/MS-based methods, Zhang et al. reveal lysine l-lactylation as the key lactylation isomer in cellular histones, responding dynamically to glycolysis and posit...

Histone deacylases are erasers of Nε-acyl-lysine post-translational modifications and have been targeted for decades for the treatment of cancer, neurodegeneration and other disorders. Due to their r...