Jan Huertas

This study introduces OpenCGChromatin, a model that simulates chromatin structure and phase separation, revealing how linker-DNA length and histone modifications affect chromatin organization.

The paper quantifies force-induced nucleosome unwrapping using a coarse-grained model, showing DNA flexibility and histone chemistry determine nucleosome stability and plasticity.

This paper maps the free-energy landscapes of chromatin structures and shows how linker DNA geometry and sequence modulate their topologies, influencing phase separation and structural polymorphism.

The paper introduces LASSI, a method to measure nucleosome spacing in chromatin interactions, revealing fiber homotypy as a structural pattern influenced by genomic features and cohesin dynamics.

This study shows that linker histone H1 acts as a liquid-like glue in chromatin domains, enabling dynamic interactions that support DNA transactions in human cells.

This study shows that electrostatic attraction compacts fragmented DNA during apoptosis, preventing its release, and demonstrates a synthetic approach to probe physical forces in genome organization.

The paper investigates the structure of chromatin condensates across scales and shows how nucleosome arrangement and histone interactions influence their physical properties.

This study shows Oct4 promotes DNA accessibility by forming clusters that deform chromatin and expose DNA through liquid-like states, enhancing gene activation during reprogramming.

This study identifies electrostatic repulsion as the mechanism driving centromere positioning at the chromatin surface, independent of condensin or microtubules.

The paper shows that nucleosome spacing affects chromatin phase separation stability and dynamics through inter- and intramolecular stacking trade-offs.

The paper shows cold-induced changes in nucleosome dynamics at the FLC locus in Arabidopsis, leading to transcriptional repression through chromatin structure transitions.

This study designs a synthetic biomolecular condensate platform using CTPR proteins and intrinsically-disordered domains to tune condensate properties and recruit target proteins.