Post-translational modification of histone H3K36 is not required to suppress cryptic transcription initiation or to include alternative exons in Drosophila; instead it promotes expression of active genes by stimulating polyadenylation.
Extensive molecular dynamics simulations enhanced by advanced sampling techniques give a detailed view of p38α canonical activation mechanism, which reveals novel key electrostatic interactions that are put in context of existing experimental data.
Surprising connections between gene architecture and splicing kinetics are illuminated using short, progressive metabolic labeling/RNA sequencing and novel computational modeling approaches in Drosophila cells.
A combination of equilibrium and nonequilibrium molecular dynamics simulations is an effective tool to study allosteric communications in ultrafast enzymes that show little or no conformational changes.
Computational methods reveal how mutations affect the conformational landscape of the kinase domain of EGFR resulting in abnormal signaling and provide a structural framework for ongoing drug discovery efforts on mutant-specific EGFR inhibition.