M. L. Martin-Fernandez

This study identifies how the T766M-EGFR mutation promotes tumor growth by utilizing new oligomer assembly mechanisms in ligand-free EGFR.

This study investigates how binding partners regulate myosin VI unfolding and activation through biochemical and single-molecule analyses of splice isoforms.

This study identifies NDP52's role in modulating RNA Polymerase II transcription by altering DNA conformation through direct dsDNA binding and interactions with chromatin regulators.

The paper develops a CRISPR/Cas9-based tool to induce targeted and tunable DNA double-strand breaks in human cells for studying repair mechanisms.

The paper introduces smfBox, an open-source confocal smFRET platform that reduces costs and provides detailed instructions and software to make smFRET accessible to non-specialists.

This study uses cryo-imaging to reveal SARS-CoV-2 replication, assembly, and egress pathways in infected cells.

This study identifies cis dimerization of FLRT2 via transmembrane and extracellular motifs, suggesting a competitive interaction mechanism with trans interactions.

This study identifies nuclear myosin VI as a molecular anchor for RNA Polymerase II clusters, showing its role in maintaining transcription factory organization and gene expression.

The paper investigates how binding partners regulate myosin VI activity, showing that Dab2 loss increases nuclear myosin VI activity, promoting estrogen receptor-driven tumourgenesis.