Electron cryo-microscopy structures of GluA1 AMPA receptors from Ingo Greger’s group in the LMB’s Neurobiology Division reveals that previously unseen structural flexibility of N-terminal domains is crucial for regulating the open-close speed of ion channel gates and recruiting the receptor into synapses.
New research from Anne Bertolotti’s group in the LMB’s Neurobiology Division reveals that nanomolar ATP-competitive inhibitors of integrated stress response (ISR) kinases unexpectedly activate the ISR at micromolar concentrations by directly binding to and activating a sister ISR kinase.
Kelly Nguyen’s group, in the LMB’s Structural Studies Division, have solved the cryo-EM structures of a telomeric nucleosome both bound and unbound to shelterin component TRF1, providing novel insights into the molecular interactions between shelterin and nucleosomes.
Nazareno Bona and Gerry Crossan, in the LMB’s PNAC Division, present a mechanistic explanation of how Fanconi anaemia factors act in a common pathway to restrict LINE-1 retrotransposition.
Sean Munro’s group in the LMB’s Cell Biology Division have investigated the potential biological significance of conserved genes of unknown function by developing an Unknome database to systematically analyse their identification and characterisation.
Cryo-EM structures from the most common type of frontotemporal lobar degeneration, determined by Benjamin Ryskeldi-Falcon’s group in the LMB’s Neurobiology Division, reveals that TDP-43 forms amyloid filaments with distinct folds in different neurodegenerative conditions.