Inter-divisional collaboration between the groups of Sjors Scheres, Michel Goedert and others identified TMEM106B as a new protein responsible for amyloid filament formation, and showed that these filaments develop in an age-dependent manner in human brains.
Insight on Research
Structural study reveals a novel activation mechanism for the fungal GPCR, Ste2
Chris Tate’s group, in the LMB’s Structural Studies Division, have used cryo-EM analysis to show that Ste2, a fungal Class D GPCR, has a fundamentally distinct activation mechanism in comparison to other types of GPCRs.
Cryo-EM structures reveal molecular basis of human telomerase recruitment
Kelly Nguyen’s group in the LMB’s Structural Studies Division has determined the molecular basis of how the TPP1 and POT1 components of shelterin recruit human telomerase to telomeres and regulate the enzyme’s activity during genomic replication.
New method to discover protease and other hydrolase substrates in live mammalian cells
Using genetic code expansion techniques, Jason Chin’s group in the LMB’s PNAC Division have designed a new mechanism-based, light-activated technique to trap and identify new protease and other hydrolase substrates.
Cryptochrome proteins are integral to maintain time within the brain’s master clock
Using synthetic biological techniques, Michael Hastings’ group have collaborated with Jason Chin to gain novel insights into the molecular and cellular processes which govern the suprachiasmatic nucleus, and identified a key regulatory role of cryptochrome clock proteins.
Atomic structures of Aβ42 filaments from the brains of individuals with Alzheimer’s disease and other neurodegenerative conditions
Collaboration between Sjors Scheres’ (Structural Studies), Benjamin Ryskeldi-Falcon’s and Michel Goedert’s (both Neurobiology) groups have used cryo-EM to reveal structures of Aβ42 filaments, the key factor behind the pathogenesis of Alzheimer’s disease.