Pamina Kazman, Marie-Theres Vielberg ... Johannes Buchner
Identifying the patient-specific mutation that shifted the antibody light chain to the deadly fibrillar species provides new insight in the molecular pathogenesis of AL amyloidosis.
Theodoros K Karamanos, Matthew P Jackson ... Sheena E Radford
Solution NMR provides structural and kinetic information about oligomers on pathway to amyloid fibrils that are precisely structured but not cytotoxic.
Debdeep Chatterjee, Reeba S Jacob ... Samir K Maji
Co-aggregation, amyloid formation, and unidirectional cross-seeding of prolactin and galanin for their efficient storage in secretory granules of pituitary and subsequent functional hormone release.
A new native prion protein aggregation assay shows that syntaxin-6, a risk factor for sporadic Creutzfeldt–Jakob disease, delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediates.
The polyQ tract of pathogenic Huntingtin causes aggregation when expanded in Huntington’s disease, but its two flanking domains control its conformational landscape, proteostasis and neurotoxicity.
Monitoring the formation of two distinct arrangements in early amyloid-ß aggregation by mass spectrometry and ion mobility allows determination of the effect of potential drug candidates.
The amyloid polymorph selection that occurs during α-synuclein aggregation is dictated by environmental conditions, in particular pH, with the largest variety of structures being observed near neutral pH.
Ricardo Guerrero-Ferreira, Nicholas MI Taylor ... Henning Stahlberg
Two new polymorphic structures of recombinant human alpha-synuclein fibrils show striking differences to previous structures, while familial PD mutation sites remain crucial for protofilament interaction and fibril stability.
