Sarah M. Lowen

1 month ago | science.org | Barbara von Hippel |Jinke Chang |Christopher A. Waudby |Elena Emili |Sarah M. Lowen |Alistair M. Jagger | +6 more

AbstractSerpins, protease inhibitors whose regulated conformational instability renders them susceptible to mutations that cause misfolding, represent a system for the study of non-amyloid protein aggregation. The E342K “Z” variant of α-1-antitrypsin (AAT) undergoes oligomeric self-assembly into polymer chains that are associated with liver and lung pathologies in AAT deficiency.