Ontology highlight
ABSTRACT:
SUBMITTER: Banerjee PR
PROVIDER: S-EPMC4752826 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Banerjee Priya R PR Mitrea Diana M DM Kriwacki Richard W RW Deniz Ashok A AA
Angewandte Chemie (International ed. in English) 20151217 5
As for many intrinsically disordered proteins, order-disorder transitions in the N-terminal oligomerization domain of the multifunctional nucleolar protein nucleophosmin (Npm-N) are central to its function, with phosphorylation and partner binding acting as regulatory switches. However, the mechanism of this transition and its regulation remain poorly understood. In this study, single-molecule and ensemble experiments revealed pathways with alternative sequences of folding and assembly steps for ...[more]