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- W4280573328 endingPage "130173" @default.
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- W4280573328 abstract "Nucleophosmin 1 (NPM1) protein is a multifunctional nucleolar chaperone and its gene is the most frequently mutated in Acute Myeloid Leukemia (AML). AML mutations cause the unfolding of the C-terminal domain (CTD) and the protein delocalizing in the cytosol (NPM1c+). Marked aggregation endowed with an amyloid character was assessed as consequences of mutations.Herein we analyzed the effects of type C mutation on two protein regions: i) a N-terminal extended version of the CTD, named Cterm_mutC and ii) a shorter polypeptide including the sequences of the second and third helices of the CTD, named H2_mutC.Both demonstrated able to self-assembly with different kinetics and conformational intermediates and to provide fibers presenting large flexible regions.The present study adds a new piece of knowledge to the effects of AML-mutations on structural biology of Nucleophosmin 1, that could be exploited in therapeutic interventions targeting selectively NPMc+." @default.
- W4280573328 created "2022-05-22" @default.
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- W4280573328 date "2022-08-01" @default.
- W4280573328 modified "2023-09-24" @default.
- W4280573328 title "Type C mutation of nucleophosmin 1 acute myeloid leukemia: Consequences of intrinsic disorder" @default.
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- W4280573328 doi "https://doi.org/10.1016/j.bbagen.2022.130173" @default.
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