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SHR Neuro Krebs Kardio Lipid

Strandback, E; Lienhart, WD; Hromic-Jahjefendic, A; Bourgeois, B; Hogler, A; Waltenstorfer, D; Winkler, A; Zangger, K; Madl, T; Gruber, K; Macheroux, P.
A small molecule chaperone rescues the stability and activity of a cancer-associated variant of NAD(P)H:quinone oxidoreductase 1 in vitro
FEBS LETT. 2019; [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG

 

Autor/innen der Med Uni Graz:
Bourgeois Benjamin Michel Rene
Madl Tobias
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Number of Figures: 7
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Abstract:
NAD(P)H:quinone oxidoreductase 1 (NQO1) is a human FAD-dependent enzyme that plays a crucial role in the antioxidant defense system. A naturally occurring single-nucleotide polymorphism (NQO1*2) in the NQO1 gene leads to an amino acid substitution (P187S), which severely compromises the activity and stability of the enzyme. The NQO1*2 genotype has been linked to a higher risk for several types of cancer and poor survival rate after anthracycline-based chemotherapy. In this study, we show that a small molecular chaperone (N-(2-bromophenyl)pyrrolidine-1-sulfonamide) repopulates the native wild-type conformation. As a consequence of the stabilizing effect, the enzymatic activity of the P187S variant protein is strongly improved in the presence of the molecular chaperone in vitro.

Find related publications in this database (Keywords)
cancer
chemical chaperone
chemotherapeutics
quinone
single-nucleotide polymorphism
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