The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase

Phenylketonuria (PKU) is caused by autosomal recessive variants in phenylalanine hydroxylase (PAH) and can lead to neurotoxicity. Here the authors describe a mouse model of PKU based on a mutation in phenylalanine hydroxylase (R261Q) which replicates traits of this disease and shows a proteostasis d...

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Autores principales:	Oscar Aubi, Karina S. Prestegård, Kunwar Jung-KC, Tie-Jun Sten Shi, Ming Ying, Ann Kari Grindheim, Tanja Scherer, Arve Ulvik, Adrian McCann, Endy Spriet, Beat Thöny, Aurora Martinez
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/020954ecba5d415e91bb8d1edb0ad49b
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spelling	oai:doaj.org-article:020954ecba5d415e91bb8d1edb0ad49b2021-12-02T14:17:30ZThe Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase10.1038/s41467-021-22107-12041-1723https://doaj.org/article/020954ecba5d415e91bb8d1edb0ad49b2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22107-1https://doaj.org/toc/2041-1723Phenylketonuria (PKU) is caused by autosomal recessive variants in phenylalanine hydroxylase (PAH) and can lead to neurotoxicity. Here the authors describe a mouse model of PKU based on a mutation in phenylalanine hydroxylase (R261Q) which replicates traits of this disease and shows a proteostasis defect and oxidative stress, implying a gain-of-function contribution to the disease phenotype.Oscar AubiKarina S. PrestegårdKunwar Jung-KCTie-Jun Sten ShiMing YingAnn Kari GrindheimTanja SchererArve UlvikAdrian McCannEndy SprietBeat ThönyAurora MartinezNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Oscar Aubi Karina S. Prestegård Kunwar Jung-KC Tie-Jun Sten Shi Ming Ying Ann Kari Grindheim Tanja Scherer Arve Ulvik Adrian McCann Endy Spriet Beat Thöny Aurora Martinez The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
description	Phenylketonuria (PKU) is caused by autosomal recessive variants in phenylalanine hydroxylase (PAH) and can lead to neurotoxicity. Here the authors describe a mouse model of PKU based on a mutation in phenylalanine hydroxylase (R261Q) which replicates traits of this disease and shows a proteostasis defect and oxidative stress, implying a gain-of-function contribution to the disease phenotype.
format	article
author	Oscar Aubi Karina S. Prestegård Kunwar Jung-KC Tie-Jun Sten Shi Ming Ying Ann Kari Grindheim Tanja Scherer Arve Ulvik Adrian McCann Endy Spriet Beat Thöny Aurora Martinez
author_facet	Oscar Aubi Karina S. Prestegård Kunwar Jung-KC Tie-Jun Sten Shi Ming Ying Ann Kari Grindheim Tanja Scherer Arve Ulvik Adrian McCann Endy Spriet Beat Thöny Aurora Martinez
author_sort	Oscar Aubi
title	The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
title_short	The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
title_full	The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
title_fullStr	The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
title_full_unstemmed	The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
title_sort	pah-r261q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/020954ecba5d415e91bb8d1edb0ad49b
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The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase

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