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- W2981278341 endingPage "1268" @default.
- W2981278341 startingPage "1259" @default.
- W2981278341 abstract "Abstract The ABCG5/G8 heterodimer is the primary neutral sterol transporter in hepatobiliary and transintestinal cholesterol excretion. Inactivating mutations on either the ABCG5 or ABCG8 subunit cause Sitosterolemia, a rare genetic disorder. In 2016, a crystal structure of human ABCG5/G8 in an apo state showed the first structural information on ATP-binding cassette (ABC) sterol transporters and revealed several structural features that were observed for the first time. Over the past decade, several missense variants of ABCG5/G8 have been associated with non-Sitosterolemia lipid phenotypes. In this review, we summarize recent pathophysiological and structural findings of ABCG5/G8, interpret the structure-function relationship in disease-causing variants and describe the available evidence that allows us to build a mechanistic view of ABCG5/G8-mediated sterol transport." @default.
- W2981278341 created "2019-10-25" @default.
- W2981278341 creator A5009256892 @default.
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- W2981278341 creator A5088259400 @default.
- W2981278341 date "2019-10-18" @default.
- W2981278341 modified "2023-10-03" @default.
- W2981278341 title "ABCG5/G8: a structural view to pathophysiology of the hepatobiliary cholesterol secretion" @default.
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- W2981278341 doi "https://doi.org/10.1042/bst20190130" @default.
- W2981278341 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6824678" @default.
- W2981278341 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31654053" @default.
- W2981278341 hasPublicationYear "2019" @default.
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