Mutations and Polymorphisms in the Human Argininosuccinate Lyase (ASL) Gene. Issue 1 (25th November 2013)

• Record Type: Journal Article
• Authors: Balmer, Cécile; Pandey, Amit V.; Rüfenacht, Véronique; Nuoffer, Jean‐Marc; Fang, Ping; Wong, Lee‐Jun; Häberle, Johannes
• Is Part Of: Human mutation. Volume 35:Issue 1(2014:Jan.)
• Page Start: 27
• Page End: 35
• Publication Date: 2013-11-25
• Subjects: Human chromosome abnormalities -- Periodicals; Mutation (Biology) -- Periodicals; 616.04205
• DOI: 10.1002/humu.22469
• Languages: English
• ISSNs: 1059-7794

Abstract

<abstract abstract-type="graphical" xml:lang="en" id="humu22469-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Argininosuccinate lyase deficiency (ASLD) is an inborn error of metabolism caused by a defect of the urea cycle enzyme argininosuccinate lyase (ASL) encoded by the ASL gene. Patients are affected by life‐threatening hyperammonemia, mental retardation and liver disease. We are providing here an update on the molecular basis of this disease by presenting all today known mutations (<italic>n</italic> = 134) as well as all known different genotypes (<italic>n</italic> = 160). To illustrate these data, we are presenting structural considerations focussing on the relevance of the known mutations for ASL homotetramer formation and function. <boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg3zsp6p54" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>