Misfolded endoplasmic reticulum retained subunits cause degradation of wild-type subunits of arylsulfatase A heteromers
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2010.07745.x/fullpdf
Reference28 articles.
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2. Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis;Lukatela;Biochemistry,1998
3. Glycosylation and phosphorylation of arylsulfatase A;Sommerlade;J Biol Chem,1994
4. Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site;Gieselmann;Proc Natl Acad Sci USA,1989
5. Pseudodeficiency of arylsulphatase A: strategy for clarification of genotype in families of subjects with low ASA activity and neurological symptoms;Leistner;J Inherit Metab Dis,1995
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