Associated Papers
Structural insights into how GlcNAc-1-phosphotransferase directs lysosomal protein transport.
Du S et al.
The Journal of Biological Chemistry, 2022
The lysosomal storage disorders mucolipidosis type II, type III alpha/beta, and type III gamma: Update on GNPTAB and GNPTG mutations.
Velho RV et al.
Human Mutation, 2019
GNPTAB missense mutations cause loss of GlcNAc-1-phosphotransferase activity in mucolipidosis type II through distinct mechanisms.
Ludwig NF et al.
The International Journal of Biochemistry & Cell Biology, 2017
Clinical, biochemical and molecular characterization of Korean patients with mucolipidosis II/III and successful prenatal diagnosis.
Yang M et al.
Orphanet Journal of Rare Diseases, 2017
Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site.
Velho RV et al.
Human Molecular Genetics, 2015
Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition.
Qian Y et al.
The Journal of Biological Chemistry, 2015
Molecular characterization of 22 novel UDP-N-acetylglucosamine-1-phosphate transferase alpha- and beta-subunit (GNPTAB) gene mutations causing mucolipidosis types IIalpha/beta and IIIalpha/beta in 46 patients.
Tappino B et al.
Human Mutation, 2009
Mucolipidosis II and III alpha/beta: mutation analysis of 40 Japanese patients showed genotype-phenotype correlation.
Otomo T et al.
Journal of Human Genetics, 2009
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