Associated Papers
Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.
Gorelik A et al.
Proceedings of the National Academy of Sciences of the United States of America, 2022
Structure of the human GlcNAc-1-phosphotransferase αβ subunits reveals regulatory mechanism for lysosomal enzyme glycan phosphorylation.
Li H et al.
Nature Structural & Molecular Biology, 2022
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
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
A compound heterozygous GNPTAB mutation causes mucolipidosis II with marked hair color change in a Han Chinese baby.
Ma GC et al.
American Journal of Medical Genetics. Part A, 2011
Missense mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTA) in a patient with mucolipidosis II induces changes in the size and cellular distribution of GNPTG.
Tiede S et al.
Human Mutation, 2006
Missense mutations in N-acetylglucosamine-1-phosphotransferase alpha/beta subunit gene in a patient with mucolipidosis III and a mild clinical phenotype.
Tiede S et al.
American Journal of Medical Genetics. Part A, 2005
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