Associated Papers
Clinical and molecular characteristics of 20 Chinese probands with Mucolipidosis type II and III alpha/beta.
Feng Y et al.
Bmc Pediatrics, 2024
The mucolipidosis III-causing mutation in GNPTAB, c.1760G>C, disrupts the development of somites in rats.
Nong T et al.
Genes & Diseases, 2024
Rare Variants Analysis of Lysosomal Related Genes in Early-Onset and Familial Parkinson's Disease in a Chinese Cohort.
Chen YP et al.
Journal of Parkinson's Disease, 2021
34250953 (PubMed )
Supplement: sj-xlsx-2-pkn-10.3233_jpd-212658.xlsx › Sheet1
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
Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase.
Velho RV et al.
Febs Letters, 2016
Subunit interactions of the disease-related hexameric GlcNAc-1-phosphotransferase complex.
De Pace R et al.
Human Molecular Genetics, 2015
Exome sequencing for mucolipidosis III: Detection of a novel GNPTAB gene mutation in a patient with a very mild phenotype.
Sperb-Ludwig F et al.
Molecular Genetics and Metabolism Reports, 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
DNA-based diagnosis of mucolipidosis type IIIA and mucopolysacchariodisis type VI in a Chinese family: a chance of 1 in 7.6 trillion.
Lam CW et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 2007
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