Associated Papers
Development of national biobank for lysosomal storage disorders in India- a step towards advancing research and precision medicine.
Sheth J et al.
Orphanet Journal of Rare Diseases, 2026
Structural insights into how GlcNAc-1-phosphotransferase directs lysosomal protein transport.
Du S et al.
The Journal of Biological Chemistry, 2022
Pathogenic variants in GNPTAB and GNPTG encoding distinct subunits of GlcNAc-1-phosphotransferase differentially impact bone resorption in patients with mucolipidosis type II and III.
Di Lorenzo G et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2021
Mucolipidosis type II and type III: a systematic review of 843 published cases.
Dogterom EJ et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2021
Targeted Sequencing of 242 Clinically Important Genes in the Russian Population From the Ivanovo Region.
Ramensky VE et al.
Frontiers in Genetics, 2021
Imbalanced cellular metabolism compromises cartilage homeostasis and joint function in a mouse model of mucolipidosis type III gamma.
Westermann LM et al.
Disease Models & Mechanisms, 2020
Identification and characterization of 30 novel pathogenic variations in 69 unrelated Indian patients with Mucolipidosis Type II and Type III.
Pasumarthi D et al.
Journal of Human Genetics, 2020
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
Clinical implementation of gene panel testing for lysosomal storage diseases.
Gheldof A et al.
Molecular Genetics & Genomic Medicine, 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
Solving a case of allelic dropout in the GNPTAB gene: implications in the molecular diagnosis of mucolipidosis type III alpha/beta.
Coutinho MF et al.
Journal of Pediatric Endocrinology & Metabolism : Jpem, 2016
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
A novel intermediate mucolipidosis II/IIIαβ caused by GNPTAB mutation in the cytosolic N-terminal domain.
Leroy JG et al.
European Journal of Human Genetics : Ejhg, 2014
Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.
van Meel E et al.
Proceedings of the National Academy of Sciences of the United States of America, 2014
Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB).
De Pace R et al.
Human Mutation, 2014
Mucolipidosis II and III alpha/beta in Brazil: analysis of the GNPTAB gene.
Cury GK et al.
Gene, 2013
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
Phenotype and genotype in mucolipidoses II and III alpha/beta: a study of 61 probands.
Cathey SS et al.
Journal of Medical Genetics, 2010
Molecular analysis of the GNPTAB and GNPTG genes in 13 patients with mucolipidosis type II or type III - identification of eight novel mutations.
Encarnação M et al.
Clinical Genetics, 2009
When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations in 24 patients.
Bargal R et al.
Molecular Genetics and Metabolism, 2006