Associated Papers
LYSET facilitates integration of both the N- and C-terminal transmembrane helices/cytoplasmic domains of GlcNAc-1-phosphotransferase.
Doray B et al.
Molecular Biology of the Cell, 2025
Engineering of a high-fidelity Cas12a nuclease variant capable of allele-specific editing.
Wei J et al.
Plos Biology, 2024
CNS Manifestations in Mucolipidosis Type II-A Retrospective Analysis of Longitudinal Data on Neurocognitive Development and Neuroimaging in Eleven Patients.
Ammer LS et al.
Journal of Clinical Medicine, 2023
Lysosomal enzyme trafficking factor LYSET enables nutritional usage of extracellular proteins.
Pechincha C et al.
Science (new York, N.y.), 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
Mucolipidoses Overview: Past, Present, and Future.
Khan SA et al.
International Journal of Molecular Sciences, 2020
Disease-causing missense mutations within the N-terminal transmembrane domain of GlcNAc-1-phosphotransferase impair endoplasmic reticulum translocation or Golgi retention.
Lee WS et al.
Human Mutation, 2020
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
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
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
Transport of the GlcNAc-1-phosphotransferase α/β-subunit precursor protein to the Golgi apparatus requires a combinatorial sorting motif.
Franke M et al.
The Journal of Biological Chemistry, 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 cell lines from patients with mucolipidosis II and mucolipidosis III.
Zarghooni M et al.
American Journal of Medical Genetics. Part A, 2009
Abnormal expressions of the subunits of the UDP-N-acetylglucosamine: lysosomal enzyme, N-acetylglucosamine-1-phosphotransferase, result in the formation of cytoplasmic vacuoles resembling those of the I-cells.
Ho CY et al.
Journal of Molecular Medicine (berlin, Germany), 2007
Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha / beta -subunits precursor gene.
Kudo M et al.
American Journal of Human Genetics, 2006