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The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition moduleAnalysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognitionDetection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes.Rare recessive loss-of-function methionyl-tRNA synthetase mutations presenting as a multi-organ phenotype.Autophagy proteins regulate the secretory component of osteoclastic bone resorption.The lysosomal enzyme receptor protein (LERP) is not essential, but is implicated in lysosomal function in Drosophila melanogaster.Multiple Domains of GlcNAc-1-phosphotransferase Mediate Recognition of Lysosomal Enzymes.Mucolipidosis III GNPTG Missense Mutations Cause Misfolding of the γ Subunit of GlcNAc-1-Phosphotransferase.Imaging and imagination: understanding the endo-lysosomal systemMislocalization of phosphotransferase as a cause of mucolipidosis III αβ.TGN exit of the cation-independent mannose 6-phosphate receptor does not require acid hydrolase binding.Vacuolization of mucolipidosis type II mouse exocrine gland cells represents accumulation of autolysosomes.Disruption of the Man-6-P targeting pathway in mice impairs osteoclast secretory lysosome biogenesis.hVps41 and VAMP7 function in direct TGN to late endosome transport of lysosomal membrane proteins.
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2000-01-01T00:00:00Z