Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. The transport of lysosomal enzymes
2. Biosynthetic intermediates of beta-glucuronidase contain high mannose oligosaccharides with blocked phosphate residues.
3. Phosphorylated oligosaccharides in lysosomal enzymes: identification of alpha-N-acetylglucosamine(1)phospho(6)mannose diester groups.
4. Structural studies of phosphorylated high mannose-type oligosaccharides.
5. Identification of a rat liver alpha-N-acetylglucosaminyl phosphodiesterase capable of removing “blocking” alpha-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes.
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1. Post-translational Modifications of the γ-Subunit Affect Intracellular Trafficking and Complex Assembly of GlcNAc-1-phosphotransferase;Journal of Biological Chemistry;2011-02
2. Proteolytic Processing of the γ-Subunit Is Associated with the Failure to Form GlcNAc-1-phosphotransferase Complexes and Mannose 6-Phosphate Residues on Lysosomal Enzymes in Human Macrophages;Journal of Biological Chemistry;2010-07
3. Mannose phosphorylation in health and disease;European Journal of Cell Biology;2010-01
4. Steps in the Phosphorylation of the High Mannose Oligosaccharides of Lysosomal Enzymes;Novartis Foundation Symposia;2008-05-30
5. Lysosomal Enzyme GlcNAc-1- Phosphotransferase;Handbook of Glycosyltransferases and Related Genes;2002
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