Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase - Wikidata - awgldk - TriplyDB

Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

http://www.wikidata.org/entity/Q24324179

about

The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module 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 Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB)Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site Post-translational modifications of the gamma-subunit affect intracellular trafficking and complex assembly of GlcNAc-1-phosphotransferase Comparative Analysis of Glycogene Expression in Different Mouse Tissues Using RNA-Seq Data Engineering of GlcNAc-1-Phosphotransferase for Production of Highly Phosphorylated Lysosomal Enzymes for Enzyme Replacement Therapy.UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the methylphosphomannosyl residues on the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins.Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease.Neurologic abnormalities in mouse models of the lysosomal storage disorders mucolipidosis II and mucolipidosis III γ.Glucosidase II and MRH-domain containing proteins in the secretory pathway.A role for inherited metabolic deficits in persistent developmental stuttering Cathepsin-Mediated Alterations in TGFß-Related Signaling Underlie Disrupted Cartilage and Bone Maturation Associated With Impaired Lysosomal Targeting.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.Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.Glyco-engineering strategies for the development of therapeutic enzymes with improved efficacy for the treatment of lysosomal storage diseases.Subunit interactions of the disease-related hexameric GlcNAc-1-phosphotransferase complex.Quantitative Proteome Analysis of Mouse Liver Lysosomes Provides Evidence for Mannose 6-phosphate-independent Targeting Mechanisms of Acid Hydrolases in Mucolipidosis II.Enzyme-specific differences in mannose phosphorylation between GlcNAc-1-phosphotransferase αβ and γ subunit deficient zebrafish support cathepsin proteases as early mediators of mucolipidosis pathology.Characterization and downstream mannose phosphorylation of human recombinant α-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds Proteolytic processing of the gamma-subunit is associated with the failure to form GlcNAc-1-phosphotransferase complexes and mannose 6-phosphate residues on lysosomal enzymes in human macrophages.Transport of the GlcNAc-1-phosphotransferase α/β-subunit precursor protein to the Golgi apparatus requires a combinatorial sorting motif.Enigmatic in vivo GlcNAc-1-phosphotransferase (GNPTG) transcript correction to wild type in two mucolipidosis III gamma siblings homozygous for nonsense mutations.Targeted Cell-to-Cell Delivery of Protein Payloads via the Granzyme-Perforin Pathway.N-glycan structures and downstream mannose-phosphorylation of plant recombinant human alpha-L-iduronidase: toward development of enzyme replacement therapy for mucopolysaccharidosis I.Identification of the interaction domains between α- and γ-subunits of GlcNAc-1-phosphotransferase.Lysosomal Proteome and Secretome Analysis Identifies Missorted Enzymes and Their Nondegraded Substrates in Mucolipidosis III Mouse Cells

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Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

http://www.wikidata.org/entity/Q24324179

description

2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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JBC.M109.068650

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Journal of Biological Chemistry

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Functions of the alpha, beta, ...... ucosamine-1-phosphotransferase

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P2093

Intaek Lee

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Mariko Kudo

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Meiqian Qian

http://www.w3.org/2001/XMLSchema#string

Peter Lobel

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Stuart Kornfeld

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Wang-Sik Lee

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William M Canfield

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Yi Qian

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P2860

NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols

Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Colorimetric Method for Determination of Sugars and Related Substances

When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations in 24 patients

Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase

Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis

Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis

Murine UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase lacking the gamma-subunit retains substantial activity toward acid hydrolases

Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis

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3360-70

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scholarly article

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10.1074/JBC.M109.068650

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5

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285

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2010-01-29T00:00:00Z

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19955174

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carbohydrate phosphorylation

N-acetylglucosamine-1-phosphate transferase subunits alpha and beta

N-acetylglucosamine-1-phosphate transferase subunit gamma

P932

2823453

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