(PDF) Engineering of GlcNAc-1-Phosphotransferase for

Engineering of GlcNAc-1-Phosphotransferase for Production of Highly Phosphorylated Lysosomal Enzymes for Enzyme Replacement Therapy

Molecular Therapy - Methods and Clinical Development - United States

doi 10.1016/j.omtm.2017.03.006

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June 1, 2017

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Elsevier BV

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Engineering of GlcNAc-1-Phosphotransferase for Production of Highly Phosphorylated Lysosomal Enzymes for Enzyme Replacement Therapy

Molecular Therapy - Methods and Clinical Development - United States

doi 10.1016/j.omtm.2017.03.006

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Promising CNS-directed Enzyme Replacement Therapy for Lysosomal Storage Diseases

Cost-Effectiveness of Enzyme Replacement Therapy for Type 1 Gaucher Disease

Psy97 - Cost-Effectiveness Analysis of Enzyme Replacement Therapy for Type 1 Gaucher Disease

Loss of Lysosomal Enzymes, Inhibition of Enzyme Pinocytosis and Decreased Activity of Lysosomal Enzymes in Chloroquine Treated Fibroblasts

Enzyme Replacement Therapy for Late-Onset Pompe Disease

Early Diagnosis of Infantile-Onset Lysosomal Acid Lipase Deficiency in the Advent of Available Enzyme Replacement Therapy

Synthesis of the Subterminally 6-O-Phosphorylated Trimannosides Found on Carbohydrate Chains of Lysosomal Enzymes

An Alternative Hypothesis of Cellular Transport of Lysosomal Enzymes in Fibroblasts. Effect of Inhibitors of Lysosomal Enzyme Endocytosis on Intra- And Extra-Cellular Lysosomal Enzyme Activities

Lysosomal Enzyme Phosphorylation in Human Fibroblasts. Kinetic Parameters Offer a Biochemical Rationale for Two Distinct Defects in the Uridine Diphospho-N-Acetylglucosamine:lysosomal Enzyme Precursor N-Acetylglucosamine-1-Phosphotransferase.