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• W1827510299 endingPage "2015" @default.
• W1827510299 startingPage "2007" @default.
• W1827510299 abstract "A major pathway to the lysosome for soluble hydrolases involves the 6-phosphorylation of mannose residues. The initial step in this reaction is catalyzed by a phosphotransferase which recognizes lysosomal precursors. We constructed mutants of human procathepsin D whose targeting to the lysosome could be assayed directly in intact cells. Eight lysine residues were individually converted to glutamic acid on the surface of the carboxyl terminal lobe of the protein. Mutants with as many as four Lys to Glu mutations were normally targeted to the lysosome and processed to the mature form of the enzyme in transfected cells. We conclude that the C-terminal lobe of procathepsin D may not carry a determinant essential for lysosomal targeting in intact fibroblasts." @default.
• W1827510299 created "2016-06-24" @default.
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• W1827510299 date "1995-05-01" @default.
• W1827510299 modified "2023-09-27" @default.
• W1827510299 title "Lysine residues in the C-terminal lobe and lysosomal targeting of procathepsin D" @default.
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• W1827510299 doi "https://doi.org/10.1242/jcs.108.5.2007" @default.
• W1827510299 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7657721" @default.
• W1827510299 hasPublicationYear "1995" @default.
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