Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: Abnormal intracellular processing and evidence for extracellular activation

Human Molecular Genetics

Volumn 5, Issue 6, 1996, Pages 737-743

  Peltola, Minna ^a   Tikkanen, Ritva ^a   Peltonen, Leena ^a   Jalanko, Anu ^a  

^a NATIONAL PUBLIC HEALTH INSTITUTE   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME PRECURSOR; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; PROLINE; SERINE;

ANIMAL CELL; ARTICLE; ASPARTYLGLYCOSAMINURIA; CELL STRAIN COS1; CLINICAL ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME PHOSPHORYLATION; ENZYME SUBUNIT; GENE MUTATION; HUMAN; LYSOSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN TARGETING;

ANIMALS; ASPARTYLGLUCOSYLAMINASE; BINDING SITES; CELL LINE, TRANSFORMED; CERCOPITHECUS AETHIOPS; ENDOPEPTIDASES; ENDOPLASMIC RETICULUM; HUMANS; LYSOSOMAL STORAGE DISEASES; LYSOSOMES; POINT MUTATION; PROLINE; PROTEIN PROCESSING, POST-TRANSLATIONAL; SERINE;

EID: 0029998354     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/5.6.737     Document Type: Article

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