Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targeting

Journal of Biological Chemistry

Volumn 273, Issue 33, 1998, Pages 21067-21076

  Cuozzo, John W ^a   Tao, Kai ^a   Cygler, Mirek ^b   Mort, John S ^c   Sahagian, G Gary ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^c SHRINERS HOSPITAL FOR CHILDREN   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; CATHEPSIN L;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL STRAIN COS1; CONFORMATIONAL TRANSITION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; GLYCOSYLATION; LYSOSOME; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ANIMALS; BASE SEQUENCE; CATHEPSIN D; CATHEPSINS; COS CELLS; CYSTEINE ENDOPEPTIDASES; DNA, COMPLEMENTARY; ENDOPEPTIDASES; HUMANS; LYSINE; LYSOSOMES; MANNOSE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN CONFORMATION;

EID: 0032516825     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.33.21067     Document Type: Article

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