Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form

International Journal of Biochemistry and Cell Biology

Volumn 39, Issue 3, 2007, Pages 638-649

  Follo, Carlo ^a   Castino, Roberta ^a   Nicotra, Giuseppina ^a   Trincheri, Nicol F ^a   Isidoro, Ciro ^a  

^a UNIVERSITY OF EASTERN PIEDMONT   (Italy)

Author keywords

Lysosomal enzyme; Lysosome; Mutagenesis; Pepstatin; Peptide processing

Indexed keywords

AMINO ACID; CATHEPSIN D; MANNOSE; MUTANT PROTEIN; PEPSTATIN; POLYPEPTIDE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL COMPARTMENTALIZATION; CONTROLLED STUDY; ENDOSOME; ENZYME ACTIVITY; GENE MUTATION; HUMAN; HUMAN CELL; LYSOSOME; MOUSE; NONHUMAN; PROTEIN BINDING; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; RAT; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CATHEPSIN D; CELL LINE; CHO CELLS; CRICETINAE; CRICETULUS; HUMANS; HYDROGEN-ION CONCENTRATION; LYSOSOMES; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPSTATINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN TRANSPORT; RATS; RECOMBINANT PROTEINS; TRANSFECTION;

RODENTIA;

EID: 33846206064     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.11.010     Document Type: Article

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