A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum

Journal of Biological Chemistry

Volumn 275, Issue 23, 2000, Pages 17863-17868

  Suokas, Marko ^a   Myllylä, Raili ^a   Kellokumpu, Sakari ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME GLYCOSYLATION; ENZYME LOCALIZATION; HYDROXYLATION; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

ANIMALS; CATHEPSIN D; CELL NUCLEUS; COS CELLS; ENDOPLASMIC RETICULUM; GOLGI APPARATUS; HUMANS; INTRACELLULAR MEMBRANES; PEPTIDE FRAGMENTS; PROCOLLAGEN-LYSINE, 2-OXOGLUTARATE 5-DIOXYGENASE; RECEPTORS, PEPTIDE; RECOMBINANT PROTEINS; TRANSFECTION;

EID: 0034625345     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M908025199     Document Type: Article

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