Pharmacological chaperones facilitate the post-ER transport of recombinant N370S mutant β-glucocerebrosidase in plant cells: Evidence that N370S is a folding mutant

Molecular Genetics and Metabolism

Volumn 106, Issue 3, 2012, Pages 323-329

  Babajani, Gholamreza ^a   Tropak, Michael B ^b   Mahuran, Don J ^b,c   Kermode, Allison R ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

^b HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

glucocerebrosidase; N370S mutation; Pharmacological chaperones; Protoplasts; Secretion; Tobacco BY2 cells

Indexed keywords

AMBROXOL; CHAPERONE; GLUCOSYLCERAMIDASE; MUTANT PROTEIN; N (N NONYL) DEOXYNOJIRIMYCIN; UNCLASSIFIED DRUG;

ARTICLE; CELL FATE; CONTROLLED STUDY; CULTURE MEDIUM; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; LYSOSOME; MISSENSE MUTATION; NONHUMAN; PLANT CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SYNTHESIS; STEADY STATE; TOBACCO; WILD TYPE;

BIOLOGICAL TRANSPORT; CATALYTIC DOMAIN; CELLS, CULTURED; ENDOPLASMIC RETICULUM; GAUCHER DISEASE; GLUCOSYLCERAMIDASE; HUMANS; MOLECULAR CHAPERONES; MUTATION; PLANT CELLS; PLANTS, GENETICALLY MODIFIED; PROTEIN FOLDING; RECOMBINANT PROTEINS;

NICOTIANA TABACUM;

EID: 84862585334     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2012.04.018     Document Type: Article

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