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Introduction: Pharmacological chaperone therapy for lysosomal storage disorders – leveraging aspects of the folding pathway to maximize activity of misfolded mutant proteins
Author(s) -
Fan JianQiang
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06043.x
Subject(s) - chemical chaperone , endoplasmic reticulum associated protein degradation , protein folding , proteostasis , chaperone (clinical) , endoplasmic reticulum , mutant , microbiology and biotechnology , osmolyte , calnexin , foldase , co chaperone , unfolded protein response , chemistry , small molecule , protein engineering , biochemistry , biology , enzyme , hsp90 , heat shock protein , medicine , pathology , groel , escherichia coli , gene , calreticulin