Introduction: molecular chaperones of the ER: their role in protein folding and genetic disease.
Brooks
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Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia.
D002352:Carrier Proteins / Q000378:metabolism; D003550:Cystic Fibrosis / Q000235:genetics; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D020022:Genetic Predisposition to Disease / Q000235:genetics*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006360:Heat-Shock Proteins; D006801:Humans; D016464:Lysosomal Storage Diseases / Q000235:genetics; D008565:Membrane Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D009154:Mutation; D017510:Protein Folding
C505032:CFTR protein, human; D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; C018551:glucose-regulated proteins; D019005:Cystic Fibrosis Transmembrane Conductance Regulator