Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 77, Issue -, Pages 701-726Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.75.103004.142532
Keywords
ABC protein; anion channel; cystic fibrosis; ER quality control; molecular therapy; protein misfolding
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Mutations in the gene coding for the cystic fibrosis transmembrane conductance regulator (CFTR) epithelial anion channel cause cystic fibrosis (CF). The multidomain integral membrane glycoprotein, a member of the adenine nucleotide-bin ding cassette (ABC) transporter family, conserved in metazoan salt-transporting tissues, is required to control ion and fluid homeostasis on epithelial surfaces. This review considers different therapeutic strategies that have arisen from knowledge of CFTR structure and function as well as its biosynthetic processing, intracellular trafficking, and turnover.
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