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| http://purl.uniprot.org/citations/24685677 | http://www.w3.org/2000/01/rdf-schema#comment | "The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-regulated chloride (Cl(-)) channel. Mutations of its gene lead to the disease of cystis fibrosis (CF) among which the most common is the deletion of phenylalanine at position 508 (Phe508del). CFTR is a multi-domain glycoprotein whose biosynthesis, maturation and functioning as an anion channel involve multi-level post-translational modifications of CFTR molecules and complex folding processes to reach its native, tertiary conformation. Only 20-40% of the nascent chains achieve folded conformation, while the remaining molecules are targeted for degradation by endoplasmic reticulum, lysosomes, or autophagy. A large number of mutations causing CF impair processing of CFTR. Growing knowledge of CFTR biosynthesis has enabled understanding the cellular basis of CF and has brought to light various potential targets for novel, promising therapies."xsd:string |
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| http://purl.uniprot.org/citations/24685677 | http://purl.uniprot.org/core/author | "Sermet-Gaudelus I."xsd:string |
| http://purl.uniprot.org/citations/24685677 | http://purl.uniprot.org/core/author | "Pranke I.M."xsd:string |
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| http://purl.uniprot.org/citations/24685677 | http://purl.uniprot.org/core/name | "Int J Biochem Cell Biol"xsd:string |
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| http://purl.uniprot.org/citations/24685677 | http://purl.uniprot.org/core/title | "Biosynthesis of cystic fibrosis transmembrane conductance regulator."xsd:string |
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