LEADER 04138nam 22006735 450 001 9910298590703321 005 20200704005852.0 010 $a3-319-65494-2 024 7 $a10.1007/978-3-319-65494-2 035 $a(CKB)4100000000882545 035 $a(DE-He213)978-3-319-65494-2 035 $a(MiAaPQ)EBC5086675 035 $a(PPN)220123276 035 $a(EXLCZ)994100000000882545 100 $a20171003d2018 u| 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aCFTR and Cystic Fibrosis $eFrom Structure to Function /$fby Carlos M. Farinha 205 $a1st ed. 2018. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2018. 215 $a1 online resource (XVIII, 56 p. 10 illus. in color.) 225 1 $aProtein Folding and Structure,$x2199-3157 311 $a3-319-65493-4 320 $aIncludes bibliographical references. 327 $aCystic fibrosis: an overview -- CFTR gene and protein -- CFTR in the cell -- CFTR function -- Therapies aimed at correcting the basic defect. 330 $aThis Brief is devoted to the CFTR protein and cystic fibrosis, and it provides an updated perspective of the genetic, functional and cellular processes involved in this conformational disorder. Starting with a historical perspective on cystic fibrosis and its clinical features, the author departs into an in-depth description of the biology of the CFTR protein, ending with a discussion on the latest approaches aimed at developing corrective therapies for cystic fibrosis. First the basic aspects of cystic fibrosis as a disorder are addressed, focusing on genetics and mutation prevalence. Then the CFTR protein is discussed in detail: its structure and classification within the ABC transporter superfamily, its biogenesis with membrane insertion and chaperone assisted folding, its glycosylation and how it regulates the endoplasmatic reticulum quality control mechanisms that assess CFTR folding status. Extra attention is given to post-ER trafficking and regulation of membrane stability and anchoring, and to CFTR functions. This is linked to the molecular mechanisms through which different CFTR mutations cause cystic fibrosis. Finally, the different efforts aiming at rescuing the basic defect, most of which aim at repairing CFTR dysfunction, are covered. Through this integrated perspective, readers will obtain a unique insight into this fascinating membrane-bound protein and its associated disease. This Brief appeals to an audience interested in human genetics, protein folding, protein trafficking and physiology. . 410 0$aProtein Folding and Structure,$x2199-3157 606 $aMedicinal chemistry 606 $aProteins  606 $aRespiratory organs?Diseases 606 $aHuman genetics 606 $aMolecular biology 606 $aMedicinal Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C28000 606 $aProtein Structure$3https://scigraph.springernature.com/ontologies/product-market-codes/L14050 606 $aPneumology/Respiratory System$3https://scigraph.springernature.com/ontologies/product-market-codes/H33134 606 $aHuman Genetics$3https://scigraph.springernature.com/ontologies/product-market-codes/B12008 606 $aMolecular Medicine$3https://scigraph.springernature.com/ontologies/product-market-codes/B1700X 615 0$aMedicinal chemistry. 615 0$aProteins . 615 0$aRespiratory organs?Diseases. 615 0$aHuman genetics. 615 0$aMolecular biology. 615 14$aMedicinal Chemistry. 615 24$aProtein Structure. 615 24$aPneumology/Respiratory System. 615 24$aHuman Genetics. 615 24$aMolecular Medicine. 676 $a572.633 700 $aFarinha$b Carlos M$4aut$4http://id.loc.gov/vocabulary/relators/aut$0768475 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910298590703321 996 $aCFTR and Cystic Fibrosis$91565462 997 $aUNINA