http://www.cnr.it/ontology/cnr/individuo/prodotto/ID285330
On the structural organization of the intracellular domains of CFTR (Articolo in rivista)
- Type
- Label
- On the structural organization of the intracellular domains of CFTR (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.biocel.2014.01.024 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.scopus.com/inward/record.url?eid=2-s2.0-84901610851&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- ISI Web of Science (WOS) (literal)
- Scopu (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Instituto di Biofisica, CNR, Via de Marini, 6, 16149 Genova, Italy (literal)
- Titolo
- On the structural organization of the intracellular domains of CFTR (literal)
- Abstract
- The cystic fibrosis transmembrane conductance regulator (CFTR) is a multidomain membrane protein forming an anion selective channel. Mutations in the gene encoding CFTR cause cystic fibrosis (CF). The intracellular side of CFTR constitutes about 80% of the total mass of the protein. This region includes domains involved in ATP-dependent gating and regulatory protein kinase-A phosphorylation sites. The high-resolution molecular structure of CFTR has not yet been solved. However, a range of lower resolution structural data, as well as functional biochemical and electrophysiological data, are now available. This information has enabled the proposition of a working model for the structural architecture of the intracellular domains of the CFTR protein. This article is part of a Directed Issue entitled: Cystic Fibrosis: From o-mics to cell biology, physiology, and therapeutic advances. © 2014 Elsevier Ltd. (literal)
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