Literature DB >> 21594795

CFTR three-dimensional structure.

Robert C Ford1, James Birtley, Mark F Rosenberg, Liang Zhang.   

Abstract

CFTR is a member of the ATP-binding cassette family of membrane proteins. This is one of the best characterised membrane protein families in terms of structure and function. CFTR operates as an ion channel, unlike nearly all other family members which are active transporters. Here, we discuss methods that have allowed such data to be obtained for CFTR.

Entities:  

Mesh:

Substances:

Year:  2011        PMID: 21594795     DOI: 10.1007/978-1-61779-117-8_22

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  3 in total

Review 1.  Cystic fibrosis transmembrane conductance regulator (ABCC7) structure.

Authors:  John F Hunt; Chi Wang; Robert C Ford
Journal:  Cold Spring Harb Perspect Med       Date:  2013-02-01       Impact factor: 6.915

2.  Functional Rescue of F508del-CFTR Using Small Molecule Correctors.

Authors:  Steven Molinski; Paul D W Eckford; Stan Pasyk; Saumel Ahmadi; Stephanie Chin; Christine E Bear
Journal:  Front Pharmacol       Date:  2012-09-26       Impact factor: 5.810

3.  Expression and purification of the cystic fibrosis transmembrane conductance regulator protein in Saccharomyces cerevisiae.

Authors:  Liam O'Ryan; Tracy Rimington; Natasha Cant; Robert C Ford
Journal:  J Vis Exp       Date:  2012-03-10       Impact factor: 1.355

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.