Asset Details
Do you wish to reserve the book?
The cystic fibrosis transmembrane conductance regulator (CFTR) and its stability
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The cystic fibrosis transmembrane conductance regulator (CFTR) and its stability
Do you wish to request the book?
The cystic fibrosis transmembrane conductance regulator (CFTR) and its stability
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The cystic fibrosis transmembrane conductance regulator (CFTR) and its stability
2017
Overview
The cystic fibrosis transmembrane conductance regulator (CFTR) is responsible for the disease cystic fibrosis (CF). It is a membrane protein belonging to the ABC transporter family functioning as a chloride/anion channel in epithelial cells around the body. There are over 1500 mutations that have been characterised as CF-causing; the most common of these, accounting for ~70 % of CF cases, is the deletion of a phenylalanine at position 508. This leads to instability of the nascent protein and the modified structure is recognised and then degraded by the ER quality control mechanism. However, even pharmacologically ‘rescued’ F508del CFTR displays instability at the cell’s surface, losing its channel function rapidly and it is rapidly removed from the plasma membrane for lysosomal degradation. This review will, therefore, explore the link between stability and structure/function relationships of membrane proteins and CFTR in particular and how approaches to study CFTR structure depend on its stability. We will also review the application of a fluorescence labelling method for the assessment of the thermostability and the tertiary structure of CFTR.
Publisher
Springer International Publishing,Springer Nature B.V
Subject
/ Animals
/ Biomedical and Life Sciences
/ Cystic Fibrosis - metabolism
/ Cystic Fibrosis Transmembrane Conductance Regulator - chemistry
/ Cystic Fibrosis Transmembrane Conductance Regulator - genetics
/ Cystic Fibrosis Transmembrane Conductance Regulator - isolation & purification
/ Cystic Fibrosis Transmembrane Conductance Regulator - metabolism
/ Humans
/ mutation
/ Proteins
