Sickly channels in mild disease

Article Abstract:

Cystic fibrosis is caused by a defective epithelial Cl- channel, the cystic fibrosis transmembrane regulator (CFTR). The most common mutation on the CFTR gene involves deletion of F508 in one of the two nucleotide-binding domains. Three less common mutations that lead to mild forms of the disease have also been studied. These involve missense mutations each altering a different arginine residue. However, it was found that the clinically severest mutant CFTR gene is much more prevalent than the less harmful variants. It is speculated that a deficiency in epithelial fluid secretion would ameliorate the severity of dehydration due to enterotoxin-slicited diarrhea.

Author: Miller, Christopher
Cystic fibrosis, Mutagenesis, Chloride channels

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Cuddling up to channel activation

Article Abstract:

An innovative technique allows researchers to analyse the functions of an allosteric membrane protein and the behaviour of a single cyclic nucleotide-gated ion channel. The experiment also shows the effects of ligands locked onto the channel's four identical cGMP-binding sites. Results of the study are discussed.

Author: Miller, Christopher
Ligand binding (Biochemistry), Allosteric proteins, Nucleotides

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Shake, rattle or roll?

Article Abstract:

A remarkable property of the voltage sensor that sharpens one's view of its transmembrane movement is described. The controversy regarding the movement of the voltage sensor is also discussed.

Author: Miller, Christopher, Blaustein, Robert O.
United States, Science & research, Nervous system, Membrane proteins

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Subjects list: Research
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