Article
A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator.
Journal of the American Chemical Society - 21 Dec 2011
Cho Hyungseoph J, Gee Heon Yung, Baek Kyung-Hwa, Ko Sung-Kyun, Park Jong-Moon, Lee Hookeun, Kim Nam-Doo, Lee Min Goo, Shin Injae
Abstract excerpt
Cystic fibrosis transmembrane conductance regulator (CFTR) is a cell-surface anion channel that permeates chloride and bicarbonate ions. The most frequent mutation of CFTR that causes cystic fibrosis is the deletion of phenylalanine at position 508 (ΔF508), which leads to defects in protein folding and cellular trafficking to the plasma membrane. The lack of the cell-surface CFTR results in a reduction in the...
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