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文献和实验Manipulating the Folding Pathway of ΔF508 CFTR Using Chemical Chaperones
in patients is the loss of a single phenylalanine residue (at position 508) within a polypeptide of 1480 amino acids (1 ). This seemingly minor alteration results in the newly synthesized CFTR protein being unable to fold properly and traffic to its proper
End Rescue from YACs Using the Vectorette
Phospho-GATCG; Y = C. (B) PCR and sequencing primers for the r(ight) and l(eft) arms of the YAC vector pYAC4 (based on sequence in ref. 3 ).
CFTR Expression and ER-Associated Degradation in Yeast
The most common cause of cystic fibrosis is the deletion of a phenylalanine at position 508 (gDF508) of the cystic fibrosis transmembrane conductance regulator (CFTR). Although the majority of wild-type CFTR is degraded in the endoplasmic
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