ABCMdb

ABCC7 p.Asp572Ala

None has been submitted yet.

Publications

PMID: 12458151 [PubMed] Powell K et al: "Therapeutic approaches to repair defects in deltaF508 CFTR folding and cellular targeting."

No. Sentence Comment

119 By studying Among the best-studied molecular chaperones are other CFTR mutations (D572A and S1251A), it was the 70-kDa heat shock proteins, including Hsp70 shown that these mutations were not sensitive to [40] and Hsc70. Login to comment

PMID: 8557666 [PubMed] Sato S et al: "Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation."

No. Sentence Comment

91 Cells expressing the missense mutants D572A and S1251A and a mutant harboring a deletion of exon 13 (⌬EX13) were pulse-labeled with [35 S]Met and chased for 5 h in the presence or absence of glycerol (Fig. 3A). Login to comment
93 Thus, some mutations in all three major cytoplasmic domains of CFTR, including the first and second nucleotide binding domains (D572A and S1251A, respectively) as well as the "R" domain, can lead to a glycerol-insensitive ER retention phenotype, suggesting that glycerol treatment does not induce a general suppression of ER retention mechanisms. Login to comment
95 Processing of mutants K464R and K464A was inefficient by comparison with wild type and was enhanced by incubation in the presence of 10% glycerol, even after accounting for the unequal label present in the immature precursor in the presence of glycerol (Fig. 3B). Login to comment
108 HEK cells expressing D572A, ⌬EX13, and S1251 (A) or various substitutions at Lys464 (B) were pulse-labeled (p) for 15 min and chased for 5 h (c) in the presence or the absence of glycerol. Login to comment
110 HEK cells expressing D572A, DEX13, and S1251 (A) or various substitutions at Lys464 (B) were pulse-labeled (p) for 15 min and chased for 5 h (c) in the presence or the absence of glycerol. Login to comment