PMID: 7680027

Thomas PJ, Pedersen PL
Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR.
J Bioenerg Biomembr. 1993 Feb;25(1):11-9., [PubMed]
Sentences
No. Mutations Sentence Comment
76 ABCC7 p.Phe508Cys
X
ABCC7 p.Phe508Cys 7680027:76:56
status: NEW
view ABCC7 p.Phe508Cys details
 This proposal is supported by genetic evidence that the F508C mutation is benign (Kobayashi et al., 1990) and that the AI506/7 mutation causes CF (Kerem et al., 1990). Login to comment 107 ABCC7 p.Gly1244Glu
X
ABCC7 p.Gly1244Glu 7680027:107:50
status: NEW
view ABCC7 p.Gly1244Glu details
ABCC7 p.Arg560Thr
X
ABCC7 p.Arg560Thr 7680027:107:185
status: NEW
view ABCC7 p.Arg560Thr details
ABCC7 p.Gly458Val
X
ABCC7 p.Gly458Val 7680027:107:17
status: NEW
view ABCC7 p.Gly458Val details
 For example, the G458V (Cuppens et al., 1990) and G1244E (Devoto et al., 1991) mutations which change the first glycine residue in the Gx 4GKT sequence of the A homology region and the R560T (Kerem et al., 1990) mutation in the Rx6.sh4D sequence of the B homology region are known to cause CF. Login to comment