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PMID: 9724814
Naren AP, Quick MW, Collawn JF, Nelson DJ, Kirk KL
Syntaxin 1A inhibits CFTR chloride channels by means of domain-specific protein-protein interactions.
Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10972-7., 1998-09-01
[PubMed]
Sentences
No.
Mutations
Sentence
Comment
136
ABCC7 p.Gly551Asp
X
ABCC7 p.Gly551Asp 9724814:136:324
status:
NEW
view ABCC7 p.Gly551Asp details
ABCC7 p.Arg117His
X
ABCC7 p.Arg117His 9724814:136:442
status:
NEW
view ABCC7 p.Arg117His details
Those CFTR mutants that produce full-length translation products can be classified into three categories (2): (i) ER processing mutants that inefficiently traffic to the Golgi apparatus (e.g., the most common allele, ⌬F508); (ii) regulation mutants that mature normally but are refractory to activation by ATP (e.g.,
G551D
); and (iii) conduction mutants that also mature normally but exhibit reduced single-channel conductances (e.g.,
R117H
).
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178
ABCC7 p.Gly551Asp
X
ABCC7 p.Gly551Asp 9724814:178:160
status:
NEW
view ABCC7 p.Gly551Asp details
The efficiency of binding of band B (i.e., binding normalized to the IP signal) at 0.13 M syn1A⌬C was 38.4%, 36.1%, and 5.7% for wild-type CFTR,
G551D
CFTR, and ⌬F508 CFTR, respectively.
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