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PMID: 12023875
Gribble FM, Reimann F
Pharmacological modulation of K(ATP) channels.
Biochem Soc Trans. 2002 Apr;30(2):333-9.,
[PubMed]
Sentences
No.
Mutations
Sentence
Comment
94
ABCC8 p.Ser1237Tyr
X
ABCC8 p.Ser1237Tyr 12023875:94:185
status:
NEW
view ABCC8 p.Ser1237Tyr details
However, the high-affinity blocking of Kir6.2/SURl channels by nateglinide and mitiglinide, which both show homology with meglitinide, has recently been reported to be abolished by the
S1237Y
mutation in SURl (see below), rather unexpectedly suggesting that their binding site overlaps with that of the sulphonylureas [37,38].
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95
ABCC8 p.Ser1237Tyr
X
ABCC8 p.Ser1237Tyr 12023875:95:185
status:
NEW
view ABCC8 p.Ser1237Tyr details
However, the high-affinity blocking of Kir6.2/SURl channels by nateglinide and mitiglinide, which both show homology with meglitinide, has recently been reported to be abolished by the
S1237Y
mutation in SURl (see below), rather unexpectedly suggesting that their binding site overlaps with that of the sulphonylureas [37,38].
Login to comment