ABCB1 p.Ser671Asn
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No.
Sentence
Comment
96
Mutation of serine 671 to asparagine in the linker region of P-glycoprotein abrogated verapamil and PKC-α-stimulated ATPase activity.
X
ABCB1 p.Ser671Asn 10388000:96:12
status: NEW
PMID: 7915139
[PubMed]
Ahmad S et al: "Modulation of P-glycoprotein by protein kinase C alpha in a baculovirus expression system."
No.
Sentence
Comment
112
To directly determine the dependence of PGP ATPase activity on PKC-mediated phosphorylation, Ser671 was mutated to Asn within a PKC consensus phosphorylation sequence in the linker region of PGP (Figure 6).
X
ABCB1 p.Ser671Asn 7915139:112:93
status: NEW117 Ser671Asn mutant exhibiteda similarlevelof ATPaseactivity as wild-type PGP; however,mutant PGP was resistant to the stimulatoryeffectof PKCa on ATPaseactivity, and exhibited an attenuated response to verapamil compared to wild-type PGP.
X
ABCB1 p.Ser671Asn 7915139:117:0
status: NEW
No.
Sentence
Comment
97
Mutation of serine 671 to asparagine in the linker region of P-glycoprotein abrogated verapamil and PKC-α-stimulated ATPase activity.
X
ABCB1 p.Ser671Asn 8820951:97:12
status: NEW
PMID: 9287320
[PubMed]
Szabo K et al: "Phosphorylation site mutations in the human multidrug transporter modulate its drug-stimulated ATPase activity."
No.
Sentence
Comment
158
Ahmad et al. (40) have also presented evidence that exchanging Ser671 to asparagine reduced ATPase activity by about 50% at 10 M verapamil when expressed in Sf9 cells.
X
ABCB1 p.Ser671Asn 9287320:158:63
status: NEW