ABCB4 p.Gln1118Ala
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 16487063
[PubMed]
Qian F et al: "Molecular model and ATPase activity of carboxyl-terminal nucleotide binding domain from human P-glycoprotein."
No.
Sentence
Comment
174
a) ATP dependence of the ATPase activities of the isolated NBD2 (1) and its mutant Q1118A (2).
X
ABCB4 p.Gln1118Ala 16487063:174:83
status: NEW176 b) Lineweaver-Burk plot of dependence of ATPase activity of NBD2 (1) and its mutant Q1118A (2).
X
ABCB4 p.Gln1118Ala 16487063:176:84
status: NEW
PMID: 25987565
[PubMed]
Loo TW et al: "The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein."
No.
Sentence
Comment
248
A study of Q loop mutations Q475A(NBD1) and Q1118A- (NBD2) suggested that the P-gp transport mechanism shows redundancy (47).
X
ABCB4 p.Gln1118Ala 25987565:248:44
status: NEW249 It was found that the single Q475A or Q1118A mutants retained transport activity and 35-50% of wild-type ATPase activity but the double Q475A/Q1118A mutant was inactive.
X
ABCB4 p.Gln1118Ala 25987565:249:38
status: NEWX
ABCB4 p.Gln1118Ala 25987565:249:142
status: NEW254 A Q475A/Q1118A control P-gp however, showed little detectable ATPase activity.
X
ABCB4 p.Gln1118Ala 25987565:254:8
status: NEW