ABCC7 p.Gln552Ala
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PMID: 12508051
[PubMed]
Vergani P et al: "On the mechanism of MgATP-dependent gating of CFTR Cl- channels."
No.
Sentence
Comment
34
Thus, the K1250A mutation dramatically prolonged burst duration, suggesting that hydrolysis at NBD2 might be coupled to burst termination (Carson et al., 1995; Gunderson and Kopito, 1995), whereas the NBD1 mutations K464A, Q552A, and Q552H somewhat slowed channel opening to a burst, suggesting that NBD1 might be a site of ATP interactions governing opening (Carson et al., 1995; Carson and Welsh 1995).
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ABCC7 p.Gln552Ala 12508051:34:223
status: NEW
No.
Sentence
Comment
375
This is consistent with the finding that in the absence predicted to decrease the rate of hydrolysis at NBD1, for example, K464A and Q552A, would thus increase the in-of ATP, the channel does not open.
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ABCC7 p.Gln552Ala 9922375:375:133
status: NEW
PMID: 8599650
[PubMed]
Carson MR et al: "Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins."
No.
Sentence
Comment
27
To test these hypotheses we used the excised inside-out patch-clamp technique to study CFTR variants containing the Q552A, Q552H, H1350Q, and H1350A mutations.
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ABCC7 p.Gln552Ala 8599650:27:116
status: NEW72 That is, Q552A and Q552H decreased the rate at A. I I 40 80 120 V (mV) I (pA) 0.50- P0 FIGURE 2 Effect of Q552 and H1350 mutations on CFTR Cl- chan- nels.
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ABCC7 p.Gln552Ala 8599650:72:9
status: NEW77 Open circles, wild-type; open triangles, Q552A; open squares, Q552H; filled circles, H1350A; filled triangles, H1350Q.
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ABCC7 p.Gln552Ala 8599650:77:41
status: NEW90 Fig. 2 A shows 0.250- B. 2000- mean closed-time between 1000- bursts (ms) 0- C. mean burst duration (ms) wild-type T T k" IffilI -.. wild- Q552A 0552H H1350Q H1350A type 3001 wilt'- type FIGURE 3 Effect of mutation of Q552 and H1350 on single channel activity.
X
ABCC7 p.Gln552Ala 8599650:90:139
status: NEW