ABCC7 p.His1350Gln
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PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
212
Q552H (NBD1) slowed CFTR channel opening without affecting closing, whereas the converse mutation, H1350Q (NBD2) accelerated channel closing without influencing the channel opening rate [68].
X
ABCC7 p.His1350Gln 16442101:212:99
status: NEW
No.
Sentence
Comment
382
In addition, the observation that the H1350Q mutation, which would be predicted to increase the ratechannel.
X
ABCC7 p.His1350Gln 9922375:382:38
status: NEW
PMID: 9922377
[PubMed]
Gadsby DC et al: "Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis."
No.
Sentence
Comment
466
opening without affecting closing, whereas making the converse mutation, H1350Q, in NBD2 accelerated channel closing without influencing the channel opening rate (27).2.
X
ABCC7 p.His1350Gln 9922377:466:73
status: NEW
No.
Sentence
Comment
323
Mutation of this residue to glutamine (H1350Q; predicted to increase ATP hydrolysis rate) but not to alanine (H1350A; predicted to have no effect on hydrolysis) destabilized the open state (138), again supporting a role for hydrolysis at NBD2 in controlling the duration of the open state.
X
ABCC7 p.His1350Gln 9558482:323:39
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.His1350Gln 8599650:27:130
status: NEW77 Open circles, wild-type; open triangles, Q552A; open squares, Q552H; filled circles, H1350A; filled triangles, H1350Q.
X
ABCC7 p.His1350Gln 8599650:77:111
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.His1350Gln 8599650:90:151
status: NEW124 A, Time course of macroscopic current in excised membrane patches from cells expressing either H1350A (top panel) or H1350Q (bottom panel) channels.
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ABCC7 p.His1350Gln 8599650:124:117
status: NEW129 There was no difference between groups (p > 0.3 for all, n = 4, 3, and 3 for wild-type, H1350A, and H1350Q, respectively).
X
ABCC7 p.His1350Gln 8599650:129:100
status: NEW130 301 ATP 1 ADP (pA) 1 D0 N 0 1.5 3.0 4.5 6.0 7.5 time (min) H1350Q 1 ATP 4; A 1 ADP 30- A.
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ABCC7 p.His1350Gln 8599650:130:59
status: NEW131 'Wo I (pA) 150 0 1.5 3.0 4.5 6.0 7.5 time (min) 75- 50- % Inhibition by ADP 250- wild- H1350A H1350Q type Carson and Welsh Similarity between CFTR and GTP-Binding Proteins 2447 from the nucleotide-binding site.
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ABCC7 p.His1350Gln 8599650:131:94
status: NEW146 First, NBD2 mutations at K1250 that are predicted to inhibit hydrolysis prolong the duration of bursts (in contrast to the H1350Q mutation, which shortens bursts) (Carson et al., 1995).
X
ABCC7 p.His1350Gln 8599650:146:123
status: NEW