ABCC8 p.Asp853Asn
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No.
Sentence
Comment
61
Mutations within the Walker A (K719A and K1385M) or Walker B (D853N, D1506A and D1506N) motifs of both NBFs of SUR1 abolished the activation of KATP channels by MgADP [43-45].
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ABCC8 p.Asp853Asn 15910875:61:62
status: NEW
PMID: 9618560
[PubMed]
Gribble FM et al: "MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit."
No.
Sentence
Comment
7
Both of these effects were abolished when mutations were made in the NBDs of SUR1 that are predicted to abolish MgATP binding and/or hydrolysis (D853N, D1505N, K719A, or K1384M).
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ABCC8 p.Asp853Asn 9618560:7:145
status: NEW106 We therefore explored the effects of mutation of the WB aspartate to asparagine in either the first (D853N) or the second (D1505N) NBD on the sensitivity of the channel to inhibition by ATP.
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ABCC8 p.Asp853Asn 9618560:106:101
status: NEW107 Giant patches excised from oocytes coinjected with mRNAs encoding Kir6.2 and either D853N-SUR1 or D1505N-SUR1 developed large Kϩ currents, which were of comparable amplitude to those observed for wild-type channels, after patch excision.
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ABCC8 p.Asp853Asn 9618560:107:84
status: NEW108 The mean macroscopic conductance was 95 Ϯ 24 nS (n ϭ 5) for D853N-SUR1 channels, 48 Ϯ 16 nS (n ϭ 8) for D1505N-SUR1 channels, and 49 Ϯ 6 nS (n ϭ 18) for wild-type channels.
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ABCC8 p.Asp853Asn 9618560:108:72
status: NEW110 Fig. 2 compares the relationship between ATP concentration and channel inhibition for wild-type, D853N-SUR1, and D1505N-SUR1 currents.
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ABCC8 p.Asp853Asn 9618560:110:97
status: NEW112 The Ki for ATP inhibition of D853N-SUR1 currents was 13.4 Ϯ 0.2 M (n ϭ 4), and that of D1505N-SUR1 was 16.0 Ϯ 2.6 M (n ϭ 5), compared with 28 M for wild-type currents (P ϭ 0.05 by ANOVA).
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ABCC8 p.Asp853Asn 9618560:112:29
status: NEW134 Mean ATP dose-response relationships for Kir6.2͞SUR1 (f, n ϭ 15), Kir6.2͞SUR1-D853N (⅜, n ϭ 4) or Kir6.2͞SUR1-D1505N (F, n ϭ 5) currents, measured in the presence of Mg2ϩ.
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ABCC8 p.Asp853Asn 9618560:134:96
status: NEW
PMID: 9350615
[PubMed]
Gribble FM et al: "The interaction of nucleotides with the tolbutamide block of cloned ATP-sensitive K+ channel currents expressed in Xenopus oocytes: a reinterpretation."
No.
Sentence
Comment
127
Mutation of the WB aspartate residues in either NBD1 (D853N) or NBD2 (D1505N) of SURI abolished the stimulatory effects of MgADP on KATP currents (Fig. 4) and prevented the MgADP-dependent enhancement of tolbutamide block (Fig. 3).
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ABCC8 p.Asp853Asn 9350615:127:54
status: NEW