ABCC7 p.Val317Gln
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PMID: 11741825
[PubMed]
Zhang ZR et al: "Voltage-sensitive gating induced by a mutation in the fifth transmembrane domain of CFTR."
No.
Sentence
Comment
29
cRNA was prepared from a construct carrying the full coding region of CFTR in the pALTER vector (Promega, Madison, WI) for WT CFTR or in pBluescript (Stratagene, La Jolla, CA) for V317E and V317Q CFTR.
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ABCC7 p.Val317Gln 11741825:29:190
status: NEW124 To clarify the mechanism leading to reduced g, we studied V317Q.
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ABCC7 p.Val317Gln 11741825:124:58
status: NEW126 The i-V relationship of V317Q CFTR was found to have slight voltage dependence, with g ϭ 7.28 Ϯ 0.16 pS at negative potentials and g ϭ 5.91 Ϯ 0.06 pS at positive potentials (n ϭ 5 patches; Fig. 2, E and F).
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ABCC7 p.Val317Gln 11741825:126:24
status: NEW127 i for V317Q CFTR was 0.59 Ϯ 0.01 pA at ϩ100 mV and 0.73 Ϯ 0.01 pA at -100 mV (P Ͻ 0.001).
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ABCC7 p.Val317Gln 11741825:127:6
status: NEW146 Unitary current (i)-V relationships for WT, V317E, and V317Q CFTR.
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ABCC7 p.Val317Gln 11741825:146:55
status: NEW153 E: closed-to-open transition of V317Q CFTR at ϩ80 (top) and -80 (bottom) mV.
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ABCC7 p.Val317Gln 11741825:153:32
status: NEW155 F: i-V relationship for V317Q CFTR was fitted with 2 linear functions yielding g ϭ 7.28 Ϯ 0.16 pS at Vm ϭ -100 to 0 mV and g ϭ 5.91 Ϯ 0.06 pS at Vm ϭ 0 to ϩ100 mV (n ϭ 5 patches).
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ABCC7 p.Val317Gln 11741825:155:24
status: NEW171 The behavior of V317Q CFTR channels was also examined at multiple potentials.
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ABCC7 p.Val317Gln 11741825:171:16
status: NEW217 Time-averaged I-V relationships for WT, V317E, and V317Q CFTR.
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ABCC7 p.Val317Gln 11741825:217:51
status: NEW222 E: mean I-V relationship for V317Q CFTR is linear.
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ABCC7 p.Val317Gln 11741825:222:29
status: NEW223 F: typical V317Q CFTR currents at positive and negative potentials.
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ABCC7 p.Val317Gln 11741825:223:11
status: NEW254 The kinetic behavior of V317Q-CFTR Fig. 6.
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ABCC7 p.Val317Gln 11741825:254:24
status: NEW290 Relative NPo was fairly constant over the tested voltage range (-100 to ϩ100 mV) for WT and V317Q CFTR, whereas relative NPo for V317E CFTR displayed a marked voltage dependence.
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ABCC7 p.Val317Gln 11741825:290:98
status: NEW317 Introduction of a similarly sized but uncharged amino acid side chain at this position (V317Q CFTR) did not affect gating, indicating that it is the charge, not the bulkiness of the side chain, that confers the voltage-dependent behavior.
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ABCC7 p.Val317Gln 11741825:317:88
status: NEW319 The small change in single-channel conductance was found for both V317E and V317Q-CFTR, indicating that it does not result from electrostatic repulsion due to introduction of the negative charge.
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ABCC7 p.Val317Gln 11741825:319:76
status: NEW