ABCC7 p.Gly91Cys
[switch to full view]Comments [show]
None has been submitted yet.
No.
Sentence
Comment
475
In three TM1 mutants, G91C, K95C, Q98C, all of which fall on the same face of a predicted TM1 a- ter`` is close to the cytoplasmic end of the pore and that R352 may play a role in determining charge selectivity forhelix, the conductance was irreversibly altered by either MTSES0 or MTSEA0 .
X
ABCC7 p.Gly91Cys 9922376:475:22
status: NEW
PMID: 9512029
[PubMed]
Mansoura MK et al: "Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the pore."
No.
Sentence
Comment
270
In fact, the data presented by Akabas et al. (1994) suggest that the activation of the G91C mutant was markedly slowed compared with that of wtCFTR.
X
ABCC7 p.Gly91Cys 9512029:270:87
status: NEW
PMID: 7515047
[PubMed]
Akabas MH et al: "Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator."
No.
Sentence
Comment
69
Application of the MTS reagents irreversibly alteredthe CFTR-induced currents of three of the cysteine substitution mutants, G91C, K95C, and Q98C.
X
ABCC7 p.Gly91Cys 7515047:69:125
status: NEW71 2B and 3A).Application of MTSEA`for 1min irreversibly inhibited the mutants G91C by 43 * 6% (n = 5) (Figs.
X
ABCC7 p.Gly91Cys 7515047:71:76
status: NEW75 The anionic reagent, MTSES-, had no effect on the K95C and G91C mutants (Fig. 3,A andB).To determine whether thelack of effect was due to inability to react with Cys-95 or lack of effect followingreaction, we sequentially applied MTSES- and MTSEA+;MTSES- did not prevent the potentiationof the current by MTSEA+(data notshown).
X
ABCC7 p.Gly91Cys 7515047:75:59
status: NEW86 A and C are from oocytesinjectedwith wild type CFTR B, Q98C; D,K95C; E, G91C.
X
ABCC7 p.Gly91Cys 7515047:86:72
status: NEW110 Based on the accessibility of the cysteine-substitution mutants G91C,K95C and Q98C to the MTS reagents, we infer that the side chains of the corresponding wild type residues, Gly-91,Lys-95, and Gln-98, line the channel ofCFTR.
X
ABCC7 p.Gly91Cys 7515047:110:64
status: NEW122 Although the Arg side chain is somewhat larger than theside chain of Cys modified by MTSEA', the reduction in whole cell current we observed following modification of G91C by MTSEA' suggests that the G91R mutant will have altered single-channel properties.
X
ABCC7 p.Gly91Cys 7515047:122:167
status: NEW