ABCC7 p.Met150Val
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PMID: 19910674
[PubMed]
Ramalho AS et al: "Deletion of CFTR translation start site reveals functional isoforms of the protein in CF patients."
No.
Sentence
Comment
126
jointly mutated into valines and the respective stable cells wereanalysedbyimmunoblotforCFTR.ResultsinFig.5A reveal the presence of two proteins (D and E) for single mutants of M82V, M150V, M152V and M156V (lanes 36, respectively) and also for the double mutants M150V/ M152, M150V/M156V and M152V/M156V (lanes 7-9).
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ABCC7 p.Met150Val 19910674:126:183
status: NEWX
ABCC7 p.Met150Val 19910674:126:263
status: NEWX
ABCC7 p.Met150Val 19910674:126:276
status: NEW130 Individual and double mutations of M82V, M150V and M152V (lanes 5-8) did not cause loss of either protein species D or E, consistent with the corresponding constructs in the in vivo assay.
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ABCC7 p.Met150Val 19910674:130:41
status: NEW131 The mutant M82V/M150V/M152V (lane 4) does not alter the production of proteins D and E either.
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ABCC7 p.Met150Val 19910674:131:16
status: NEW140 Lanes 3-10 correspond to the proteins produced by the methionines mutants all in the c.120del23-CFTR pNUT background: lane 3, M82V; lane 4, M150V; lane 5 M152V; lane 6, M156V; lane 7, M150V/M152V; lane 8, M150V/M156V; lane 9, M152V/M156V; lane 10, M150V/M152V/M156V.
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ABCC7 p.Met150Val 19910674:140:140
status: NEWX
ABCC7 p.Met150Val 19910674:140:184
status: NEWX
ABCC7 p.Met150Val 19910674:140:205
status: NEWX
ABCC7 p.Met150Val 19910674:140:248
status: NEW144 Lanes 2-8 all in pSP73: 2, CFTR exons 2-24; 3, M82V/ M150V/M152V/M156V; 4, M82V/M150V/M152V; 5, M82/M152V; 6, M82V/M150V;7, M150; 8, M82V.
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ABCC7 p.Met150Val 19910674:144:53
status: NEWX
ABCC7 p.Met150Val 19910674:144:80
status: NEWX
ABCC7 p.Met150Val 19910674:144:115
status: NEW148 However, when the triple mutant (M150V/M152V/M156V) was analysed (lane 10, Fig.5A), only the lower form (E ~128 kDa) could be detected.
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ABCC7 p.Met150Val 19910674:148:33
status: NEW
No.
Sentence
Comment
54
A119CFTR (the first 118 amino acids were deleted creating the next functional methionine at Met150 ), and MIV-M150V (both methionines at positions 1and 150 were Table I. Single Channel Characteristics of CFTR Channelsin Oocytes PS WT R117H 9.3 ±0.4(4) 6.5 ±0.5(4)* Po 0.65 ±0.02(7) 0.49±0.01(7)* Selectivity Br > Cl > I(4:3) Br > Cl > 1(5:4) * Denotes significantly different from wild type (WT).
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ABCC7 p.Met150Val 9511929:54:110
status: NEW70 Generation of Cl- currents by the double mutant (MIV-M150V) suggests that methionines beyond amino acid 150may also be able to initiate translation initiation of CFTR.
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ABCC7 p.Met150Val 9511929:70:53
status: NEW