ABCC8 p.Leu31Met
Predicted by SNAP2: | A: D (53%), C: N (61%), D: D (75%), E: D (75%), F: N (78%), G: D (71%), H: D (66%), I: N (82%), K: D (75%), M: N (61%), N: D (53%), P: D (80%), Q: D (66%), R: D (75%), S: D (63%), T: D (59%), V: N (87%), W: D (63%), Y: D (66%), |
Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: N, G: D, H: D, I: N, K: D, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, V: N, W: D, Y: D, |
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[hide] Caspase 3 activation is controlled by a sequence l... Biochem Biophys Res Commun. 2004 Mar 26;316(1):93-9. Pelletier M, Cartron PF, Delaval F, Meflah K, Vallette FM, Oliver L
Caspase 3 activation is controlled by a sequence located in the N-terminus of its large subunit.
Biochem Biophys Res Commun. 2004 Mar 26;316(1):93-9., [PMID:15003516]
Abstract [show]
We report that the induction and completion of the apoptotic program is delayed in a doxorubicin-resistant cell line (HL60/ADR). This hindrance to cell death occurred downstream of the multidrug-resistant protein (mrp), a transmembrane transporter. In vitro studies showed that these cells were incapable of correctly activating procaspase 3 (pC3), the main executioner of apoptosis. Sequencing of HL60/ADR pC3 revealed point mutations in a sequence located in the N-terminal region of the large subunit of caspase 3 (C3, amino acids 31-37; i.e., immediately after the propeptide). We called this particular form of C3, the C3 N-terminal modified (C3-NTM), and show that it is partially active when transfected into MCF-7 cells shown to have little or no endogenous pC3. As a deletion of the amino acids 31-37 in wild-type C3 leads to the same phenotype, we conclude that this sequence is involved in C3 activation during apoptosis.
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No. Sentence Comment
62 Oligonucleotides C3/I31M, C3/L31M, C3/ L33W, C3/N35T, and C3/S36G were used with C3 AS to generate the corresponding single acid amino substitution in the wild-type C3 sequence.
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ABCC8 p.Leu31Met 15003516:62:29
status: NEW61 Oligonucleotides C3/I31M, C3/L31M, C3/ L33W, C3/N35T, and C3/S36G were used with C3 AS to generate the corresponding single acid amino substitution in the wild-type C3 sequence.
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ABCC8 p.Leu31Met 15003516:61:29
status: NEW