ABCD1 p.Asn13Thr
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PMID: 16949688
[PubMed]
Berger J et al: "X-linked adrenoleukodystrophy: clinical, biochemical and pathogenetic aspects."
No.
Sentence
Comment
72
Interestingly, in one X-ALD patient two single base pair substitutions in exon 1 have been observed, both causing amino acid exchanges (N13T and K217E).
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ABCD1 p.Asn13Thr 16949688:72:136
status: NEW74 The N13T amino acid exchange, on the other hand, did not affect ALDP function, which is in agreement with the hypothesis that there is a reduced functional importance of the first 66 N-terminal amino acids of ALDP.
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ABCD1 p.Asn13Thr 16949688:74:4
status: NEW
PMID: 11438993
[PubMed]
Dvorakova L et al: "Eight novel ABCD1 gene mutations and three polymorphisms in patients with X-linked adrenoleukodystrophy: The first polymorphism causing an amino acid exchange."
No.
Sentence
Comment
5
In the 11th family we detected two novel single-base pair substitutions in exon 1 (c.38 A>C and c.649 A>G), both causing amino acid exchanges (N13T and K217E).
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ABCD1 p.Asn13Thr 11438993:5:143
status: NEW7 The N13T amino acid exchange, on the other hand, did not affect ALDP function.
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ABCD1 p.Asn13Thr 11438993:7:4
status: NEW8 Thus, N13T represents the first polymorphism causing an amino acid exchange in the ABCD1 gene.
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ABCD1 p.Asn13Thr 11438993:8:6
status: NEW80 The two plasmids, one carrying human ABCD1 cDNA with point mutation c.38A>C (resulting in amino acid exchange N13T) and another carrying point mutation c.649A>G (amino acid exchange K217E), were used for transfection experiments, together with the non-mutated human ABCD1 plasmid as a control.
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ABCD1 p.Asn13Thr 11438993:80:110
status: NEW98 In patients 7a and 7b (Table 1) we identified two different one-base substitutions in exon 1 (c.38A>C and c.649A>G), both of them causing an amino acid exchange (N13T and K217E).
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ABCD1 p.Asn13Thr 11438993:98:162
status: NEW105 In contrast, the second nucleotide exchange, c.38A>C (N13T), exhibits wild type ALDP function.
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ABCD1 p.Asn13Thr 11438993:105:54
status: NEW107 We conclude that N13T represents a polymorphism, but not a disease-causing mutation.
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ABCD1 p.Asn13Thr 11438993:107:17
status: NEW121 The β-oxidation of lignoceric acid versus palmitic acid (C24:C16) in X-ALD fibroblasts after transfection with normal (wt) and two mutatedABCD1 cDNA constructs (nucleotide exchanges c.38A>C and c.649A>G, leading to amino acid exchanges N13T and K217E, respectively).
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ABCD1 p.Asn13Thr 11438993:121:242
status: NEW126 Polymorphisms in the ABCD1 Gene Nucleotide Restriction Allele Exon changea Frequency site 5'UTR 1 -59C/T 0.073 (11/150)b +BsmAI N13T 1 38A/C Unique +BsmFI L515L 6 1548G/A 0.85 vs 0.15c F673F 10 2019C/T 0.013 (2/150)b +TaqI 3'UTR 10 2246C/G 0.76 vs 0.24c a Novel variants in boldface type.
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ABCD1 p.Asn13Thr 11438993:126:128
status: NEW153 The other novel polymorphism, N13T, is the first polymorphism in the ABCD1 gene ever found to exchange an amino acid.
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ABCD1 p.Asn13Thr 11438993:153:30
status: NEW
PMID: 22483867
[PubMed]
Kemp S et al: "X-linked adrenoleukodystrophy: clinical, metabolic, genetic and pathophysiological aspects."
No.
Sentence
Comment
234
The mutation p.Asn13Thr, for example, has been shown to represent a polymorphism, as this mutation did not affect the ability to compensate for the lack of functional ALDP after transfection [65].
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ABCD1 p.Asn13Thr 22483867:234:15
status: NEW