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- Cameron, AD, et al.
(författare)
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Crystal structure of human glyoxalase .1. Evidence for gene duplication and 3D domain swapping
- 1997
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Ingår i: EMBO JOURNAL. - : OXFORD UNIV PRESS. - 0261-4189. ; 16:12, s. 3386-3395
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and r
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- Dahl, Niklas, et al.
(författare)
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Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction
- 1997
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Ingår i: Human Molecular Genetics. - : Oxford University Press (OUP). - 0964-6906 .- 1460-2083. ; 6:7, s. 1147-1152
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Tidskriftsartikel (refereegranskat)abstract
- Severe glutathione synthetase (GS) deficiency is a rare genetic disorder with neonatal onset. The enzymatic block of the gamma-glutamyl cycle leads to a generalized glutathione deficiency. Clinically affected patients present with severe metabolic acidosis, 5-oxoprolinuria, increased rate of hemolysis and defective function of the central nervous system. The disorder is inherited in an autosomal recessive mode and, until recently, the molecular basis has remained unknown. We have sequenced 18 GS alleles associated with enzyme deficiency and we detected missense mutations by direct sequencing of cDNAs and genomic DNA. In total, 13 different mutations were identified. Four patients were found to be compound heterozygotes and two individuals were apparently homozygous. Reduced enzymatic activities were demonstrated in recombinant protein expressed from cDNAs in four cases with different missense mutations. The results from biochemical analysis of patient specimens, supported by the properties of the expressed mutant proteins, indicate that a residual activity is present in affected individuals. Our results suggest that complete loss of function of both GS alleles is probably lethal. It is postulated that missense mutations will account for the phenotype in the majority of patients with severe GS deficiency.
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- Dragani, B, et al.
(författare)
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Role of conserved local motifs in folding and stability of hGSTP1-1
- 2001
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Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 17-18
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Tidskriftsartikel (refereegranskat)abstract
- We investigated, by site directed mutagenesis, the role played by a conserved N-capping box and hydrophobic staple motif in the folding and stability of human GSTPl-1. The corresponding mutants, I149A, S150A, D153A and Y154A, in which these motifs have be
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