Molecular modelling of human red blood cell pyruvate kinase: structural implications of a novel G1091 to a mutation causing severe nonspherocytic hemolytic anemia.

@article{Solinge1997MolecularMO,
  title={Molecular modelling of human red blood cell pyruvate kinase: structural implications of a novel G1091 to a mutation causing severe nonspherocytic hemolytic anemia.},
  author={Wouter W van Solinge and Rob J. Kraaijenhagen and Gert Rijksen and Richard van Wijk and B B Stoffer and Michael Gajhede and Finn Cilius Nielsen},
  journal={Blood},
  year={1997},
  volume={90 12},
  pages={4987-95}
}
We present a novel G1091 to A mutation in the human liver and red blood cell (RBC) pyruvate kinase (PK) gene causing severe hemolytic anemia. In two families, three children were severely PK-deficient compound heterozygotes exhibiting the G1091 to A mutation and a common G1529 to A mutation on the other allele. In one family, the mother, a G1091 to A heterozygote, later had a second baby with a new husband, also a G1091 to A carrier. The baby was homozygous for the G1091 to A mutation and died… CONTINUE READING

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We present a novel G1091 to A mutation in the human liver and red blood cell ( RBC ) pyruvate kinase ( PK ) gene causing severe hemolytic anemia .
Molecular modelling of human red blood cell pyruvate kinase : structural implications of a novel G1091 to a mutation causing severe nonspherocytic hemolytic anemia .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
ArginineNo subtypeGlycine
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
GlycineNo subtypeArginine
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The baby was homozygous for the G1091 to A mutation and died 6 weeks after birth from severe hemolysis .
The baby was homozygous for the G1091 to A mutation and died 6 weeks after birth from severe hemolysis .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
The G1091 to A mutation results in the substitution of a conserved glycine by an aspartate in domain A of RBC PK , whereas the G1529 to A mutation leads to the substitution of a conserved arginine residue with glutamine in the C - domain .
In this way the Gly364 to Asp and Arg510 to Gln substitutions may cause PK deficiency by influencing the allosteric properties of the enzyme .
In this way the Gly364 to Asp and Arg510 to Gln substitutions may cause PK deficiency by influencing the allosteric properties of the enzyme .
We present a novel G1091 to A mutation in the human liver and red blood cell ( RBC ) pyruvate kinase ( PK ) gene causing severe hemolytic anemia .
Molecular modelling of human red blood cell pyruvate kinase : structural implications of a novel G1091 to a mutation causing severe nonspherocytic hemolytic anemia .
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