Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with Primary Hyperoxaluria Type I()

Ítems similars

• Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I
  per: Cellini, Barbara, et al.
  Publicat: (2010)
• Molecular Insight into the Synergism between the Minor Allele of Human Liver Peroxisomal Alanine:Glyoxylate Aminotransferase and the F152I Mutation
  per: Cellini, Barbara, et al.
  Publicat: (2009)
• Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis
  per: Giardina, Giorgio, et al.
  Publicat: (2017)
• Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications
  per: Cellini, Barbara, et al.
  Publicat: (2007)
• Oligomeric State and Thermal Stability of Apo- and Holo- Human Ornithine δ-Aminotransferase
  per: Montioli, Riccardo, et al.
  Publicat: (2017)