Associated Papers
Functional analysis of amino acid substitutions within human AGT1 in a cell-based platform to support the diagnosis of primary hyperoxaluria type 1.
Gatticchi L et al.
The Journal of Biological Chemistry, 2025
Electrostatic interactions drive native-like aggregation of human alanine:glyoxylate aminostransferase.
Dindo M et al.
The Febs Journal, 2017
Effects of alanine:glyoxylate aminotransferase variants and pyridoxine sensitivity on oxalate metabolism in a cell-based cytotoxicity assay.
Fargue S et al.
Biochimica Et Biophysica Acta, 2016
Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele.
Fargue S et al.
The Journal of Biological Chemistry, 2013
The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I.
Mesa-Torres N et al.
Plos One, 2013
Rapid profiling of disease alleles using a tunable reporter of protein misfolding.
Pittman AM et al.
Genetics, 2012
Molecular insights into primary hyperoxaluria type 1 pathogenesis.
Cellini B et al.
Frontiers in Bioscience (landmark Edition), 2012
Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants.
Cellini B et al.
Biochimica Et Biophysica Acta, 2011
In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase.
Hopper ED et al.
The Journal of Biological Chemistry, 2008
The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1.
Coulter-Mackie MB et al.
Molecular Genetics and Metabolism, 0
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