Associated Papers
A scalable approach to resolving variants of uncertain significance.
Tejura M et al.
Biorxiv : the Preprint Server for Biology, 2026
Global genetic prevalence estimates of primary hyperoxaluria are greater than previously reported.
Mandrile G et al.
Clinical Kidney Journal, 2025
Two Novel AGXT Mutations Cause the Infantile Form of Primary Hyperoxaluria Type I in a Chinese Family: Research on Missed Mutation.
Lu X et al.
Frontiers in Pharmacology, 2019
A Putative Mutation Hotspot of the AGXT Gene Associated with Primary Hyperoxaluria Type 1 in the Chinese Population.
Li X et al.
The Tohoku Journal of Experimental Medicine, 2018
Updated Genetic Testing of Primary Hyperoxaluria Type 1 in a Chinese Population: Results from a Single Center Study and a Systematic Review.
Du DF et al.
Current Medical Science, 2018
Folding Defects Leading to Primary Hyperoxaluria.
Oppici E et al.
Handbook of Experimental Pharmacology, 2018
Sources of discordance among germ-line variant classifications in ClinVar.
Yang S et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2017
Mutational analysis of AGXT in two Chinese families with primary hyperoxaluria type 1.
Li GM et al.
Bmc Nephrology, 2014
Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.
Pey AL et al.
Biomed Research International, 2013
Rapid profiling of disease alleles using a tunable reporter of protein misfolding.
Pittman AM et al.
Genetics, 2012
Primary hyperoxalurias: disorders of glyoxylate detoxification.
Salido E et al.
Biochimica Et Biophysica Acta, 2012
A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution.
Kawai C et al.
Acta Histochemica Et Cytochemica, 2012
Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases.
Ryu GM et al.
Nucleic Acids Research, 2009
Partial trypsin digestion as an indicator of mis-folding of mutant alanine:glyoxylate aminotransferase and chaperone effects of specific ligands. Study of a spectrum of missense mutants.
Coulter-Mackie MB et al.
Molecular Genetics and Metabolism, 2008
Comprehensive mutation screening in 55 probands with type 1 primary hyperoxaluria shows feasibility of a gene-based diagnosis.
Monico CG et al.
Journal of the American Society of Nephrology : Jasn, 2007
Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations.
Coulter-Mackie MB et al.
Molecular Genetics and Metabolism, 2006
The molecular basis of kidney stones.
Langman CB
Current Opinion in Pediatrics, 2004
Molecular aetiology of primary hyperoxaluria and its implications for clinical management.
Danpure CJ et al.
Expert Reviews in Molecular Medicine, 2004
Molecular aetiology of primary hyperoxaluria type 1.
Danpure CJ
Nephron. Experimental Nephrology, 2004
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1.
Zhang X et al.
Journal of Molecular Biology, 2003
Preliminary evidence for ethnic differences in primary hyperoxaluria type 1 genotype.
Coulter-Mackie MB
American Journal of Nephrology, 0