Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference19 articles.
1. Crystal Structure of Alanine:Glyoxylate Aminotransferase and the Relationship Between Genotype and Enzymatic Phenotype in Primary Hyperoxaluria Type 1
2. Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications
3. Mammalian alanine/glyoxylate aminotransferase 1 is imported into peroxisomes via the PTS1 translocation pathway. Increased degeneracy and context specificity of the mammalian PTS1 motif and implications for the peroxisome-to-mitochondrion mistargeting of AGT in primary hyperoxaluria type 1.
4. Molecular Etiology of Primary Hyperoxaluria Type 1: New Directions for Treatment
5. Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.
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1. A molecular journey on the pathogenesis of primary hyperoxaluria;Current Opinion in Nephrology & Hypertension;2024-04-11
2. Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants;FEBS Letters;2024-01-19
3. Enzymatic reactions towards aldehydes: An overview;Flavour and Fragrance Journal;2023-04-10
4. Phosphorylation of Thr9 Affects the Folding Landscape of the N-Terminal Segment of Human AGT Enhancing Protein Aggregation of Disease-Causing Mutants;Molecules;2022-12-10
5. Identification of Human Alanine–Glyoxylate Aminotransferase Ligands as Pharmacological Chaperones for Variants Associated with Primary Hyperoxaluria Type 1;Journal of Medicinal Chemistry;2022-07-13
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