Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations (Q28144619)

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scientific article (publication date: 17 November 2000)

Language	Label	Description	Also known as
English	Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations	scientific article (publication date: 17 November 2000)

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scholarly article

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Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations (English)

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author name string

M J Lumb

1

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C J Danpure

2

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language of work or name

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publication date

17 November 2000

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Journal of Biological Chemistry

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275

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46

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36415-22

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Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I

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Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1

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Immunocytochemical localization of human hepatic alanine: glyoxylate aminotransferase in control subjects and patients with primary hyperoxaluria type 1

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An enzyme trafficking defect in two patients with primary hyperoxaluria type 1: peroxisomal alanine/glyoxylate aminotransferase rerouted to mitochondria

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Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation

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Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1.

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ATP-dependent degradation of a mutant serine: pyruvate/alanine:glyoxylate aminotransferase in a primary hyperoxaluria type 1 case

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Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon

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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 mistargeti

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Further studies on the activity and subcellular distribution of alanine: Glyoxylate aminotransferase in the livers of patients with primary hyperoxaluria type 1

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Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light

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Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene

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A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1

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Pyridoxal 5'-phosphate binding of a recombinant rat serine: pyruvate/alanine:glyoxylate aminotransferase.

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Nucleotide sequence of the cDNA encoding the precursor for mitochondrial serine:pyruvate aminotransferase of rat liver

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Unexpected influence of a C-terminal-fused His-tag on the processing of an enzyme and on the kinetic and folding parameters

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An intronic duplication in the alanine: glyoxylate aminotransferase gene facilitates identification of mutations in compound heterozygote patients with primary hyperoxaluria type 1.

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Molecular characterization and clinical use of a polymorphic tandem repeat in an intron of the human alanine:glyoxylate aminotransferase gene.

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Molecular adaptation of alanine:glyoxylate aminotransferase targeting in primates

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Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular targeting. Analysis of the marmoset and rabbit genes

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Variable peroxisomal and mitochondrial targeting of alanine: glyoxylate aminotransferase in mammalian evolution and disease

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Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism

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Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene

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Peroxisomal localization of alanine: Glyoxylate aminotransferase in human liver

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Subcellular distribution, and physical and immunological properties of hepathic alanine: Glyoxylate aminotransferase isoenzymes in different mammalian species

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Primary hyperoxaluria type 1: diagnostic relevance of mutations and polymorphisms in the alanine:glyoxylate aminotransferase gene (AGXT)

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Primary hyperoxaluria type 1: genotypic and phenotypic heterogeneity

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Effect of N-terminal alpha-helix formation on the dimerization and intracellular targeting of alanine:glyoxylate aminotransferase

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A semiautomated alanine:glyoxylate aminotransferase assay for the tissue diagnosis of primary hyperoxaluria type 1

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Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method

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The organ distribution of human alanine-2-oxoglutarate aminotransferase and alanine-glyoxylate aminotransferase

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A new micro-assay for human liver alanine: glyoxylate aminotransferase

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Flux of the L-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase

1 reference

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Aminooxy acetic acid: a selective inhibitor of alanine:glyoxylate aminotransferase and its use in the diagnosis of primary hyperoxaluria type I

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The cause of idiopathic calcium stone disease: hypercalciuria or hyperoxaluria?

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Identifiers

10.1074/JBC.M006693200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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