(Q46617816)

English

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.

scientific article published on 29 April 2008

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6 January 2020

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 (English)

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6 January 2020

molecular chaperones

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Marion Coulter-Mackie

1

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author name string

Q Lian

2

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29 April 2008

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Molecular Genetics and Metabolism

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94

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368-374

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3

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6 January 2020

Experimental investigation of protein folding and misfolding

1 reference

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Role of quality control pathways in human diseases involving protein misfolding

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Protein misfolding and human disease

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Quality control in the endoplasmic reticulum

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Quality control of mitochondria: protection against neurodegeneration and ageing

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Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations

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Missense mutations in the phenylalanine hydroxylase gene (PAH) can cause accelerated proteolytic turnover of PAH enzyme: a mechanism underlying phenylketonuria

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Primary hyperoxaluria type 1: genotypic and phenotypic heterogeneity

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Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase

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

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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

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Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1

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Chemical chaperone rescue of mutant human cystathionine beta-synthase

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Pyridoxine effect in type I primary hyperoxaluria is associated with the most common mutant allele

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Clinical implications of mutation analysis in primary hyperoxaluria type 1.

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Binding of pyridoxal 5'-phosphate to the heme protein human cystathionine beta-synthase

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Release of pyridoxal 5'-phosphate upon unfolding of mitochondrial aspartate aminotransferase

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Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor

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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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Identification of 5 novel mutations in the AGXT gene

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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 serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1

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

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Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria

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10.1016/J.YMGME.2008.03.010

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