(Q46617816)

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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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6 January 2020

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Q Lian

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6 January 2020

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29 April 2008

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6 January 2020

Molecular Genetics and Metabolism

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6 January 2020

94

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6 January 2020

3

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6 January 2020

368-374

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6 January 2020

Experimental investigation of protein folding and misfolding

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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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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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Primary hyperoxaluria: from gene defects to designer drugs?

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Chemical chaperone rescue of mutant human cystathionine beta-synthase

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Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs.

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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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The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1.

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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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10.1016/J.YMGME.2008.03.010

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18448374%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18448374%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

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