| http://purl.uniprot.org/citations/15277241 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15277241 | http://www.w3.org/2000/01/rdf-schema#comment | "Glutathione transferase zeta (GSTZ1-1) is the major enzyme that catalyzes the metabolism of alpha-halo acids such as dichloroacetic acid, a carcinogenic contaminant of chlorinated water. GSTZ1-1 is identical with maleylacetoacetate isomerase, which catalyzes the penultimate step in the catabolic pathways for phenylalanine and tyrosine. In this study we have deleted the Gstz1 gene in BALB/c mice and characterized their phenotype. Gstz1(-/-) mice do not have demonstrable activity with maleylacetone and alpha-halo acid substrates, and other GSTs do not compensate for the loss of this enzyme. When fed a standard diet, the GSTZ1-1-deficient mice showed enlarged liver and kidneys as well as splenic atrophy. Light and electron microscopic examination revealed multifocal hepatitis and ultrastructural changes in the kidney. The addition of 3% (w/v) phenylalanine to the drinking water was lethal for young mice (<28 days old) and caused liver necrosis, macrovesicular steatosis, splenic atrophy, and a significant loss of circulating leukocytes in older surviving mice. GSTZ1-1-deficient mice showed constitutive induction of alpha, mu, and pi class GSTs as well as NAD(P)H:quinone oxidoreductase 1. The overall response is consistent with the chronic accumulation of a toxic metabolite(s). We detected the accumulation of succinylacetone in the serum of deficient mice but cannot exclude the possibility that maleylacetoacetate and maleylacetone may also accumulate."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0002-9440(10)63332-9"xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Board P.G."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Lim C.E."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Matthaei K.I."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Anders M.W."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Blackburn A.C."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Koina M.E."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Davis R.P."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/author | "Dahlstrom J.E."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/name | "Am J Pathol"xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/pages | "679-693"xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/title | "Mice deficient in glutathione transferase zeta/maleylacetoacetate isomerase exhibit a range of pathological changes and elevated expression of alpha, mu, and pi class glutathione transferases."xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://purl.uniprot.org/core/volume | "165"xsd:string |
| http://purl.uniprot.org/citations/15277241 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15277241 |
| http://purl.uniprot.org/citations/15277241 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15277241 |
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| http://purl.uniprot.org/uniprot/Q9JJA0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15277241 |
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