Biomaterial Database

Thioredoxin and glutathione in cultured fibroblasts from human cases with 5-oxoprolinuria and cystinosis. 1978

A Larsson, and A Holmgren, and I Bratt

UI	MeSH Term	Description	Entries
D010453	Peptide Synthases	Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.	Peptide Synthetases,Acid-Amino-Acid Ligases,Acid Amino Acid Ligases,Ligases, Acid-Amino-Acid,Synthases, Peptide,Synthetases, Peptide
D003554	Cystinosis	A metabolic disease characterized by the defective transport of CYSTINE across the lysosomal membrane due to mutation of a membrane protein cystinosin. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. In the KIDNEY, nephropathic cystinosis is a common cause of RENAL FANCONI SYNDROME.	Cystine Diathesis,Cystine Disease,Cystine Storage Disease,Cystinoses,Cystinosin, Defect of,Cystinosis, Nephropathic,Lysosomal Cystine Transport Protein, Defect Of,Nephropathic Cystinosis,Cystine Diatheses,Cystine Diseases,Cystine Storage Diseases,Cystinoses, Nephropathic,Defect of Cystinosin,Diatheses, Cystine,Diathesis, Cystine,Nephropathic Cystinoses,Storage Disease, Cystine,Storage Diseases, Cystine
D005347	Fibroblasts	Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.	Fibroblast
D005978	Glutathione	A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.	Reduced Glutathione,gamma-L-Glu-L-Cys-Gly,gamma-L-Glutamyl-L-Cysteinylglycine,Glutathione, Reduced,gamma L Glu L Cys Gly,gamma L Glutamyl L Cysteinylglycine
D005981	Glutathione Synthase	One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.	Glutathione Synthetase,Synthase, Glutathione,Synthetase, Glutathione
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000592	Amino Acid Metabolism, Inborn Errors	Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.	Amino Acidopathies, Congenital,Amino Acid Metabolism Disorders, Inborn,Amino Acid Metabolism, Inborn Error,Amino Acid Metabolism, Inherited Disorders,Amino Acidopathies, Inborn,Congenital Amino Acidopathies,Inborn Errors, Amino Acid Metabolism,Inherited Errors of Amino Acid Metabolism,Amino Acidopathy, Congenital,Amino Acidopathy, Inborn,Congenital Amino Acidopathy,Inborn Amino Acidopathies,Inborn Amino Acidopathy
D000743	Anemia, Hemolytic	A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).	Anemia, Hemolytic, Acquired,Anemia, Microangiopathic,Haemolytic Anaemia,Hemolytic Anemia,Hemolytic Anemia, Acquired,Microangiopathic Hemolytic Anemia,Acquired Hemolytic Anemia,Anaemia, Haemolytic,Anemia, Acquired Hemolytic,Anemia, Microangiopathic Hemolytic,Haemolytic Anaemias,Hemolytic Anemia, Microangiopathic,Microangiopathic Anemia,Microangiopathic Hemolytic Anemias
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D013879	Thioredoxins	Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.	Thioredoxin,Thioredoxin 1,Thioredoxin 2,Thioredoxin-1,Thioredoxin-2