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Lindh",{"url":346,"publisher":390,"properties":436},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":391,"slug":10,"properties":392,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":396,"manageAffiliations":405,"indexDatabases":416,"url":89,"thumbnailPath":20,"statistic":431,"gsStatistic":20,"type":96,"analyzePriority":20},[],{"issn":393,"title":394,"eissn":395},{"VOID":13},{"EN":15},{"VOID":17},[397,401],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":398,"label":399,"description":400,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":402,"label":403,"description":404,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},[406,411],{"id":37,"createTime":20,"updateTime":20,"relativeEntities":407,"slug":20,"properties":408,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":410,"statistic":20},[],{"title":409},{"EN":41},[43],{"id":45,"createTime":20,"updateTime":20,"relativeEntities":412,"slug":20,"properties":413,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":415,"statistic":20},[],{"title":414},{"EN":49},[],[417,424],{"id":53,"indexDatabase":418,"url":64,"indexYears":65,"academicFieldIds":423,"indexDatabaseRanking":69},{"id":55,"createTime":20,"updateTime":20,"relativeEntities":419,"label":420,"description":421,"key":61,"publicationTags":422,"standard":20},[],{"EN":58,"VI":58},{"EN":58,"VI":60},[63],[67,68],{"id":71,"indexDatabase":425,"url":84,"indexYears":20,"academicFieldIds":430,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":426,"label":427,"description":428,"key":80,"publicationTags":429,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86,87,88],{"impactFactor":21,"impactFactorByYear":432,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":92,"totalPublicationByYear":433,"totalCitation":21,"totalCitationByYear":434,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":435,"hindexLast5Year":21,"hindex":21},{},{"2017":92},{},{},{"pages":437,"volume":439},{"VOID":438},"571-575",{"VOID":440},"25","2002-11-01",2002,"2026-08-14T18:12:03.406+00:00",[69,82],{"id":446,"createTime":447,"updateTime":448,"relativeEntities":449,"slug":450,"properties":451,"entityType":114,"verifyStatus":115,"verifyTime":464,"verifyNote":117,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":465,"fullTextUrl":20,"authors":466,"publicationType":149,"publisherRelationship":552,"citationCount":21,"citationInfo":599,"publishDate":602,"publishYear":600,"citationAnalyzeStatus":603,"lastCitationAnalyze":604,"indexDatabases":605,"openAccess":20,"references":20,"isForceReanalyzing":207},"f832bc17-4c3b-409a-8141-3a4c50d6df4f","2024-04-06T10:19:00.138+00:00","2026-07-29T07:36:54.013+00:00",[],"Muscle-cell-cultures-in-Menkes-disease-Copper-accumulation-in-myotubes",{"abstract":452,"title":454,"gsPaper":456,"keywords":458,"references":460,"doi":462},{"EN":453},"We present64Cu uptake studies in cultured muscle cells from a one-year-old patient with Menkes' disease. The cultured muscle cells from the patient showed a five-fold higher64Cu uptake than control muscle cells. Copper uptake in muscle cells was of the same magnitude as that found in fibroblasts from the patient and also from other Menkes' patients. The copper content of a muscle biopsy from the patient was twice that of a control biopsy. The enhanced uptake is probably copper specific, since zinc uptake was unaltered in both muscle cells and fibroblasts from the patient. Cytochrome c oxidase in the muscle of the patient was reduced to one-third of the value for controls, which is in agreement with the hypothesis that in Menkes' disease copper accumulates in a biologically non-active form. However, in cultured muscle cells and fibroblasts from the patient the cytochrome c oxidase activity was in the normal range, probably because of the relatively large amount of copper already available in the culture medium.",{"EN":455},"Muscle cell cultures in Menkes' disease: Copper accumulation in myotubes",{"VOID":457},"[\"17213076076074051810\"]",{"EN":459},"",{"VOID":461},"Bolhuis, P. A., De Zwart, H. J. D., Ponne, N. J. and De Jong, J. M. B. V. Free energy carriers in human cultured muscle cells.Muscle and Nerve 8 (1985) 22–26\nDanks, D. M., Campbell, P. E., Stevens, B. J., Mayne, V. and Cartwright, E. Menkes' kinky hair syndrome: an inherited defect in copper absorption with widespread effects.Pediatrics 50 (1972) 188–200\nGray, B. A. and Gollin, S. M. Rapid cell culture procedure for tissue samples.Am. J. Med. Genet. 28 (1987) 521–526\nHerd, S. M., Camakaris, J., Christofferson, R., Wookey, P. and Danks, D. M. Uptake and efflux of copper-64 in Menkes' disease and normal continuous lymphoid cells.Biochem. J. 247 (1987) 341–347\nHoltzman, N. A. Menkes' kinky hair syndrome: a genetic disease involving copper.Fed. Proc. 35 (1976) 2276–2280\nHorn, N. Menkes' X-linked disease: prenatal diagnosis of hemizygous males and heterozygous females.Prenatal Diagnosis 1 (1981) 107–120\nHorn, N., Heydorn, K., Damsgaard, E., Tygstrup, I. and Vestermark, S. Is Menkes' syndrome a copper storage disorder?Clin. Genet. 14 (1978) 186–187\nIyengar, G. V., Kollmer, W. E. and Bowen, H. J. M.The Elemental Composition of Human Tissues and Body Fluids, Verlag Chemie, Weinheim, 1978\nLowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. Protein measurement with the folin-phenol reagent.J. Biol. Chem. 193 (1951) 265–275\nMenkes, J. H., Alter, M., Steigleder, G. K., Weakly, D. R. and Sung, J. H. A sex-linked recessive disorder with retardation of growth, peculiar hair and focal cerebral and cerebellar degeneration.Pediatrics 29 (1962) 764–779\nNooyen, J. L., De Groot, C. J., van den Hamer, C. J. A., Monnens, A. H., Willemse, J. and Niermeijer, M. F. Trace element studies in three patients and a fetus with Menkes' disease. Effect of copper therapy.Pediatr. Res. 15 (1981) 284–289\nPackmann, S. and O'Toole, C. Trace metal metabolism in cultured skin fibroblasts of the mottled mouse: response to metallothionein inducers.Pediatr. Res. 18 (1984a) 1282–1286\nPackman, S. and O'Toole, C. Copper utilization in cultured skin fibroblasts of the mottled mouse, an animal model for Menkes' kinky hair syndrome.J. Inher. Metab. Dis. 7 (1984b) 168–170\nPrins, H. W. and van den Hamer, C. J. A. Abnormal copper-thionein synthesis and impaired copper utilization in mutated Brindled mice: model for Menkes' disease.J. Nutr. 110 (1980) 151–157\nScheinberg, I. H. and Collins, J. C. Menkes' disease: A disorder of zinc metabolism?Lancet 1 (1989) 619\nSinjorgo, K. M. C., Hakvoort, T. B. M., Muysers, A. O., Schram, A. W. and Tager, J. M. Cytochrome c oxidase: organ-specific isoenzymes and deficiencies.J. Inher. Metab. Dis. Suppl. 2 (1988) 202–204\nTjioe, P. S., De Goeij, J. J. M. and Houtman, J. P. W. Extended automated separation techniques in destructive neutron activation analysis; application to various biological materials, including human tissues and blood.J. Radioanal. Chem. 37 (1977) 511–522\nTonnesen, T., Muller-Schauenburg, G., Damsgaard, E. and Horn, N. Copper measurement in a muscle biopsy. A possible method for postmortem diagnosis of Menkes' disease.Clin. Genet. 29 (1986) 258–261\nvan den Berg, G. J. and van den Hamer, C. J. A. 64-Copper uptake in fibroblasts in Menkes' disease.Pediatr. Res. 20 (1986) 1048\nWitkowski, J. A. Tissue culture studies of muscle disorders. Part 1: Techniques, cell growth, morphology, cell surface.Muscle and Nerve 9 (1986a) 191–207\nWitkowski, J. A. Tissue culture studies of muscle disorders. Part 2: Biochemical studies, nerve-muscle culture, metabolic myopathies, and animal models.Muscle and Nerve 9 (1986b) 283–298",{"VOID":463},"10.1007\u002FBF01799687","2024-06-26T22:47:09.756+00:00","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002FBF01799687",[467,482,495,510,524,538],{"id":468,"sortIndex":21,"researcher":20,"roles":469,"affiliations":470,"properties":479,"displayName":481,"givenName":20,"familyName":20},"dcd4d8a1-a34b-4215-9475-e44bcf59b775",[123],[471],{"id":472,"sortIndex":21,"affiliation":473,"properties":20},"17a3c9b3-e996-4c5f-afcd-687384a45a87",{"id":472,"createTime":20,"updateTime":20,"relativeEntities":474,"slug":20,"properties":475,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":478,"statistic":20},[],{"title":476},{"VI":477},"Department of Radiochemistry, Interfaculty Reactor Institute, Delft University of Technology, Delft, The Netherlands",[],{"title":480},{"VI":481},"G. J. van den Berg",{"id":483,"sortIndex":92,"researcher":20,"roles":484,"affiliations":485,"properties":492,"displayName":494,"givenName":20,"familyName":20},"f4770b91-163d-4ea1-83ea-e7bc3ae88a57",[123],[486],{"id":472,"sortIndex":21,"affiliation":487,"properties":20},{"id":472,"createTime":20,"updateTime":20,"relativeEntities":488,"slug":20,"properties":489,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":491,"statistic":20},[],{"title":490},{"VI":477},[],{"title":493},{"VI":494},"J. J. Kroon",{"id":496,"sortIndex":295,"researcher":20,"roles":497,"affiliations":498,"properties":507,"displayName":509,"givenName":20,"familyName":20},"f418ba37-d1d7-4ef0-b6ff-642601245a22",[123],[499],{"id":500,"sortIndex":21,"affiliation":501,"properties":20},"cb8c774d-4a2f-4990-8052-e2221ee600be",{"id":500,"createTime":20,"updateTime":20,"relativeEntities":502,"slug":20,"properties":503,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":506,"statistic":20},[],{"title":504},{"VI":505},"Departments of Paediatrics, Biochemistry and Neurology, Academic Medical Centre, AZ Amsterdam, The Netherlands",[],{"title":508},{"VI":509},"F. A. Wijburg",{"id":511,"sortIndex":512,"researcher":20,"roles":513,"affiliations":514,"properties":521,"displayName":523,"givenName":20,"familyName":20},"afa67e0a-c7d8-41b2-beca-dfd2e09877c8",3,[123],[515],{"id":500,"sortIndex":21,"affiliation":516,"properties":20},{"id":500,"createTime":20,"updateTime":20,"relativeEntities":517,"slug":20,"properties":518,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":520,"statistic":20},[],{"title":519},{"VI":505},[],{"title":522},{"VI":523},"K. M. C. Sinjorgo",{"id":525,"sortIndex":526,"researcher":20,"roles":527,"affiliations":528,"properties":535,"displayName":537,"givenName":20,"familyName":20},"18abb59b-9c75-4c8f-9dad-d7843267cf58",4,[123],[529],{"id":500,"sortIndex":21,"affiliation":530,"properties":20},{"id":500,"createTime":20,"updateTime":20,"relativeEntities":531,"slug":20,"properties":532,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":534,"statistic":20},[],{"title":533},{"VI":505},[],{"title":536},{"VI":537},"N. H. Herzberg",{"id":539,"sortIndex":540,"researcher":20,"roles":541,"affiliations":542,"properties":549,"displayName":551,"givenName":20,"familyName":20},"505d4187-570a-4d9e-beca-ade126b173c6",5,[123],[543],{"id":500,"sortIndex":21,"affiliation":544,"properties":20},{"id":500,"createTime":20,"updateTime":20,"relativeEntities":545,"slug":20,"properties":546,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":548,"statistic":20},[],{"title":547},{"VI":505},[],{"title":550},{"VI":551},"P. A. Bolhuis",{"url":20,"publisher":553,"properties":20},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":554,"slug":10,"properties":555,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":559,"manageAffiliations":568,"indexDatabases":579,"url":89,"thumbnailPath":20,"statistic":594,"gsStatistic":20,"type":96,"analyzePriority":20},[],{"issn":556,"title":557,"eissn":558},{"VOID":13},{"EN":15},{"VOID":17},[560,564],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":561,"label":562,"description":563,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":565,"label":566,"description":567,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},[569,574],{"id":37,"createTime":20,"updateTime":20,"relativeEntities":570,"slug":20,"properties":571,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":573,"statistic":20},[],{"title":572},{"EN":41},[43],{"id":45,"createTime":20,"updateTime":20,"relativeEntities":575,"slug":20,"properties":576,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":578,"statistic":20},[],{"title":577},{"EN":49},[],[580,587],{"id":53,"indexDatabase":581,"url":64,"indexYears":65,"academicFieldIds":586,"indexDatabaseRanking":69},{"id":55,"createTime":20,"updateTime":20,"relativeEntities":582,"label":583,"description":584,"key":61,"publicationTags":585,"standard":20},[],{"EN":58,"VI":58},{"EN":58,"VI":60},[63],[67,68],{"id":71,"indexDatabase":588,"url":84,"indexYears":20,"academicFieldIds":593,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":589,"label":590,"description":591,"key":80,"publicationTags":592,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86,87,88],{"impactFactor":21,"impactFactorByYear":595,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":92,"totalPublicationByYear":596,"totalCitation":21,"totalCitationByYear":597,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":598,"hindexLast5Year":21,"hindex":21},{},{"2017":92},{},{},{"total":21,"publishYear":600,"statisticByYear":601},1990,{},"1990-03-01","DONE_ANALYZE_CITATION","2026-07-29T07:36:54.012+00:00",[69,82],{"id":607,"createTime":608,"updateTime":609,"relativeEntities":610,"slug":611,"properties":612,"entityType":114,"verifyStatus":115,"verifyTime":623,"verifyNote":117,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":624,"fullTextUrl":20,"authors":625,"publicationType":149,"publisherRelationship":641,"citationCount":21,"citationInfo":693,"publishDate":696,"publishYear":694,"citationAnalyzeStatus":603,"lastCitationAnalyze":697,"indexDatabases":698,"openAccess":20,"references":20,"isForceReanalyzing":207},"5e94f8d8-b244-4dea-80bd-098dbe5970da","2024-01-05T21:19:33.497+00:00","2026-07-27T20:29:54.617+00:00",[],"Disorders-of-mitochondrial-%CE%B2-oxidation-Prenatal-and-early-postnatal-diagnosis-and-their-relevance-to-Reye-s-syndrome-and-sudden-infant-death",{"abstract":613,"title":615,"gsPaper":617,"references":619,"doi":621},{"EN":614},"There are still many problems with the diagnosis and classification of inherited disorders of mitochondrial β-oxidation. At present only the acyl-CoA dehydrogenase step of the β-oxidation spiral has been explored in any detail and a large number of patients have disorders that cannot be properly characterized. β-Oxidation defects may present in a wide variety of ways, the most dramatic being acute encephalopathy with hepatic involvement (atypical Reye's syndrome) or ‘sudden’ death. Investigations may include urinary and plasma organic acids, metabolic stress tests and assays of overall metabolic pathways or of specific enzymes in cultured fibroblasts, lymphocytes, or other material. Early postnatal diagnosis presents particular difficulties but in medium-chain acyl-CoA dehydrogenase deficiency the diagnosis may be apparent from careful examination of urine. There is as yet little general experience in prenatal diagnosis of this group of disorders except for glutaric aciduria type II. Single prenatal diagnoses of medium-chain acyl-CoA dehydrogenase deficiency and of an incompletely characterized defect of medium-chain fatty acid oxidation have been performed.",{"EN":616},"Disorders of mitochondrial β-oxidation: Prenatal and early postnatal diagnosis and their relevance to Reye's syndrome and sudden infant death",{"VOID":618},"[\"4873501374401446333\"]",{"VOID":620},"Allison, F., Bennett, M. J., Variend, S. and Engel, P. C. Acyl-coenzyme A dehydrogenase deficiency in heart tissue from infants who died unexpectedly with fatty change in the liver.Br. Med. J. 296 (1988a) 11–12\nAllison, F., Barnes, I. C. S. and Bennett, M. J. The oxidation of octanoic acid by amniotic fluid cells; The effect of cell type and passage number.Prenat. Diagn. 8 (1988b) 397–398\nAmendt, B. A., Greene, C., Sweetman, L., Cloherty, J., Shih, V., Moon, A., Teel, L. and Rhead, W. J. Short-chain acyl-CoA dehydrogenase deficiency. Clinical and biochemical studies in two patients.J. Clin. Invest. 79 (1987) 1303–1309\nAnonymous. Sudden infant death and inherited disorders of fat oxidation.Lancet 2 (1986) 1073–1075\nBennett, M. J., Curnock, D. A., Engel, P. C., Shaw, L., Gray, R. G. F., Hull, D., Patrick, A. D. and Pollitt, R. J. Glutaric aciduria type II: Biochemical investigation and treatment of a child diagnosed prenatally.J. Inher. Metab. Dis. 7 (1984) 57–61\nBennett, M. J., Gray, R. G. F., Isherwood, D. M., Murphy, N. and Pollitt, R. J. Diagnosis and biochemical investigation of a patient with a short-chain fatty acid oxidation defect.J. Inher. Metab. Dis. 8 Suppl. 2 (1985) 99–100\nBennett, M. J., Variend, S. and Pollitt, R. J. Screening siblings for inborn errors of fatty acid metabolism in families with a history of sudden infant death.Lancet 2 (1986) 1470\nBennett, M. J., Pollitt, R. J., Land, J. M., Turner, M. J. and Cheetham, C. H. Lethal multiple acyl-CoA dehydrogenase deficiency with dysmorphic features.J. Inher. Metab. Dis. 10 (1987a) 95–96\nBennett, M. J., Allison, F., Pollitt, R. J., Manning, N. J., Gray, R. G. F., Green, A., Hale, D. E. and Coates, P. M. Prenatal diagnosis of medium-chain acyl-CoA dehydrogenase deficiency in family with sudden infant death.Lancet 1 (1987b) 440–441\nBennett, M. J., Allison, F., Lowther, G. W., Gray, R. G. F., Johnston, D. I., Fitzsimmons, J. S., Manning, N. J. and Pollitt, R. J. Prenatal diagnosis of medium-chain acyl-coenzyme A dehydrogenase deficiency.Prenat. Diagn. 7 (1987c) 135–141\nBennett, M. J., Allison, F., Pollitt, R. J. and Variend, S. Fatty acid oxidation defects as causes of unexpected death in infancy. In Coates, P. M. (Ed.)Enzymes of Fatty Acid Oxidation and Their Genetic Defects. Alan R. Liss, New York, 1989\nCoates, P. M., Hale, D. E., Stanley, C. A., Corkey, B. E. and Cortner, J. A. Genetic deficiency of medium-chain acyl coenzyme A dehydrogenase: Studies in cultured skin fibroblasts and peripheral mononuclear leukocytes.Pediatr. Res. 19 (1985) 671–676\nCoates, P. M., Hale, D. E., Finocchiaro, G., Tanaka, K. and Winter, S. C. Genetic deficiency of short-chain acyl-coenzyme A dehydrogenase in cultured fibroblasts from a patient with muscle carnitine deficiency and severe skeletal muscle weakness.J. Clin. Invest. 81 (1988) 171–175\nDowning, M., Rose, P., Bennett, M. J., Manning, N. J. and Pollitt, R. J. Generalized dicarboxylic aciduria: A common finding in neonates.J. Inher. Metab. Dis. 12 Suppl. 2 (1989) 321–324\nDusheiko, G., Kew, M. C., Joffe, B. I., Lewin, J. R., Mantagos, S. and Tanaka, K. Recurrent hypoglycemia associated with glutaric aciduria type II in an adult.N. Engl. J. Med. 301 (1979) 1405–1409\nEmery, J., Howat, A. J., Variend, S. and Vawter, G. F. Investigation of inborn errors of metabolism in unexpected infant death.Lancet 2 (1988) 29–31\nFrerman, F. E. and Goodman, S. I. Deficiency of electron transfer flavoprotein or electron transfer flavoprotein: ubiquinone oxidoreductase in glutaric acidemia type II fibroblasts.Proc. Natl. Acad. Sci. USA 82 (1985a) 4517–4520\nFrerman, F. E. and Goodman, S. I. Fluorimetric assay of acyl-CoA dehydrogenase in normal and mutant human fibroblasts.Biochem. Med. 33 (1985b) 38–44\nGreen, A., Marshall, T. G., Bennett, M. J., Gray, R. G. F. and Pollitt, R. J. Riboflavin responsive ethylamlonic-adipic aciduria.J. Inher. Metab. Dis. 8 (1985) 67–70\nGregersen, N., Christensen, M. F., Christensen, E. and Kølvraa, F. Riboflavin responsive multiple acyl-CoA dehydrogenase deficiency. Assessment of three years of riboflavin treatment.Acta Paediatr. Scand. 77 (1986) 676–681\nHale, D. E., Batshaw, M. L., Coates, P. M., Frerman, F. E., Goodman, S. I., Singh, I. and Stanley, C. A. Long-chain acyl coenzyme A dehydrogenase deficiency: an inherited cause of non-ketotic hypoglycemia.Pediatr. Res. 19 (1985) 666–671\nHarpey, J.-P., Charpentier, C. and Paterneau-Jouas, M. Sudden infant death syndrome and inherited disorders of fat metabolism.Lancet 2 (1986) 1332\nHarpey, J.-P., Charpentier, C. and Paterneau-Jouas, M. Fatty acid oxidation defects and sudden infant death.Lancet 1 (1987) 163\nHowat, A. J., Bennett, M. J., Variend, S., Shaw, L. and Engel, P. C. Defects in the metabolism of fatty acids in the sudden infant death syndrome.Br. Med. J. 290 (1985) 1771–1773\nIkeda, Y., Keese, S. M. and Tanaka, K. Biosynthesis of electron-transfer flavoprotein in a cell-free system and in cultured human fibroblasts. Defect in the α-subunit synthesis is a primary lesion in glutaric aciduria type II.J. Clin. Invest. 78 (1986) 997–1002\nJakobs, C., Sweetman, L., Wadman, S. K., Duran, M., Saudubray, J.-M., and Nyhan, W. L. Prenatal diagnosis of glutaric aciduria type II by direct chemical analysis of dicarboxylic acids in amniotic fluid.Eur. J. Pediatr. 141 (1984) 153–157\nKelley, R. I. and Morton, H. 3-Hydroxyoctanoic aciduria: Identification of a new organic acid in the urine of a patient with non-ketotic hypoglycemia.Clin. Chim. Acta 175 (1988) 19–26\nMantagos, S., Genel, M. and Tanaka, K. Ethylmalonic-adipic aciduria. In vivo and in vitro studies indicating deficiency of activities of multiple acyl-CoA dehydrogenases.J. Clin. Invest. 64 (1979) 1580–1589\nMitchell, G., Saudubray, J.-M., Benoit, Y., Rocchiccioli, F., Charpentier, C., Ogier, H. and Boué, J. Antenatal diagnosis of glutaric aciduria type II.Lancet 1 (1983) 1099\nMoon, A. and Rhead, W. J. Complementation analysis of fatty acid oxidation disorders.J. Clin. Invest. 79 (1987) 59–64\nNiederwieser, A., Steinmann, B., Exner, U., Neuheiser, F., Redweik, U., Wang, M., Rampini, S. and Wendel, U. Multiple acyl-CoA dehydrogenase deficiency (MADD) in a boy with non-ketotic hypoglycemia, hepatomegaly, muscle hypotonia and cardiomyopathy. Detection ofN-isovalerylglutamic acid and its monoamide.Helvet. Paediatr. Acta 38 (1983) 9–26\nPollitt, R. J., Losty, H. and Westwood, A. 3-Hydroxydicarboxylic aciduria; A distinctive type of intermittent dicarboxylic aciduria of possible diagnostic significance.J. Inher. Metab. Dis. 10 Suppl. 2 (1987) 266–269\nRiudor, E., Ribes, A., Boronat, M., Sabado, C., Dominguez, C. and Ballabriga, A. A new case of C6–C14 dicarboxylic aciduria with favourable evolution.J. Inher. Metab. Dis. 9 Suppl. 2 (1986) 297–299\nRoe, C. R., Millington, D. S., Maltby, D. A. and Kinnebrew, P. Recognition of mediumchain acyl-CoA dehydrogenase deficiency in asymptomatic siblings of children dying of sudden infant death or Reye-like syndromes.J. Pediatr. 108 (1986) 13–18\nRumsby, G., Seakins, J. W. T. and Leonard, J. V. A simple screening test for mediumchain acyl CoA dehydrogenase deficiency.Lancet 2 (1986) 467\nSeakins, J. W. T. and Rumsby, G. The use of phenylpropionic acid as a loading test for medium-chain acyl-CoA dehydrogenase deficiency.J. Inher. Metab. Dis. 11 Suppl. 2 (1988) 221–224\nSherratt, H. S. A. (ed.) The enzymology of β-oxidation.Biochem. Soc. Trans. 16 (1988) 409–427\nTonsgard, J. H. Urinary dicarboxylic acids in Reye's syndrome.J. Pediatr. 107 (1985) 79–84\nTonsgard, J. H. Plasma dicarboxylic acids in Reye's syndrome.J. Pediatr. 109 (1986) 440–445\nTracey, B. M., Chalmers, R. A., Mehta, A., English, N., Purkiss, P., Valman, H. B. and Stacey, T. E. Studies on abnormal metabolic function in Reye's syndrome.J. Inher. Metab. Dis. 10 Suppl. 2 (1987) 263–265\nTreem, W. L., Witzleben, C. A., Piccoli, D. A., Stanley, C. A., Hale, D. E., Coates, P. M. and Watkins, J. B. Medium-chain and long-chain acyl CoA dehydrogenase deficiency: Clinical, pathologic and ultrastructural differentiation from Reye's syndrome.Hepatology 6 (1986) 1270–1278\nTurnbull, D. M., Shepherd, I. M. and Aynsley-Green, A. Inherited defects of mitochondrial fatty acid oxidation.Biochem. Soc. Trans. 16 (1988) 424–427\nvan Hoof, F., Vamecq, J., Draye, J.-P. and Veitch, K. The catabolism of medium- and long-chain dicarboxylic acids.Biochem. Soc. Trans. 16 (1988) 423–424\nVianey-Liaud, C., Divry, P., Gregersen, N. and Mathieu, M. The inborn errors of mitochondrial fatty acid oxidation.J. Inher. Metab. Dis. 10 Suppl. 1 (1987) 159–198",{"VOID":622},"10.1007\u002FBF01799297","2024-05-13T06:35:51.619+00:00","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002FBF01799297",[626],{"id":627,"sortIndex":21,"researcher":20,"roles":628,"affiliations":629,"properties":638,"displayName":640,"givenName":20,"familyName":20},"6d7bf8aa-16c6-44fb-9ebc-8c30db877693",[123],[630],{"id":631,"sortIndex":21,"affiliation":632,"properties":20},"120545ea-129f-421a-a58d-48253fb555ca",{"id":631,"createTime":20,"updateTime":20,"relativeEntities":633,"slug":20,"properties":634,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":637,"statistic":20},[],{"title":635},{"VI":636},"University Department of Paediatrics, The Children's Hospital, Sheffield, UK",[],{"title":639},{"VI":640},"R. J. Pollitt",{"url":624,"publisher":642,"properties":688},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":643,"slug":10,"properties":644,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":648,"manageAffiliations":657,"indexDatabases":668,"url":89,"thumbnailPath":20,"statistic":683,"gsStatistic":20,"type":96,"analyzePriority":20},[],{"issn":645,"title":646,"eissn":647},{"VOID":13},{"EN":15},{"VOID":17},[649,653],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":650,"label":651,"description":652,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":654,"label":655,"description":656,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},[658,663],{"id":37,"createTime":20,"updateTime":20,"relativeEntities":659,"slug":20,"properties":660,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":662,"statistic":20},[],{"title":661},{"EN":41},[43],{"id":45,"createTime":20,"updateTime":20,"relativeEntities":664,"slug":20,"properties":665,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":667,"statistic":20},[],{"title":666},{"EN":49},[],[669,676],{"id":53,"indexDatabase":670,"url":64,"indexYears":65,"academicFieldIds":675,"indexDatabaseRanking":69},{"id":55,"createTime":20,"updateTime":20,"relativeEntities":671,"label":672,"description":673,"key":61,"publicationTags":674,"standard":20},[],{"EN":58,"VI":58},{"EN":58,"VI":60},[63],[67,68],{"id":71,"indexDatabase":677,"url":84,"indexYears":20,"academicFieldIds":682,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":678,"label":679,"description":680,"key":80,"publicationTags":681,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86,87,88],{"impactFactor":21,"impactFactorByYear":684,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":92,"totalPublicationByYear":685,"totalCitation":21,"totalCitationByYear":686,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":687,"hindexLast5Year":21,"hindex":21},{},{"2017":92},{},{},{"pages":689,"volume":691},{"VOID":690},"215-230",{"VOID":692},"12",{"total":21,"publishYear":694,"statisticByYear":695},1989,{},"1989-03-01","2026-07-27T20:29:54.616+00:00",[69,82],{"id":700,"createTime":701,"updateTime":702,"relativeEntities":703,"slug":704,"properties":705,"entityType":114,"verifyStatus":115,"verifyTime":716,"verifyNote":117,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":717,"fullTextUrl":20,"authors":718,"publicationType":149,"publisherRelationship":783,"citationCount":21,"citationInfo":835,"publishDate":838,"publishYear":836,"citationAnalyzeStatus":603,"lastCitationAnalyze":839,"indexDatabases":840,"openAccess":20,"references":20,"isForceReanalyzing":207},"63aca87f-9803-4e63-808d-aeccb24da4cf","2024-02-14T02:54:58.450+00:00","2026-07-25T18:23:29.997+00:00",[],"Treatment-products-and-approaches-for-phenylketonuria-improved-palatability-and-flexibility-demonstrate-safety-efficacy-and-acceptance-in-US-clinical-trials",{"abstract":706,"title":708,"gsPaper":710,"references":712,"doi":714},{"EN":707},"A new amino acid formulation and a variety of treatment products incorporating it were evaluated for long-term safety, efficacy, and acceptance in 25 subjects with phenylketonuria over a period of 5 years. Palatability of the treatment was improved by reducing the required intake of amino acids, reformulating the mixture to have better taste, and providing vitamins and minerals as tablets. The hypotheses were that these strategies would improve compliance and metabolic control and maintain nutritional status in subjects. Compliance with treatment was determined from mean reported intakes (4-day diet records) and from mean ‘received’ intakes using receipts of treatment products actually shipped to individuals upon request. Mean amino acid intakes prescribed were significantly reduced from study entry to end, from 1.2 g\u002Fkg to 0.7 g\u002Fkg (p \u003C 0.001). Reported intakes were similarly reduced from 1.3 g\u002Fkg to 0.7 g\u002Fkg (p \u003C 0.001). While actually ‘received’ intakes of amino acid formula were also significantly reduced (p \u003C 0.001), intakes by this measure were much lower than either prescribed or reported, 0.9 g\u002Fkg at entry and 0.4 g\u002Fkg at the end of the study, suggesting that acceptance of the treatment (usage of products), even when made more palatable, is below clinical expectations. In spite of these findings, mean serum proteins and minerals, height and weight were not significantly reduced during the study, supporting the safety of lowered intakes of amino acids and of nutritionally incomplete products. While the increase in mean serum phenylalanine concentration from 0.38 to 0.48 mmol\u002FL was significant (p \u003C 0.03), this mean rise of 0.1 mmol\u002FL during a corresponding mean age increase of 4.2 years (from 6.9 to 11.1 years) is lower than in other recent reports from longitudinal studies of outcomes during this age range in subjects treated with traditional products. These data support the safety and efficacy of a more palatable and flexible approach to treatment.",{"EN":709},"Treatment products and approaches for phenylketonuria: improved palatability and flexibility demonstrate safety, efficacy and acceptance in US clinical trials",{"VOID":711},"[\"7954491629183887889\"]",{"VOID":713},"Acosta PB, Yanicelli S (1993) Protocol 1 — phenylketonuria (PKU). In Cameron AM, Russell C, eds. Ross Metabolic System Nutrition Support Protocols. Columbus OH: Ross, 1–35.\nAcosta PB, Fernhoff PM, Warshaw HS, et al (1981) Zinc and copper status of treated children with phenylketonuria. J Parent Ent Nutr 5: 406–409.\nArmstrong MD, Stave U (1973) A study of plasma free amino acid levels. II. Normal values for children and adults. Metabolism 22, 561–578.\nAzen CG, Koch R, Friedman EG, et al (1991) Intellectual development in 12-year-old children treated for phenylketonuria. Am J Dis Child 145: 35–39.\nBeatriz DO, da Cruz M, Seidler H, Widhalm K (1993) Iron status and iron supplementation in children with classical phenylketonuria. J Am Coll Nutr 12: 531–536.\nDarling G, Mathias P, O'Regan M, Naughten E (1992) Serum selenium levels in individuals on PKU diets. J Inher Metab Dis 15: 769–773.\nFrancis DEM (1987) Phenylketonuria. In Francis DEM ed. Diets for Sick Children, 4th edn. Oxford: Blackwell, 224–261.\nGordis L (1979) Conceptual and methodologic problems in measuring patient compliance. In Haynes RB, Taylor DW, Sackett DL, eds. Compliance in Health Care. Baltimore, MD: Johns Hopkins University Press, 23–48.\nGuthrie R, Susi A (1963) A simple phenylalanine method for detecting phenylketonuria in large populations of newborn infants. Pediatrics 32: 338–342.\nHamill PVV, Drizd TA, Johnson CL, Reed RB, Roche AF, Moore WM (1979) Physical growth: National Center for Health Statistics percentiles. Am J Clin Nutr 32: 607–629.\nLife Sciences Research Office (1991) Development of Medical Foods for Rare Diseases: Proceedings of a Workshop. Bethesda, MD: Federation of American Societies for Experimental Biology.\nLou HC, Toft PB, Andresen J, et al (1992) An occipito-temporal syndrome in adolescents with optimally controlled hyperphenylalaninaemia. J Inher Metab Dis 15: 687–695.\nMalvy DJ-M, Poveda J-D, Dubruyne M, Montagnon B, Burtschy B, Herbert C (1992) Laser immunonephelometry reference intervals for eight serum proteins in healthy children. Clin Chem 31: 394–399.\nMedical Research Council (1993) Recommendations on the dietary management of phenylketonuria. Arch Dis Child 68: 426–427.\nMcBurnie MA, Kronmally RA, Schuett VE, Azen CG (1991) Physical growth of children treated for phenylketonuria. Ann Hum Biol 18: 357–368.\nMcMurry MP, Chan GM, Leonard CO, Ernst SL (1992) Bone mineral status in children with phenylketonuria — relationship to nutritional intake and phenylalanine control. Am J Clin Nutr 55: 997–1004.\nNational Research Council (US) Subcommittee on the Tenth Edition of the RDAs (1989) Recommended Dietary Allowances. Washington DC: National Academy Press.\nNixon DE, Moyer TP, Johnson P (1986) Routine measurement of calcium, magnesium, copper, zinc, and iron in urine and serum by inductively coupled plasma emission spectroscopy. Clin Chem 32: 1660–1665.\nPietz J, Benninger Ch, Schmidt H, Scheffner D, Bickel H (1988) Long-term development of intelligence (IQ) and EEG in 34 children with phenylketonuria treated early. Eur J Pediatr 147: 361–367.\nScriver CR, Kaufman S, Eisensmith RC, Woo SLC (1995) The hyperphenylalaninemias. In Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic and Molecular Bases of Inherited Disease, 7th edn. McGraw-Hill: New York, 1015–1076.\nStepnick-Gropper S, Acosta PB, Clark-Sheehan N, Wenz E, Cheng M, Koch R (1988) Trace element status of children with PKU and normal children. J Am Diet Assoc 88: 459–464.\nThompson DD, Allen RJ (1981) Rapid determination of selenium in nutritional supplements by a flameless atomic absorption technique using a novel sample preparation. Atom Spectrosc 2: 53–58.",{"VOID":715},"10.1023\u002FA:1005337126669","2024-05-10T11:54:50.196+00:00","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1023\u002FA%3A1005337126669",[719,743,763],{"id":720,"sortIndex":21,"researcher":20,"roles":721,"affiliations":722,"properties":740,"displayName":742,"givenName":20,"familyName":20},"42c39e23-3d29-4774-92e1-7c80ca51a12c",[123],[723,731],{"id":724,"sortIndex":21,"affiliation":725,"properties":20},"0d6c168e-7898-4f7a-ba75-4da2f8ecd041",{"id":724,"createTime":20,"updateTime":20,"relativeEntities":726,"slug":20,"properties":727,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":730,"statistic":20},[],{"title":728},{"VI":729},"Department of Chemistry, Portland State University, USA",[],{"id":732,"sortIndex":92,"affiliation":733,"properties":739},"186489d6-6630-4ba7-9c4a-68b7a7033e1b",{"id":732,"createTime":20,"updateTime":20,"relativeEntities":734,"slug":20,"properties":735,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":738,"statistic":20},[],{"title":736},{"VI":737},"Divisions of Pediatrics\u002FMedical and Molecular Genetics, School of Medicine, Oregon Health Sciences University, Portland, USA",[],{},{"title":741},{"VI":742},"A. P. Prince",{"id":744,"sortIndex":92,"researcher":20,"roles":745,"affiliations":746,"properties":760,"displayName":762,"givenName":20,"familyName":20},"17097934-81d9-4c12-a1c7-b3dc727ae9ad",[123],[747,753],{"id":724,"sortIndex":21,"affiliation":748,"properties":20},{"id":724,"createTime":20,"updateTime":20,"relativeEntities":749,"slug":20,"properties":750,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":752,"statistic":20},[],{"title":751},{"VI":729},[],{"id":732,"sortIndex":92,"affiliation":754,"properties":759},{"id":732,"createTime":20,"updateTime":20,"relativeEntities":755,"slug":20,"properties":756,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":758,"statistic":20},[],{"title":757},{"VI":737},[],{},{"title":761},{"VI":762},"M. P. McMurry",{"id":764,"sortIndex":295,"researcher":20,"roles":765,"affiliations":766,"properties":780,"displayName":782,"givenName":20,"familyName":20},"8c44bf56-aed6-4aa3-93da-1757d62ab8ae",[123],[767,773],{"id":724,"sortIndex":21,"affiliation":768,"properties":20},{"id":724,"createTime":20,"updateTime":20,"relativeEntities":769,"slug":20,"properties":770,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":772,"statistic":20},[],{"title":771},{"VI":729},[],{"id":732,"sortIndex":92,"affiliation":774,"properties":779},{"id":732,"createTime":20,"updateTime":20,"relativeEntities":775,"slug":20,"properties":776,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":778,"statistic":20},[],{"title":777},{"VI":737},[],{},{"title":781},{"VI":782},"N. R. M. Buist",{"url":717,"publisher":784,"properties":830},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":785,"slug":10,"properties":786,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":790,"manageAffiliations":799,"indexDatabases":810,"url":89,"thumbnailPath":20,"statistic":825,"gsStatistic":20,"type":96,"analyzePriority":20},[],{"issn":787,"title":788,"eissn":789},{"VOID":13},{"EN":15},{"VOID":17},[791,795],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":792,"label":793,"description":794,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":796,"label":797,"description":798,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},[800,805],{"id":37,"createTime":20,"updateTime":20,"relativeEntities":801,"slug":20,"properties":802,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":804,"statistic":20},[],{"title":803},{"EN":41},[43],{"id":45,"createTime":20,"updateTime":20,"relativeEntities":806,"slug":20,"properties":807,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":809,"statistic":20},[],{"title":808},{"EN":49},[],[811,818],{"id":53,"indexDatabase":812,"url":64,"indexYears":65,"academicFieldIds":817,"indexDatabaseRanking":69},{"id":55,"createTime":20,"updateTime":20,"relativeEntities":813,"label":814,"description":815,"key":61,"publicationTags":816,"standard":20},[],{"EN":58,"VI":58},{"EN":58,"VI":60},[63],[67,68],{"id":71,"indexDatabase":819,"url":84,"indexYears":20,"academicFieldIds":824,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":820,"label":821,"description":822,"key":80,"publicationTags":823,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86,87,88],{"impactFactor":21,"impactFactorByYear":826,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":92,"totalPublicationByYear":827,"totalCitation":21,"totalCitationByYear":828,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":829,"hindexLast5Year":21,"hindex":21},{},{"2017":92},{},{},{"pages":831,"volume":833},{"VOID":832},"486-498",{"VOID":834},"20",{"total":21,"publishYear":836,"statisticByYear":837},1997,{},"1997-08-01","2026-07-25T18:23:29.996+00:00",[69,82],{"id":842,"createTime":843,"updateTime":844,"relativeEntities":845,"slug":846,"properties":847,"entityType":114,"verifyStatus":115,"verifyTime":856,"verifyNote":117,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":857,"fullTextUrl":20,"authors":858,"publicationType":149,"publisherRelationship":926,"citationCount":21,"citationInfo":978,"publishDate":981,"publishYear":979,"citationAnalyzeStatus":19,"lastCitationAnalyze":982,"indexDatabases":983,"openAccess":20,"references":984,"isForceReanalyzing":207},"219964c2-ee7e-4949-801e-0475eef35f38","2024-01-25T12:39:05.666+00:00","2026-07-22T21:51:53.157+00:00",[],"Effect-of-cysteine-dosage-on-erythrocyte-glutathione-synthesis-rate-in-a-patient-with-cystathionine-beta-synthase-deficiency",{"abstract":848,"title":850,"gsPaper":852,"doi":854},{"EN":849},"Cystathionine β-synthase (CBS)-deficient patients develop premature arteriosclerosis and thrombosis leading to a high risk of a vascular event before the age of 30 years. In CBS deficiency the transsulfuration pathway is impaired, leading to markedly elevated levels of homocysteine and methionine, and severely decreased levels of cystathionine and cysteine. Through autooxidation these elevated levels of homocysteine might induce excessive production of reactive oxygen species (ROS). ROS are involved in endothelial damage and are neutralized by antioxidants. In humans the main antioxidant is glutathione (GSH). Its production mainly depends on the amount of available cysteine. Since cysteine levels in CBS deficiency are decreased, GSH production is presumed to be low. Accordingly, all CBS-deficient patients receive cysteine supplements, which supposedly stimulate GSH synthesis. However, data on the effect of cysteine dosage on GSH synthesis in CBS-deficient patients are lacking. Therefore, in a CBS-deficient pyridoxine non-responsive female patient, concentration and fractional synthesis rate (FSR) of erythrocyte GSH were measured by infusion of l-[3,3-2H2]cysteine tracer during prolonged cysteine supplementation with 88 and 40 mg\u002Fkg per day. Erythrocyte GSH concentration and its FSR at cysteine supplementation with 88 versus 40 mg\u002Fkg per day were 1.25 versus 1.30 mmol\u002FL and 230 versus 254% per day, respectively. These data suggest that in a CBS-deficient patient exogenous supply of 40 mg cysteine\u002Fkg per day is sufficient to maintain GSH synthesis in erythrocytes. Further studies in larger patient groups should be initiated to measure the effects on GSH metabolism to further elucidate the correct dose of cysteine supplements in CBS-deficient patients.",{"EN":851},"Effect of cysteine dosage on erythrocyte glutathione synthesis rate in a patient with cystathionine beta synthase deficiency",{"VOID":853},"[\"4489794238272972354\"]",{"VOID":855},"10.1007\u002Fs10545-007-0629-4","2024-04-24T05:51:37.330+00:00","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002Fs10545-007-0629-4",[859,884,898,913],{"id":860,"sortIndex":21,"researcher":20,"roles":861,"affiliations":862,"properties":879,"displayName":881,"givenName":20,"familyName":20},"f9379f5a-d3a8-47f8-b8e8-f38555f6a2c6",[123],[863,871],{"id":864,"sortIndex":21,"affiliation":865,"properties":20},"4c6c2e99-443e-4cd3-a003-db44191bf830",{"id":864,"createTime":20,"updateTime":20,"relativeEntities":866,"slug":20,"properties":867,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":870,"statistic":20},[],{"title":868},{"VI":869},"DBG Department of Clinical Genetics, University Medical Center Utrecht (Wilhelmina Children’s Hospital), Utrecht, The Netherlands",[],{"id":872,"sortIndex":92,"affiliation":873,"properties":20},"432aa411-f314-4d97-afdb-7defbd12aab3",{"id":872,"createTime":20,"updateTime":20,"relativeEntities":874,"slug":20,"properties":875,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":878,"statistic":20},[],{"title":876},{"VI":877},"Department of Endocrinology and Metabolism, Academic Medical Center, Amsterdam, The Netherlands",[],{"title":880,"gsAuthor":882},{"VI":881},"S. N. van der Crabben",{"VOID":883},"[\"GhMFcI0AAAAJ\"]",{"id":885,"sortIndex":92,"researcher":20,"roles":886,"affiliations":887,"properties":896,"displayName":509,"givenName":20,"familyName":20},"46e09eb0-9177-42e3-8b81-4ea0cfbfe64b",[123],[888],{"id":889,"sortIndex":21,"affiliation":890,"properties":20},"b686b133-8b98-4559-b407-2fd7f967ba73",{"id":889,"createTime":20,"updateTime":20,"relativeEntities":891,"slug":20,"properties":892,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":895,"statistic":20},[],{"title":893},{"VI":894},"Department of Paediatrics, Emma Children’s Hospital, Academic Medical Center, Amsterdam, The Netherlands",[],{"title":897},{"VI":509},{"id":899,"sortIndex":295,"researcher":20,"roles":900,"affiliations":901,"properties":910,"displayName":912,"givenName":20,"familyName":20},"cec34a80-a848-4435-a2b0-538fd894f6bf",[123],[902],{"id":903,"sortIndex":21,"affiliation":904,"properties":20},"a16384af-d0a3-4f70-9522-86de049f7d34",{"id":903,"createTime":20,"updateTime":20,"relativeEntities":905,"slug":20,"properties":906,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":909,"statistic":20},[],{"title":907},{"VI":908},"Department of Clinical Chemistry, Laboratory of Endocrinology and Radiochemistry, Academic Medical Center, Amsterdam, The Netherlands",[],{"title":911},{"VI":912},"M. T. Ackermans",{"id":914,"sortIndex":512,"researcher":20,"roles":915,"affiliations":916,"properties":923,"displayName":925,"givenName":20,"familyName":20},"ce2569bd-be78-4c8f-bcd6-7d86a4aa5f48",[123],[917],{"id":872,"sortIndex":21,"affiliation":918,"properties":20},{"id":872,"createTime":20,"updateTime":20,"relativeEntities":919,"slug":20,"properties":920,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":922,"statistic":20},[],{"title":921},{"VI":877},[],{"title":924},{"VI":925},"H. P. 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Circ Res 94: 28–36.",{"doi":319},{"id":315,"text":989,"url":317,"identifiers":990},"Badaloo A, Reid M, Forrester T, Heird WC, Jahoor F (2002) Cysteine supplementation improves the erythrocyte glutathione synthesis rate in children with severe edematous malnutrition. Am J Clin Nutr 76: 646–652.",{"doi":319},{"id":315,"text":992,"url":317,"identifiers":993},"Capitan P, Malmezat T, Breuille D, Obled C (1999) Gas chromatographic-mass spectrometric analysis of stable isotopes of cysteine and glutathione in biological samples. J Chromatogr B Biomed Sci Appl 732: 127–135.",{"doi":319},{"id":315,"text":995,"url":317,"identifiers":996},"Castro R, Rivera I, Blom HJ, Jakobs C, de Almeida Tavares I (2006) Homocysteine metabolism, hyperhomocysteinaemia and vascular disease: an overview. J Inherit Metab Dis 29: 3–20.",{"doi":319},{"id":315,"text":998,"url":317,"identifiers":999},"Davi G, Di Minno G, Coppola A, et al (2001) Oxidative stress and platelet activation in homozygous homocystinuria. Circulation 104: 1124–1128.",{"doi":319},{"id":315,"text":1001,"url":317,"identifiers":1002},"De Rosa SC, Zaretsky MD, Dubs JG, et al (2000) N-Acetylcysteine replenishes glutathione in HIV infection. Eur J Clin Invest 30: 915–929.",{"doi":319},{"id":1004,"text":1005,"url":1006,"identifiers":1007},"9ba91fd6-cc37-465c-ad98-16fc9d6648d1","Griffith OW (1999) Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 27: 922–935.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0891584999001768",{"doi":1008},"10.1016\u002FS0891-5849(99)00176-8",{"id":315,"text":1010,"url":317,"identifiers":1011},"Haber CA, Lam TK, Yu Z, et al (2003) N-Acetylcysteine and taurine prevent hyperglycemia-induced insulin resistance in vivo: possible role of oxidative stress. Am J Physiol Endocrinol Metab 285: E744–E753.",{"doi":319},{"id":315,"text":1013,"url":317,"identifiers":1014},"Humbert B, Nguyen P, Obled C, et al (2001) Use of l-[15N] glutamic acid and homoglutathione to determine both glutathione synthesis and concentration by gas chromatography-mass spectrometry (GCMS). J Mass Spectrom 36: 726–735.",{"doi":319},{"id":315,"text":1016,"url":317,"identifiers":1017},"Jahoor F, Jackson A, Gazzard B, et al (1999) Erythrocyte glutathione deficiency in symptom-free HIV infection is associated with decreased synthesis rate. Am J Physiol 276: E205–E211.",{"doi":319},{"id":315,"text":1019,"url":317,"identifiers":1020},"Kluijtmans LA, Boers GH, Kraus JP, et al (1999) The molecular basis of cystathionine beta-synthase deficiency in Dutch patients with homocystinuria: effect of CBS genotype on biochemical and clinical phenotype and on response to treatment. Am J Hum Genet 65: 59–67.",{"doi":319},{"id":1022,"text":1023,"url":1024,"identifiers":1025},"7ab40536-1145-467a-bb7d-71ad25375a47","Lee PL, Briddon A (2007) A rationale for cystine supplementation in severe homocystinuria. J Inherit Metab Dis 30: 35–38.","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1007\u002Fs10545-006-0452-3",{"doi":1026},"10.1007\u002Fs10545-006-0452-3",{"id":315,"text":1028,"url":317,"identifiers":1029},"Lu SC (1999) Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J 13: 1169–1183.",{"doi":319},{"id":315,"text":1031,"url":317,"identifiers":1032},"Lyons J, Rauh-Pfeiffer A, Yu YM, et al (2000) Blood glutathione synthesis rates in healthy adults receiving a sulfur amino acid-free diet. Proc Natl Acad Sci USA 97: 5071–5076.",{"doi":319},{"id":315,"text":1034,"url":317,"identifiers":1035},"MacCoss MJ, Fukagawa NK, Matthews (2001) Measurement of intracellular sulfur amino acid metabolism in humans. Am J Physiol Endocrinol Metab 280: E947–E955.",{"doi":319},{"id":20,"text":1037,"url":20,"identifiers":1038},"Millward DJ (1998) Metabolic demands for amino acids and the human dietary requirement: Millward and Rivers (1988) revisited. J Nutr 128: 2563S–2576S.",{},{"id":315,"text":1040,"url":317,"identifiers":1041},"Mudd SH, Skovby F, Levy HL, et al (1985) The natural history of homocystinuria due to cystathionine beta-synthase deficiency. Am J Hum Genet 37: 1–31.",{"doi":319},{"id":315,"text":1043,"url":317,"identifiers":1044},"Obled C, Papet I, Breuille D (2002) Metabolic bases of amino acid requirements in acute diseases. Curr Opin Clin Nutr Metab Care 5: 189–197.",{"doi":319},{"id":315,"text":1046,"url":317,"identifiers":1047},"Orendac M, Zeman J, Stabler SP, et al (2003) Homocystinuria due to cystathionine beta-synthase deficiency: novel biochemical findings and treatment efficacy. J Inherit Metab Dis 26: 761–773.",{"doi":319},{"id":315,"text":1049,"url":317,"identifiers":1050},"Perna AF, Ingrosso D, De Santo NG (2003) Homocysteine and oxidative stress. Amino Acids 25: 409–417.",{"doi":319},{"id":315,"text":1052,"url":317,"identifiers":1053},"Raguso CA, Regan MM, Young VR (2000) Cysteine kinetics and oxidation at different intakes of methionine and cystine in young adults. Am J Clin Nutr 71: 491–499.",{"doi":319},{"id":1055,"text":1056,"url":1057,"identifiers":1058},"5d8429f8-ae7b-4e31-b59d-ffa75e751015","Refsum H, Fredriksen A, Meyer K, Ueland PM, Kase BF (2004) Birth prevalence of homocystinuria. J Pediatr 144: 830–832.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0022347604001805",{"doi":1059},"10.1016\u002Fj.jpeds.2004.03.004",{"id":1061,"text":1062,"url":1063,"identifiers":1064},"bb1f9c28-0386-4af1-a793-83790ae01d27","Sharma P, Senthilkumar RD, Brahmachari V, et al (2006) Mining literature for a comprehensive pathway analysis: a case study for retrieval of homocysteine related genes for genetic and epigenetic studies. Lipids Health Dis 5: 1.","https:\u002F\u002Flipidworld.biomedcentral.com\u002Farticles\u002F10.1186\u002F1476-511X-5-1",{"doi":1065},"10.1186\u002F1476-511x-5-1",{"id":315,"text":1067,"url":317,"identifiers":1068},"Walter JH, Wraith JE, White FJ, Bridge C, Till J (1998) Strategies for the treatment of cystathionine beta-synthase deficiency: the experience of the Willink Biochemical Genetics Unit over the past 30 years. Eur J Pediatr 157: S71–S76.",{"doi":319},{"id":315,"text":1070,"url":317,"identifiers":1071},"Weiss N, Zhang YY, Heydrick S, Bierl C, Loscalzo J (2001) Overexpression of cellular glutathione peroxidase rescues homocyst(e)ine-induced endothelial dysfunction. Proc Natl Acad Sci USA 98: 12503–12508.",{"doi":319},{"id":315,"text":1073,"url":317,"identifiers":1074},"Weiss N, Heydrick S, Zhang YY, Bierl C, Cap A, Loscalzo J (2002) Cellular redox state and endothelial dysfunction in mildly hyperhomocysteinemic cystathionine beta-synthase-deficient mice. Arterioscler Thromb Vasc Biol 22: 34–41.",{"doi":319},{"id":20,"text":1076,"url":1077,"identifiers":1078},"Yap S (2005) Homocystinuria due to cystathionine β-synthase deficiency. Professor Jean-Marie Saudubray. Orphanet encyclopedia 2005. http:\u002F\u002Fwww.orpha.net\u002Fdata\u002Fpatho\u002FGB\u002Fuk-CbS.pdf.","http:\u002F\u002Fwww.orpha.net\u002Fdata\u002Fpatho\u002FGB\u002Fuk-CbS.pdf",{},{"id":20,"text":1080,"url":20,"identifiers":1081},"Yap S, Boers GH, Wilcken B, et al (2001) Vascular outcome in patients with homocystinuria due to cystathionine beta-synthase deficiency treated chronically: a multicenter observational study. Arterioscler Thromb Vasc Biol 21: 2080–2085.",{},{"id":1083,"createTime":1084,"updateTime":1085,"relativeEntities":1086,"slug":1087,"properties":1088,"entityType":114,"verifyStatus":115,"verifyTime":1099,"verifyNote":117,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1100,"fullTextUrl":20,"authors":1101,"publicationType":149,"publisherRelationship":1117,"citationCount":21,"citationInfo":1168,"publishDate":1170,"publishYear":979,"citationAnalyzeStatus":19,"lastCitationAnalyze":1171,"indexDatabases":1172,"openAccess":20,"references":20,"isForceReanalyzing":207},"1d36ee22-1d13-44ad-80ee-68ceb466fc5f","2024-01-18T16:02:18.752+00:00","2026-07-22T15:57:56.569+00:00",[],"Classifying-tetrahydrobiopterin-responsiveness-in-the-hyperphenylalaninaemias",{"abstract":1089,"title":1091,"gsPaper":1093,"references":1095,"doi":1097},{"EN":1090},"A significant percentage of patients with hyperphenylalaninaemia (HPA) due to primary deficiency of the phenylalanine hydroxylase enzyme (PAH) respond to a dose of tetrahydrobiopterin (BH4) with an increased rate of phenylalanine (Phe) disposal. The effect is exploited therapeutically, with some patients on BH4 even tolerating a normal diet. Classification of the Phe blood level response to a BH4 load by percentage reduction (PR) suffers from loss of information: only part of usually more extensive test data is used, and PR values for different times after load cannot be compared directly. Calculation of half-life (t\n                           1\u002F2) of blood Phe is proposed as an alternative. This classic measure unifies interpretation of tests of different duration (e.g. 8 or 15 h). t\n                           1\u002F2 subsumes first-order formation of tyrosine, of Phe metabolites, and renal Phe excretion; zero-order net protein synthesis can be neglected during short-time tests. \n                           t\n                           1\u002F2 is easily and robustly obtained by fit-ting the total set of (3–4) data points to a log-linear regression. The advantage of calculating t\n                           1\u002F2 is exemplified by the analysis of selected published data. The results clearly speak in favour of an 8 h test period because so-called ‘slow’ responders could also be detected within this time window and because tests of longer duration are less reliable kinetically. Sequential Phe and Phe\u002FBH4 loading tests appear advantageous because the ‘natural’ t\n                           1\u002F2 (without supplementation of BH4) is not normally known beforehand. With t\n                           1\u002F2 as a reliable parameter of BH4 responsiveness, therapeutic decisions would be more rational and genotype–phenotype analysis may also profit.",{"EN":1092},"Classifying tetrahydrobiopterin responsiveness in the hyperphenylalaninaemias",{"VOID":1094},"[\"18038613729473607512\"]",{"VOID":1096},"Bartholomé K (1974) Letter: A new molecular defect in phenylketonuria. Lancet 2 (7896): 1580.\nBernegger C, Blau N (2002) High frequency of tetrahydrobiopterin-responsiveness among hyperphenylalaninemias: a study of 1919 patients observed from 1988 to 2002. Mol Genet Metab 77: 304–313.\nBélanger-Quintana A, Garcia MJ, Castro M, et al (2005) Spanish BH4-responsive phenylalanine hydoxylase-deficient patients: Evolution of seven patients on long-term treatment with tetrahydrobiopterin. Mol Gen Metab 86(Supplement 1): S61–S66.\nBlau N, Erlandsen H (2004) The metabolic and molecular bases of tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. Mol Genet Metab 82: 101–111.\nBoneh A, Francis DM, Humphrey M, et al (2006) Three-year audit of the hyperphenylalaninaemia\u002Fphenylketonuria spectrum in Victoria. J Pediatr Child Health 42: 496–498.\nCurtius HC, Niederwieser A, Viscontini M, et al (1979) Atypical phenylketonuria due to tetrahydrobiopterin deficiency. Diagnosis and treatment with tetrahydrobiopterin, dihydrobiopterin and sepiapterin. Clin Chim Acta 93: 251–262.\nDanks DM, Bartholomé K, Clayton BE, et al (1978) Malignant hyperphenylalaninaemia – Current status (June 1977). J Inherit Metab Dis 1: 49–53.\nDanks DM, Cotton RGH, Schlesinger P (1979) Diagnosis of malignant hyperphenylalaninemia. Arch Dis Child 54: 329–330.\nDesviat LR, Pérez B, Bèlanger-Quintana A, et al (2004) Tetrahydrobiopterin responsiveness: results of the BH4 loading test in 31 Spanish PKU patients and correlation with their genotype. Mol Genet Metab 83: 157–162.\nErlandsen H, Pey AL, Gámez A, et al (2004) Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proc Natl Acad Sci USA 101: 16903–16908.\nEMEA: European Medicines Agency, Committee for Orphan Medicinal Products (29 May 2007) Public summary of positive opinion for orphan designation of tetrahydrobiopterin for the treatment of hyperphenylalaninemia. Doc.Ref.: EMEA\u002FCOMP\u002F258\u002F04 Rev. 2.\nFiege B, Blau N (2007) Assessment of tetrahydrobiopterin (BH4) responsiveness in phenylketonuria. J Pediatr 150: 627–630.\nFiege B, Bonafé L, Ballhausen D, et al (2005) Extended tetrahydrobiopterin loading test in the diagnosis of cofactor-responsive phenylketonuria: A pilot study. Mol Genet Metab 86: S91–S95.\nFiori L, Fiege B, Riva E, et al (2005) Incidence of BH4-responsiveness in phenylalanine-hydroxylase-deficient Italian patients. Mol Genet Metab 86: S67–S74.\nHabich MS (2006) Pharmakologische Therapie der Phenylketonurie durch Defekt der Phenylalaninhydroxylase mit Tetrahydrobiopterin: Effekt auf Metabolite, in vivo Enzymaktivität und Proteintoleranz. Med. Thesis, Ludwig-Maximilian-University, Munich.\nKure S, Hou DC, Ohura T, et al (1999) Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency. J Pediatr 135: 375–378.\nLangenbeck U, Wendel U (1997) Kinetic analysis of phenylalanine disposal in phenylalanine hydroxylase (PAH) deficiency. Int Pediatr 12: 19–22.\nLangenbeck U, Zschocke J, Wendel U, Hönig V (2001) Modelling the phenylalanine blood level response during treatment of phenylketonuria. J Inherit Metab Dis 24: 805–814.\nLeatherbarrow RJ (1987) ENZFITTER. A Non-linear Regression Data Analysis Program for the IBM PC (and True Compatibles). Cambridge, UK: Elsevier-BIOSOFT.\nLindner M, Steinfeld R, Burgard P, et al (2003) Tetrahydrobiopterin sensitivity in German patients with mild phenylalanine hydroxylase deficiency. Hum Mutat 21: 400 (Mutation in brief #588).\nMuntau AC, Röschinger W, Habich M, et al (2002) Tetrahydrobiopterin as an alternative treatment for mild phenylketonuria. N Engl J Med 347: 2122–2132.\nNiederwieser A, Ponzone A, Curtius H-Ch (1985) Differential diagnosis of tetrahydrobiopterin deficiency. J Inherit Metab Dis 8(Supplement 1): 34–38.\nPorta F, MussaA, Ferraris S, et al (2007) ‘Responsiveness’ and unresponsiveness to BH4 of PAH deficiency. J Inherit Metab Dis 30(Supplement 1): 16.\nRey F, Blandin-Savoja F, Rey J (1979) Kinetics of phenylalanine disappearance after intra-venous load in phenylketonuria and its variants. Pediatr Res 13: 21–25.\nRitschel WA (1982) Handbook of Basic Pharmakokinetics, 2nd edn. Hamilton, IL: Drug Intelligence Publications.\nRosenberg LE (1976) Vitamin-responsive inherited metabolic disorders. Adv Hum Genet 6: 1–74.\nSchadewaldt P, Dalle-Feste C, Langenbeck U, Wendel U (1991) Oral l-alloisoleucine loading studies in healthy subjects and in patients with maple syrup urine disease. Pediatr Res 30: 430–434.\nShintaku H, Kure S, Ohura T, et al (2004) Long-term treatment and diagnosis of tetrahydrobiopterin-responsive hyperphenylalaninemia with a mutant phenylalanine hydroxylase gene. Pediatr Res 55: 425–430.\nSmith I, Lloyd J (1974) Proceedings: Atypical phenylketonuria accompanied by severe progressive neurological illness unresponsive to dietary treatment. Arch Dis Child 49: 245.\nSnyderman SE, Norton PM, Roitman E, Holt LE Jr (1964) Maple syrup urine disease, with particular reference to dietotherapy. Pediatrics 34: 454–472.\nSteinfeld R, Kohlschütter A, Zschocke J, Lindner M, Ullrich K, Lukacs Z (2002) Tetrahydrobiopterin monotherapy for phenylketonuria patients with common mild mutations. Eur J Pediatr 161: 403–405.\nTrefz FK, Aulehla-Scholz C, Blau N (2001) Successful treatment of phenylketonuria with tetrahydrobiopterin. Eur J Pediatr 160: 315.\nTrefz F, Burton B, Longo N, et al (2007) The effect of sapropterin dihydrochloride (tetrahydrobiopterin or 6R-BH4) treatment on phenylalanine (Phe) tolerance in children with phenylketonuria controlled on a Phe-restricted diet. J Inherit Metab Dis 30(Supplement 1): 17.\nZurflüh MR, Fiori L, Fiege B, et al (2006) Pharmacokinetics of orally administered tetrahydrobiopterin in patients with phenylalanine hydroxylase deficiency. 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To date, DHTKD1 mutations have been reported in two alpha-aminoadipic and alpha-ketoadipic aciduria patients. We have now sequenced DHTKD1 in nine patients diagnosed with alpha-aminoadipic and alpha-ketoadipic aciduria as well as one patient with isolated alpha-aminoadipic aciduria, and identified causal mutations in eight. We report nine novel mutations, including three missense mutations, two nonsense mutations, two splice donor mutations, one duplication, and one deletion and insertion. Two missense mutations, one of which was reported before, were observed in the majority of cases. The clinical presentation of this group of patients was inhomogeneous. Our results confirm that alpha-aminoadipic and alpha-ketoadipic aciduria is caused by mutations in DHTKD1, and further establish that DHTKD1 encodes the E1 subunit of the alpha-ketoadipic acid dehydrogenase complex.",{"EN":1183},"Genetic basis of alpha-aminoadipic and alpha-ketoadipic aciduria",{"VOID":1185},"[\"15907346746988680976\"]",{"VOID":1187},"Bunik VI, Degtyarev D (2008) Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins. Proteins 71:874–890\nCasey RE, Zaleski WA, Philp M, Mendelson IS, MacKenzie SL (1978) Biochemical and clinical studies of a new case of alpha-aminoadipic aciduria. J Inherit Metab Dis 1:129–135\nDanhauser K, Sauer SW, Haack TB et al (2012) DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria. Am J Hum Genet 91:1082–1087\nde Ligt J, Willemsen MH, van Bon BW et al (2012) Diagnostic exome sequencing in persons with severe intellectual disability. N Engl J Med 367:1921–1929\nDuran M, Beemer FA, Wadman SK, Wendel U, Janssen B (1984) A patient with alpha-ketoadipic and alpha-aminoadipic aciduria. J Inherit Metab Dis 7:61\nDuran M, Dorland L, Wadman SK, Berger R (1994) Group tests for selective screening of inborn errors of metabolism. Eur J Pediatr 153:S27–S32\nFiermonte G, Dolce V, Palmieri L et al (2001) Identification of the human mitochondrial oxodicarboxylate carrier. Bacterial expression, reconstitution, functional characterization, tissue distribution, and chromosomal location. J Biol Chem 276:8225–8230\nFischer MH, Brown RR (1980) Tryptophan and lysine metabolism in alpha-aminoadipic aciduria. Am J Med Genet 5:35–41\nFischer MH, Gerritsen T, Opitz JM (1974) Alpha-aminoadipic aciduria, a non-deleterious inborn metabolic defect. Humangenetik 24:265–270\nGilissen C, Hehir-Kwa JY, Thung DT et al (2014) Genome sequencing identifies major causes of severe intellectual disability. Nature 511:344–347\nGoodman SI, Duran M (2014) Biochemical phenotypes of questionable clinical significance. In Blau N, Duran M, Gibson KM, Dionisi-Vici C eds. Physician’s guide to the diagnosis, treatment, and follow-up of inherited metabolic diseases. Heidelberg: Springer, pp 691–705\nGray RGF, O’Neill EM, Pollitt RJ (1979) α-aminoadipic aciduria: chemical and enzymatic studies. J Inherit Metab Dis 2:89–92\nGuescini M, Sisti D, Rocchi MB, Stocchi L, Stocchi V (2008) A new real-time PCR method to overcome significant quantitative inaccuracy due to slight amplification inhibition. BMC Bioinformatics 9:326\nHouten SM, te Brinke H, Denis S et al (2013) Genetic basis of hyperlysinemia. Orphanet J Rare Dis 8:57\nLehnert W (1994) Long-term results of selective screening for inborn errors of metabolism. Eur J Pediatr 153:S9–S13\nLormans S, Lowenthal A (1974) Alpha-amino adipic aciduria in an oligophrenic child. Clin Chim Acta 57:97–101\nManders AJ, von Oostrom CG, Trijbels JM, Rutten FJ, Kleijer WJ (1981) alpha-Aminoadipic aciduria and persistence of fetal haemoglobin in an oligophrenic child. Eur J Pediatr 136:51–55\nPeng H, Shinka T, Inoue Y et al (1999) Asymptomatic alpha-ketoadipic aciduria detected during a pilot study of neonatal urine screening. Acta Paediatr 88:911–914\nPrzyrembel H, Bachmann D, Lombeck I et al (1975) Alpha-ketoadipic aciduria, a new inborn error of lysine metabolism; biochemical studies. Clin Chim Acta 58:257–269\nSewell AC, Herwig J, Bohles H, Abeling NG, van Gennip AH (1999) Normal kynurenine metabolism in 2-oxoadipic aciduria. J Inherit Metab Dis 22:949–950\nTakechi T, Okada T, Wakiguchi H et al (1993) Identification of N-acetyl-alpha-aminoadipic acid in the urine of a patient with alpha-aminoadipic and alpha-ketoadipic aciduria. J Inherit Metab Dis 16:119–126\nVianey-Liaud C, Divry P, Cotte J, Teyssier G (1985) alpha-Aminoadipic and alpha-ketoadipic aciduria: detection of a new case by a screening program using two-dimensional thin layer chromatography of amino acids. J Inherit Metab Dis 8(Suppl 2):133–134\nWendel U, Rudiger HW, Przyrembel H, Bremer HJ (1975) Alpha-ketoadipic aciduria: degradation studies with fibroblasts. Clin Chim Acta 58:271–276\nWilcken B, Smith A, Brown DA (1980) Urine screening for aminoacidopathies: is it beneficial? Results of a long-term follow-up of cases detected by screening one millon babies. J Pediatr 97:492–497\nWilson RW, Wilson CM, Gates SC, Higgins JV (1975) Alpha-ketoadipic aciduria: a description of a new metabolic error in lysine-tryptophan degradation. Pediatr Res 9:522–526\nWu Y, Williams EG, Dubuis S et al (2014) Multilayered genetic and omics dissection of mitochondrial activity in a mouse reference population. Cell 158:1415–1430\nXu WY, Gu MM, Sun LH et al (2012) A nonsense mutation in DHTKD1 causes Charcot-Marie-Tooth disease type 2 in a large Chinese pedigree. Am J Hum Genet 91:1088–1094\nXu W, Zhu H, Gu M et al (2013) DHTKD1 is essential for mitochondrial biogenesis and function maintenance. FEBS Lett 587:3587–3592\nYang Y, Muzny DM, Reid JG et al (2013) Clinical whole-exome sequencing for the diagnosis of mendelian disorders. 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Although the primary manifestations of the disease are hepatic or neurological in scope, the factors that cause a very diverse picture of WD are not well researched. We compared the first clinical presentation, ages of onset and diagnosis, copper metabolism parameters, and ceruloplasmin levels between index cases (ICs) and their siblings. We examined 73 ICs and 95 siblings from 73 families, including a total of 168 patients with biochemical and genetically confirmed WD diagnoses. We observed an 86 % concordance rate of primary clinical symptoms among ICs with hepatic symptoms and their siblings. There was 66 % concordance among ICs with neurological symptoms and their siblings. No differences regarding age at onset of symptoms or copper metabolism parameters at diagnosis were identified between hepatic ICs and their siblings. The age at symptom onset did not differ between neurological ICs and their siblings, although ICs presented lower ceruloplasmin and serum copper levels. 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Nat Clin Pract Neurol 2(9):482–493\nDeguti MM, Genschel J, Cancado ELR et al (2004) Wilson disease: novel mutations in the ATP7B gene and clinical correlation in Brazilian patients. Hum Mutat 23:398\nFerenci P, Caca K, Loudianos G et al (2003) Diagnosis and phenotypic classification of Wilson disease. Liver Int 23:139–142\nGromadzka G, Członkowska A (2011) Influence of IL-1RN intron 2 variable number of tandem repeats (VNTR) polymorphism on the age at onset of neuropsychiatric symptoms in Wilson’s disease. Int J Neurosci 121:8–15\nGromadzka G, Schmidt HH, Genschel J et al (2005) Frameshift and nonsense mutations in the gene for ATPase7B are associated with severe impairment of copper metabolism and with an early clinical manifestation of Wilson’s disease. Clin Genet 68:524–532\nGromadzka G, Schmidt HH, Genschel J et al (2006) p.H1069Q mutation in ATP7B and biochemical parameters of copper metabolism and clinical manifestation of Wilson’s disease. Mov Disord 21:245–248\nGromadzka G, Rudnicka M, Chabik G, Przybyłkowski A, Członkowska A (2011) Genetic variability in the methylenetetrahydrofolate reductase gene (MTHFR) affects clinical expression of Wilson’s diseases. J Hepatol 55:913–919\nGupta A, Chattopadhyay I, Dey S et al (2007) Molecular pathogenesis of Wilson disease among Indians: a perspective on mutation spectrum in ATP7B gene, prevalent defects, clinical heterogeneity and implication towards diagnosis. Cell Mol Neurobiol 27(8):1023–1033\nGutteridge JMC (1978) Ceruloplasmin: a plasma protein, enzyme and anti-oxidant. Ann Clin Biochem 15:293–296\nHa-Hao D, Hefter H, Stremmel W et al (1998) His1069Gln and six novel Wilson disease mutations: analysis of relevance for early diagnosis and phenotype. Eur J Hum Genet 6:616–623\nHouwen RH, Juyn J, Hoogenraad TU, Ploos van Amstel JK, Berger R (1995) H714Q mutation in Wilson disease is associated with late, neurological presentation. J Med Genet 32:480–482\nLinder MC, Wooten L, Cerveza P, Cotton S, Shulze R, Lomeli N (1998) Copper transport. Am J Clin Nutr 67:965–971\nLitwin T, Członkowska A (2013) Wilson disease—factors affecting clinical presentation. Neurol Neurochir Pol 47:161–169\nLitwin T, Gromadzka G, Członkowska A (2012) Apolipoprotein E gene (APOE) genotype in Wilson’s disease: impact on clinical presentation. Parkinsonism Relat Disord 18:367–369\nMcGue M (1992) When assessing twin concordance, use the probandwise not the pairwise rate. Schizophr Bull 18:171–176\nMerle U, Stremmel W, Gesner R (2006) Influence of homozygosity for methionine at codon 129 of the human prion gene on the onset of neurological and hepatic symptoms in Wilson’s disease. Arch Neurol 63:982–985\nMillhauser GL (2004) Copper binding in the prion protein. Acc Chem Res 37:79–85\nMulthaup G, Schlicksupp A, Hesse L et al (1996) The amyloid precursor protein of Alzheimer’s disease in the reduction of copper(II) to copper(I). Science 271:1406–1409\nOlsson C, Waldenström E, Westermark K, Landegren U, Syvänen AC (2000) Determination of the frequencies of ten allelic variants of the Wilson disease gene (ATP7B), in pooled DNA samples. Eur J Hum Genet 8:933–938\nProdan CI, Holland NR, Wisdom PJ, Burstein SA, Bottomley SS (2002) CNS demyelination associated with copper deficiency and hyperzincemia. Neurology 59:1453–1456\nRankin J, Auer-Grumbach M, Bagg W et al. (2008) Extreme phenotypic diversity and nonpenetrance in families with the LMNA gene mutation R644C. Am J Med Genet 146:1530–1542.\nRavin HA (1961) An improved colorimetric assay of ceruloplasmin. J Lab Clin Med 61:161–168\nSanthosh S, Shaji RV, Eapen CE et al (2008) Genotype phenotype correlation in Wilson’s disease within families—a report on four south Indian families. World J Gastroenterol 14:4672–4676\nScheinberg IH, Sternlieb I (1984) Wilson’s disease. In: Lloyd H, Smith J (eds) Major problems in internal medicine. Saunders, Philadelphia, p 23\nSchiefermeier M, Kollegger H, Madl C et al (2000) The impact of, apolipoprotein E genotypes on age at onset of, symptoms and phenotypic expression in Wilson’s disease. Brain 123:585–590\nScriver CR, Waters PJ (1999) Monogenic traits are not simple: lessons from phenylketonuria. Trends Genet 15:267–272\nSmith C (1974) Concordance in twins: methods and interpretation. Am J Hum Genet 26:454–466\nStapelbroek JM, Bollen CW, van Amstel JK et al (2004) The H1069Q mutation in ATP7B is associated with late and neurologic presentation in Wilson disease: results of a meta-analysis. J Hepatol 41:758–763\nTakeshita Y, Shimizu N, Yamaguchi Y et al (2002) Two families with Wilson disease in which siblings showed different phenotypes. J Hum Genet 47:543–547\nVrabelova S, Letocha O, Borsky M, Kozak L (2005) Mutation analysis of the ATP7B gene and genotype\u002Fphenotype correlation in 227 patients with Wilson disease. 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