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Volumn , Issue , 2012, Pages 311-321

Disorders of sulfur amino acid metabolism

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EID: 84897093600     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-15720-2_21     Document Type: Chapter
Times cited : (4)

References (47)
  • 1
    • 0032521543 scopus 로고    scopus 로고
    • Homozygous cystathionine beta-synthase deficiency, combined with factor V Leiden or thermolabile methylenetetrahydrofolate reductase in the risk of venous thrombosis
    • Kluijtmans LA, Boers GH, Verbruggen B et al. (1998) Homozygous cystathionine beta-synthase deficiency, combined with factor V Leiden or thermolabile methylenetetrahydrofolate reductase in the risk of venous thrombosis. Blood 91:2015-2018
    • (1998) Blood , vol.91 , pp. 2015-2018
    • Kluijtmans, L.A.1    Boers, G.H.2    Verbruggen, B.3
  • 2
    • 77953558673 scopus 로고    scopus 로고
    • The clinical aspects of cystathionine B-synthase deficiency: How wide is the spectrum? Italian Collaborative Study Group on Homocystinuria
    • De Franchis R, Sperandeo MP, Sebastio G, Andria G (1998) The clinical aspects of cystathionine B-synthase deficiency: how wide is the spectrum? Italian Collaborative Study Group on Homocystinuria. Eur J Pediatr 157:867-870
    • (1998) Eur J Pediatr , vol.157 , pp. 867-870
    • De Franchis, R.1    Sperandeo, M.P.2    Sebastio, G.3    Ria, G.4
  • 3
    • 0021894152 scopus 로고
    • The natural history of homocystinuria due to cystathionine R-synthase deficiency
    • Mudd SH, Skovby F, Levy HL et al. (1985) The natural history of homocystinuria due to cystathionine R-synthase deficiency. Am J Hum Genet 37:1-31
    • (1985) Am J Hum Genet , vol.37 , pp. 1-31
    • Mudd, S.H.1    Skovby, F.2    Levy, H.L.3
  • 4
    • 71649116022 scopus 로고    scopus 로고
    • A revisit to the natural history of homocystinuria due to cystathionine beta-synthase deficiency
    • Skovby F, Gaustadnes M, Mudd SH (2010) A revisit to the natural history of homocystinuria due to cystathionine beta-synthase deficiency. Mol Genet Metab 99:1-3
    • (2010) Mol Genet Metab , vol.99 , pp. 1-3
    • Skovby, F.1    Gaustadnes, M.2    Mudd, S.H.3
  • 5
    • 0036689371 scopus 로고    scopus 로고
    • Reproductive fitness in maternal homocystinuria due to cystathionine beta-synthase deficiency
    • Levy HL, Vargas JE, Waisbren SE et al. (2002) Reproductive fitness in maternal homocystinuria due to cystathionine beta-synthase deficiency. J Inherit Metab Dis 25:299-314
    • (2002) J Inherit Metab Dis , vol.25 , pp. 299-314
    • Levy, H.L.1    Vargas, J.E.2    Waisbren, S.E.3
  • 6
    • 0022262196 scopus 로고
    • Recent advances in the mechanism of pyridoxine- responsive disorders
    • Fowler B (1985) Recent advances in the mechanism of pyridoxine- responsive disorders. J Inherit Metab Dis 8 [Suppl 1]:76-83
    • (1985) J Inherit Metab Dis , vol.8 , pp. 76-83
    • Fowler, B.1
  • 7
    • 64049095638 scopus 로고    scopus 로고
    • The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease
    • Jakubowski H (2008) The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease. J Physiol Pharmacol. 59 (S9)155-167
    • (2008) J Physiol Pharmacol , vol.59 , pp. 155-167
    • Jakubowski, H.1
  • 8
    • 0028937163 scopus 로고
    • Mice deficient in cystathionine beta-synthase: Animal models for mild and severe homocyst(e)inemia
    • Watanabe M, Osada J, Aratani Y et al. (1995) Mice deficient in cystathionine beta-synthase: animal models for mild and severe homocyst(e)inemia Proc Natl Acad Sci U S A 92:1585-1589
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1585-1589
    • Watanabe, M.1    Osada, J.2    Aratani, Y.3
  • 9
    • 3142749051 scopus 로고    scopus 로고
    • Cystathionine beta-synthase: Structure, function, regulation, and location of homocystinuria-causing mutations
    • Miles EW, Kraus JP (2004) Cystathionine beta-synthase: structure, function, regulation, and location of homocystinuria-causing mutations. J Biol Chem 279:29871-29874
    • (2004) J Biol Chem , vol.279 , pp. 29871-29874
    • Miles, E.W.1    Kraus, J.P.2
  • 10
    • 0029852838 scopus 로고    scopus 로고
    • A 68 bp insertion found in a homocystinuric patient is a common variant and is skipped by alternative splicing of the cystathionine β-synthase mRNA
    • Sperandeo MP, de Franchis R, Andria G, Sebastio G (1996) A 68 bp insertion found in a homocystinuric patient is a common variant and is skipped by alternative splicing of the cystathionine β-synthase mRNA. Am J Hum Genet 59:1391-1393
    • (1996) Am J Hum Genet , vol.59 , pp. 1391-1393
    • Sperandeo, M.P.1    De Franchis, R.2    Ria, G.3    Sebastio, G.4
  • 11
    • 0037110456 scopus 로고    scopus 로고
    • Regulation of 3’ splice site selection in the 844ins68 polymorphism of the cystathionine beta-synthase gene
    • Romano M, Marcucci R, Buratti E et al. (2002) Regulation of 3’ splice site selection in the 844ins68 polymorphism of the cystathionine beta-synthase gene. J Biol Chem 277:43821-43829
    • (2002) J Biol Chem , vol.277 , pp. 43821-43829
    • Romano, M.1    Marcucci, R.2    Buratti, E.3
  • 12
    • 9144225352 scopus 로고    scopus 로고
    • Facts and recommendations about total homocysteine determinations: An expert opinion
    • Refsum H, Smith AD, Ueland PM et al. (2004) Facts and recommendations about total homocysteine determinations: an expert opinion. Clin Chem 50:3-32
    • (2004) Clin Chem , vol.50 , pp. 3-32
    • Refsum, H.1    Smith, A.D.2    Ueland, P.M.3
  • 13
    • 0032750462 scopus 로고    scopus 로고
    • Reduction of false negative results in screening of newborns for homocystinuria
    • Peterschmitt MJ, Simmons JR, Levy HL (1999) Reduction of false negative results in screening of newborns for homocystinuria. N Engl J Med 341:1572-1576
    • (1999) N Engl J Med , vol.341 , pp. 1572-1576
    • Peterschmitt, M.J.1    Simmons, J.R.2    Levy, H.L.3
  • 14
    • 77049123198 scopus 로고    scopus 로고
    • Newborn population screening for classic homocystinuria by determination of total homocysteine from Guthrie cards
    • Gan-Schreier H, Kebbewar M, Fang-Hoffmann J et al. (2010) Newborn population screening for classic homocystinuria by determination of total homocysteine from Guthrie cards. J Pediatr 156:427-432
    • (2010) J Pediatr , vol.156 , pp. 427-432
    • Gan-Schreier, H.1    Kebbewar, M.2    Fang-Hoffmann, J.3
  • 15
    • 84920230174 scopus 로고
    • Prenatal diagnosis of homocystinuria
    • Fowler B, Borresen AL, Boman N (1982) Prenatal diagnosis of homocystinuria. Lancet 2:875
    • (1982) Lancet , vol.2 , pp. 875
    • Fowler, B.1    Borresen, A.L.2    Boman, N.3
  • 16
    • 0028917268 scopus 로고
    • Hyperhomocysteinemia in premature arterial disease: Examination of cystathionine beta-synthase alleles at the molecular level
    • Kozich V, Kraus E, de Franchis R et al. (1995) Hyperhomocysteinemia in premature arterial disease: examination of cystathionine beta-synthase alleles at the molecular level. Hum Mol Genet 4:623-629
    • (1995) Hum Mol Genet , vol.4 , pp. 623-629
    • Kozich, V.1    Kraus, E.2    De Franchis, R.3
  • 17
    • 18244379372 scopus 로고    scopus 로고
    • Progressive cerebral edema associated with high methionine levels and betaine therapy in a patient with cystathionine beta-synthase (CBS) deficiency
    • Yaghmai R, Kashani AH, Geraghty MT et al. (2002) Progressive cerebral edema associated with high methionine levels and betaine therapy in a patient with cystathionine beta-synthase (CBS) deficiency. Am J Med Genet 108:57-63
    • (2002) Am J Med Genet , vol.108 , pp. 57-63
    • Yaghmai, R.1    Kashani, A.H.2    Geraghty, M.T.3
  • 18
    • 0034828509 scopus 로고    scopus 로고
    • The intellectual abilities of early-treated individuals with pyridoxine-nonresponsive homocystinuria due to cystathionine beta-synthase deficiency
    • Yap S, Rushe H, Howard PM, Naughten ER (2001) The intellectual abilities of early-treated individuals with pyridoxine-nonresponsive homocystinuria due to cystathionine beta-synthase deficiency. J Inherit Metab Dis 24:437-447
    • (2001) J Inherit Metab Dis , vol.24 , pp. 437-447
    • Yap, S.1    Rushe, H.2    Howard, P.M.3    Naughten, E.R.4
  • 19
    • 0038497517 scopus 로고    scopus 로고
    • Classical homocystinuria: Vascular risk and its prevention
    • Yap S (2003) Classical homocystinuria: vascular risk and its prevention. J Inherit Metab Dis 26:259-265
    • (2003) J Inherit Metab Dis , vol.26 , pp. 259-265
    • Yap, S.1
  • 20
    • 77952368285 scopus 로고    scopus 로고
    • Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: Purification and characterization of eight CBS mutant enzymes
    • Majtan T, Liu L, Carpenter JF, Kraus JP (2010) Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes. J Biol Chem 285:15866-15873
    • (2010) J Biol Chem , vol.285 , pp. 15866-15873
    • Majtan, T.1    Liu, L.2    Carpenter, J.F.3    Kraus, J.P.4
  • 21
    • 77954134566 scopus 로고    scopus 로고
    • Restoring assembly and activity of cystathionine beta-synthase mutants by ligands and chemical chaperones
    • Kopecka J, Krijt J, Rakova K, Kožich V (2010) Restoring assembly and activity of cystathionine beta-synthase mutants by ligands and chemical chaperones. J Inherit Metab Dis 34:39-48
    • (2010) J Inherit Metab Dis , vol.34 , pp. 39-48
    • Kopecka, J.1    Krijt, J.2    Rakova, K.3    Kožich, V.4
  • 22
    • 76749160942 scopus 로고    scopus 로고
    • Kruger WD (2010) Activation of mutant enzyme function in vivo by proteasome inhibitors and treatments that induce Hsp70
    • Singh LR, Gupta S, Honig NH, Kraus JP, Kruger WD (2010) Activation of mutant enzyme function in vivo by proteasome inhibitors and treatments that induce Hsp70. PLoS Genet 2010 6:e1000807
    • (2010) Plos Genet , vol.6
    • Singh, L.R.1    Gupta, S.2    Honig, N.H.3    Kraus, J.P.4
  • 23
    • 0034535031 scopus 로고    scopus 로고
    • Isolated hypermethioninemia: Measurements of S-adenosylmethionine and choline
    • Mudd SH, Jenden DJ, Capdevila A et al. (2000) Isolated hypermethioninemia: measurements of S-adenosylmethionine and choline. Metabolism 49:1542-1547
    • (2000) Metabolism , vol.49 , pp. 1542-1547
    • Mudd, S.H.1    Jenden, D.J.2    Capdevila, A.3
  • 24
    • 69449103947 scopus 로고    scopus 로고
    • Inherited disorders in the conversion of methionine to homocysteine
    • Barić I (2009) Inherited disorders in the conversion of methionine to homocysteine. J Inherit Metab Dis 32:459-471
    • (2009) J Inherit Metab Dis , vol.32 , pp. 459-471
    • Barić, I.1
  • 25
    • 0036975282 scopus 로고    scopus 로고
    • Methionine adenosyltransferase I/III deficiency: Two Korean compound heterozygous siblings with a novel mutation
    • Kim SZ, Santamaria E, Jeong TE et al. (2002) Methionine adenosyltransferase I/III deficiency: two Korean compound heterozygous siblings with a novel mutation. J Inherit Metab Dis 25:661-671
    • (2002) J Inherit Metab Dis , vol.25 , pp. 661-671
    • Kim, S.Z.1    Santamaria, E.2    Jeong, T.E.3
  • 26
    • 0031020197 scopus 로고    scopus 로고
    • Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene
    • Chamberlin ME, Ubagai T, Mudd SH et al. (1997) Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet 60:540-546
    • (1997) Am J Hum Genet , vol.60 , pp. 540-546
    • Chamberlin, M.E.1    Ubagai, T.2    Mudd, S.H.3
  • 27
    • 31644449016 scopus 로고    scopus 로고
    • Methionine adenosyltransferase (MAT) I/III deficiency with concurrent hyperhomocysteinaemia: Two novel cases
    • Linnebank M, Lagler F, Muntau AC et al. (2005) Methionine adenosyltransferase (MAT) I/III deficiency with concurrent hyperhomocysteinaemia: two novel cases. J Inherit Metab Dis 28:1167-1168
    • (2005) J Inherit Metab Dis , vol.28 , pp. 1167-1168
    • Linnebank, M.1    Lagler, F.2    Muntau, A.C.3
  • 28
    • 0029788238 scopus 로고    scopus 로고
    • Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency
    • Chamberlin ME, Ubagai T, Mudd SH et al. (1996) Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest 98:1021-1027
    • (1996) J Clin Invest , vol.98 , pp. 1021-1027
    • Chamberlin, M.E.1    Ubagai, T.2    Mudd, S.H.3
  • 29
    • 0032477711 scopus 로고    scopus 로고
    • Normal brain myelination in a patient homozygous for a mutation that encodes a severely truncated methionine adenosyltransferase I/III
    • Hazelwood S, Barnardini I, Shotelersuk V et al. (1998) Normal brain myelination in a patient homozygous for a mutation that encodes a severely truncated methionine adenosyltransferase I/III. Am J Med Genet 75:395-400
    • (1998) Am J Med Genet , vol.75 , pp. 395-400
    • Hazelwood, S.1    Barnardini, I.2    Shotelersuk, V.3
  • 30
    • 0042329126 scopus 로고    scopus 로고
    • Maternal methionine adenosyltransferase I/III deficiency: Reproductive outcomes in a woman with four pregnancies
    • Mudd SH, Tangerman A, Stabler SP et al. (2003) Maternal methionine adenosyltransferase I/III deficiency: reproductive outcomes in a woman with four pregnancies. J Inherit Metab Dis 26:443-458
    • (2003) J Inherit Metab Dis , vol.26 , pp. 443-458
    • Mudd, S.H.1    Tangerman, A.2    Stabler, S.P.3
  • 31
    • 0034827802 scopus 로고    scopus 로고
    • Glycine N-methyltransferase deficiency: A novel inborn error causing persistent isolated hypermethioninaemia
    • Mudd SH, Cerone R, Schiaffino MC et al. (2001) Glycine N-methyltransferase deficiency: a novel inborn error causing persistent isolated hypermethioninaemia. J Inherit Metab Dis 24:448-464
    • (2001) J Inherit Metab Dis , vol.24 , pp. 448-464
    • Mudd, S.H.1    Cerone, R.2    Schiaffino, M.C.3
  • 32
    • 0942298956 scopus 로고    scopus 로고
    • Glycine N-methyltransferase deficiency: A new patient with a novel mutation
    • Augoustides-Savvopoulou P, Luka Z, Karyda S et al. (2003) Glycine N-methyltransferase deficiency: a new patient with a novel mutation. J Inherit Metab Dis 26:745-759
    • (2003) J Inherit Metab Dis , vol.26 , pp. 745-759
    • Augoustides-Savvopoulou, P.1    Luka, Z.2    Karyda, S.3
  • 33
    • 0036461162 scopus 로고    scopus 로고
    • Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism
    • Luka Z, Cerone R, Phillips JA 3rd et al. (2002) Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism. Hum Genet 110:68-74
    • (2002) Hum Genet , vol.110 , pp. 68-74
    • Luka, Z.1    Cerone, R.2    Phillips, J.A.3
  • 34
    • 36349011287 scopus 로고    scopus 로고
    • Glycine N-methyltransferase-/- mice develop chronic hepatitis and glycogen storage disease in the liver
    • Liu SP, Li YS, Chen YJ et al. (2007) Glycine N-methyltransferase-/- mice develop chronic hepatitis and glycogen storage disease in the liver. Hepatology 46:1413-1425
    • (2007) Hepatology , vol.46 , pp. 1413-1425
    • Liu, S.P.1    Li, Y.S.2    Chen, Y.J.3
  • 35
    • 12144286157 scopus 로고    scopus 로고
    • S
    • Baric I, Fumic K, Glenn B et al. (2004) S-Adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci USA 101:4234-4239
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4234-4239
    • Baric, I.1    Fumic, K.2    Glenn, B.3
  • 36
    • 67649635646 scopus 로고    scopus 로고
    • Cystathionine gammalyase: Clinical, metabolic, genetic, and structural studies
    • Kraus JP, Hasek J, Kozich V et al. (2009) Cystathionine gammalyase: clinical, metabolic, genetic, and structural studies. Mol Genet Metab 97:250-259
    • (2009) Mol Genet Metab , vol.97 , pp. 250-259
    • Kraus, J.P.1    Hasek, J.2    Kozich, V.3
  • 37
    • 77956194462 scopus 로고    scopus 로고
    • Cystathionine {gamma}-lyase-deficient mice require dietary cysteine to protect against acute lethal myopathy and oxidative injury
    • Ishii I, Akahoshi N, Yamada H et al. (2010) Cystathionine {gamma}-lyase-deficient mice require dietary cysteine to protect against acute lethal myopathy and oxidative injury. J Biol Chem 285:26358-26368
    • (2010) J Biol Chem , vol.285 , pp. 26358-26368
    • Ishii, I.1    Akahoshi, N.2    Yamada, H.3
  • 38
    • 0027067067 scopus 로고
    • Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase
    • Lu Y, Odowd BF, Orrego H, Israel Y (1992) Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun 189:749-758
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 749-758
    • Lu, Y.1    Odowd, B.F.2    Orrego, H.3    Israel, Y.4
  • 39
    • 0038147273 scopus 로고    scopus 로고
    • Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine γ-lyase (CTH)
    • Wang J, Hegele RA (2003) Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine γ-lyase (CTH). Hum Genet 112:404-408
    • (2003) Hum Genet , vol.112 , pp. 404-408
    • Wang, J.1    Hegele, R.A.2
  • 40
    • 0020441660 scopus 로고
    • Transsulphuration and methylation of homocysteine in control and mutant human fibroblasts
    • Fowler B (1982) Transsulphuration and methylation of homocysteine in control and mutant human fibroblasts. Biochim Biophys Acta 721:201-207
    • (1982) Biochim Biophys Acta , vol.721 , pp. 201-207
    • Fowler, B.1
  • 41
    • 33644625000 scopus 로고    scopus 로고
    • Isolated sulfite oxidase deficiency: A case report with a novel mutation and review of the literature
    • Tan WH, Eichler FS, Hoda S et al. (2005) Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature. Pediatrics 116:757-766
    • (2005) Pediatrics , vol.116 , pp. 757-766
    • Tan, W.H.1    Eichler, F.S.2    Hoda, S.3
  • 43
    • 0032568532 scopus 로고    scopus 로고
    • Human sulfite oxidase Rl60Q: Identification of the mutation in a sulfite oxidasedeficient patient and expression of the mutant enzyme
    • Garrett RM, Johnson JL, Graf TN et al. (1998) Human sulfite oxidase Rl60Q: identification of the mutation in a sulfite oxidasedeficient patient and expression of the mutant enzyme. Proc Natl Acad Sci USA 95:6394-6398
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6394-6398
    • Garrett, R.M.1    Johnson, J.L.2    Graf, T.N.3
  • 44
    • 17144439627 scopus 로고    scopus 로고
    • Isolated sulfite oxidase deficiency: Identification of 12 novel SUOX mutations in 10 patients
    • Johnson JL, Coyne KE, Garrett RM et al. (2002) Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat 20:74
    • (2002) Hum Mutat , vol.20 , pp. 74
    • Johnson, J.L.1    Coyne, K.E.2    Garrett, R.M.3
  • 45
    • 1942469923 scopus 로고    scopus 로고
    • New approaches towards laboratory diagnosis of isolated sulphite oxidase deficiency
    • Sass JO, Nakanishi T, Sato T, Shimizu A (2004) New approaches towards laboratory diagnosis of isolated sulphite oxidase deficiency. Ann Clin Biochem 41:157–159
    • (2004) Ann Clin Biochem , vol.41 , pp. 157-159
    • Sass, J.O.1    Nakanishi, T.2    Sato, T.3    Shimizu, A.4
  • 46
    • 0033983433 scopus 로고    scopus 로고
    • Dietary therapy in two patients with a mild form of sulphite oxidase deficiency. Evidence for clinical and biological improvement
    • Touati G, Rusthoven E, Depondt E et al. (2000) Dietary therapy in two patients with a mild form of sulphite oxidase deficiency. Evidence for clinical and biological improvement. J Inherit Metab Dis 23:45-53
    • (2000) J Inherit Metab Dis , vol.23 , pp. 45-53
    • Touati, G.1    Rusthoven, E.2    Depondt, E.3
  • 47
    • 0024554955 scopus 로고
    • Attempt at therapy in sulphite oxidase deficiency
    • Tardy P, Parvy P, Charpentier C et al. (1989) Attempt at therapy in sulphite oxidase deficiency. J Inherit Metab Dis 12:94-95
    • (1989) J Inherit Metab Dis , vol.12 , pp. 94-95
    • Tardy, P.1    Parvy, P.2    Charpentier, C.3


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