메뉴 건너뛰기




Volumn 247, Issue 2, 2000, Pages 169-178

Molecular aspects of the inherited porphyrias

Author keywords

Erythropoietic porphyria; Haem biosynthesis; Hepatic porphyria; Porphyria

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; COPROPORPHYRIN; COPROPORPHYRINOGEN OXIDASE; FERROCHELATASE; PORPHOBILINOGEN DEAMINASE; PORPHOBILINOGEN SYNTHASE; PORPHYRIN; PROTOPORPHYRIN; PROTOPORPHYRINOGEN OXIDASE; UROPORPHYRIN; UROPORPHYRINOGEN DECARBOXYLASE; UROPORPHYRINOGEN III SYNTHASE;

EID: 0033981851     PISSN: 09546820     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2796.2000.00618.x     Document Type: Review
Times cited : (77)

References (21)
  • 2
    • 0033528697 scopus 로고    scopus 로고
    • X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution
    • 2 Erskine PT, Norton E, Cooper JB et al. X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution. Biochemistry 1999; 38: 4266-76.
    • (1999) Biochemistry , vol.38 , pp. 4266-4276
    • Erskine, P.T.1    Norton, E.2    Cooper, J.B.3
  • 3
    • 0031941533 scopus 로고    scopus 로고
    • ALAD porphyria
    • Berk PD, eds. New York: Thieme
    • 3 Sassa S. ALAD porphyria. In: Berk PD, eds. Seminars in Liver Disease. New York: Thieme, 1998; 95-101.
    • (1998) Seminars in Liver Disease , pp. 95-101
    • Sassa, S.1
  • 4
    • 0023713201 scopus 로고
    • Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression
    • 4 Chretien S, Dubart A, Beaupain D et al. Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc Natl Acad Sci USA 1988; 85: 6-10.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6-10
    • Chretien, S.1    Dubart, A.2    Beaupain, D.3
  • 5
    • 0030959246 scopus 로고    scopus 로고
    • Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria
    • 5 Puy H, Deybach JC, Lamoril J, Da Robreau AMS, Gouya VI. et al. Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria. Am J Hum Genet 1997; 60: 1373-83.
    • (1997) Am J Hum Genet , vol.60 , pp. 1373-1383
    • Puy, H.1    Deybach, J.C.2    Lamoril, J.3    Da Robreau, A.M.S.4    Gouya, V.I.5
  • 6
    • 0027946035 scopus 로고
    • The three-dimensional structures of mutants of porphobilinogen deaminase: Toward an understanding of the structural basis of acute intermittent porphyria
    • 6 Brownlie PD, Lambert R, Louie GV et al. The three-dimensional structures of mutants of porphobilinogen deaminase: toward an understanding of the structural basis of acute intermittent porphyria. Protein Sci 1994; 3: 1644-50.
    • (1994) Protein Sci , vol.3 , pp. 1644-1650
    • Brownlie, P.D.1    Lambert, R.2    Louie, G.V.3
  • 7
    • 0030069657 scopus 로고    scopus 로고
    • Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria
    • 7 Lindberg RLP, Porcher C, Grandchamp B et al. Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria. Nature Genet 1996; 12: 195-99.
    • (1996) Nature Genet , vol.12 , pp. 195-199
    • Lindberg, R.L.P.1    Porcher, C.2    Grandchamp, B.3
  • 8
    • 0027409758 scopus 로고
    • Hydroxy-methylbilane synthase: Complete genomic sequence and amplifiable polymorphisms in the human gene
    • 8 Yoo HW, Warner CA, Chen CH, Desnick RJ. Hydroxy-methylbilane synthase: complete genomic sequence and amplifiable polymorphisms in the human gene. Genomics 1993; 15: 21-29.
    • (1993) Genomics , vol.15 , pp. 21-29
    • Yoo, H.W.1    Warner, C.A.2    Chen, C.H.3    Desnick, R.J.4
  • 10
    • 0030905555 scopus 로고    scopus 로고
    • Gene transfer of the uroporphyrinogen III synthase cDNA into haematopoietic progenitor cells in view of a future gene therapy in congenital erythropoietic porphyria
    • 10 Mazurier F, Moreau-Gaudry F, Salesse S et al. Gene transfer of the uroporphyrinogen III synthase cDNA into haematopoietic progenitor cells in view of a future gene therapy in congenital erythropoietic porphyria. J Inh Metab Dis 1997; 20: 247-57.
    • (1997) J Inh Metab Dis , vol.20 , pp. 247-257
    • Mazurier, F.1    Moreau-Gaudry, F.2    Salesse, S.3
  • 11
    • 0028169056 scopus 로고
    • Coproporphyrinogen oxidase: Gene organization and description of a mutation leading to exon 6 skipping
    • 11 Delfau-Larue MH, Martasek P, Grandchamp B. Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. Hum Mol Genet 1994; 3: 1325-30.
    • (1994) Hum Mol Genet , vol.3 , pp. 1325-1330
    • Delfau-Larue, M.H.1    Martasek, P.2    Grandchamp, B.3
  • 12
    • 0032211177 scopus 로고    scopus 로고
    • Differential regulation of mouse coproporphyrinogen oxidase gene expression in erythroid and non-erythroid cells
    • 12 Takahashi S, Taketani S, Akasaka J et al. Differential regulation of mouse coproporphyrinogen oxidase gene expression in erythroid and non-erythroid cells. Blood 1998; 92: 3436-44.
    • (1998) Blood , vol.92 , pp. 3436-3444
    • Takahashi, S.1    Taketani, S.2    Akasaka, J.3
  • 13
    • 0030568860 scopus 로고    scopus 로고
    • Protoporphyrinogen oxidase: Complete genomic sequence and polymorphisms in the human gene
    • 13 Puy H, Robreau AM, Rosipal R, Nordmann Y, Deybach JC. Protoporphyrinogen oxidase: complete genomic sequence and polymorphisms in the human gene. Biochem Biophys Res Commun 1996; 226: 226-30.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 226-230
    • Puy, H.1    Robreau, A.M.2    Rosipal, R.3    Nordmann, Y.4    Deybach, J.C.5
  • 14
    • 0030140415 scopus 로고    scopus 로고
    • A R 59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria
    • 14 Meissner PN, Dailey TA, Hift RJ et al. A R 59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Nature 1996; 13: 95-97.
    • (1996) Nature , vol.13 , pp. 95-97
    • Meissner, P.N.1    Dailey, T.A.2    Hift, R.J.3
  • 15
    • 0031779289 scopus 로고    scopus 로고
    • Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria
    • 15 Rüfenacht U, Gouya L, Schneider-Yin X et al. Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria. Am J Hum Genet 1998; 62: 1341-52.
    • (1998) Am J Hum Genet , vol.62 , pp. 1341-1352
    • Rüfenacht, U.1    Gouya, L.2    Schneider-Yin, X.3
  • 16
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • 16 Dailey HA, Finnegan MG, Johnson MK. Human ferrochelatase is an iron-sulfur protein. Biochemistry 1994; 33: 403-407.
    • (1994) Biochemistry , vol.33 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 17
    • 0028234733 scopus 로고
    • Mammalian ferrochelatase, a new addition to the metalloenzyme family
    • 17 Ferreira GC, Franco R, Lloyd SG et al. Mammalian ferrochelatase, a new addition to the metalloenzyme family. J Biol Chem 1994; 269: 7062-65.
    • (1994) J Biol Chem , vol.269 , pp. 7062-7065
    • Ferreira, G.C.1    Franco, R.2    Lloyd, S.G.3
  • 18
    • 0031573454 scopus 로고    scopus 로고
    • Crystal structure of ferrochelatase: The terminal enzyme in heme biosynthesis
    • 18 Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hedersledt L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure 1997; 5: 1501-10.
    • (1997) Structure , vol.5 , pp. 1501-1510
    • Al-Karadaghi, S.1    Hansson, M.2    Nikonov, S.3    Jonsson, B.4    Hedersledt, L.5
  • 19
    • 0027952902 scopus 로고
    • Screening for ferrochelatase mutations: Molecular heterogeneity of erythropoietic protoporphyria
    • 19 Wang X. Poh-Fitzpatrick M, Taketani S, Chen T, Piomelli S. Screening for ferrochelatase mutations: molecular heterogeneity of erythropoietic protoporphyria. Biochim Biophys Acta 1994; 1225: 187-90.
    • (1994) Biochim Biophys Acta , vol.1225 , pp. 187-190
    • Wang, X.1    Poh-Fitzpatrick, M.2    Taketani, S.3    Chen, T.4    Piomelli, S.5
  • 20
    • 0027167487 scopus 로고
    • Ferrochelatase structural mutant (Fechm I Pas) in the house mouse
    • 20 Boulechfar S, Lamoril J, Montagutelli X et al. Ferrochelatase structural mutant (Fechm I Pas) in the house mouse. Genomics 1993; 16: 645-48.
    • (1993) Genomics , vol.16 , pp. 645-648
    • Boulechfar, S.1    Lamoril, J.2    Montagutelli, X.3
  • 21
    • 0025748882 scopus 로고
    • Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease
    • 21 Tutois S, Montagutelli X, Da Silva V et al. Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease. J Clin Invest 1991; 88: 1730-36.
    • (1991) J Clin Invest , vol.88 , pp. 1730-1736
    • Tutois, S.1    Montagutelli, X.2    Da Silva, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.