메뉴 건너뛰기




Volumn 39, Issue 9, 2002, Pages

Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; FRUCTOSE BISPHOSPHATE ALDOLASE; GENOMIC DNA; OLIGONUCLEOTIDE; PROLINE; RESTRICTION ENDONUCLEASE; DNA;

EID: 0036727703     PISSN: 00222593     EISSN: 14686244     Source Type: Journal    
DOI: 10.1136/jmg.39.9.e56     Document Type: Article
Times cited : (13)

References (33)
  • 2
    • 0022728428 scopus 로고
    • Characterisation of the human aldolase B gene
    • Tolan DR, Penhoet EE. Characterisation of the human aldolase B gene. Mol Biol Med 1986;3:245-64.
    • (1986) Mol Biol Med , vol.3 , pp. 245-264
    • Tolan, D.R.1    Penhoet, E.E.2
  • 3
    • 0029097210 scopus 로고
    • Molecular basis of hereditary fructose intolerance: Mutations and polymorphisms in the human aldolase B gene
    • Tolan DR. Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene. Hum Mutat 1995;6:210-18.
    • (1995) Hum Mutat , vol.6 , pp. 210-218
    • Tolan, D.R.1
  • 4
    • 0031945356 scopus 로고    scopus 로고
    • Hereditary fructose intolerance
    • Ali M, Rellos P, Cox TM. Hereditary fructose intolerance. J Med Genet 1998;35:353-65.
    • (1998) J Med Genet , vol.35 , pp. 353-365
    • Ali, M.1    Rellos, P.2    Cox, T.M.3
  • 5
    • 0032977720 scopus 로고    scopus 로고
    • Novel six-nucleotide deletion in the hepatic fructose-1,6-bisphosphate aldolase gene in a patient with hereditary fructose intolerance and enzyme structure-function implications
    • Santamaria R, Vitagliano L, Tamasi S, Izzo P, Zancan L, Zagari A, Salvatore F. Novel six-nucleotide deletion in the hepatic fructose-1,6-bisphosphate aldolase gene in a patient with hereditary fructose intolerance and enzyme structure-function implications. Eur J Hum Genet 1999;7:409-14.
    • (1999) Eur J Hum Genet , vol.7 , pp. 409-414
    • Santamaria, R.1    Vitagliano, L.2    Tamasi, S.3    Izzo, P.4    Zancan, L.5    Zagari, A.6    Salvatore, F.7
  • 7
    • 0033979904 scopus 로고    scopus 로고
    • Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis
    • Rellos P, Sygusch J, Cox TM. Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis. J Biol Chem 2000;275:1145-51.
    • (2000) J Biol Chem , vol.275 , pp. 1145-1151
    • Rellos, P.1    Sygusch, J.2    Cox, T.M.3
  • 8
    • 0034664941 scopus 로고    scopus 로고
    • Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase
    • Santamaria R, Esposito G, Vitagliano L, Race V, Paglionico I, Zancan L, Zagari A, Salvatore F. Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase. Biochem J 2000;350:823-8.
    • (2000) Biochem J , vol.350 , pp. 823-828
    • Santamaria, R.1    Esposito, G.2    Vitagliano, L.3    Race, V.4    Paglionico, I.5    Zancan, L.6    Zagari, A.7    Salvatore, F.8
  • 9
    • 0023935910 scopus 로고
    • Catalytic deficiency of human aldolase b in hereditary fructose intolerance caused by a common missense mutation
    • Cross NCP, Tolan DR, Cox TM. Catalytic deficiency of human aldolase b in hereditary fructose intolerance caused by a common missense mutation. Cell 1988;53:881-5.
    • (1988) Cell , vol.53 , pp. 881-885
    • Cross, N.C.P.1    Tolan, D.R.2    Cox, T.M.3
  • 10
    • 0029954183 scopus 로고    scopus 로고
    • Neonatal screening for hereditary fructose intolerance: Frequency of the most common mutant aldolase B allele (A149P) in the British population
    • James CL, Rellos P, Ali M, Heeley AF, Cox TM. Neonatal screening for hereditary fructose intolerance: frequency of the most common mutant aldolase B allele (A149P) in the British population. J Med Genet 1996;33:837-41.
    • (1996) J Med Genet , vol.33 , pp. 837-841
    • James, C.L.1    Rellos, P.2    Ali, M.3    Heeley, A.F.4    Cox, T.M.5
  • 11
    • 0027958074 scopus 로고
    • Aldolase B and fructose intolerance
    • Cox TM. Aldolase B and fructose intolerance. FASEB J 1994;8:62-71.
    • (1994) FASEB J , vol.8 , pp. 62-71
    • Cox, T.M.1
  • 15
    • 0025282839 scopus 로고
    • Molecular evidence for compound heterozygosity in hereditary fructose intolerance
    • Dazzo C, Tolan DR. Molecular evidence for compound heterozygosity in hereditary fructose intolerance. Am J Hum Genet 1990;46:1194-9.
    • (1990) Am J Hum Genet , vol.46 , pp. 1194-1199
    • Dazzo, C.1    Tolan, D.R.2
  • 16
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987;162:156-9.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 17
    • 0021430276 scopus 로고
    • Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones
    • Rottman WH, Tolan DR, Penhoet EE. Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. Proc Natl Acad Sci USA 1984;81:2738-42.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2738-2742
    • Rottman, W.H.1    Tolan, D.R.2    Penhoet, E.E.3
  • 18
    • 0001571983 scopus 로고
    • Comparative studies of liver and muscle aldolase. II. Immunochemical and chromatographic differentiation
    • Blostein R, Rutter WJ. Comparative studies of liver and muscle aldolase. II. Immunochemical and chromatographic differentiation. J Biol Chem 1963;238:3280-5.
    • (1963) J Biol Chem , vol.238 , pp. 3280-3285
    • Blostein, R.1    Rutter, W.J.2
  • 20
    • 0025352949 scopus 로고
    • Partial aldolase B gene deletions in hereditary fructose intolerance
    • Cross NCP, Cox TM. Partial aldolase B gene deletions in hereditary fructose intolerance. Am J Hum Genet 1990;47:101-6.
    • (1990) Am J Hum Genet , vol.47 , pp. 101-106
    • Cross, N.C.P.1    Cox, T.M.2
  • 21
    • 0031612929 scopus 로고    scopus 로고
    • Recommendations for a nomenclature system for human gene mutations
    • Antonarakis SE, Nomenclature Working Group. Recommendations for a nomenclature system for human gene mutations. Hum Mutat 1998;11:1-3.
    • (1998) Hum Mutat , vol.11 , pp. 1-3
    • Antonarakis, S.E.1
  • 22
    • 0033987736 scopus 로고    scopus 로고
    • Mutation nomenclature extensions and suggestions to describe complex mutations: A discussion
    • den Dunnen JT, Antonarakis SE. Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion. Hum Mutat 2000;15:7-12.
    • (2000) Hum Mutat , vol.15 , pp. 7-12
    • Den Dunnen, J.T.1    Antonarakis, S.E.2
  • 23
    • 0026794668 scopus 로고
    • The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: Causes and consequences
    • Krawczak M, Reiss J, Cooper DN. The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences. Hum Genet 1992;90:41-54.
    • (1992) Hum Genet , vol.90 , pp. 41-54
    • Krawczak, M.1    Reiss, J.2    Cooper, D.N.3
  • 24
    • 0028222873 scopus 로고
    • Construction of a novel database containing aberrant splicing mutations of mammalian genes
    • The mutation database described is following internet address
    • Nakai K, Sakamoto H. Construction of a novel database containing aberrant splicing mutations of mammalian genes. Gene 1994;141:171-7. (The mutation database described is available at the following internet address: http://www.hgc.ims.u-tokyo.ac.jp/∼knakai/asdb.html).
    • (1994) Gene , vol.141 , pp. 171-177
    • Nakai, K.1    Sakamoto, H.2
  • 25
    • 0023905495 scopus 로고
    • Transcription of the dystrophin gene in human muscle and non-muscle tissues
    • Chelly J, Kaplan JC, Maire P, Gautron S, Kahn A. Transcription of the dystrophin gene in human muscle and non-muscle tissues. Nature 1988;333:858-60.
    • (1988) Nature , vol.333 , pp. 858-860
    • Chelly, J.1    Kaplan, J.C.2    Maire, P.3    Gautron, S.4    Kahn, A.5
  • 27
    • 0033024566 scopus 로고    scopus 로고
    • Identification of conserved promoter elements for aldB and isozyme specific residues in aldolase B
    • Berardini T, Amsden AB, Penhoet EE, Tolan DR. Identification of conserved promoter elements for aldB and isozyme specific residues in aldolase B. Comp Biochem Physiol B 1999;122:53-61.
    • (1999) Comp Biochem Physiol B , vol.122 , pp. 53-61
    • Berardini, T.1    Amsden, A.B.2    Penhoet, E.E.3    Tolan, D.R.4
  • 28
    • 0023446039 scopus 로고
    • Molecular achitectures of rabbit skeletal muscle aldolase at 2.7- Resolution
    • Sygusch J, Beaudry D, Allaire M. Molecular achitectures of rabbit skeletal muscle aldolase at 2.7- resolution. Proc Natl Acad Sci USA 1987;84:7846-50.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7846-7850
    • Sygusch, J.1    Beaudry, D.2    Allaire, M.3
  • 29
    • 0024423389 scopus 로고
    • Temperature-dependent expression of a collagen splicing defect in the fibroblasts of a patient with Ehlers-Danlos syndrome type VII
    • Weil D, D’Alessio M, Ramirez F, Steinmann B, Wirtz MK, Glanville RW, Hollister DW. Temperature-dependent expression of a collagen splicing defect in the fibroblasts of a patient with Ehlers-Danlos syndrome type VII. J Biol Chem 1989;264:16804-9.
    • (1989) J Biol Chem , vol.264 , pp. 16804-16809
    • Weil, D.1    D’Alessio, M.2    Ramirez, F.3    Steinmann, B.4    Wirtz, M.K.5    Glanville, R.W.6    Hollister, D.W.7
  • 30
    • 0025344432 scopus 로고
    • A “G” to “A” mutation at position –1 of a 5′ splice site in a late infantile form of Tay-Sachs disease
    • Akli S, Chelly J, Mezard C, Gandy S, Kahn A, Poenaru L. A “G” to “A” mutation at position –1 of a 5′ splice site in a late infantile form of Tay-Sachs disease. J Biol Chem 1990;265:7324-30.
    • (1990) J Biol Chem , vol.265 , pp. 7324-7330
    • Akli, S.1    Chelly, J.2    Mezard, C.3    Gandy, S.4    Kahn, A.5    Poenaru, L.6
  • 31
    • 0026560818 scopus 로고
    • Branched chain acyltransferase absence due to an Alu-based genomic deletion allele and an exon skipping allele in a compound heterozygote proband expressing maple syrup urine disease
    • Herring WJ, McKean M, Dracopoli N, Danner DJ. Branched chain acyltransferase absence due to an Alu-based genomic deletion allele and an exon skipping allele in a compound heterozygote proband expressing maple syrup urine disease. Biochim Biophys Acta 1992;1138:236-42.
    • (1992) Biochim Biophys Acta , vol.1138 , pp. 236-242
    • Herring, W.J.1    McKean, M.2    Dracopoli, N.3    Danner, D.J.4
  • 32
    • 0020620321 scopus 로고
    • Specific transcription and RNA splicing defects in five cloned β-thalassaemia genes
    • Treisman R, Orkin SH, Maniatis T. Specific transcription and RNA splicing defects in five cloned β-thalassaemia genes. Nature 1983;302:591-6.
    • (1983) Nature , vol.302 , pp. 591-596
    • Treisman, R.1    Orkin, S.H.2    Maniatis, T.3
  • 33
    • 0032004354 scopus 로고    scopus 로고
    • Efficient 3′-end formation of human β-globin mRNA in vivo requires sequences within the last intron but occurs independently of the splicing reaction
    • Antoniou M, Geraghty F, Hurst J, Grosveld F. Efficient 3′-end formation of human β-globin mRNA in vivo requires sequences within the last intron but occurs independently of the splicing reaction. Nucleic Acids Res 1998;26:721-9.
    • (1998) Nucleic Acids Res , vol.26 , pp. 721-729
    • Antoniou, M.1    Geraghty, F.2    Hurst, J.3    Grosveld, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.