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Volumn 83, Issue 6, 2007, Pages 349-354

ACP1 and offspring sex ratio in smoking puerperae: A study at population level

Author keywords

ACP1; Sex ratio; Smoke

Indexed keywords

PROTEIN ACP1; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 34247248434     PISSN: 03783782     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.earlhumdev.2006.07.005     Document Type: Article
Times cited : (2)

References (29)
  • 1
    • 4444362676 scopus 로고    scopus 로고
    • Genetics of signal transduction and the effect of maternal smoking on sex ratio of offspring
    • Bottini N., Magrini A., Cosmi E., Gloria-Bottini F., Saccucci P., Di Iorio R., et al. Genetics of signal transduction and the effect of maternal smoking on sex ratio of offspring. Am J Human Biol 16 (2004) 588-592
    • (2004) Am J Human Biol , vol.16 , pp. 588-592
    • Bottini, N.1    Magrini, A.2    Cosmi, E.3    Gloria-Bottini, F.4    Saccucci, P.5    Di Iorio, R.6
  • 3
    • 0037140202 scopus 로고    scopus 로고
    • Parental periconceptional smoking and male:female ratio of newborn infants
    • Fukuda M., Fukuda K., Shimizu T., Andersen C.Y., and Byskov A.G. Parental periconceptional smoking and male:female ratio of newborn infants. Lancet 359 (2002) 1407-1408
    • (2002) Lancet , vol.359 , pp. 1407-1408
    • Fukuda, M.1    Fukuda, K.2    Shimizu, T.3    Andersen, C.Y.4    Byskov, A.G.5
  • 4
    • 0001579404 scopus 로고
    • Red cell acid phosphatase variants: a new human polymorphism
    • Hopkinson D.A., Spencer N., and Harris H. Red cell acid phosphatase variants: a new human polymorphism. Nature 199 (1963) 969-971
    • (1963) Nature , vol.199 , pp. 969-971
    • Hopkinson, D.A.1    Spencer, N.2    Harris, H.3
  • 5
    • 0027265973 scopus 로고
    • A Taq1 site identifies the *A allele at the ACP1 locus
    • Sensabaugh G.F., and Lazaruk K.A. A Taq1 site identifies the *A allele at the ACP1 locus. Hum Mol Genet 2 (1993) 1079
    • (1993) Hum Mol Genet , vol.2 , pp. 1079
    • Sensabaugh, G.F.1    Lazaruk, K.A.2
  • 6
    • 0023546712 scopus 로고
    • Immunochemical characterization of human red cell acid phosphatase isozymes
    • Dissing J. Immunochemical characterization of human red cell acid phosphatase isozymes. Biochem Genet 25 (1987) 901-918
    • (1987) Biochem Genet , vol.25 , pp. 901-918
    • Dissing, J.1
  • 7
    • 0014689995 scopus 로고
    • Purification and characterization of a low molecular weight acid phosphatase from bovine liver
    • Heinrikson R.L. Purification and characterization of a low molecular weight acid phosphatase from bovine liver. J Biol Chem 244 (1969) 299-307
    • (1969) J Biol Chem , vol.244 , pp. 299-307
    • Heinrikson, R.L.1
  • 8
    • 0030032729 scopus 로고    scopus 로고
    • The molecular basis of the differing kinetic behavior of the two low molecular mass phosphotyrosine protein phosphatase isoforms
    • Cirri P., Fiaschi T., Chiarugi P., Camici G., Manao G., Raugei G., et al. The molecular basis of the differing kinetic behavior of the two low molecular mass phosphotyrosine protein phosphatase isoforms. J Biol Chem 271 (1996) 2604-2607
    • (1996) J Biol Chem , vol.271 , pp. 2604-2607
    • Cirri, P.1    Fiaschi, T.2    Chiarugi, P.3    Camici, G.4    Manao, G.5    Raugei, G.6
  • 9
    • 0027447059 scopus 로고
    • Activity modulation of the fast and slow isozymes of human cytosolic low-molecular-weight acid phosphates (ACP1) by purines
    • Dissing J., Rangaard B., and Christensen U. Activity modulation of the fast and slow isozymes of human cytosolic low-molecular-weight acid phosphates (ACP1) by purines. Biochim Biophys Acta 1162 (1993) 275-282
    • (1993) Biochim Biophys Acta , vol.1162 , pp. 275-282
    • Dissing, J.1    Rangaard, B.2    Christensen, U.3
  • 10
    • 0027324757 scopus 로고
    • Dephosphorylation of tyrosine phosphorylated synthetic peptides by rat liver phosphotyrosine protein phosphatase isoenzymes
    • Stefani M., Caselli A., Bucciantini M., Pazzagli L., Dolfi F., Camici G., et al. Dephosphorylation of tyrosine phosphorylated synthetic peptides by rat liver phosphotyrosine protein phosphatase isoenzymes. FEBS Lett 326 (1993) 131-134
    • (1993) FEBS Lett , vol.326 , pp. 131-134
    • Stefani, M.1    Caselli, A.2    Bucciantini, M.3    Pazzagli, L.4    Dolfi, F.5    Camici, G.6
  • 11
    • 0028829766 scopus 로고
    • Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1
    • Bryson G.L., Massa H., Trask B.J., and Van Etten R.L. Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1. Genemics 30 (1995) 133-140
    • (1995) Genemics , vol.30 , pp. 133-140
    • Bryson, G.L.1    Massa, H.2    Trask, B.J.3    Van Etten, R.L.4
  • 12
    • 0025838222 scopus 로고
    • Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele
    • Dissing J., Johnsen A.H., and Sensabaugh G.F. Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele. J Biol Chem 266 (1991) 20619-20625
    • (1991) J Biol Chem , vol.266 , pp. 20619-20625
    • Dissing, J.1    Johnsen, A.H.2    Sensabaugh, G.F.3
  • 13
    • 0026727801 scopus 로고
    • Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase
    • Wo Y.Y.P., McCormack A.L., Shabanowitz J., Hunt D.F., Davis J.P., Mitchell G.L., et al. Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. J Biol Chem 267 (1992) 10856-10865
    • (1992) J Biol Chem , vol.267 , pp. 10856-10865
    • Wo, Y.Y.P.1    McCormack, A.L.2    Shabanowitz, J.3    Hunt, D.F.4    Davis, J.P.5    Mitchell, G.L.6
  • 14
    • 0026755209 scopus 로고
    • Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles
    • Dissing J., and Johnsen A.H. Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles. Biochim Biophys Acta 1121 (1992) 261-268
    • (1992) Biochim Biophys Acta , vol.1121 , pp. 261-268
    • Dissing, J.1    Johnsen, A.H.2
  • 15
    • 0027432174 scopus 로고
    • Exon structure at the human ACP1 locus supports alternative splicing model for F and S isozyme generation
    • Lazaruk K.D., Dissing J., and Sensabaugh G.F. Exon structure at the human ACP1 locus supports alternative splicing model for F and S isozyme generation. Biochem Biophys Res Commun 196 (1993) 440-446
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 440-446
    • Lazaruk, K.D.1    Dissing, J.2    Sensabaugh, G.F.3
  • 16
    • 0022452352 scopus 로고
    • The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3
    • Boivin P., and Galand C. The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3. Biochem Biophys Res Commun 134 (1986) 557-564
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 557-564
    • Boivin, P.1    Galand, C.2
  • 18
    • 0025859158 scopus 로고
    • Role of band 3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis
    • Harrison M.L., Rathinavelu P., Arese P., Geahlen R.L., and Low P.S. Role of band 3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis. J Biol Chem 266 (1991) 4106-4111
    • (1991) J Biol Chem , vol.266 , pp. 4106-4111
    • Harrison, M.L.1    Rathinavelu, P.2    Arese, P.3    Geahlen, R.L.4    Low, P.S.5
  • 19
    • 0020004374 scopus 로고
    • gua-1-1: a low activity variant of human erythrocyte acid phosphatase: association with increased glutathione reductase activity
    • gua-1-1: a low activity variant of human erythrocyte acid phosphatase: association with increased glutathione reductase activity. Am J Hum Genet 34 (1982) 425
    • (1982) Am J Hum Genet , vol.34 , pp. 425
    • Mohrenweiser, H.W.1    Novotny, J.E.2
  • 20
    • 0037025315 scopus 로고    scopus 로고
    • Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP)
    • Bottini N., Stefanini L., Williams S., Alonso A., Merlo J., Jascur T., et al. Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP). J Biol Chem 277 (2002) 24220-24224
    • (2002) J Biol Chem , vol.277 , pp. 24220-24224
    • Bottini, N.1    Stefanini, L.2    Williams, S.3    Alonso, A.4    Merlo, J.5    Jascur, T.6
  • 21
    • 34247251703 scopus 로고    scopus 로고
    • Lazaruk KDA. Molecular genetics of human red cell acid phosphatase, PhD dissertation, University of California, Berkeley, CA, Professor Sensabaugh GF, Chair; 1995.
  • 23
    • 0004249246 scopus 로고
    • Freeman, New York, NY
    • Sokal R.R., and Rohlf F.J. Biometry (1981), Freeman, New York, NY 253-261
    • (1981) Biometry , pp. 253-261
    • Sokal, R.R.1    Rohlf, F.J.2
  • 24
    • 0032775640 scopus 로고    scopus 로고
    • Polynitroxylated hemoglobin-based oxygen carrier: inhibition of free radical-induced microcirculatory dysfunction
    • Saetzler R.K., Arfors K.E., Tuma R.F., Vashtare V., Ma L., Hsia C.J.C., et al. Polynitroxylated hemoglobin-based oxygen carrier: inhibition of free radical-induced microcirculatory dysfunction. Free Radic Biol Med 27 (1999) 1-6
    • (1999) Free Radic Biol Med , vol.27 , pp. 1-6
    • Saetzler, R.K.1    Arfors, K.E.2    Tuma, R.F.3    Vashtare, V.4    Ma, L.5    Hsia, C.J.C.6
  • 25
    • 0014977481 scopus 로고
    • Studies of the in vitro effects of oxidized glutathione and acetylphenylhydrazine on acid phosphatises of human red blood cells. An experimental model for the investigation of haemolytic drug action at the molecular level
    • Bottini E., Modiano G., Santolamazza C., Filippi G., and Businco L. Studies of the in vitro effects of oxidized glutathione and acetylphenylhydrazine on acid phosphatises of human red blood cells. An experimental model for the investigation of haemolytic drug action at the molecular level. Clin Chim Acta 31 (1971) 243-254
    • (1971) Clin Chim Acta , vol.31 , pp. 243-254
    • Bottini, E.1    Modiano, G.2    Santolamazza, C.3    Filippi, G.4    Businco, L.5
  • 27
    • 22744441523 scopus 로고    scopus 로고
    • Up-regulated expression of low molecular weight protein tyrosine phosphatases in different human cancers
    • Maletacchi F., Marzocchini R., Gelmini S., Orlando C., Serio M., Ramponi G., et al. Up-regulated expression of low molecular weight protein tyrosine phosphatases in different human cancers. Biochem Biophys Res Commun 334 (2005) 875-883
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 875-883
    • Maletacchi, F.1    Marzocchini, R.2    Gelmini, S.3    Orlando, C.4    Serio, M.5    Ramponi, G.6
  • 28
    • 84941325107 scopus 로고
    • Studies on red cell acid phosphatase in Sardinia and Rome absence of correlation with past malarial morbidity
    • Modiano G., Filippi F., Brunelli F., Frattaroli W., Siniscalco M., Palmarino R., et al. Studies on red cell acid phosphatase in Sardinia and Rome absence of correlation with past malarial morbidity. Acta Genet 17 (1967) 17-28
    • (1967) Acta Genet , vol.17 , pp. 17-28
    • Modiano, G.1    Filippi, F.2    Brunelli, F.3    Frattaroli, W.4    Siniscalco, M.5    Palmarino, R.6
  • 29
    • 0001579404 scopus 로고
    • Red cell acid phosphatase variants: a new human polymorphism
    • Hopkinson D.A., Spencer N., and Harris H. Red cell acid phosphatase variants: a new human polymorphism. Nature 199 (1963) 969-971
    • (1963) Nature , vol.199 , pp. 969-971
    • Hopkinson, D.A.1    Spencer, N.2    Harris, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.