메뉴 건너뛰기




Volumn 10, Issue 3, 2010, Pages 417-434

Prenatal alcohol exposure alters phosphorylation and glycosylation of proteins in rat offspring liver

Author keywords

Animal proteomics; Liver proteins; Prenatal exposure; Programming

Indexed keywords

3 HYDROXYANTHRANILATE DIOXYGENASE; ACTIN; ADENOSINE; ADENOSINE KINASE; ADENOSYLHOMOCYSTEINASE; ALDOKETO REDUCTASE; ALPHA ENOLASE; AMINO ACID; CALMODULIN; DIOXYGENASE; ELONGATION FACTOR 1BETA; FERRITIN; FRUCTOSE BISPHOSPHATASE; GLUCOSE; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 58; GLUTATHIONE TRANSFERASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; LIVER PROTEIN; MALATE DEHYDROGENASE; ORNITHINE CARBAMOYLTRANSFERASE; OXIDOREDUCTASE; PHOSPHORIBOSYLTRANSFERASE; RIBOPROTEIN LARGE P2; TUMOR REJECTION ANTIGEN; TUMOR REJECTION ANTIGEN GP96; UNCLASSIFIED DRUG;

EID: 76649100754     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800969     Document Type: Article
Times cited : (19)

References (69)
  • 1
    • 0027513981 scopus 로고
    • Fetal nutrition and cardiovascular disease in adult life
    • Barker, D. J., Gluckman, P. D., Godfrey, K. M., Harding, J. E. et al., Fetal nutrition and cardiovascular disease in adult life. Lancet 1993, 341, 938-941.
    • (1993) Lancet , vol.341 , pp. 938-941
    • Barker, D.J.1    Gluckman, P.D.2    Godfrey, K.M.3    Harding, J.E.4
  • 3
    • 0037320307 scopus 로고    scopus 로고
    • Glucose intolerance and resistin expression in rat offspring exposed to ethanol in utero: Modulation by postnatal high fat diet
    • Chen, L., Nyomba, B. L. G., Glucose intolerance and resistin expression in rat offspring exposed to ethanol in utero: modulation by postnatal high fat diet. Endocrinology 2003, 144, 500-508.
    • (2003) Endocrinology , vol.144 , pp. 500-508
    • Chen, L.1    Nyomba, B.L.G.2
  • 4
    • 0347993715 scopus 로고    scopus 로고
    • Whole body insulin resistance in rat offspring of mothers consuming alcohol during pregnancy or lactation: Comparing prenatal and postnatal exposure
    • Chen, L., Nyomba, B. L., Whole body insulin resistance in rat offspring of mothers consuming alcohol during pregnancy or lactation: comparing prenatal and postnatal exposure. J. Appl. Physiol. 2004, 96, 167-172.
    • (2004) J. Appl. Physiol , vol.96 , pp. 167-172
    • Chen, L.1    Nyomba, B.L.2
  • 5
    • 23044432133 scopus 로고    scopus 로고
    • In vivo insulin signaling through PI3-Kinase is impaired in skeletal muscle of adult rat offspring exposed to ethanol in utero
    • Chen, L., Yao, X. H., Nyomba, B. L., In vivo insulin signaling through PI3-Kinase is impaired in skeletal muscle of adult rat offspring exposed to ethanol in utero. J. Appl. Physiol. 2005, 99, 528-534.
    • (2005) J. Appl. Physiol , vol.99 , pp. 528-534
    • Chen, L.1    Yao, X.H.2    Nyomba, B.L.3
  • 6
    • 33646351086 scopus 로고    scopus 로고
    • Adult rats prenatally exposed to ethanol have increased gluconeogenesis and impaired insulin response of hepatic gluconeogenic genes
    • Yao, X. H., Chen, L., Nyomba, B. L. G., Adult rats prenatally exposed to ethanol have increased gluconeogenesis and impaired insulin response of hepatic gluconeogenic genes. J. Appl. Physiol. 2006, 100, 642-648.
    • (2006) J. Appl. Physiol , vol.100 , pp. 642-648
    • Yao, X.H.1    Chen, L.2    Nyomba, B.L.G.3
  • 7
    • 0041864127 scopus 로고    scopus 로고
    • In vivo measurement of fluxes through metabolic pathways: The missing link in functional genomics and pharmaceutical research
    • Hellerstein, M., In vivo measurement of fluxes through metabolic pathways: the missing link in functional genomics and pharmaceutical research. Annu. Rev. Nutr. 2003, 23, 379-402.
    • (2003) Annu. Rev. Nutr , vol.23 , pp. 379-402
    • Hellerstein, M.1
  • 8
    • 33846590457 scopus 로고    scopus 로고
    • Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis
    • Kleinert, P., Kuster, T., Arnold, D., Jaeken, J. et al., Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis. Proteomics. 2007, 7, 15-22.
    • (2007) Proteomics , vol.7 , pp. 15-22
    • Kleinert, P.1    Kuster, T.2    Arnold, D.3    Jaeken, J.4
  • 9
    • 21244495253 scopus 로고    scopus 로고
    • 2D fluorescence difference gel analysis technology
    • The development of the DIGE system
    • Marouga, R., David, S., Hawkins, E., The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal. Bioanal. Chem. 2005, 382, 669-678.
    • (2005) Anal. Bioanal. Chem , vol.382 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 10
    • 3543138968 scopus 로고    scopus 로고
    • Proteomic analysis of post-mitochondrial fractions of young and old rat kidney
    • Kim, C. H., Park, D. U., Chung, A. S., Zou, Y. et al., Proteomic analysis of post-mitochondrial fractions of young and old rat kidney. Exp. Gerontol. 2004, 39, 1155-1168.
    • (2004) Exp. Gerontol , vol.39 , pp. 1155-1168
    • Kim, C.H.1    Park, D.U.2    Chung, A.S.3    Zou, Y.4
  • 11
    • 36048999199 scopus 로고    scopus 로고
    • Serum proteomics of lung adenocarcinomas induced by targeted overexpression of c-raf in alveolar epithelium identifies candidate biomarkers
    • Chatterji, B., Borlak, J., Serum proteomics of lung adenocarcinomas induced by targeted overexpression of c-raf in alveolar epithelium identifies candidate biomarkers. Proteomics 2007, 7, 3980-3991.
    • (2007) Proteomics , vol.7 , pp. 3980-3991
    • Chatterji, B.1    Borlak, J.2
  • 12
    • 35348958886 scopus 로고    scopus 로고
    • Proteomics analysis of hypothalamic response to energy restriction in dairy cows
    • Kuhla, B., Kuhla, S., Rudolph, P. E., Albrecht, D.,Metges, C. C., Proteomics analysis of hypothalamic response to energy restriction in dairy cows. Proteomics 2007, 7, 3602-3617.
    • (2007) Proteomics , vol.7 , pp. 3602-3617
    • Kuhla, B.1    Kuhla, S.2    Rudolph, P.E.3    Albrecht, D.4    Metges, C.C.5
  • 13
    • 34248155673 scopus 로고    scopus 로고
    • Abnormal glucose homeostasis in adult female rat offspring after intrauterine ethanol exposure
    • Yao, X. H., Nyomba, B. L., Abnormal glucose homeostasis in adult female rat offspring after intrauterine ethanol exposure. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2007, 292, R1926-R1933.
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.292
    • Yao, X.H.1    Nyomba, B.L.2
  • 14
    • 47549092773 scopus 로고    scopus 로고
    • Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring
    • Yao, X. H., Nyomba, B. L., Hepatic insulin resistance induced by prenatal alcohol exposure is associated with reduced PTEN and TRB3 acetylation in adult rat offspring. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2008, 294, R1797-R1806.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.294
    • Yao, X.H.1    Nyomba, B.L.2
  • 15
    • 33645470420 scopus 로고    scopus 로고
    • Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction
    • Rampitsch, C., Bykolva, N. V., McCallum, B., Beimcik, E., Ens, W., Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction. Proteomics 2006, 6, 1897-1907.
    • (2006) Proteomics , vol.6 , pp. 1897-1907
    • Rampitsch, C.1    Bykolva, N.V.2    McCallum, B.3    Beimcik, E.4    Ens, W.5
  • 16
  • 17
    • 0141926488 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins from the SARS virus: A preliminary report
    • Krokhin, O., Li, Y., Andonov, A., Feldmann, H. et al., Mass spectrometric characterization of proteins from the SARS virus: a preliminary report. Mol. Cell Proteomics 2003, 2, 346-356.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 346-356
    • Krokhin, O.1    Li, Y.2    Andonov, A.3    Feldmann, H.4
  • 18
    • 0842284006 scopus 로고    scopus 로고
    • Overexpression of adenosine kinase in epileptic hippocampus contributes to epileptogenesis
    • Gouder, N., Scheurer, L., Fritschy, J. M., Boison, D., Overexpression of adenosine kinase in epileptic hippocampus contributes to epileptogenesis. J. Neurosci. 2004, 24, 692-701.
    • (2004) J. Neurosci , vol.24 , pp. 692-701
    • Gouder, N.1    Scheurer, L.2    Fritschy, J.M.3    Boison, D.4
  • 19
    • 0029961930 scopus 로고    scopus 로고
    • Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase
    • Yuan, C. S., Ault-Riché , D. B., Borchardt, R. T., Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase. J. Biol. Chem. 1996, 271, 28009-28016.
    • (1996) J. Biol. Chem , vol.271 , pp. 28009-28016
    • Yuan, C.S.1    Ault-Riché, D.B.2    Borchardt, R.T.3
  • 21
    • 0021451019 scopus 로고
    • Fructose-1,6-biphosphatase activity in the intestinal mucosa of developing rats
    • Westbury, K., Hahn, P., Fructose-1,6-biphosphatase activity in the intestinal mucosa of developing rats. Am. J. Physiol. 1984, 246, G386-G686.
    • (1984) Am. J. Physiol , vol.246
    • Westbury, K.1    Hahn, P.2
  • 22
    • 33846632394 scopus 로고    scopus 로고
    • A comparative proteome and phosphoproteome analysis of differentially regulated proteins during fertilization in the self-incompatible species Solanum chacoense Bitt
    • Vyetrogon, K., Tebbji, F., Olson, D. J., Ross, A. R., Matton, D. P., A comparative proteome and phosphoproteome analysis of differentially regulated proteins during fertilization in the self-incompatible species Solanum chacoense Bitt. Proteomics 2007, 7, 232-247.
    • (2007) Proteomics , vol.7 , pp. 232-247
    • Vyetrogon, K.1    Tebbji, F.2    Olson, D.J.3    Ross, A.R.4    Matton, D.P.5
  • 23
    • 0023067301 scopus 로고    scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, and microorganisms
    • Theil, E. C., Ferritin: structure, gene regulation, and cellular function in animals, and microorganisms. Annu. Rev. Biochem. 2007, 56, 289-315.
    • (2007) Annu. Rev. Biochem , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 24
    • 0036613984 scopus 로고    scopus 로고
    • Proteomic analysis and molecular characterization of tissue ferritin light chain in hepatocellular carcinoma
    • Park, K. S., Kim, H., Kim, N. G., Cho, S. Y. et al., Proteomic analysis and molecular characterization of tissue ferritin light chain in hepatocellular carcinoma. Hepatology 2002, 35, 1459-1466.
    • (2002) Hepatology , vol.35 , pp. 1459-1466
    • Park, K.S.1    Kim, H.2    Kim, N.G.3    Cho, S.Y.4
  • 25
    • 0028928738 scopus 로고
    • Induction of ferritin synthesis by oxidative stress Transcriptional and post-transcriptional regulation by expansion of the 'free' iron pool
    • Cairo, G., Tacchini, L., Pogliaghi, G., Anzon, E. et al., Induction of ferritin synthesis by oxidative stress Transcriptional and post-transcriptional regulation by expansion of the 'free' iron pool. J. Biol. Chem. 1995, 270, 700-703.
    • (1995) J. Biol. Chem , vol.270 , pp. 700-703
    • Cairo, G.1    Tacchini, L.2    Pogliaghi, G.3    Anzon, E.4
  • 26
    • 0024333867 scopus 로고
    • The aldo-keto reductase superfamily cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • Bohren, K. M., Bullock, B., Wermuth, B., Gabbay, K. H., The aldo-keto reductase superfamily cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 1989, 264, 9547-9551.
    • (1989) J. Biol. Chem , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wermuth, B.3    Gabbay, K.H.4
  • 27
    • 34548509753 scopus 로고    scopus 로고
    • Aldoketo reductase 1 family B7 is the gene induced in response to oxidative stress in the livers of Long-Evans Cinnamon rats
    • Jia, G., Takahashi, R., Zhang, Z., Tsuji, Y., Sone, H., Aldoketo reductase 1 family B7 is the gene induced in response to oxidative stress in the livers of Long-Evans Cinnamon rats. Int. J. Oncol. 2006, 29, 829-838.
    • (2006) Int. J. Oncol , vol.29 , pp. 829-838
    • Jia, G.1    Takahashi, R.2    Zhang, Z.3    Tsuji, Y.4    Sone, H.5
  • 28
    • 33748456961 scopus 로고    scopus 로고
    • Intrauterine ethanol exposure results in hypothalamic oxidative stress and neuroendocrine alterations in adult rat offspring
    • Dembele, K., Yao, X. H., Chen, L., Nyomba, B. L., Intrauterine ethanol exposure results in hypothalamic oxidative stress and neuroendocrine alterations in adult rat offspring. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2006, 291, R796-R802.
    • (2006) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.291
    • Dembele, K.1    Yao, X.H.2    Chen, L.3    Nyomba, B.L.4
  • 29
    • 0025863978 scopus 로고
    • The rat fructose-1,6-bisphosphatase gene Structure and regulation of expression
    • el-Maghrabi, M. R., Lange, A. J., Kummel, L., Pilkis, S. J., The rat fructose-1,6-bisphosphatase gene Structure and regulation of expression. J. Biol. Chem. 1991, 266, 2115-2120.
    • (1991) J. Biol. Chem , vol.266 , pp. 2115-2120
    • el-Maghrabi, M.R.1    Lange, A.J.2    Kummel, L.3    Pilkis, S.J.4
  • 30
    • 10344259661 scopus 로고    scopus 로고
    • Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events
    • Hung, G. C., Brown, C. R., Wolfe, A. B., Liu, J., Chiang, H. L., Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J. Biol. Chem. 2004, 279, 49138-49150.
    • (2004) J. Biol. Chem , vol.279 , pp. 49138-49150
    • Hung, G.C.1    Brown, C.R.2    Wolfe, A.B.3    Liu, J.4    Chiang, H.L.5
  • 31
    • 0032842869 scopus 로고    scopus 로고
    • Rat muscle fructose-1,6-bisphosphatase: Cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues
    • Al-Robaiy, S., Eschrich, K., Rat muscle fructose-1,6-bisphosphatase: cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues. Biol. Chem. 1999, 380, 1079-1085.
    • (1999) Biol. Chem , vol.380 , pp. 1079-1085
    • Al-Robaiy, S.1    Eschrich, K.2
  • 32
    • 34250828455 scopus 로고    scopus 로고
    • Proteomic analysis of membrane-associated proteins from rat liver autophagosomes
    • Overbye, A., Fengsrud, M., Seglen, P. O., Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy 2007, 3, 300-322.
    • (2007) Autophagy , vol.3 , pp. 300-322
    • Overbye, A.1    Fengsrud, M.2    Seglen, P.O.3
  • 33
    • 8744270079 scopus 로고    scopus 로고
    • A strain-specific alteration of proteomic expression in mouse liver fructose 1,6-bisphosphatase isoforms by alcohol
    • Park, B., Oh, S. H., Seong, J. K., Paik, Y. K., A strain-specific alteration of proteomic expression in mouse liver fructose 1,6-bisphosphatase isoforms by alcohol. Proteomics 2004, 4, 3413-3421.
    • (2004) Proteomics , vol.4 , pp. 3413-3421
    • Park, B.1    Oh, S.H.2    Seong, J.K.3    Paik, Y.K.4
  • 34
    • 0026520193 scopus 로고
    • Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis
    • Pilkis, S. J., Granner, D. K., Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Annu. Rev. Physiol. 1992, 54, 885-909.
    • (1992) Annu. Rev. Physiol , vol.54 , pp. 885-909
    • Pilkis, S.J.1    Granner, D.K.2
  • 35
    • 67349230151 scopus 로고    scopus 로고
    • Nuclear targeting of FBPase in HL-1 cells is controlled by beta-1 adrenergic receptor-activated Gs protein signaling cascade
    • Gizak, A., Zarzycki, M., Rakus, D., Nuclear targeting of FBPase in HL-1 cells is controlled by beta-1 adrenergic receptor-activated Gs protein signaling cascade. Biochim. Biophys. Acta 2009, 1793, 871-877.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 871-877
    • Gizak, A.1    Zarzycki, M.2    Rakus, D.3
  • 36
    • 3042783224 scopus 로고    scopus 로고
    • Mice with deletion of the mitochondrial glycerol-3-phosphate dehydrogenase gene exhibit a thrifty phenotype: Effect of gender
    • Alfadda, A., DosSantos, R. A., Stepanyan, Z., Marrif, H., Silva, J. E., Mice with deletion of the mitochondrial glycerol-3-phosphate dehydrogenase gene exhibit a thrifty phenotype: effect of gender. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2004, 287, R147-R156.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.287
    • Alfadda, A.1    DosSantos, R.A.2    Stepanyan, Z.3    Marrif, H.4    Silva, J.E.5
  • 37
    • 58249092949 scopus 로고    scopus 로고
    • Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues
    • Overbye, A., Seglen, P. O., Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues. Biochem. J. 2009, 417, 535-545.
    • (2009) Biochem. J , vol.417 , pp. 535-545
    • Overbye, A.1    Seglen, P.O.2
  • 38
    • 0028970539 scopus 로고
    • Cytochrome b5, its functions, structure and membrane topology
    • Vergéres, G., Waskell, L, Cytochrome b5, its functions, structure and membrane topology. Biochimie 1995, 77, 604-620.
    • (1995) Biochimie , vol.77 , pp. 604-620
    • Vergéres, G.1    Waskell, L.2
  • 40
    • 0028432912 scopus 로고
    • Peptide-chain elongation in eukaryotes
    • Proud, C. G., Peptide-chain elongation in eukaryotes. Mol Biol Rep. 1994, 19, 161-170.
    • (1994) Mol Biol Rep , vol.19 , pp. 161-170
    • Proud, C.G.1
  • 41
    • 0034867233 scopus 로고    scopus 로고
    • Interplay between insulin and nutrients in the regulation of translation factors
    • Proud, C. G., Wang, X., Patel, J. V., Campbell, L. E. et al., Interplay between insulin and nutrients in the regulation of translation factors. Biochem. Soc.Trans. 2001, 29, 541-547.
    • (2001) Biochem. Soc.Trans , vol.29 , pp. 541-547
    • Proud, C.G.1    Wang, X.2    Patel, J.V.3    Campbell, L.E.4
  • 42
    • 2542527672 scopus 로고    scopus 로고
    • Putrescine biosynthesis in mammalian tissues
    • Coleman, C. S., Hu, G., Pegg, A. E., Putrescine biosynthesis in mammalian tissues. Biochem. J. 2004, 379, 849-855.
    • (2004) Biochem. J , vol.379 , pp. 849-855
    • Coleman, C.S.1    Hu, G.2    Pegg, A.E.3
  • 43
    • 0024555785 scopus 로고
    • Stimulussecretion coupling of arginine-induced insulin release Insulinotropic action of agmatine
    • Sener, A., Lebrun, P., Blachier, F., Malaisse, W. J., Stimulussecretion coupling of arginine-induced insulin release Insulinotropic action of agmatine. Biochem. Pharmacol. 1989, 38, 327-330.
    • (1989) Biochem. Pharmacol , vol.38 , pp. 327-330
    • Sener, A.1    Lebrun, P.2    Blachier, F.3    Malaisse, W.J.4
  • 44
    • 17844362774 scopus 로고    scopus 로고
    • Activation of imidazoline receptors in adrenal gland to lower plasma glucose in streptozotocin-induced diabetic rats
    • Hwang, S. L., Liu, I. M., Tzeng, T. F., Cheng, J. T., Activation of imidazoline receptors in adrenal gland to lower plasma glucose in streptozotocin-induced diabetic rats. Diabetologia 2005, 48, 767-775.
    • (2005) Diabetologia , vol.48 , pp. 767-775
    • Hwang, S.L.1    Liu, I.M.2    Tzeng, T.F.3    Cheng, J.T.4
  • 45
    • 33646839950 scopus 로고    scopus 로고
    • Agmatine stimulates hepaticfatty acid oxidation: A possible mechanism for up-regulation of ureagenesis
    • Nissim, I., Daikhin, Y., Luhovyy, B., Horyn, O. et al., Agmatine stimulates hepaticfatty acid oxidation: a possible mechanism for up-regulation of ureagenesis. J. Biol. Chem. 2006, 281, 8486-8496.
    • (2006) J. Biol. Chem , vol.281 , pp. 8486-8496
    • Nissim, I.1    Daikhin, Y.2    Luhovyy, B.3    Horyn, O.4
  • 46
    • 34548800397 scopus 로고    scopus 로고
    • Activation of protein kinase B/Akt and endothelial nitric oxide synthase mediates agmatine-induced endothelium-dependent relaxation
    • Santhanam, A. V., Viswanathan, S., Dikshit, M., Activation of protein kinase B/Akt and endothelial nitric oxide synthase mediates agmatine-induced endothelium-dependent relaxation. Eur. J. Pharmacol. 2007, 572, 189-196.
    • (2007) Eur. J. Pharmacol , vol.572 , pp. 189-196
    • Santhanam, A.V.1    Viswanathan, S.2    Dikshit, M.3
  • 48
    • 0032521641 scopus 로고    scopus 로고
    • Metabolism of agmatine in macrophages: Modulation by lipopolysaccharide and inhibitory cytokines
    • Sastre, M. G. E., Feinstein, D., Reis, D. J., Regunathan, S., Metabolism of agmatine in macrophages: modulation by lipopolysaccharide and inhibitory cytokines. Biochem. J. 1998, 330, 1405-1409
    • (1998) Biochem. J , vol.330 , pp. 1405-1409
    • Sastre, M.G.E.1    Feinstein, D.2    Reis, D.J.3    Regunathan, S.4
  • 49
  • 50
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari, D. M., Sling, H. D., The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 1999, 339, 1-10.
    • (1999) Biochem. J , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Sling, H.D.2
  • 51
    • 0030046449 scopus 로고    scopus 로고
    • Isolation from spleen of a 57 kDa protein substrate of the tyrosine kinase Lyn Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites
    • Donella-Deana, A., James, P., Staudenmann, W., Cesaro, L. et al., Isolation from spleen of a 57 kDa protein substrate of the tyrosine kinase Lyn Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites. Eur. J. Biochem. 1996, 235, 18-25.
    • (1996) Eur. J. Biochem , vol.235 , pp. 18-25
    • Donella-Deana, A.1    James, P.2    Staudenmann, W.3    Cesaro, L.4
  • 52
    • 29344442591 scopus 로고    scopus 로고
    • Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin
    • Kita, K., Okumura, N., Takao, T., Watanabe, M. et al., Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin. FEBS Lett. 2006, 580, 199-205.
    • (2006) FEBS Lett , vol.580 , pp. 199-205
    • Kita, K.1    Okumura, N.2    Takao, T.3    Watanabe, M.4
  • 54
    • 0031590635 scopus 로고    scopus 로고
    • Actin: A target of lipopolysaccharid-induced phosphorylation in human monocytes
    • Hauschildt, S., Schwarz, C., Heine, H., Ulmer, A. J. et al., Actin: A target of lipopolysaccharid-induced phosphorylation in human monocytes. Biochem. Biophys. Res. Commun. 1997, 241, 670-674.
    • (1997) Biochem. Biophys. Res. Commun , vol.241 , pp. 670-674
    • Hauschildt, S.1    Schwarz, C.2    Heine, H.3    Ulmer, A.J.4
  • 55
    • 0036678475 scopus 로고    scopus 로고
    • Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization
    • Papakonstanti, E. A., Stournaras, C., Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization. Mol. Biol. Cell. 2002, 13, 2946-2962.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2946-2962
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 56
    • 0032702020 scopus 로고    scopus 로고
    • Biochemical characterization of a casein kinase I-like actin kinase responsible for the actin-induced suppression of casein kinase II activity in vitro
    • Karino, A., Okano, M., Hatomi, M., Nakamura, T., Ohtsuki, K., Biochemical characterization of a casein kinase I-like actin kinase responsible for the actin-induced suppression of casein kinase II activity in vitro. Biochim. Biophys. Acta 1999, 1472, 603-616.
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 603-616
    • Karino, A.1    Okano, M.2    Hatomi, M.3    Nakamura, T.4    Ohtsuki, K.5
  • 57
    • 33645233517 scopus 로고    scopus 로고
    • Protein kinase CK2 subunits are positive regulators of AKT kinase
    • Guerra, B., Protein kinase CK2 subunits are positive regulators of AKT kinase. Int. J. Oncol. 2006, 28, 685-693.
    • (2006) Int. J. Oncol , vol.28 , pp. 685-693
    • Guerra, B.1
  • 58
    • 0024816772 scopus 로고
    • Prenatal exposure to ethanol alters the synthesis and glycosylation of proteins in fetal hepatocytes
    • Renau-Piqueras, J., Sancho-Tello, M., Baguena, C. R., Guerri, C., Prenatal exposure to ethanol alters the synthesis and glycosylation of proteins in fetal hepatocytes. Alcohol Clin. Exp. Res. 1989, 13, 817-823.
    • (1989) Alcohol Clin. Exp. Res , vol.13 , pp. 817-823
    • Renau-Piqueras, J.1    Sancho-Tello, M.2    Baguena, C.R.3    Guerri, C.4
  • 59
    • 2342535877 scopus 로고    scopus 로고
    • Prenatal ethanol exposure alters the cytoskeleton and induces glycoprotein microheterogeneity in rat newborn hepatocytes
    • Azorin, I., Portoles, M., Marin, P., Lazaro-Dieguez, F. et al., Prenatal ethanol exposure alters the cytoskeleton and induces glycoprotein microheterogeneity in rat newborn hepatocytes. Alcohol Alcohol 2004, 39, 203-212.
    • (2004) Alcohol Alcohol , vol.39 , pp. 203-212
    • Azorin, I.1    Portoles, M.2    Marin, P.3    Lazaro-Dieguez, F.4
  • 60
    • 0025080436 scopus 로고
    • Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter
    • Nagy, L. E., Diamond, I., Casso, D. J. S., Franklin, C., Gordon, A. S., Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. J. Biol. Chem. 1990, 265, 1946-1951.
    • (1990) J. Biol. Chem , vol.265 , pp. 1946-1951
    • Nagy, L.E.1    Diamond, I.2    Casso, D.J.S.3    Franklin, C.4    Gordon, A.S.5
  • 61
    • 0033954723 scopus 로고    scopus 로고
    • Chronic hypoxia enhances adenosine release in rat PC12 cells by altering adenosine metabolism and membrane transport
    • Kobayashi, S., Zimmermann, H., Millhorn, E. D., Chronic hypoxia enhances adenosine release in rat PC12 cells by altering adenosine metabolism and membrane transport. J. Neurochem. 2000, 74, 621-632.
    • (2000) J. Neurochem , vol.74 , pp. 621-632
    • Kobayashi, S.1    Zimmermann, H.2    Millhorn, E.D.3
  • 62
    • 0025820148 scopus 로고
    • Modulation of maximal glycogenolysis in perfused rat liver by adenosine and ATP
    • Vanstapel, F., Waebens, M., Van Hecke, P., Decanniere, C., Stalmans, W., Modulation of maximal glycogenolysis in perfused rat liver by adenosine and ATP. Biochem. J. 1991, 277, 597-602.
    • (1991) Biochem. J , vol.277 , pp. 597-602
    • Vanstapel, F.1    Waebens, M.2    Van Hecke, P.3    Decanniere, C.4    Stalmans, W.5
  • 63
    • 33745815985 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling in metabolic regulation
    • Long, Y. C., Zierath, J. R., AMP-activated protein kinase signaling in metabolic regulation. J. Clin. Invest 2006, 116, 1776-1783.
    • (2006) J. Clin. Invest , vol.116 , pp. 1776-1783
    • Long, Y.C.1    Zierath, J.R.2
  • 64
    • 1642328617 scopus 로고    scopus 로고
    • Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398
    • Browne, G. J., Finn, S. G., Proud, C. G., Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. J. Biol. Chem. 2004, 279, 12220-12231.
    • (2004) J. Biol. Chem , vol.279 , pp. 12220-12231
    • Browne, G.J.1    Finn, S.G.2    Proud, C.G.3
  • 65
    • 2542450761 scopus 로고    scopus 로고
    • Identification of novel molecular candidates for fatty liver in the hyperlipidemic mouse model, HcB19
    • Van Greevenbroek, M. M., Vermeulen, V. M., De Bruin, T. W., Identification of novel molecular candidates for fatty liver in the hyperlipidemic mouse model, HcB19. J. Lipid Res. 2004, 45, 1148-1154.
    • (2004) J. Lipid Res , vol.45 , pp. 1148-1154
    • Van Greevenbroek, M.M.1    Vermeulen, V.M.2    De Bruin, T.W.3
  • 66
    • 19644363211 scopus 로고    scopus 로고
    • Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of a complex oxidation involved in NAD biosynthesis
    • Zhang, Y., Colabroy, K. L., Begley, T. P., Ealick, S. E., Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry 2005, 44, 7632-7643.
    • (2005) Biochemistry , vol.44 , pp. 7632-7643
    • Zhang, Y.1    Colabroy, K.L.2    Begley, T.P.3    Ealick, S.E.4
  • 67
    • 0027257930 scopus 로고
    • A mechanism for increased quinolinic acid formation following acute systemic immune stimulation
    • Saito, K., Crowley, J. S., Markey, S. P., Heyes, M. P., A mechanism for increased quinolinic acid formation following acute systemic immune stimulation. J. Biol. Chem. 1993, 268, 15496-15503.
    • (1993) J. Biol. Chem , vol.268 , pp. 15496-15503
    • Saito, K.1    Crowley, J.S.2    Markey, S.P.3    Heyes, M.P.4
  • 68
    • 38049056756 scopus 로고    scopus 로고
    • Lelli, S. M., Mazzetti, M. B., San Martin de Viale, L. C., Hepatic alteration of tryptophan metabolism in an acute porphyria model Its relation with gluconeogenic blockage. Biochem. Pharmacol. 2008, 75, 704-712.
    • Lelli, S. M., Mazzetti, M. B., San Martin de Viale, L. C., Hepatic alteration of tryptophan metabolism in an acute porphyria model Its relation with gluconeogenic blockage. Biochem. Pharmacol. 2008, 75, 704-712.
  • 69
    • 20444452928 scopus 로고    scopus 로고
    • Prenatal alcohol exposure and fetal programming: Effects on neuroendocrine and immune function
    • Zhang, X., Sliwowska, J. H., Weinberg, J., Prenatal alcohol exposure and fetal programming: effects on neuroendocrine and immune function. Exp. Biol. Med. (Maywood) 2005, 230, 376-388.
    • (2005) Exp. Biol. Med. (Maywood) , vol.230 , pp. 376-388
    • Zhang, X.1    Sliwowska, J.H.2    Weinberg, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.