메뉴 건너뛰기




Volumn 30, Issue 3, 2005, Pages 142-150

Multifaceted roles of glycolytic enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ENOLASE; GLUCOKINASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEXOKINASE; ISOENZYME; LACTATE DEHYDROGENASE;

EID: 14744284637     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.01.005     Document Type: Review
Times cited : (545)

References (93)
  • 1
    • 0037197960 scopus 로고    scopus 로고
    • The global phylogeny of glycolytic enzymes
    • B. Canback The global phylogeny of glycolytic enzymes Proc. Natl. Acad. Sci. U. S. A. 99 2002 6097 6102
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6097-6102
    • Canback, B.1
  • 2
  • 4
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein
    • M. Ohh Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein Nat. Cell Biol. 2 2000 423 427
    • (2000) Nat. Cell Biol. , vol.2 , pp. 423-427
    • Ohh, M.1
  • 5
    • 0033776182 scopus 로고    scopus 로고
    • VHL takes HIF's breath away
    • W. Krek VHL takes HIF's breath away Nat. Cell Biol. 2 2000 E121 E123
    • (2000) Nat. Cell Biol. , vol.2
    • Krek, W.1
  • 6
    • 0035917808 scopus 로고    scopus 로고
    • 2-regulated prolyl hydroxylation
    • 2-regulated prolyl hydroxylation Science 292 2001 468 472
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 7
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase a gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • G.L. Semenza Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1 J. Biol. Chem. 271 1996 32529 32537
    • (1996) J. Biol. Chem. , vol.271 , pp. 32529-32537
    • Semenza, G.L.1
  • 8
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • G.L. Semenza Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1 J. Biol. Chem. 269 1994 23757 23763
    • (1994) J. Biol. Chem. , vol.269 , pp. 23757-23763
    • Semenza, G.L.1
  • 9
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • O. Warburg On the origin of cancer cells Science 123 1956 309 314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 10
  • 11
    • 2542561169 scopus 로고    scopus 로고
    • Akt stimulates aerobic glycolysis in cancer cells
    • R.L. Elstrom Akt stimulates aerobic glycolysis in cancer cells Cancer Res. 64 2004 3892 3899
    • (2004) Cancer Res. , vol.64 , pp. 3892-3899
    • Elstrom, R.L.1
  • 12
    • 2942701935 scopus 로고    scopus 로고
    • Evaluation of myc E-box phylogenetic footprints in glycolytic genes by chromatin immunoprecipitation assays
    • J.W. Kim Evaluation of myc E-box phylogenetic footprints in glycolytic genes by chromatin immunoprecipitation assays Mol. Cell. Biol. 24 2004 5923 5936
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5923-5936
    • Kim, J.W.1
  • 13
    • 4444313558 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumour suppressor: A multi-faceted inhibitor of tumourigenesis
    • R.E. Barry, and W. Krek The von Hippel-Lindau tumour suppressor: a multi-faceted inhibitor of tumourigenesis Trends Mol. Med. 10 2004 466 472
    • (2004) Trends Mol. Med. , vol.10 , pp. 466-472
    • Barry, R.E.1    Krek, W.2
  • 14
    • 0025748777 scopus 로고
    • A regulated RNA binding protein also possesses aconitase activity
    • S. Kaptain A regulated RNA binding protein also possesses aconitase activity Proc. Natl. Acad. Sci. U. S. A. 88 1991 10109 10113
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10109-10113
    • Kaptain, S.1
  • 15
    • 0026062191 scopus 로고
    • Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: Functional implications
    • T.A. Rouault Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications Cell 64 1991 881 883
    • (1991) Cell , vol.64 , pp. 881-883
    • Rouault, T.A.1
  • 16
    • 5644229499 scopus 로고    scopus 로고
    • Regulation of gene expression by a metabolic enzyme
    • D.A. Hall Regulation of gene expression by a metabolic enzyme Science 306 2004 482 484
    • (2004) Science , vol.306 , pp. 482-484
    • Hall, D.A.1
  • 17
    • 0026512705 scopus 로고
    • Glucose repression in the yeast Saccharomyces cerevisiae
    • R.J. Trumbly Glucose repression in the yeast Saccharomyces cerevisiae Mol. Microbiol. 6 1992 15 21
    • (1992) Mol. Microbiol. , vol.6 , pp. 15-21
    • Trumbly, R.J.1
  • 18
    • 0035319651 scopus 로고    scopus 로고
    • Physiological properties of Saccharomyces cerevisiae from which hexokinase II has been deleted
    • J.A. Diderich Physiological properties of Saccharomyces cerevisiae from which hexokinase II has been deleted Appl. Environ. Microbiol. 67 2001 1587 1593
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1587-1593
    • Diderich, J.A.1
  • 19
    • 0029890767 scopus 로고    scopus 로고
    • Identification and characterisation of two transcriptional repressor elements within the coding sequence of the Saccharomyces cerevisiae HXK2 gene
    • P. Herrero Identification and characterisation of two transcriptional repressor elements within the coding sequence of the Saccharomyces cerevisiae HXK2 gene Nucleic Acids Res. 24 1996 1822 1828
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1822-1828
    • Herrero, P.1
  • 20
    • 0028797325 scopus 로고
    • Transcriptional regulation of the Saccharomyces cerevisiae HXK1, HXK2 and GLK1 genes
    • P. Herrero Transcriptional regulation of the Saccharomyces cerevisiae HXK1, HXK2 and GLK1 genes Yeast 11 1995 137 144
    • (1995) Yeast , vol.11 , pp. 137-144
    • Herrero, P.1
  • 21
    • 0025901117 scopus 로고
    • Characterization of Hex2 protein, a negative regulatory element necessary for glucose repression in yeast
    • D. Niederacher, and K.D. Entian Characterization of Hex2 protein, a negative regulatory element necessary for glucose repression in yeast Eur. J. Biochem. 200 1991 311 319
    • (1991) Eur. J. Biochem. , vol.200 , pp. 311-319
    • Niederacher, D.1    Entian, K.D.2
  • 22
    • 0035339662 scopus 로고    scopus 로고
    • The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae
    • A. Rodriguez The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae Biochem. J. 355 2001 625 631
    • (2001) Biochem. J. , vol.355 , pp. 625-631
    • Rodriguez, A.1
  • 23
    • 0345647082 scopus 로고    scopus 로고
    • The hexokinase 2 protein participates in regulatory DNA-protein complexes necessary for glucose repression of the SUC2 gene in Saccharomyces cerevisiae
    • P. Herrero The hexokinase 2 protein participates in regulatory DNA-protein complexes necessary for glucose repression of the SUC2 gene in Saccharomyces cerevisiae FEBS Lett. 434 1998 71 76
    • (1998) FEBS Lett. , vol.434 , pp. 71-76
    • Herrero, P.1
  • 24
    • 1842790124 scopus 로고    scopus 로고
    • The glucose-regulated nuclear localization of hexokinase 2 in Saccharomyces cerevisiae is Mig1-dependent
    • D. Ahuatzi The glucose-regulated nuclear localization of hexokinase 2 in Saccharomyces cerevisiae is Mig1-dependent J. Biol. Chem. 279 2004 14440 14446
    • (2004) J. Biol. Chem. , vol.279 , pp. 14440-14446
    • Ahuatzi, D.1
  • 25
    • 0036301441 scopus 로고    scopus 로고
    • Mediator factor Med8p interacts with the hexokinase 2: Implication in the glucose signalling pathway of Saccharomyces cerevisiae
    • T. de la Cera Mediator factor Med8p interacts with the hexokinase 2: implication in the glucose signalling pathway of Saccharomyces cerevisiae J. Mol. Biol. 319 2002 703 714
    • (2002) J. Mol. Biol. , vol.319 , pp. 703-714
    • De La Cera, T.1
  • 26
    • 0030468365 scopus 로고    scopus 로고
    • Glucose regulates protein interactions within the yeast SNF1 protein kinase complex
    • R. Jiang, and M. Carlson Glucose regulates protein interactions within the yeast SNF1 protein kinase complex Genes Dev. 10 1996 3105 3115
    • (1996) Genes Dev. , vol.10 , pp. 3105-3115
    • Jiang, R.1    Carlson, M.2
  • 27
    • 0035338114 scopus 로고    scopus 로고
    • Subcellular localization of the Snf1 kinase is regulated by specific β subunits and a novel glucose signaling mechanism
    • O. Vincent Subcellular localization of the Snf1 kinase is regulated by specific β subunits and a novel glucose signaling mechanism Genes Dev. 15 2001 1104 1114
    • (2001) Genes Dev. , vol.15 , pp. 1104-1114
    • Vincent, O.1
  • 28
    • 0033974002 scopus 로고    scopus 로고
    • Regulatory interactions between the Reg1-Glc7 protein phosphatase and the Snf1 protein kinase
    • P. Sanz Regulatory interactions between the Reg1-Glc7 protein phosphatase and the Snf1 protein kinase Mol. Cell. Biol. 20 2000 1321 1328
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1321-1328
    • Sanz, P.1
  • 29
    • 0022408729 scopus 로고
    • Nuclear localization of a lactic dehydrogenase with single-stranded DNA-binding properties
    • A. Cattaneo Nuclear localization of a lactic dehydrogenase with single-stranded DNA-binding properties Exp. Cell Res. 161 1985 130 140
    • (1985) Exp. Cell Res. , vol.161 , pp. 130-140
    • Cattaneo, A.1
  • 30
    • 0022894808 scopus 로고
    • Lactate dehydrogenase and glyceraldehyde-phosphate dehydrogenase are single-stranded DNA-binding proteins that affect the DNA-polymerase-α- primase complex
    • F. Grosse Lactate dehydrogenase and glyceraldehyde-phosphate dehydrogenase are single-stranded DNA-binding proteins that affect the DNA-polymerase-α-primase complex Eur. J. Biochem. 160 1986 459 467
    • (1986) Eur. J. Biochem. , vol.160 , pp. 459-467
    • Grosse, F.1
  • 31
    • 0021845990 scopus 로고
    • Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5
    • K.R. Williams Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5 Proc. Natl. Acad. Sci. U. S. A. 82 1985 5260 5264
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 5260-5264
    • Williams, K.R.1
  • 32
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • L. Zheng S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component Cell 114 2003 255 266
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1
  • 33
    • 0021254544 scopus 로고
    • Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro
    • J.A. Cooper Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro J. Biol. Chem. 259 1984 7835 7841
    • (1984) J. Biol. Chem. , vol.259 , pp. 7835-7841
    • Cooper, J.A.1
  • 34
    • 0022834087 scopus 로고
    • Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase
    • N. Reiss Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase Biochem. J. 239 1986 691 697
    • (1986) Biochem. J. , vol.239 , pp. 691-697
    • Reiss, N.1
  • 35
    • 0025174640 scopus 로고
    • Phosphotyrosine-containing lactate dehydrogenase is restricted to the nuclei of PC12 pheochromocytoma cells
    • X.H. Zhong, and B.D. Howard Phosphotyrosine-containing lactate dehydrogenase is restricted to the nuclei of PC12 pheochromocytoma cells Mol. Cell. Biol. 10 1990 770 776
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 770-776
    • Zhong, X.H.1    Howard, B.D.2
  • 36
    • 0034726714 scopus 로고    scopus 로고
    • Identification of the NAD(+)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain
    • E. Nagy Identification of the NAD(+)-binding fold of glyceraldehyde-3- phosphate dehydrogenase as a novel RNA-binding domain Biochem. Biophys. Res. Commun. 275 2000 253 260
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 253-260
    • Nagy, E.1
  • 37
    • 0019334977 scopus 로고
    • Study of the interaction of glyceraldehyde-3-phosphate dehydrogenase with DNA
    • M. Perucho Study of the interaction of glyceraldehyde-3-phosphate dehydrogenase with DNA Biochim. Biophys. Acta 606 1980 181 195
    • (1980) Biochim. Biophys. Acta , vol.606 , pp. 181-195
    • Perucho, M.1
  • 38
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • M.A. Sirover New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase Biochim. Biophys. Acta 1432 1999 159 184
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 39
    • 1242294390 scopus 로고    scopus 로고
    • Rapid shortening of telomere length in response to ceramide involves the inhibition of telomere binding activity of nuclear glyceraldehyde-3-phosphate dehydrogenase
    • K.P. Sundararaj Rapid shortening of telomere length in response to ceramide involves the inhibition of telomere binding activity of nuclear glyceraldehyde-3-phosphate dehydrogenase J. Biol. Chem. 279 2004 6152 6162
    • (2004) J. Biol. Chem. , vol.279 , pp. 6152-6162
    • Sundararaj, K.P.1
  • 40
    • 0034078845 scopus 로고    scopus 로고
    • Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro
    • S. Choudhary Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro J. Virol. 74 2000 3634 3641
    • (2000) J. Virol. , vol.74 , pp. 3634-3641
    • Choudhary, S.1
  • 41
    • 0029760743 scopus 로고    scopus 로고
    • Specific interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and la protein with cis-acting RNAs of human parainfluenza virus type 3
    • B.P. De Specific interaction in vitro and in vivo of glyceraldehyde-3- phosphate dehydrogenase and LA protein with cis-acting RNAs of human parainfluenza virus type 3 J. Biol. Chem. 271 1996 24728 24735
    • (1996) J. Biol. Chem. , vol.271 , pp. 24728-24735
    • De B., P.1
  • 42
    • 0037316278 scopus 로고    scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with secondary and tertiary RNA structural elements of the hepatitis a virus 3′ translated and non-translated regions
    • G. Dollenmaier, and M. Weitz Interaction of glyceraldehyde-3-phosphate dehydrogenase with secondary and tertiary RNA structural elements of the hepatitis A virus 3′ translated and non-translated regions J. Gen. Virol. 84 2003 403 414
    • (2003) J. Gen. Virol. , vol.84 , pp. 403-414
    • Dollenmaier, G.1    Weitz, M.2
  • 43
    • 0029927267 scopus 로고    scopus 로고
    • Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis a virus
    • D.E. Schultz Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis A virus J. Biol. Chem. 271 1996 14134 14142
    • (1996) J. Biol. Chem. , vol.271 , pp. 14134-14142
    • Schultz, D.E.1
  • 44
    • 0029870382 scopus 로고    scopus 로고
    • Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3- phosphate dehydrogenase
    • M. Sioud, and L. Jespersen Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase J. Mol. Biol. 257 1996 775 789
    • (1996) J. Mol. Biol. , vol.257 , pp. 775-789
    • Sioud, M.1    Jespersen, L.2
  • 45
    • 0037144420 scopus 로고    scopus 로고
    • Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1
    • P.A. Pioli Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1 J. Biol. Chem. 277 2002 35738 35745
    • (2002) J. Biol. Chem. , vol.277 , pp. 35738-35745
    • Pioli, P.A.1
  • 46
    • 0028816615 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold)
    • E. Nagy, and W.F. Rigby Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold) J. Biol. Chem. 270 1995 2755 2763
    • (1995) J. Biol. Chem. , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.2
  • 47
    • 0029691198 scopus 로고    scopus 로고
    • Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • M.A. Sirover Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells Life Sci. 58 1996 2271 2277
    • (1996) Life Sci. , vol.58 , pp. 2271-2277
    • Sirover, M.A.1
  • 48
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • M.A. Sirover Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology J. Cell. Biochem. 66 1997 133 140
    • (1997) J. Cell. Biochem. , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 49
    • 0029101797 scopus 로고
    • Human breast carcinoma cells transfected with the gene encoding a c-myc promoter-binding protein (MBP-1) inhibits tumors in nude mice
    • R.B. Ray Human breast carcinoma cells transfected with the gene encoding a c-myc promoter-binding protein (MBP-1) inhibits tumors in nude mice Cancer Res. 55 1995 3747 3751
    • (1995) Cancer Res. , vol.55 , pp. 3747-3751
    • Ray, R.B.1
  • 50
    • 0032940198 scopus 로고    scopus 로고
    • Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation
    • A.K. Ghosh Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation Mol. Cell. Biol. 19 1999 2880 2886
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2880-2886
    • Ghosh, A.K.1
  • 51
    • 0034009502 scopus 로고    scopus 로고
    • Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene
    • A. Subramanian, and D.M. Miller Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene J. Biol. Chem. 275 2000 5958 5965
    • (2000) J. Biol. Chem. , vol.275 , pp. 5958-5965
    • Subramanian, A.1    Miller, D.M.2
  • 52
    • 0033526809 scopus 로고    scopus 로고
    • MBP-1 physically associates with histone deacetylase for transcriptional repression
    • A.K. Ghosh MBP-1 physically associates with histone deacetylase for transcriptional repression Biochem. Biophys. Res. Commun. 260 1999 405 409
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 405-409
    • Ghosh, A.K.1
  • 53
    • 0035159316 scopus 로고    scopus 로고
    • A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1
    • A.K. Ghosh A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1 Mol. Cell. Biol. 21 2001 655 662
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 655-662
    • Ghosh, A.K.1
  • 54
    • 0034604055 scopus 로고    scopus 로고
    • ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: Relationship with Myc promoter-binding protein 1 (MBP-1)
    • S. Feo ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1) FEBS Lett. 473 2000 47 52
    • (2000) FEBS Lett. , vol.473 , pp. 47-52
    • Feo, S.1
  • 55
    • 0141679425 scopus 로고    scopus 로고
    • Enolase-α is frequently down-regulated in non-small cell lung cancer and predicts aggressive biological behavior
    • Y.S. Chang Enolase-α is frequently down-regulated in non-small cell lung cancer and predicts aggressive biological behavior Clin. Cancer Res. 9 2003 3641 3644
    • (2003) Clin. Cancer Res. , vol.9 , pp. 3641-3644
    • Chang, Y.S.1
  • 56
    • 0037013865 scopus 로고    scopus 로고
    • LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional enolase
    • H. Lee LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional enolase EMBO J. 21 2002 2692 2702
    • (2002) EMBO J. , vol.21 , pp. 2692-2702
    • Lee, H.1
  • 57
    • 0034815951 scopus 로고    scopus 로고
    • Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome
    • T. Ogino Enolase, a cellular glycolytic enzyme, is required for efficient transcription of Sendai virus genome Biochem. Biophys. Res. Commun. 285 2001 447 455
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 447-455
    • Ogino, T.1
  • 58
    • 0025218127 scopus 로고
    • Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA encoding a mitochondrial bindable form of hexokinase
    • K.K. Arora Glucose phosphorylation in tumor cells. Cloning, sequencing, and overexpression in active form of a full-length cDNA encoding a mitochondrial bindable form of hexokinase J. Biol. Chem. 265 1990 6481 6488
    • (1990) J. Biol. Chem. , vol.265 , pp. 6481-6488
    • Arora, K.K.1
  • 59
    • 0029891049 scopus 로고    scopus 로고
    • Glucose catabolism in cancer cells: Amplification of the gene encoding type II hexokinase
    • A. Rempel Glucose catabolism in cancer cells: amplification of the gene encoding type II hexokinase Cancer Res. 56 1996 2468 2471
    • (1996) Cancer Res. , vol.56 , pp. 2468-2471
    • Rempel, A.1
  • 60
    • 0030670597 scopus 로고    scopus 로고
    • Hexokinase binding to mitochondria: A basis for proliferative energy metabolism
    • S.G. Golshani-Hebroni, and S.P. Bessman Hexokinase binding to mitochondria: a basis for proliferative energy metabolism J. Bioenerg. Biomembr. 29 1997 331 338
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 331-338
    • Golshani-Hebroni, S.G.1    Bessman, S.P.2
  • 61
    • 0041309460 scopus 로고    scopus 로고
    • Hexokinase II: The integration of energy metabolism and control of apoptosis
    • J.G. Pastorino, and J.B. Hoek Hexokinase II: the integration of energy metabolism and control of apoptosis Curr. Med. Chem. 10 2003 1535 1551
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1535-1551
    • Pastorino, J.G.1    Hoek, J.B.2
  • 62
    • 0037192787 scopus 로고    scopus 로고
    • Increased hexokinase activity, of either ectopic or endogenous origin, protects renal epithelial cells against acute oxidant-induced cell death
    • J.M. Bryson Increased hexokinase activity, of either ectopic or endogenous origin, protects renal epithelial cells against acute oxidant-induced cell death J. Biol. Chem. 277 2002 11392 11400
    • (2002) J. Biol. Chem. , vol.277 , pp. 11392-11400
    • Bryson, J.M.1
  • 63
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • K. Gottlob Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase Genes Dev. 15 2001 1406 1418
    • (2001) Genes Dev. , vol.15 , pp. 1406-1418
    • Gottlob, K.1
  • 64
    • 0347986675 scopus 로고    scopus 로고
    • Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases
    • N. Majewski Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases Mol. Cell. Biol. 24 2004 730 740
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 730-740
    • Majewski, N.1
  • 65
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • J.G. Pastorino Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis J. Biol. Chem. 277 2002 7610 7618
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1
  • 66
    • 0141863388 scopus 로고    scopus 로고
    • Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival
    • J.C. Rathmell Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival Mol. Cell. Biol. 23 2003 7315 7328
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7315-7328
    • Rathmell, J.C.1
  • 67
    • 0041357164 scopus 로고    scopus 로고
    • BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
    • N.N. Danial BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis Nature 424 2003 952 956
    • (2003) Nature , vol.424 , pp. 952-956
    • Danial, N.N.1
  • 68
    • 0032972037 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis
    • P.A. Saunders Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis J. Neurochem. 72 1999 925 932
    • (1999) J. Neurochem. , vol.72 , pp. 925-932
    • Saunders, P.A.1
  • 69
    • 0029838525 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons
    • R. Ishitani, and D.M. Chuang Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside- induced apoptosis in cultured cerebellar neurons Proc. Natl. Acad. Sci. U. S. A. 93 1996 9937 9941
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 9937-9941
    • Ishitani, R.1    Chuang, D.M.2
  • 70
    • 0033551557 scopus 로고    scopus 로고
    • Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs
    • H. Tajima Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs Neuroreport 10 1999 2029 2033
    • (1999) Neuroreport , vol.10 , pp. 2029-2033
    • Tajima, H.1
  • 71
    • 0035017658 scopus 로고    scopus 로고
    • Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress
    • Z. Dastoor, and J.L. Dreyer Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress J. Cell Sci. 114 2001 1643 1653
    • (2001) J. Cell Sci. , vol.114 , pp. 1643-1653
    • Dastoor, Z.1    Dreyer, J.L.2
  • 72
    • 0033528794 scopus 로고    scopus 로고
    • Nuclear translocation of GAPDH-GFP fusion protein during apoptosis
    • P. Shashidharan Nuclear translocation of GAPDH-GFP fusion protein during apoptosis Neuroreport 10 1999 1149 1153
    • (1999) Neuroreport , vol.10 , pp. 1149-1153
    • Shashidharan, P.1
  • 73
    • 0035145627 scopus 로고    scopus 로고
    • Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts
    • J.L. Mazzola, and M.A. Sirover Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts J. Neurochem. 76 2001 442 449
    • (2001) J. Neurochem. , vol.76 , pp. 442-449
    • Mazzola, J.L.1    Sirover, M.A.2
  • 74
    • 1242316968 scopus 로고    scopus 로고
    • A novel CRM1-mediated nuclear export signal governs nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase following genotoxic stress
    • V.M. Brown A novel CRM1-mediated nuclear export signal governs nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase following genotoxic stress J. Biol. Chem. 279 2004 5984 5992
    • (2004) J. Biol. Chem. , vol.279 , pp. 5984-5992
    • Brown, V.M.1
  • 75
    • 0032489392 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(-)-deprenyl
    • E. Kragten Glyceraldehyde-3-phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(-)-deprenyl J. Biol. Chem. 273 1998 5821 5828
    • (1998) J. Biol. Chem. , vol.273 , pp. 5821-5828
    • Kragten, E.1
  • 76
    • 0037228781 scopus 로고    scopus 로고
    • A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues
    • E.Y. Krynetski A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues Cancer Res. 63 2003 100 106
    • (2003) Cancer Res. , vol.63 , pp. 100-106
    • Krynetski, E.Y.1
  • 77
    • 1942501739 scopus 로고    scopus 로고
    • Identification of GAPDH as a protein target of the saframycin antiproliferative agents
    • C. Xing Identification of GAPDH as a protein target of the saframycin antiproliferative agents Proc. Natl. Acad. Sci. U. S. A. 101 2004 5862 5866
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 5862-5866
    • Xing, C.1
  • 78
    • 0037438118 scopus 로고    scopus 로고
    • Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts
    • J.L. Mazzola, and M.A. Sirover Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts J. Neurosci. Res. 71 2003 279 285
    • (2003) J. Neurosci. Res. , vol.71 , pp. 279-285
    • Mazzola, J.L.1    Sirover, M.A.2
  • 79
    • 0031788691 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts
    • A.J. Cooper Glyceraldehyde 3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts Dev. Neurosci. 20 1998 462 468
    • (1998) Dev. Neurosci. , vol.20 , pp. 462-468
    • Cooper, A.J.1
  • 80
    • 0033545874 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin
    • Y.J. Sun The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin Proc. Natl. Acad. Sci. U. S. A. 96 1999 5412 5417
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5412-5417
    • Sun, Y.J.1
  • 81
    • 0022492694 scopus 로고
    • Tumor cell autocrine motility factor
    • L.A. Liotta Tumor cell autocrine motility factor Proc. Natl. Acad. Sci. U. S. A. 83 1986 3302 3306
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 3302-3306
    • Liotta, L.A.1
  • 82
    • 0032525859 scopus 로고    scopus 로고
    • Expression and secretion of neuroleukin/phosphohexose isomerase/maturation factor as autocrine motility factor by tumor cells
    • Y. Niinaka Expression and secretion of neuroleukin/phosphohexose isomerase/maturation factor as autocrine motility factor by tumor cells Cancer Res. 58 1998 2667 2674
    • (1998) Cancer Res. , vol.58 , pp. 2667-2674
    • Niinaka, Y.1
  • 83
    • 0025134024 scopus 로고
    • Identification of B16-F1 melanoma autocrine motility-like factor receptor
    • I.R. Nabi Identification of B16-F1 melanoma autocrine motility-like factor receptor Cancer Res. 50 1990 409 414
    • (1990) Cancer Res. , vol.50 , pp. 409-414
    • Nabi, I.R.1
  • 84
    • 0030469819 scopus 로고    scopus 로고
    • Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer
    • Y. Hirono Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer Br. J. Cancer 74 1996 2003 2007
    • (1996) Br. J. Cancer , vol.74 , pp. 2003-2007
    • Hirono, Y.1
  • 85
    • 0037224507 scopus 로고    scopus 로고
    • Overexpression of the autocrine motility factor/phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts
    • S. Tsutsumi Overexpression of the autocrine motility factor/ phosphoglucose isomerase induces transformation and survival of NIH-3T3 fibroblasts Cancer Res. 63 2003 242 249
    • (2003) Cancer Res. , vol.63 , pp. 242-249
    • Tsutsumi, S.1
  • 86
    • 0027939436 scopus 로고
    • Autocrine motility factor induces differential 12-lipoxygenase expression and activity in high- and low-metastatic K1735 melanoma cell variants
    • S. Silletti Autocrine motility factor induces differential 12-lipoxygenase expression and activity in high- and low-metastatic K1735 melanoma cell variants Cancer Res. 54 1994 5752 5756
    • (1994) Cancer Res. , vol.54 , pp. 5752-5756
    • Silletti, S.1
  • 87
    • 0033757239 scopus 로고    scopus 로고
    • Autocrine motility factor (neuroleukin, phosphohexose isomerase) induces cell movement through 12-lipoxygenase-dependent tyrosine phosphorylation and serine dephosphorylation events
    • J. Timar Autocrine motility factor (neuroleukin, phosphohexose isomerase) induces cell movement through 12-lipoxygenase-dependent tyrosine phosphorylation and serine dephosphorylation events Clin. Exp. Metastasis 17 1999 809 816
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 809-816
    • Timar, J.1
  • 88
    • 0034955987 scopus 로고    scopus 로고
    • Autocrine motility factor enhances hepatoma cell invasion across the basement membrane through activation of beta1 integrins
    • T. Torimura Autocrine motility factor enhances hepatoma cell invasion across the basement membrane through activation of beta1 integrins Hepatology 34 2001 62 71
    • (2001) Hepatology , vol.34 , pp. 62-71
    • Torimura, T.1
  • 89
    • 0036682378 scopus 로고    scopus 로고
    • Activation of small GTPase Rho is required for autocrine motility factor signaling
    • S. Tsutsumi Activation of small GTPase Rho is required for autocrine motility factor signaling Cancer Res. 62 2002 4484 4490
    • (2002) Cancer Res. , vol.62 , pp. 4484-4490
    • Tsutsumi, S.1
  • 90
    • 1942442191 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein-3 interacts with autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and inhibits the AMF/PGI function
    • S. Mishra Insulin-like growth factor binding protein-3 interacts with autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and inhibits the AMF/PGI function Cancer Res. 64 2004 2516 2522
    • (2004) Cancer Res. , vol.64 , pp. 2516-2522
    • Mishra, S.1
  • 91
    • 0037448448 scopus 로고    scopus 로고
    • The enzymatic activity of phosphoglucose isomerase is not required for its cytokine function
    • S. Tsutsumi The enzymatic activity of phosphoglucose isomerase is not required for its cytokine function FEBS Lett. 534 2003 49 53
    • (2003) FEBS Lett. , vol.534 , pp. 49-53
    • Tsutsumi, S.1
  • 92
    • 2942542677 scopus 로고    scopus 로고
    • Potential endocrine function of the glycolytic enzyme glucose-6-phosphate isomerase during implantation
    • L.C. Schulz, and J.M. Bahr Potential endocrine function of the glycolytic enzyme glucose-6-phosphate isomerase during implantation Gen. Comp. Endocrinol. 137 2004 283 287
    • (2004) Gen. Comp. Endocrinol. , vol.137 , pp. 283-287
    • Schulz, L.C.1    Bahr, J.M.2
  • 93
    • 0030012538 scopus 로고    scopus 로고
    • Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide
    • H. Watanabe Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide Cancer Res. 56 1996 2960 2963
    • (1996) Cancer Res. , vol.56 , pp. 2960-2963
    • Watanabe, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.