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Volumn 1432, Issue 2, 1999, Pages 159-184

New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase

Author keywords

Apoptosis; Gene expression; Glyceraldehyde 3 phosphate dehydrogenase; Neurodegenerative disease; Nitric oxide; Protein structure

Indexed keywords

CYTOSKELETON PROTEIN; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MEMBRANE PROTEIN;

EID: 0032973950     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00119-3     Document Type: Review
Times cited : (727)

References (166)
  • 2
    • 0015177154 scopus 로고
    • The isolation and functional identification of a protein from the human erythrocyte 'ghost'
    • Tanner M.J.A., Gray W.R. The isolation and functional identification of a protein from the human erythrocyte 'ghost'. Biochem. J. 125:1971;1109-1117.
    • (1971) Biochem. J. , vol.125 , pp. 1109-1117
    • Tanner, M.J.A.1    Gray, W.R.2
  • 3
    • 0017231735 scopus 로고
    • Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid
    • Wooster M.S., Wrigglesworth J.M. Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid. Biochem. J. 153:1976;93-100.
    • (1976) Biochem. J. , vol.153 , pp. 93-100
    • Wooster, M.S.1    Wrigglesworth, J.M.2
  • 4
    • 0015740243 scopus 로고
    • Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes
    • Kant J.A., Steck T.L. Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes. J. Biol. Chem. 248:1973;8457-8464.
    • (1973) J. Biol. Chem. , vol.248 , pp. 8457-8464
    • Kant, J.A.1    Steck, T.L.2
  • 5
    • 0016272502 scopus 로고
    • The interaction of glyceraldehyde 3-phosphate dehydrogenase with human erythrocyte membranes
    • McDaniel C.F., Kirtley M.E., Tanner M.J.A. The interaction of glyceraldehyde 3-phosphate dehydrogenase with human erythrocyte membranes. J. Biol. Chem. 249:1974;6478-6485.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6478-6485
    • McDaniel, C.F.1    Kirtley, M.E.2    Tanner, M.J.A.3
  • 6
    • 0016817229 scopus 로고
    • Associations of Band 3, the predominant polypeptide of the human erythrocyte membrane
    • Yu J., Steck T.L. Associations of Band 3, the predominant polypeptide of the human erythrocyte membrane. J. Biol. Chem. 250:1975;9176-9184.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9176-9184
    • Yu, J.1    Steck, T.L.2
  • 7
    • 0019308713 scopus 로고
    • Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane: A kinetic analysis
    • Kliman H.J., Steck T.L. Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane: a kinetic analysis. J. Biol. Chem. 255:1980;6314-6321.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6314-6321
    • Kliman, H.J.1    Steck, T.L.2
  • 8
    • 0020478636 scopus 로고
    • Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase
    • Tsai I.-H., Prasanna Murthy S.N., Steck T.L. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 257:1982;1438-1442.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1438-1442
    • Tsai, I.-H.1    Prasanna Murthy, S.N.2    Steck, T.L.3
  • 9
    • 0026763880 scopus 로고
    • Colocalization of GAPDH and band 3 (AE1) proteins in rat erythrocytes and kidney intercalated cell membranes
    • Ercolani L., Brown D., Stuart-Tilley A., Alper S.L. Colocalization of GAPDH and band 3 (AE1) proteins in rat erythrocytes and kidney intercalated cell membranes. Am. J. Phys. 262:1992;892-896.
    • (1992) Am. J. Phys. , vol.262 , pp. 892-896
    • Ercolani, L.1    Brown, D.2    Stuart-Tilley, A.3    Alper, S.L.4
  • 10
    • 0020536186 scopus 로고
    • Reorientation of membrane polypeptides during erythrocyte maturation
    • Allen R.W., Hoover B.A. Reorientation of membrane polypeptides during erythrocyte maturation. Blood. 61:1983;803-806.
    • (1983) Blood , vol.61 , pp. 803-806
    • Allen, R.W.1    Hoover, B.A.2
  • 11
    • 0022000527 scopus 로고
    • Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells
    • Allen R.W., Hoover B.A. Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells. Blood. 65:1985;1048-1059.
    • (1985) Blood , vol.65 , pp. 1048-1059
    • Allen, R.W.1    Hoover, B.A.2
  • 12
    • 0023098484 scopus 로고
    • Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase
    • Allen R.W., Trach K.A., Hoch J.A. Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 262:1987;649-653.
    • (1987) J. Biol. Chem. , vol.262 , pp. 649-653
    • Allen, R.W.1    Trach, K.A.2    Hoch, J.A.3
  • 13
    • 0021854754 scopus 로고
    • Fusion of phospholipid vesicles induced by muscle glyceraldehyde-3-phosphate dehydrogenase in the absence of calcium
    • Morero R.D., Lopez Vinals A., Bloj B., Farias R.N. Fusion of phospholipid vesicles induced by muscle glyceraldehyde-3-phosphate dehydrogenase in the absence of calcium. Biochemistry. 24:1985;1904-1909.
    • (1985) Biochemistry , vol.24 , pp. 1904-1909
    • Morero, R.D.1    Lopez Vinals, A.2    Bloj, B.3    Farias, R.N.4
  • 14
    • 0023151496 scopus 로고
    • Characterization of the fusogenic properties of glyceraldehyde-3-phosphate dehydrogenase: Fusion of phospholipid vesicles
    • Lopez Vinals A.E., Farias R.N., Morero R.D. Characterization of the fusogenic properties of glyceraldehyde-3-phosphate dehydrogenase: fusion of phospholipid vesicles. Biochem. Biophys. Res. Commun. 143:1987;403-409.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 403-409
    • Lopez Vinals, A.E.1    Farias, R.N.2    Morero, R.D.3
  • 15
    • 0028301321 scopus 로고
    • II phase with its ability to promote membrane fusion
    • II phase with its ability to promote membrane fusion. Biochemistry. 33:1994;5805-5812.
    • (1994) Biochemistry , vol.33 , pp. 5805-5812
    • Glaser, P.E.1    Gross, R.W.2
  • 16
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3 phosphate dehydrogenase: Discrimination between glycolytic and fusogenic roles of individual isoforms
    • Glaser P.E., Gross R.W. Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3 phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry. 34:1995;12194-12203.
    • (1995) Biochemistry , vol.34 , pp. 12194-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 17
    • 0031474883 scopus 로고    scopus 로고
    • Localization of the phosphatidylserine-binding site of glyceraldehyde-3-phosphate dehydrogenase responsible for membrane fusion
    • Kaneda M., Takeuchi K., Inoue K., Umeda M. Localization of the phosphatidylserine-binding site of glyceraldehyde-3-phosphate dehydrogenase responsible for membrane fusion. J. Biochem. 122:1997;1233-1240.
    • (1997) J. Biochem. , vol.122 , pp. 1233-1240
    • Kaneda, M.1    Takeuchi, K.2    Inoue, K.3    Umeda, M.4
  • 18
    • 0032508856 scopus 로고    scopus 로고
    • Reconstitution of membrane fusion between pancreatic islet secretory granules and plasma membranes: Catalysis by a protein constituent recognized by monoclonal antibodies directed against glyceraldehyde-3-phosphate dehydrogenase
    • Han X., Ramanadham S., Turk J., Gross R.W. Reconstitution of membrane fusion between pancreatic islet secretory granules and plasma membranes: catalysis by a protein constituent recognized by monoclonal antibodies directed against glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 1414:1998;95-107.
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 95-107
    • Han, X.1    Ramanadham, S.2    Turk, J.3    Gross, R.W.4
  • 20
    • 0029095105 scopus 로고
    • A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells
    • Robbins A.R., Ward R.D., Oliver C. A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells. J. Cell Biol. 130:1995;1093-1104.
    • (1995) J. Cell Biol. , vol.130 , pp. 1093-1104
    • Robbins, A.R.1    Ward, R.D.2    Oliver, C.3
  • 21
    • 0020758755 scopus 로고
    • A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
    • Kumagai H., Sakai A. A porcine brain protein (35 K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase. J. Biochem. 93:1983;1259-1269.
    • (1983) J. Biochem. , vol.93 , pp. 1259-1269
    • Kumagai, H.1    Sakai, A.2
  • 22
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel P., Pantaloni D. Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP. Eur. J. Biochem. 150:1985;265-269.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 265-269
    • Huitorel, P.1    Pantaloni, D.2
  • 23
    • 0021804407 scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle
    • Caswell A.H., Corbett A.M. Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. J. Biol. Chem. 260:1985;6892-6898.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6892-6898
    • Caswell, A.H.1    Corbett, A.M.2
  • 24
    • 0024342987 scopus 로고
    • Glycolytic enzyme interactions with tubulin and microtubules
    • Walsh J.L., Keith T.J., Knull H.R. Glycolytic enzyme interactions with tubulin and microtubules. Biochim. Biophys. Acta. 999:1989;64-70.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 64-70
    • Walsh, J.L.1    Keith, T.J.2    Knull, H.R.3
  • 25
    • 0024341331 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a microtubule binding protein in a human colon tumor cell line
    • Launay J.F., Jellali A., Vanier M.T. Glyceraldehyde-3-phosphate dehydrogenase is a microtubule binding protein in a human colon tumor cell line. Biochim. Biophys. Acta. 996:1989;103-109.
    • (1989) Biochim. Biophys. Acta , vol.996 , pp. 103-109
    • Launay, J.F.1    Jellali, A.2    Vanier, M.T.3
  • 26
  • 27
    • 0025083511 scopus 로고
    • Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect
    • Somers M., Engelborghs Y., Baer J. Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect. Eur. J. Biochem. 193:1990;437-444.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 437-444
    • Somers, M.1    Engelborghs, Y.2    Baer, J.3
  • 28
    • 0031568822 scopus 로고    scopus 로고
    • A glycolytic enzyme binding domain on tubulin
    • Volker K.W., Knull H.R. A glycolytic enzyme binding domain on tubulin. Arch. Biochem. Biophys. 338:1997;237-243.
    • (1997) Arch. Biochem. Biophys. , vol.338 , pp. 237-243
    • Volker, K.W.1    Knull, H.R.2
  • 29
    • 0023099854 scopus 로고
    • Microtubules bind glyceraldehyde 3-phosphate dehydrogenase and modulate its enzyme activity and quaternary structure
    • Durrieu C., Bernier-Valentin F., Rousset B. Microtubules bind glyceraldehyde 3-phosphate dehydrogenase and modulate its enzyme activity and quaternary structure. Arch. Biochem. Biophys. 252:1987;32-40.
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 32-40
    • Durrieu, C.1    Bernier-Valentin, F.2    Rousset, B.3
  • 30
    • 0023305006 scopus 로고
    • Binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules
    • Durrieu C., Bernier-Valentin F., Rousset B. Binding of glyceraldehyde 3-phosphate dehydrogenase to microtubules. Mol. Cell. Biochem. 74:1987;55-65.
    • (1987) Mol. Cell. Biochem. , vol.74 , pp. 55-65
    • Durrieu, C.1    Bernier-Valentin, F.2    Rousset, B.3
  • 31
    • 0028068464 scopus 로고
    • Binding constants and stoichiometries of glyceraldehyde 3-phosphate dehydrogenase-tubulin complexes
    • Muronetz V.I., Wang Z.-X., Keith T.J., Knull H.R., Srivastava D.K. Binding constants and stoichiometries of glyceraldehyde 3-phosphate dehydrogenase-tubulin complexes. Arch. Biochem. Biophys. 313:1994;253-260.
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 253-260
    • Muronetz, V.I.1    Wang, Z.-X.2    Keith, T.J.3    Knull, H.R.4    Srivastava, D.K.5
  • 32
    • 0014690989 scopus 로고
    • Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into trimers and monomers by adenosine triphosphate
    • Constantinides S.M., Deal W.C. Jr. Reversible dissociation of tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase into trimers and monomers by adenosine triphosphate. J. Biol. Chem. 244:1969;5695-5702.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5695-5702
    • Constantinides, S.M.1    Deal W.C., Jr.2
  • 33
    • 0014592228 scopus 로고
    • Reversible dissociation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine triphosphate
    • Stancel G.M., Deal W.C. Jr. Reversible dissociation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine triphosphate. Biochemistry. 8:1969;4005-4011.
    • (1969) Biochemistry , vol.8 , pp. 4005-4011
    • Stancel, G.M.1    Deal W.C., Jr.2
  • 34
    • 0015911437 scopus 로고
    • Regulation of glyceraldehyde 3-phosphate dehydrogenase by phosphocreatine and adenosine triphosphate. IV. Factors affecting in vivo control of enzymatic activity
    • Oguchi M., Gerth E., Fitzgerald B., Park J.H. Regulation of glyceraldehyde 3-phosphate dehydrogenase by phosphocreatine and adenosine triphosphate. IV. Factors affecting in vivo control of enzymatic activity. J. Biol. Chem. 248:1973;5571-5576.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5571-5576
    • Oguchi, M.1    Gerth, E.2    Fitzgerald, B.3    Park, J.H.4
  • 35
    • 0017855075 scopus 로고
    • Reassociation and reactivation of yeast glyceraldehyde-3-phosphate dehydrogenase after dissociation in the presence of ATP
    • Bartholmes P., Jaenicke R. Reassociation and reactivation of yeast glyceraldehyde-3-phosphate dehydrogenase after dissociation in the presence of ATP. Eur. J. Biochem. 87:1978;563-567.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 563-567
    • Bartholmes, P.1    Jaenicke, R.2
  • 36
    • 0022477471 scopus 로고
    • Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
    • Kawamoto R.M., Caswell A.H. Autophosphorylation of glyceraldehydephosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry. 25:1986;656-661.
    • (1986) Biochemistry , vol.25 , pp. 656-661
    • Kawamoto, R.M.1    Caswell, A.H.2
  • 37
    • 0030693787 scopus 로고    scopus 로고
    • The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide
    • Wu K., Aoki C., Elste A., Rogalski-Wilk A.A., Siekevitz P. The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide. Proc. Natl. Acad. Sci. USA. 94:1997;13273-13278.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13273-13278
    • Wu, K.1    Aoki, C.2    Elste, A.3    Rogalski-Wilk, A.A.4    Siekevitz, P.5
  • 38
    • 0031854353 scopus 로고    scopus 로고
    • Phosphorylation of the hepatitis core protein by glyceraldhyde-3-phosphate dehydrogenase protein kinase activity
    • Duclos-Vallee J.C., Capel F., Mabit H., Petit M.-A. Phosphorylation of the hepatitis core protein by glyceraldhyde-3-phosphate dehydrogenase protein kinase activity. J. Gen. Virol. 79:1998;1665-1670.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1665-1670
    • Duclos-Vallee, J.C.1    Capel, F.2    Mabit, H.3    Petit, M.-A.4
  • 39
    • 0032493656 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/nucleoside diphosphate kinase A: Two old enzymes combine for the novel Nm23 protein phosphotransferase function
    • Engel M., Seifert M., Theisinger B., Seyfert U., Welter C. Glyceraldehyde-3-phosphate dehydrogenase and Nm23-H1/nucleoside diphosphate kinase A: two old enzymes combine for the novel Nm23 protein phosphotransferase function. J. Biol. Chem. 273:1998;20058-20065.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20058-20065
    • Engel, M.1    Seifert, M.2    Theisinger, B.3    Seyfert, U.4    Welter, C.5
  • 40
    • 0029741376 scopus 로고    scopus 로고
    • Interactions of purified protein kinase C with key proteins of energy metabolism and cellular motility
    • Reiss N., Hermon J., Oplatka A., Naor Z. Interactions of purified protein kinase C with key proteins of energy metabolism and cellular motility. Biochem. Mol. Biol. Int. 38:1996;711-719.
    • (1996) Biochem. Mol. Biol. Int. , vol.38 , pp. 711-719
    • Reiss, N.1    Hermon, J.2    Oplatka, A.3    Naor, Z.4
  • 41
    • 0030449503 scopus 로고    scopus 로고
    • Phosphatidylserine directs differential phosphorylation of acting and glyceraldehyde-3-phosphate dehydrogenase by protein kinase C: Possible implications for regulation of actin polymerization
    • Reiss N., Oplatka A., Hermon J., Naor Z. Phosphatidylserine directs differential phosphorylation of acting and glyceraldehyde-3-phosphate dehydrogenase by protein kinase C: possible implications for regulation of actin polymerization. Biochem. Mol. Biol. Int. 40:1996;1191-1200.
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 1191-1200
    • Reiss, N.1    Oplatka, A.2    Hermon, J.3    Naor, Z.4
  • 42
    • 0022834087 scopus 로고
    • Five enzymes of the glycolytic pathway serve as substrates for purified epidermal-growth-factor-receptor kinase
    • Reiss N., Kanety H., Schlessinger J. 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    Kanety, H.2    Schlessinger, J.3
  • 45
    • 0027518424 scopus 로고
    • Sequence-specificity binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R., Green M.R. Sequence-specificity binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science. 259:1993;365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 46
    • 0032529511 scopus 로고    scopus 로고
    • Identification of glyceraldehyde-3-phosphate as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element
    • Zang W.-Q., Fieno A.M., Grant R.A., Yen T.S.B. Identification of glyceraldehyde-3-phosphate as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element. Virology. 28:1998;46-52.
    • (1998) Virology , vol.28 , pp. 46-52
    • Zang, W.-Q.1    Fieno, A.M.2    Grant, R.A.3    Yen, T.S.B.4
  • 47
    • 0008959903 scopus 로고
    • Cell cycle regulation of DNA repair enzymes and pathways
    • in: G.E. Milo, B.C. Casto (Eds.), CRC Press, Boca Raton
    • M.A. Sirover, Cell cycle regulation of DNA repair enzymes and pathways, in: G.E. Milo, B.C. Casto (Eds.), Transformation of Human Fibroblasts: Molecular and Genetic Mechanisms, CRC Press, Boca Raton, 1990, pp. 29-54.
    • (1990) Transformation of Human Fibroblasts: Molecular and Genetic Mechanisms , pp. 29-54
    • Sirover, M.A.1
  • 48
    • 0004948306 scopus 로고
    • Isolation and characterization of monoclonal antibodies directed against the DNA repair enzyme uracil DNA glycosylase from human placenta
    • Arenaz P., Sirover M.A. Isolation and characterization of monoclonal antibodies directed against the DNA repair enzyme uracil DNA glycosylase from human placenta. Proc. Natl. Acad. Sci. USA. 80:1983;5822-5826.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5822-5826
    • Arenaz, P.1    Sirover, M.A.2
  • 49
    • 0023099062 scopus 로고
    • Biosynthesis of the human base excision repair enzyme uracil-DNA glycosylase
    • Vollberg T.M., Cool B.L., Sirover M.A. Biosynthesis of the human base excision repair enzyme uracil-DNA glycosylase. Cancer Res. 47:1987;123-128.
    • (1987) Cancer Res. , vol.47 , pp. 123-128
    • Vollberg, T.M.1    Cool, B.L.2    Sirover, M.A.3
  • 52
    • 0029119458 scopus 로고
    • Transcriptional regulation of glyceraldehyde-3-phosphate dehydrogenase by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • McNulty S.E., Toscano W.A. Jr. Transcriptional regulation of glyceraldehyde-3-phosphate dehydrogenase by 2,3,7,8-tetrachlorodibenzo-p-dioxin. Biochem. Biophys. Res. Commun. 212:1995;165-171.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 165-171
    • McNulty, S.E.1    Toscano W.A., Jr.2
  • 53
    • 0022406559 scopus 로고
    • Glyceraldehyde-3-phosophate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes
    • Ryazanov A.G. Glyceraldehyde-3-phosophate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes. FEBS Lett. 192:1985;131-134.
    • (1985) FEBS Lett. , vol.192 , pp. 131-134
    • Ryazanov, A.G.1
  • 54
    • 0028816615 scopus 로고
    • +-binding region (Rossman Fold)
    • +-binding region (Rossman Fold). J. Biol. Chem. 270:1995;2755-2763.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2755-2763
    • Nagy, E.1    Rigby, W.F.C.2
  • 55
    • 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
    • De B.P., Gupta S., Zhao H., Drazba J.A., Banerjee A.K. 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    Gupta, S.2    Zhao, H.3    Drazba, J.A.4    Banerjee, A.K.5
  • 56
    • 0029927267 scopus 로고    scopus 로고
    • Specific interaction of glyceraldehyde-3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis A virus
    • Schultz D.E., Hardin C.C., Lemon S.M. 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    Hardin, C.C.2    Lemon, S.M.3
  • 57
    • 0032211790 scopus 로고    scopus 로고
    • Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase
    • Carlile G.W., Tatton W.G., Borden D.L.B. Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase. Biochem. J. 335:1998;691-696.
    • (1998) Biochem. J. , vol.335 , pp. 691-696
    • Carlile, G.W.1    Tatton, W.G.2    Borden, D.L.B.3
  • 58
    • 0019889692 scopus 로고
    • A basic isozyme of yeast glyceraldehyde-3-phosphate dehydrogenase with nucleic acid helix-destabilizing activity
    • Karpel R.L., Burchard A.C. A basic isozyme of yeast glyceraldehyde-3-phosphate dehydrogenase with nucleic acid helix-destabilizing activity. Biochim. Biophys. Acta. 654:1981;256-267.
    • (1981) Biochim. Biophys. Acta , vol.654 , pp. 256-267
    • Karpel, R.L.1    Burchard, A.C.2
  • 59
    • 0029870382 scopus 로고    scopus 로고
    • Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase
    • Sioud M., Jespersen L. 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
  • 60
    • 0026582161 scopus 로고
    • Diadenosine tetraphosphate binding protein from human HeLa cells: Purification and characterization
    • Vishwanatha J.K., Wei Z. Diadenosine tetraphosphate binding protein from human HeLa cells: purification and characterization. Biochemistry. 31:1992;1631-1635.
    • (1992) Biochemistry , vol.31 , pp. 1631-1635
    • Vishwanatha, J.K.1    Wei, Z.2
  • 63
    • 0030461710 scopus 로고    scopus 로고
    • 6A: Synergism with granulocyte-macrophage colony stimulating factor
    • 6A: synergism with granulocyte-macrophage colony stimulating factor. Br. J. Hematol. 95:1996;637-639.
    • (1996) Br. J. Hematol. , vol.95 , pp. 637-639
    • Gasmi, L.1    McLennan, A.G.2    Edwards, S.W.3
  • 64
    • 0029664543 scopus 로고    scopus 로고
    • 4A and adenosine triphosphate interact with granulocyte-macrophage colony-stimulating factor to delay neutrophil apoptosis: Implications for neutrophil:plated interactions during inflammation
    • 4A and adenosine triphosphate interact with granulocyte-macrophage colony-stimulating factor to delay neutrophil apoptosis: Implications for neutrophil:plated interactions during inflammation. Blood. 87:1996;3442-3449.
    • (1996) Blood , vol.87 , pp. 3442-3449
    • Gasmi, L.1    McLennan, A.G.2    Edwards, S.W.3
  • 66
    • 0028204459 scopus 로고
    • S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koistinen I., Moldeus P., Bergman T., Cotgreave L.A. S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. Eur. J. Biochem. 221:1994;1033-1037.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1033-1037
    • Schuppe-Koistinen, I.1    Moldeus, P.2    Bergman, T.3    Cotgreave, L.A.4
  • 67
    • 0032543374 scopus 로고    scopus 로고
    • Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin
    • Lind C., Gerdes R., Schuppe-Koistinen I., Cotgreave L.A. Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin. Biochem. Biophys. Res. Commun. 247:1998;481-486.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 481-486
    • Lind, C.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Cotgreave, L.A.4
  • 68
    • 0030887909 scopus 로고    scopus 로고
    • Glutathione conjugates recognize the Rossman fold of glyceraldehyde-3-phosphate dehydrogenase
    • Puder M., Soberman R.J. Glutathione conjugates recognize the Rossman fold of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 272:1997;10936-10940.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10936-10940
    • Puder, M.1    Soberman, R.J.2
  • 70
    • 0030724073 scopus 로고    scopus 로고
    • Reduced glutathione prevents nitric oxide-induced apoptosis in vascular smooth muscle cells
    • Zhao Z., Francis C.E., Welch G., Loscalzo J., Ravid K. Reduced glutathione prevents nitric oxide-induced apoptosis in vascular smooth muscle cells. Biochim. Biophys. Acta. 1359:1997;143-152.
    • (1997) Biochim. Biophys. Acta , vol.1359 , pp. 143-152
    • Zhao, Z.1    Francis, C.E.2    Welch, G.3    Loscalzo, J.4    Ravid, K.5
  • 71
    • 0030927533 scopus 로고    scopus 로고
    • Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal-like PC12 cells
    • Froissard P., Monroca H., Duval D. Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal-like PC12 cells. Eur. J. Pharmacol. 326:1997;93-99.
    • (1997) Eur. J. Pharmacol. , vol.326 , pp. 93-99
    • Froissard, P.1    Monroca, H.2    Duval, D.3
  • 73
    • 1542563485 scopus 로고
    • Evolutionary and structural relationships among dehydrogenases
    • in: P.D. Boyer (Ed.), Academic Press, New York
    • M.G. Rossman, A. Liljas, C.-I. Branden, L.J. Banaszak, Evolutionary and structural relationships among dehydrogenases, in: P.D. Boyer (Ed.), The Enzymes, 3rd ed., Academic Press, New York, 1975, pp. 61-102.
    • (1975) The Enzymes, 3rd Ed. , pp. 61-102
    • Rossman, M.G.1    Liljas, A.2    Branden, C.-I.3    Banaszak, L.J.4
  • 74
    • 63849332835 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase
    • in: P.D. Boyer (Ed.) Academic Press, New York
    • J.I. Harris, M. Waters, Glyceraldehyde-3-phosphate dehydrogenase, in: P.D. Boyer (Ed.) The Enzymes, 3rd ed., Academic Press, New York, 1976, pp. 1-49.
    • (1976) The Enzymes, 3rd Ed. , pp. 1-49
    • Harris, J.I.1    Waters, M.2
  • 75
    • 0019332463 scopus 로고
    • Structure of lobster apo-d-glyceraldehyde-3-phosphate dehydrogenase at 3.0 A resolution
    • Murthy M.R.N., Garavito R.M., Johnson T.E., Rossman M.G. Structure of lobster apo-d-glyceraldehyde-3-phosphate dehydrogenase at 3.0 A resolution. J. Mol. Biol. 138:1980;859-872.
    • (1980) J. Mol. Biol. , vol.138 , pp. 859-872
    • Murthy, M.R.N.1    Garavito, R.M.2    Johnson, T.E.3    Rossman, M.G.4
  • 76
    • 0020513891 scopus 로고
    • Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase
    • Leslie A.G., Wonacott A.J. Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 165:1983;375-391.
    • (1983) J. Mol. Biol. , vol.165 , pp. 375-391
    • Leslie, A.G.1    Wonacott, A.J.2
  • 77
    • 0021095725 scopus 로고
    • Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase from Bacillus coagulans
    • Griffith J.P., Lee B., Murdock A.L., Amelunzen R.E. Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase from Bacillus coagulans. J. Mol. Biol. 169:1983;963-974.
    • (1983) J. Mol. Biol. , vol.169 , pp. 963-974
    • Griffith, J.P.1    Lee, B.2    Murdock, A.L.3    Amelunzen, R.E.4
  • 78
    • 0023644310 scopus 로고
    • Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution
    • Skarzynski T., Moody P.C., Wonacott A.J. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. J. Mol. Biol. 193:1987;171-187.
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.2    Wonacott, A.J.3
  • 79
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossman M.G., Moras D., Olsen K.W. Chemical and biological evolution of a nucleotide-binding protein. Nature. 250:1974;194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossman, M.G.1    Moras, D.2    Olsen, K.W.3
  • 81
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 347:1990;203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 83
    • 0017070826 scopus 로고
    • Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase
    • Mercer W.D., Winn S.I., Watson H.C. Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 104:1976;277-283.
    • (1976) J. Mol. Biol. , vol.104 , pp. 277-283
    • Mercer, W.D.1    Winn, S.I.2    Watson, H.C.3
  • 84
    • 0017767882 scopus 로고
    • Crystallographic data for sturgeon holo-D-glyceraldehyde-3-phosphate dehydrogenase: A holo-D-glyceraldehyde-3-phosphate dehydrogenase with crystallographic 2-fold symmetry
    • Holmes M.A., Remington S.J., Schwendimann B., Christie G.E., Matthews B.W. Crystallographic data for sturgeon holo-D-glyceraldehyde-3-phosphate dehydrogenase: a holo-D-glyceraldehyde-3-phosphate dehydrogenase with crystallographic 2-fold symmetry. J. Mol. Biol. 112:1977;651-652.
    • (1977) J. Mol. Biol. , vol.112 , pp. 651-652
    • Holmes, M.A.1    Remington, S.J.2    Schwendimann, B.3    Christie, G.E.4    Matthews, B.W.5
  • 85
    • 0025769785 scopus 로고
    • Molecular modeling of phytochrome
    • Gabriel J.L., Hoober J.K. Molecular modeling of phytochrome. J. Theor. Biol. 151:1991;541-556.
    • (1991) J. Theor. Biol. , vol.151 , pp. 541-556
    • Gabriel, J.L.1    Hoober, J.K.2
  • 86
    • 0027266977 scopus 로고
    • Proposed atomic structure of a truncated human immunodeficiency virus glycoprotein gp120 derived by molecular modeling: Target CD4 recognition and docking mechanism
    • Gabriel J.L., Mitchell W.M. Proposed atomic structure of a truncated human immunodeficiency virus glycoprotein gp120 derived by molecular modeling: target CD4 recognition and docking mechanism. Proc. Natl. Acad. Sci. USA. 90:1992;4186-4190.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4186-4190
    • Gabriel, J.L.1    Mitchell, W.M.2
  • 87
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry. 28:1989;2586-2592.
    • (1989) Biochemistry , vol.28 , pp. 2586-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.4    Branlant, C.5    Branlant, G.6
  • 88
    • 0016772655 scopus 로고
    • Studies of asymmetry in the three-dimensional structure of lobster d-glyceraldehyde-3-phosphate dehydrogenase
    • Moras D., Olsen K.W., Sabesan M.N., Buehner M., Ford G.C., Rossman M.G. Studies of asymmetry in the three-dimensional structure of lobster d-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250:1975;9137-9162.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9137-9162
    • Moras, D.1    Olsen, K.W.2    Sabesan, M.N.3    Buehner, M.4    Ford, G.C.5    Rossman, M.G.6
  • 89
    • 0015921473 scopus 로고
    • SH groups masked by subunit interaction in glyceraldehyde-3-phosphate dehydrogenase
    • Ovadi J., Nuridsany M., Keleti T. SH groups masked by subunit interaction in glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 302:1973;191-199.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 191-199
    • Ovadi, J.1    Nuridsany, M.2    Keleti, T.3
  • 90
    • 0016828716 scopus 로고
    • Sequence variability and structure of D-glyceraldehyde-3-phosphate dehydrogenase
    • Olsen K.W., Moras D., Rossman M.G., Harris J.I. Sequence variability and structure of D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250:1975;9313-9321.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9313-9321
    • Olsen, K.W.1    Moras, D.2    Rossman, M.G.3    Harris, J.I.4
  • 91
    • 0021116725 scopus 로고
    • Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranes
    • Eby D., Kirley M.E. Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranes. Biochem. Biophys. Res. Commun. 116:1983;423-427.
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 423-427
    • Eby, D.1    Kirley, M.E.2
  • 92
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus
    • Dingwall C., Laskey R.A. Nuclear targeting sequences - a consensus. Trends Biochem. Sci. 16:1991;478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 93
    • 0028071526 scopus 로고
    • Nuclear signaling pathways for polypeptide ligands and their membrane receptors
    • Jans D.A. Nuclear signaling pathways for polypeptide ligands and their membrane receptors. FASEB J. 8:1994;841-847.
    • (1994) FASEB J. , vol.8 , pp. 841-847
    • Jans, D.A.1
  • 94
    • 0030913267 scopus 로고    scopus 로고
    • How proteins are transported from cytoplasm to nucleus
    • Yoneda Y. How proteins are transported from cytoplasm to nucleus. J. Biochem. 121:1997;811-817.
    • (1997) J. Biochem. , vol.121 , pp. 811-817
    • Yoneda, Y.1
  • 95
    • 0029786994 scopus 로고    scopus 로고
    • 2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal
    • 2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J. Biol. Chem. 271:1996;20024-20028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukada, M.1    Gotoh, I.2    Gotoh, Y.3    Nishida, E.4
  • 96
    • 0024308384 scopus 로고
    • Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells
    • Cool B.L., Sirover M.A. Immunocytochemical localization of the base excision repair enzyme uracil DNA glycosylase in quiescent and proliferating normal human cells. Cancer Res. 49:1989;3029-3036.
    • (1989) Cancer Res. , vol.49 , pp. 3029-3036
    • Cool, B.L.1    Sirover, M.A.2
  • 97
    • 0030868934 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death
    • Sawa A., Khan A.A., Hester L.D., Snyder S.H. Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death. Proc. Natl. Acad. Sci. USA. 94:1997;11669-11674.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11669-11674
    • Sawa, A.1    Khan, A.A.2    Hester, L.D.3    Snyder, S.H.4
  • 98
    • 0030809974 scopus 로고    scopus 로고
    • Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis
    • Saunders P.A., Chalecka-Franaszek E., Chuang D.-M. Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis. J. Neurochem. 69:1997;1820-1828.
    • (1997) J. Neurochem. , vol.69 , pp. 1820-1828
    • Saunders, P.A.1    Chalecka-Franaszek, E.2    Chuang, D.-M.3
  • 99
    • 0031968628 scopus 로고    scopus 로고
    • Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis
    • Ishitani R., Tanaka M., Sunaga K., Katsube N., Chuang D.-M. Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol. Pharmacol. 53:1998;701-707.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 701-707
    • Ishitani, R.1    Tanaka, M.2    Sunaga, K.3    Katsube, N.4    Chuang, D.-M.5
  • 100
    • 0017255365 scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids
    • Bruns G.A.P., Gerald P.S. Human glyceraldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids. Science. 192:1976;54-56.
    • (1976) Science , vol.192 , pp. 54-56
    • Bruns, G.A.P.1    Gerald, P.S.2
  • 104
    • 0021524768 scopus 로고
    • The glyceraldehyde 3 phosphate dehydrogenase gene family: Structure of a human cDNA and of an X chromosome linked pseudogene; Amazing complexity of the gene family in mouse
    • Hanauer A., Mandel J.T. The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse. EMBO J. 3:1984;2627-2633.
    • (1984) EMBO J. , vol.3 , pp. 2627-2633
    • Hanauer, A.1    Mandel, J.T.2
  • 105
    • 0021524602 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase pseudogene on the short arm of the human X chromosome defines a multigene family
    • Benham F.J., Hodgkinson S., Kavies K.E. A glyceraldehyde-3-phosphate dehydrogenase pseudogene on the short arm of the human X chromosome defines a multigene family. EMBO J. 3:1984;2635-2640.
    • (1984) EMBO J. , vol.3 , pp. 2635-2640
    • Benham, F.J.1    Hodgkinson, S.2    Kavies, K.E.3
  • 106
    • 0024711577 scopus 로고
    • Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to dispersed chromosomal locations
    • Benham F.J., Povey S. Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to dispersed chromosomal locations. Genomics. 5:1989;209-214.
    • (1989) Genomics , vol.5 , pp. 209-214
    • Benham, F.J.1    Povey, S.2
  • 107
    • 0027959519 scopus 로고
    • Isolation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) cDNA from the distal half of mouse chromosome 16: Further indication of a link between Alzheimer's disease and glycolysis
    • Seipp S., Busemaier W. Isolation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) cDNA from the distal half of mouse chromosome 16: further indication of a link between Alzheimer's disease and glycolysis. Neurosci. Lett. 182:1994;91-94.
    • (1994) Neurosci. Lett. , vol.182 , pp. 91-94
    • Seipp, S.1    Busemaier, W.2
  • 109
    • 0022423216 scopus 로고
    • Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
    • Fort P.H., Marty L., Piechaczyk M., El Sabouty S., Dani C.H., Jeanteur P.H., Blanchard J.M. Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family. Nucleic Acids. Res. 13:1985;1431-1443.
    • (1985) Nucleic Acids. Res. , vol.13 , pp. 1431-1443
    • Fort, P.H.1    Marty, L.2    Piechaczyk, M.3    El Sabouty, S.4    Dani, C.H.5    Jeanteur, P.H.6    Blanchard, J.M.7
  • 110
    • 0026459818 scopus 로고
    • Proliferation-dependent regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in human cells
    • Meyer-Siegler K., Mansur N.R., Wurzer J.C., Sirover M.A. Proliferation-dependent regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in human cells. Carcinogenesis. 13:1992;2127-2132.
    • (1992) Carcinogenesis , vol.13 , pp. 2127-2132
    • Meyer-Siegler, K.1    Mansur, N.R.2    Wurzer, J.C.3    Sirover, M.A.4
  • 111
    • 0027198854 scopus 로고
    • Cell cycle regulation of the glyceraldehyde-3-phosphate/uracil DNA glycosylase gene in normal human cells
    • Mansur N.R., Meyer-Siegler K., Wurzer J.C., Sirover M.A. Cell cycle regulation of the glyceraldehyde-3-phosphate/uracil DNA glycosylase gene in normal human cells. Nucleic Acids Res. 21:1993;993-998.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 993-998
    • Mansur, N.R.1    Meyer-Siegler, K.2    Wurzer, J.C.3    Sirover, M.A.4
  • 112
    • 0028568174 scopus 로고
    • Expression of glycolytic isozymes in rat thymocytes during cell cycle progression
    • Netzker R., Hermfisse U., Wein K.-H., Brand K. Expression of glycolytic isozymes in rat thymocytes during cell cycle progression. Biochim. Biophys. Acta. 124:1994;371-376.
    • (1994) Biochim. Biophys. Acta , vol.124 , pp. 371-376
    • Netzker, R.1    Hermfisse, U.2    Wein, K.-H.3    Brand, K.4
  • 113
    • 0029985996 scopus 로고    scopus 로고
    • Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression in human hepatocellular carcinoma
    • Gong Y., Cui L., Minuk G.Y. Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28S-ribosomal RNA gene expression in human hepatocellular carcinoma. Hepatology. 23:1996;734-737.
    • (1996) Hepatology , vol.23 , pp. 734-737
    • Gong, Y.1    Cui, L.2    Minuk, G.Y.3
  • 114
    • 0032188955 scopus 로고    scopus 로고
    • Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis
    • Mezquita J., Pau M., Mezquita C. Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis. J. Cell. Biochem. 71:1998;127-139.
    • (1998) J. Cell. Biochem. , vol.71 , pp. 127-139
    • Mezquita, J.1    Pau, M.2    Mezquita, C.3
  • 115
    • 0015690736 scopus 로고
    • Structure and determination of FDF aldolase and the fine resolution of some glycolytic enzymes by isoelectric focusing
    • Susor W.A., Kochman M., Rutter W.J. Structure and determination of FDF aldolase and the fine resolution of some glycolytic enzymes by isoelectric focusing. Ann. NY Acad. Sci. 209:1973;328-344.
    • (1973) Ann. NY Acad. Sci. , vol.209 , pp. 328-344
    • Susor, W.A.1    Kochman, M.2    Rutter, W.J.3
  • 116
    • 0017748754 scopus 로고
    • Changes in glycolytic enzyme levels and isozyme expression in human lymphocytes during blast transformation
    • Kester M.V., Phillips T.L., Gracy R.W. Changes in glycolytic enzyme levels and isozyme expression in human lymphocytes during blast transformation. Arch. Biochem. Biophys. 183:1977;700-709.
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 700-709
    • Kester, M.V.1    Phillips, T.L.2    Gracy, R.W.3
  • 117
    • 0023000162 scopus 로고
    • Isolation and characterization of a 37,000-dalton protein associated with the erythrocyte membrane
    • Lin T., Allen R.W. Isolation and characterization of a 37,000-dalton protein associated with the erythrocyte membrane. J. Biol. Chem. 261:1986;4594-4599.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4594-4599
    • Lin, T.1    Allen, R.W.2
  • 118
    • 0023921027 scopus 로고
    • Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain
    • Ryzlak M., Pietruszko R. Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain. Biochim. Biophys. Acta. 954:1988;309-324.
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 309-324
    • Ryzlak, M.1    Pietruszko, R.2
  • 119
    • 0028872557 scopus 로고
    • Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis
    • Soukri A., Valverde F., Hafid N., Elkebbaj M.S., Serrano A. Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis. Biochim. Biophys. Acta. 1243:1995;161-168.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 161-168
    • Soukri, A.1    Valverde, F.2    Hafid, N.3    Elkebbaj, M.S.4    Serrano, A.5
  • 120
    • 0030021049 scopus 로고    scopus 로고
    • Evidence for a posttranslational modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating Jaculus orientalis
    • Soukri A., Hafid N., Valverde F., Elkebbaj M.S., Serrano A. Evidence for a posttranslational modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating Jaculus orientalis. Biochim. Biophys. Acta. 1293:1996;177-187.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 177-187
    • Soukri, A.1    Hafid, N.2    Valverde, F.3    Elkebbaj, M.S.4    Serrano, A.5
  • 121
    • 0029864851 scopus 로고    scopus 로고
    • Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: Role of p36
    • Mazurek S., Hugo F., Failing K., Eigenbrodt E. Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: role of p36. J. Cell. Phys. 167:1996;238-250.
    • (1996) J. Cell. Phys. , vol.167 , pp. 238-250
    • Mazurek, S.1    Hugo, F.2    Failing, K.3    Eigenbrodt, E.4
  • 122
    • 0027325255 scopus 로고
    • Nitric oxide synthetase structure and mechanism
    • Marletta M.A. Nitric oxide synthetase structure and mechanism. J. Biol. Chem. 268:1993;12231-12234.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12231-12234
    • Marletta, M.A.1
  • 123
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S., Palmer R.M.J., Higgs E.A. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43:1991;109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 125
    • 0023092102 scopus 로고
    • Macrophage cytotoxicity: Role for L-arginine deiminase and imino nitrogen oxidation to nitrite
    • Hibbs J.B. Jr., Taintor R.R., Vavrin Z. Macrophage cytotoxicity: role for L-arginine deiminase and imino nitrogen oxidation to nitrite. Science. 235:1987;473-476.
    • (1987) Science , vol.235 , pp. 473-476
    • Hibbs J.B., Jr.1    Taintor, R.R.2    Vavrin, Z.3
  • 126
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate and neurodegenerative disorders
    • Coyle J.T., Puttfarcken P. Oxidative stress, glutamate and neurodegenerative disorders. Science. 262:1993;689-694.
    • (1993) Science , vol.262 , pp. 689-694
    • Coyle, J.T.1    Puttfarcken, P.2
  • 129
    • 0024324347 scopus 로고
    • Activation of a cytosolic ADP-ribosyltransferase by nitric oxide-generating agents
    • Brune B., Lapetina E.G. Activation of a cytosolic ADP-ribosyltransferase by nitric oxide-generating agents. J. Biol. Chem. 264:1989;8455-8458.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8455-8458
    • Brune, B.1    Lapetina, E.G.2
  • 130
    • 0026446228 scopus 로고
    • Characterization of a nitric-oxide-catalyzed ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase
    • Dimmeler S., Brune B. Characterization of a nitric-oxide-catalyzed ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 210:1992;305-310.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 305-310
    • Dimmeler, S.1    Brune, B.2
  • 131
    • 0027390918 scopus 로고
    • Nitric oxide preferentially stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase compared to alcohol or lactate dehydrogenase
    • Dimmeler S., Brune B. Nitric oxide preferentially stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase compared to alcohol or lactate dehydrogenase. FEBS Lett. 315:1993;21-24.
    • (1993) FEBS Lett. , vol.315 , pp. 21-24
    • Dimmeler, S.1    Brune, B.2
  • 132
    • 0029442232 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase: A target for nitric oxide signaling
    • Brune B., Lapetina E.G. Glyceraldehyde-3-phosphate dehydrogenase: A target for nitric oxide signaling. Adv. Pharmacol. 34:1995;351-360.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 351-360
    • Brune, B.1    Lapetina, E.G.2
  • 133
    • 0026453106 scopus 로고
    • Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzyme activity and increases ADP-ribosylation
    • Molina y Vedia L., McDonald B., Reep B., Brune B., DiSilvio M., Billiar T.R., Lapetina E.G. Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzyme activity and increases ADP-ribosylation. J. Biol. Chem. 267:1992;24929-24932.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24929-24932
    • Molina, Y.1    Vedia, L.2    McDonald, B.3    Reep, B.4    Brune, B.5    Disilvio, M.6    Billiar, T.R.7    Lapetina, E.G.8
  • 134
    • 0027264855 scopus 로고
    • Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase
    • McDonald L.J., Moss J. Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA. 90:1993;6238-6241.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6238-6241
    • McDonald, L.J.1    Moss, J.2
  • 135
    • 0027369074 scopus 로고
    • Inverse relationship of the dehydrogenase and ADP-ribosylation activities in sodium-nitroprusside-treated glyceraldehyde-3-phosphate dehydrogenase is coincidental
    • Vaidyanathan V.V., Sastry P.S., Ramasarra T. Inverse relationship of the dehydrogenase and ADP-ribosylation activities in sodium-nitroprusside-treated glyceraldehyde-3-phosphate dehydrogenase is coincidental. Biochim. Biophys. Acta. 1203:1993;36-44.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 36-44
    • Vaidyanathan, V.V.1    Sastry, P.S.2    Ramasarra, T.3
  • 136
    • 0026686667 scopus 로고
    • Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase
    • Zhang J., Synder S. Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA. 89:1992;9382-9385.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9382-9385
    • Zhang, J.1    Synder, S.2
  • 137
    • 0026795982 scopus 로고
    • Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase
    • Dimmeler S., Lottspeich F., Brune B. Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 267:1992;16771-16774.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16771-16774
    • Dimmeler, S.1    Lottspeich, F.2    Brune, B.3
  • 138
    • 0032004726 scopus 로고    scopus 로고
    • S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase decreases the enzyme affinity to the erythrocyte membrane
    • Galli F., Rovidati S., Ghibelli L., Canestrari F. S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase decreases the enzyme affinity to the erythrocyte membrane. Nitric Oxide. 2:1998;17-27.
    • (1998) Nitric Oxide , vol.2 , pp. 17-27
    • Galli, F.1    Rovidati, S.2    Ghibelli, L.3    Canestrari, F.4
  • 139
    • 0028865070 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain
    • Sunaga K., Takahashi H., Chuang D.-M., Ishitani R. Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Neurosci. Lett. 200:1995;133-136.
    • (1995) Neurosci. Lett. , vol.200 , pp. 133-136
    • Sunaga, K.1    Takahashi, H.2    Chuang, D.-M.3    Ishitani, R.4
  • 140
    • 0030045251 scopus 로고    scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture
    • Ishitani R., Sunaga K., Hirano A., Saunders P., Katsube N., Chuang D.-M. Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture. J. Neurochem. 66:1996;928-935.
    • (1996) J. Neurochem. , vol.66 , pp. 928-935
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Saunders, P.4    Katsube, N.5    Chuang, D.-M.6
  • 141
    • 0029838525 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons
    • Ishitani R., Chuang D.-M. Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons. Proc. Natl. Acad. Sci. USA. 93:1996;9937-9941.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9937-9941
    • Ishitani, R.1    Chuang, D.-M.2
  • 142
    • 0030426279 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture
    • Ishitani R., Kimura M., Sunaga K., Katsube N., Tanaka M., Chuang D.-M. An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture. J. Pharmacol. Exp. Ther. 278:1996;447-454.
    • (1996) J. Pharmacol. Exp. Ther. , vol.278 , pp. 447-454
    • Ishitani, R.1    Kimura, M.2    Sunaga, K.3    Katsube, N.4    Tanaka, M.5    Chuang, D.-M.6
  • 144
    • 0030930536 scopus 로고    scopus 로고
    • Koningic acid (a potent glyceraldehyde-3-phosphate dehydrogenase inhibitor)-induced fragmentation and condensation of DNA in NG108-15 cells
    • Nakazawa M., Uehara T., Nomura Y. Koningic acid (a potent glyceraldehyde-3-phosphate dehydrogenase inhibitor)-induced fragmentation and condensation of DNA in NG108-15 cells. J. Neurochem. 68:1997;2493-2499.
    • (1997) J. Neurochem. , vol.68 , pp. 2493-2499
    • Nakazawa, M.1    Uehara, T.2    Nomura, Y.3
  • 145
    • 0030224620 scopus 로고    scopus 로고
    • Neuronal apoptosis by glial NO: Involvement of inhibition of potent glyceraldehyde-3-phosphate dehydrogenase
    • Nomura Y., Uehara T., Nakazawa M. Neuronal apoptosis by glial NO: Involvement of inhibition of potent glyceraldehyde-3-phosphate dehydrogenase. Human Cell. 9:1996;205-214.
    • (1996) Human Cell , vol.9 , pp. 205-214
    • Nomura, Y.1    Uehara, T.2    Nakazawa, M.3
  • 146
    • 0032935542 scopus 로고    scopus 로고
    • ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons
    • Katsube N., Sunaga K., Aishita H., Chuang D.-M., Ishitani R. ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons. J. Pharmacol. Exp. Ther. 288:1999;6-13.
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 6-13
    • Katsube, N.1    Sunaga, K.2    Aishita, H.3    Chuang, D.-M.4    Ishitani, R.5
  • 147
    • 0015929604 scopus 로고
    • Studies on a mammalian cell protein (P8) with affinity for DNA in vitro
    • Tsai R., Green H. Studies on a mammalian cell protein (P8) with affinity for DNA in vitro. J. Mol. Biol. 73:1973;307-316.
    • (1973) J. Mol. Biol. , vol.73 , pp. 307-316
    • Tsai, R.1    Green, H.2
  • 148
    • 0016592052 scopus 로고
    • Deoxyribonucleic acid-binding proteins in virus-transformed cell lines
    • Melero J.A., Salas M.L., Salas J., Macpherson I.A. Deoxyribonucleic acid-binding proteins in virus-transformed cell lines. J. Biol. Chem. 250:1975;3683-3689.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3683-3689
    • Melero, J.A.1    Salas, M.L.2    Salas, J.3    Macpherson, I.A.4
  • 149
    • 0017753166 scopus 로고
    • Identification of the mammalian DNA-binding protein P8 as glyceraldehyde-3-phosphate dehydrogenase
    • Perucho M., Salas J., Salas M.L. Identification of the mammalian DNA-binding protein P8 as glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 81:1977;557-562.
    • (1977) Eur. J. Biochem. , vol.81 , pp. 557-562
    • Perucho, M.1    Salas, J.2    Salas, M.L.3
  • 150
    • 0022535636 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons
    • Morgenegg G., Winkler G.C., Hubscher U., Heizmann C.W., Mous J., Kuenzle C.C. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J. Neurochem. 47:1986;54-62.
    • (1986) J. Neurochem. , vol.47 , pp. 54-62
    • Morgenegg, G.1    Winkler, G.C.2    Hubscher, U.3    Heizmann, C.W.4    Mous, J.5    Kuenzle, C.C.6
  • 151
    • 0022894808 scopus 로고
    • Lactate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase are single-stranded DNA-binding proteins that affect the DNA-polymerase-α-primase complex
    • Grosse F., Nasheuer H.-P., Scholtissek S., Schomburg U. Lactate dehydrogenase and glyceraldehyde-3-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    Nasheuer, H.-P.2    Scholtissek, S.3    Schomburg, U.4
  • 152
    • 0027214981 scopus 로고
    • Glycolytic enzymes as DNA binding proteins
    • Ronai Z. Glycolytic enzymes as DNA binding proteins. Int. J. Biochem. 25:1993;1073-1076.
    • (1993) Int. J. Biochem. , vol.25 , pp. 1073-1076
    • Ronai, Z.1
  • 153
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein
    • Schulze H., Schuyler A., Stuber D., Dobeli H., Langen H., Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein. J. Neurochem. 60:1993;1915-1922.
    • (1993) J. Neurochem. , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuyler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 155
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B., Matilla T., Burright E.N., Merry D.E., Fischbeck K.H., Orr H.T., Zoghbi H.Y. Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Hum. Mol. Genet. 5:1996;1311-1318.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3    Merry, D.E.4    Fischbeck, K.H.5    Orr, H.T.6    Zoghbi, H.Y.7
  • 159
    • 0031788691 scopus 로고    scopus 로고
    • Brain glyceraldehyde-3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts
    • Cooper A.J.L., Sheu K.-W.R., Burke J.R., Strittmatter W.J., Blass J.P. Brain 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.L.1    Sheu, K.-W.R.2    Burke, J.R.3    Strittmatter, W.J.4    Blass, J.P.5
  • 161
    • 0030812593 scopus 로고    scopus 로고
    • Translutaminase-catalyzed inactivation of glyceraldehyde-3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length
    • Cooper A.J.L., Sheu K.F.R., Burke J.R., Onodera O., Strittmatter W.J., Roses A.D., Blass J.P. Translutaminase-catalyzed inactivation of glyceraldehyde-3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length. Proc. Natl. Acad. Sci. USA. 94:1997;12604-12609.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12604-12609
    • Cooper, A.J.L.1    Sheu, K.F.R.2    Burke, J.R.3    Onodera, O.4    Strittmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 162
    • 0027230458 scopus 로고
    • Association of glyceraldehyde-3-phosphate dehydrogenase expression with cell motility and metastatic potential of rat prostatic adenocarcinoma
    • Epner D.E., Partin A.W., Schalken J.A., Issacs J.T., Coffey D.S. Association of glyceraldehyde-3-phosphate dehydrogenase expression with cell motility and metastatic potential of rat prostatic adenocarcinoma. Cancer Res. 53:1993;1995-1997.
    • (1993) Cancer Res. , vol.53 , pp. 1995-1997
    • Epner, D.E.1    Partin, A.W.2    Schalken, J.A.3    Issacs, J.T.4    Coffey, D.S.5
  • 163
    • 0028303449 scopus 로고
    • Expression of human prostatic acid phosphatase and prostate specific antigen genes in neoplastic and benign tissues
    • Sharief F.S., Mohler J.L., Sharief Y., Li S.S.-L. Expression of human prostatic acid phosphatase and prostate specific antigen genes in neoplastic and benign tissues. Biochem. Mol. Biol. Int. 33:1994;567-574.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 567-574
    • Sharief, F.S.1    Mohler, J.L.2    Sharief, Y.3    Li, S.S.-L.4
  • 164
    • 0002332187 scopus 로고    scopus 로고
    • Increased glyceraldehyde-3-phosphate dehydrogenase gene expression in late pathological state human prostate cancer
    • Rondinelli R.H., Epner D.E., Tricoli J.V. Increased glyceraldehyde-3-phosphate dehydrogenase gene expression in late pathological state human prostate cancer. Prostate Cancer Prostatic Dis. 1:1997;66-72.
    • (1997) Prostate Cancer Prostatic Dis. , vol.1 , pp. 66-72
    • Rondinelli, R.H.1    Epner, D.E.2    Tricoli, J.V.3
  • 165
    • 0029028955 scopus 로고
    • Alteration of glyceraldehyde-3-phosphate dehydrogenase activity and messenger RNA content by androgen in human prostate carcinoma cells
    • Ripple M.O., Wilding G. Alteration of glyceraldehyde-3-phosphate dehydrogenase activity and messenger RNA content by androgen in human prostate carcinoma cells. Cancer Res. 55:1995;4234-4236.
    • (1995) Cancer Res. , vol.55 , pp. 4234-4236
    • Ripple, M.O.1    Wilding, G.2
  • 166
    • 0029888396 scopus 로고    scopus 로고
    • There are multiple forms of glyceraldehyde-3-phosphate dehydrogenase in prostate cancer cells and normal prostate cells
    • Epner D.E. There are multiple forms of glyceraldehyde-3-phosphate dehydrogenase in prostate cancer cells and normal prostate cells. Prostate. 28:1996;372-378.
    • (1996) Prostate , vol.28 , pp. 372-378
    • Epner, D.E.1


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