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Volumn 1622, Issue 1, 2003, Pages 50-56

Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function

Author keywords

Glyceraldehyde 3 phosphate dehydrogenase; Protein structure function; Subcellular localization

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; TETRAMER;

EID: 0038771936     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(03)00117-X     Document Type: Article
Times cited : (66)

References (50)
  • 2
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. 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
  • 3
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
    • Sirover M.A. 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
  • 4
    • 0034949123 scopus 로고    scopus 로고
    • Enzymes on microbial pathogens and Trichomonas vaginalis: Molecular mimicry and functional diversity
    • Alderete J.F., Millsap K.W., Lehker M.W., Benchimol M. Enzymes on microbial pathogens and Trichomonas vaginalis: molecular mimicry and functional diversity. Cell. Microbiol. 3:2001;359-370.
    • (2001) Cell. Microbiol. , vol.3 , pp. 359-370
    • Alderete, J.F.1    Millsap, K.W.2    Lehker, M.W.3    Benchimol, M.4
  • 5
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0022359757 scopus 로고
    • Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP
    • Huitorel P., Pantaloni P.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, P.D.2
  • 10
    • 0031854353 scopus 로고    scopus 로고
    • Phosphorylation of the hepatitis core protein by glyceraldehyde-3-phosphate dehydrogenase protein kinase activity
    • Duclos-Vallee J.C., Capel F., Mabit H., Petit M.-A. Phosphorylation of the hepatitis core protein by glyceraldehyde-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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 16
    • 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
  • 17
    • 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
    • Krynetski E.Y., Krynetskaia N.F., Bianchi M.E., Evans W.E. 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    Krynetskaia, N.F.2    Bianchi, M.E.3    Evans, W.E.4
  • 18
    • 0022406559 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes
    • Ryazanov A.G. Glyceraldehyde-3-phosphate 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0034713424 scopus 로고    scopus 로고
    • Specific interaction between the Hepatitis delta virus RNA and glyceraldehyde-3-phosphate dehydrogenase: An enhancement on ribozyme catalysis
    • Lin S.-S., Chang S.C.-S., Wang Y.H., Sun C.-Y., Chang M.-F. Specific interaction between the Hepatitis delta virus RNA and glyceraldehyde-3-phosphate dehydrogenase: an enhancement on ribozyme catalysis. Virology. 271:2000;46-57.
    • (2000) Virology , vol.271 , pp. 46-57
    • Lin, S.-S.1    Chang, S.C.-S.2    Wang, Y.H.3    Sun, C.-Y.4    Chang, M.-F.5
  • 23
    • 0033934137 scopus 로고    scopus 로고
    • Functional significance of the interaction of hepatitis A virus RNA with glyceraldehyde-3-phosphate dehydrogenase (GAPDH): Opposing effects of GAPDH and polypyrimidine tract binding protein on internal ribosome entry site function
    • Yi M., Schultz D.E., Lemon S.M. Functional significance of the interaction of hepatitis A virus RNA with glyceraldehyde-3-phosphate dehydrogenase (GAPDH): opposing effects of GAPDH and polypyrimidine tract binding protein on internal ribosome entry site function. J. Virol. 74:2000;6459-6468.
    • (2000) J. Virol. , vol.74 , pp. 6459-6468
    • Yi, M.1    Schultz, D.E.2    Lemon, S.M.3
  • 24
    • 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
    • Dollenmaier G., Weitz M. 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
  • 25
    • 0035951872 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
    • Tisdale E.J. Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. J. Biol. Chem. 276:2001;2480-2486.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2480-2486
    • Tisdale, E.J.1
  • 26
    • 0036479109 scopus 로고    scopus 로고
    • L/λ and plays a role in microtubule dynamics in the early secretory pathway required for vesicular transport
    • L/λ and plays a role in microtubule dynamics in the early secretory pathway required for vesicular transport. J. Biol. Chem. 277:2002;3334-3341.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 27
    • 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
  • 28
    • 0036091876 scopus 로고    scopus 로고
    • Proliferative and nutritional dependent regulation of glyceraldehyde-3-phosphate dehydrogenase expression in the rat liver
    • Corbin I.R., Gong Y., Zhang M., Minuk G.Y. Proliferative and nutritional dependent regulation of glyceraldehyde-3-phosphate dehydrogenase expression in the rat liver. Cell Prolif. 38:2002;173-182.
    • (2002) Cell Prolif. , vol.38 , pp. 173-182
    • Corbin, I.R.1    Gong, Y.2    Zhang, M.3    Minuk, G.Y.4
  • 29
    • 0037197778 scopus 로고    scopus 로고
    • Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts
    • Mazzola J.L., Sirover M.A. Alteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts. Mol. Brain Res. 100:2002;95-101.
    • (2002) Mol. Brain Res. , vol.100 , pp. 95-101
    • Mazzola, J.L.1    Sirover, M.A.2
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 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
  • 40
    • 0032972037 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis
    • Saunders P.A., Chen R.-W., Chuang D.-W. 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    Chen, R.-W.2    Chuang, D.-W.3
  • 42
    • 0037438118 scopus 로고    scopus 로고
    • Subcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts
    • Mazzola J.L., Sirover M.A. 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
  • 43
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • Glazer P.E., Han X., Gross R.W. Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: implications for the coordinated regulation of glycolysis and membrane fusion. Proc. Natl. Acad. Sci. U. S. A. 99:2002;14104-14109.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14104-14109
    • Glazer, P.E.1    Han, X.2    Gross, R.W.3
  • 44
    • 0024399951 scopus 로고
    • Physical association of base excision repair enzymes with parental or replicating DNA in BHK-21 cells
    • Lee K.A., Sirover M.A. Physical association of base excision repair enzymes with parental or replicating DNA in BHK-21 cells. Cancer Res. 49:1989;3037-3044.
    • (1989) Cancer Res. , vol.49 , pp. 3037-3044
    • Lee, K.A.1    Sirover, M.A.2
  • 45
    • 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. U. S. A. 94:1997;11669-11674.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11669-11674
    • Sawa, A.1    Khan, A.A.2    Hester, L.D.3    Snyder, S.H.4
  • 46
    • 0034957426 scopus 로고    scopus 로고
    • Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum stimulation
    • Schmitz H.-D. Reversible nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase upon serum stimulation. Eur. J. Cell Biol. 80:2001;419-427.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 419-427
    • Schmitz, H.-D.1
  • 47
    • 0036348974 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phsophate dehydrogenase associates with actin filaments in serum deprived NIH 3T3 cells only
    • Schmitz H.-D., Bereiter-Hahn J. Glyceraldehyde-3-phsophate dehydrogenase associates with actin filaments in serum deprived NIH 3T3 cells only. Cell Biol. Int. 26:2002;155-164.
    • (2002) Cell Biol. Int. , vol.26 , pp. 155-164
    • Schmitz, H.-D.1    Bereiter-Hahn, J.2
  • 48
    • 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
  • 49
    • 0034235250 scopus 로고    scopus 로고
    • Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction
    • Vila M.R., Nicolas A., Morote J., de Torres I., Meseguer A. Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction. Cancer. 89:2000;152-164.
    • (2000) Cancer , vol.89 , pp. 152-164
    • Vila, M.R.1    Nicolas, A.2    Morote, J.3    De Torres, I.4    Meseguer, A.5
  • 50
    • 0343619342 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer
    • Revillion F., Pawlowski V., Hornez L., Peyrat J.-P. Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer. Eur. J. Cancer. 36:2000;1038-1042.
    • (2000) Eur. J. Cancer , vol.36 , pp. 1038-1042
    • Revillion, F.1    Pawlowski, V.2    Hornez, L.3    Peyrat, J.-P.4


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