메뉴 건너뛰기




Volumn 3, Issue 10, 2004, Pages 998-1008

Global investigation of p53-induced apoptosis through quantitative proteomic profiling using comparative amino acid-coded tagging

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIOXIDANT; BINDING PROTEIN; CALPAIN; CHAPERONE; CYCLOPHILIN A; CYCLOPHILIN B; DEUTERIUM; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; ISOENZYME; LEUCINE; LIPOCORTIN 1; LIPOCORTIN 2; LIPOCORTIN 4; LIPOCORTIN 5; LYSINE; MEMBRANE PROTEIN; METHIONINE; PEROXIREDOXIN; PROTEIN 14 3 3; PROTEIN DISULFIDE ISOMERASE; PROTEIN P53; TRYPSIN; TYROSINE; CYCLOPHILIN; CYCLOPHILIN D; PEPTIDYLPROLYL ISOMERASE; PROTEIN;

EID: 11144333835     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400033-MCP200     Document Type: Article
Times cited : (70)

References (60)
  • 1
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. (2000) The biochemistry of apoptosis. Nature 407, 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 2
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K. F., and Kroemer, G. (2001) Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3, E255-E263
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 4
    • 0038205745 scopus 로고    scopus 로고
    • Targeting programmed cell death in neurodegenerative diseases
    • Vila, M., and Przedborski, S. (2003) Targeting programmed cell death in neurodegenerative diseases. Nat. Rev. Neurosci. 4, 365-375
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 365-375
    • Vila, M.1    Przedborski, S.2
  • 5
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • Scorrano, L., and Korsmeyer, S. J. (2003) Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem. Biophys. Res. Commun. 304, 437-444
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 6
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer, D. D., and Ferguson-Miller, S. (2003) Mitochondria: Releasing power for life and unleashing the machineries of death. Cell 112, 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 7
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B., Lane, D., and Levine, A. J. (2000) Surfing the p53 network. Nature 408, 307-310
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 8
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden, K. H., and Lu, X. (2002) Live or let die: the cell's response to p53. Nat. Rev. Cancer 2, 594-604
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 10
    • 0035266127 scopus 로고    scopus 로고
    • Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species
    • Donald, S. P., Sun, X. Y., Hu, C. A., Yu, J., Mei, J. M., Valle, D., and Phang, J. M. (2001) Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species. Cancer Res. 61, 1810-1815
    • (2001) Cancer Res. , vol.61 , pp. 1810-1815
    • Donald, S.P.1    Sun, X.Y.2    Hu, C.A.3    Yu, J.4    Mei, J.M.5    Valle, D.6    Phang, J.M.7
  • 11
    • 0038322048 scopus 로고    scopus 로고
    • Proline oxidase induces apoptosis in tumor cells, and its expression is frequently absent or reduced in renal carcinomas
    • Maxwell, S. A., and Rivera, A. (2003) Proline oxidase induces apoptosis in tumor cells, and its expression is frequently absent or reduced in renal carcinomas. J. Biol. Chem. 278, 9784-9789
    • (2003) J. Biol. Chem. , vol.278 , pp. 9784-9789
    • Maxwell, S.A.1    Rivera, A.2
  • 14
    • 0030802364 scopus 로고    scopus 로고
    • A novel p53-inducible gene, PAG608, encodes a nuclear zinc finger protein whose overexpression promotes apoptosis
    • Israeli, D., Tessler, E., Haupt, Y., Elkeles, A., Wilder, S., Amson, R., Telerman, A., and Oren, M. (1997) A novel p53-inducible gene, PAG608, encodes a nuclear zinc finger protein whose overexpression promotes apoptosis. EMBO J. 16, 4384-4392
    • (1997) EMBO J. , vol.16 , pp. 4384-4392
    • Israeli, D.1    Tessler, E.2    Haupt, Y.3    Elkeles, A.4    Wilder, S.5    Amson, R.6    Telerman, A.7    Oren, M.8
  • 18
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P., Rochon, Y., Franza, B. R., and Aebersold, R. (1999) Correlation between protein and mRNA abundance in yeast. Mol. Cell. Biol. 19, 1720-1730
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 19
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 20
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A., and Mann, M. (2000) Proteomics to study genes and genomes. Nature 405, 837-846
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 21
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 22
    • 0037307816 scopus 로고    scopus 로고
    • Advances in quantitative proteomics via stable isotope tagging and mass spectrometry
    • Tao, W. A., and Aebersold, R. (2003) Advances in quantitative proteomics via stable isotope tagging and mass spectrometry. Curr. Opin. Biotechnol. 14, 110-118
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 110-118
    • Tao, W.A.1    Aebersold, R.2
  • 23
    • 0034654593 scopus 로고    scopus 로고
    • Site-specific mass tagging with stable isotopes in proteins for accurate and efficient protein identification
    • Chen, X., Smith, L. M., and Bradbury, E. M. (2000) Site-specific mass tagging with stable isotopes in proteins for accurate and efficient protein identification. Anal. Chem. 72, 1134-1143
    • (2000) Anal. Chem. , vol.72 , pp. 1134-1143
    • Chen, X.1    Smith, L.M.2    Bradbury, E.M.3
  • 24
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 25
    • 0037270746 scopus 로고    scopus 로고
    • Precise peptide sequencing and protein quantification in the human proteome through in vivo lysine-specific mass tagging
    • Gu, S., Pan, S., Bradbury, E. M., and Chen, X. (2003) Precise peptide sequencing and protein quantification in the human proteome through in vivo lysine-specific mass tagging. J. Am. Soc. Mass Spectrom. 14, 1-7
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 1-7
    • Gu, S.1    Pan, S.2    Bradbury, E.M.3    Chen, X.4
  • 26
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu, H., Pan, S., Gu, S., Bradbury, E. M., and Chen, X. (2002) Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid Commun. Mass Spectrom. 16, 2115-2123
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5
  • 27
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S. E., Foster, L. J., and Mann, M. (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 28
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., and Vogelstein, B. (2001) PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell 7, 673-682
    • (2001) Mol. Cell , vol.7 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 29
    • 0037112472 scopus 로고    scopus 로고
    • Use of deuterium-labeled lysine for efficient protein identification and peptide de novo sequencing
    • Gu, S., Pan, S., Bradbury, E. M., and Chen, X. (2002) Use of deuterium-labeled lysine for efficient protein identification and peptide de novo sequencing. Anal. Chem. 74, 5774-5785
    • (2002) Anal. Chem. , vol.74 , pp. 5774-5785
    • Gu, S.1    Pan, S.2    Bradbury, E.M.3    Chen, X.4
  • 30
    • 0037444607 scopus 로고    scopus 로고
    • Single peptide-based protein identification in human proteome through MALDI-TOF MS coupled with amino acids coded mass tagging
    • Pan, S., Gu, S., Bradbury, E. M., and Chen, X. (2003) Single peptide-based protein identification in human proteome through MALDI-TOF MS coupled with amino acids coded mass tagging. Anal. Chem. 75, 1316-1324
    • (2003) Anal. Chem. , vol.75 , pp. 1316-1324
    • Pan, S.1    Gu, S.2    Bradbury, E.M.3    Chen, X.4
  • 31
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • Gu, S., Chen, J., Dobos, K M., Bradbury, E. M., Belisle, J. T., and Chen, X. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell. Proteomics 2, 1284-1296
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 32
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence data-bases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence data-bases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 33
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., and Gygi, S. P. (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome. J. Proteome Res. 2, 43-50
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 34
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko, A., Sunyaev, S., Loboda, A., Shevchenko, A., Bork, P., Ens, W., and Standing, K. G. (2001) Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem. 73, 1917-1926
    • (2001) Anal. Chem. , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 35
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B., Kratchmarova, I., Ong, S. E., Nielsen, M., Foster, L. J., and Mann, M. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 36
    • 0035228786 scopus 로고    scopus 로고
    • P53-responsive genes and the potential for cancer diagnostics and therapeutics development
    • Xu, H., and el-Gewely, M. R. (2001) P53-responsive genes and the potential for cancer diagnostics and therapeutics development. Biotechnol. Annu. Rev. 7, 131-164
    • (2001) Biotechnol. Annu. Rev. , vol.7 , pp. 131-164
    • Xu, H.1    el-Gewely, M.R.2
  • 37
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris, A. L. (2002) Hypoxia - A key regulatory factor in tumour growth. Nat. Rev. Cancer 2, 38-47
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 38-47
    • Harris, A.L.1
  • 39
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama, S., Reed, J. C., and Homma, S. (2003) Heat-shock proteins as regulators of apoptosis. Oncogene 22, 9041-9047
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 41
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N., and Kroemer, G. (2001) The mitochondrion in apoptosis: How Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2, 67-71
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 42
    • 0038481271 scopus 로고    scopus 로고
    • Mitochondrial regulation of apoptosis
    • Mayer, B., and Oberbauer, R. (2003) Mitochondrial regulation of apoptosis. News Physiol. Sci. 18, 89-94
    • (2003) News Physiol. Sci. , vol.18 , pp. 89-94
    • Mayer, B.1    Oberbauer, R.2
  • 43
    • 0036478993 scopus 로고    scopus 로고
    • The adenine nucleotide translocator in apoptosis
    • Belzacq, A. S., Vieira, H. L., Kroemer, G., Brenner, C. (2002) The adenine nucleotide translocator in apoptosis. Biochimie 84, 167-176
    • (2002) Biochimie , vol.84 , pp. 167-176
    • Belzacq, A.S.1    Vieira, H.L.2    Kroemer, G.3    Brenner, C.4
  • 44
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • Lin, D. T., and Lechleiter, J. D. (2002) Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J. Biol. Chem. 277, 31134-31141
    • (2002) J. Biol. Chem. , vol.277 , pp. 31134-31141
    • Lin, D.T.1    Lechleiter, J.D.2
  • 45
    • 1542332908 scopus 로고    scopus 로고
    • Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor
    • Schubert, A., and Grimm, S. (2004) Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor. Cancer Res. 64, 85-93
    • (2004) Cancer Res. , vol.64 , pp. 85-93
    • Schubert, A.1    Grimm, S.2
  • 46
    • 0036644582 scopus 로고    scopus 로고
    • Cyclophilins: Unexpected messengers in intercellular communications
    • Bukrinsky, M. I. (2002) Cyclophilins: Unexpected messengers in intercellular communications. Trends Immunol. 23, 323-325
    • (2002) Trends Immunol. , vol.23 , pp. 323-325
    • Bukrinsky, M.I.1
  • 47
    • 0036789573 scopus 로고    scopus 로고
    • Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export
    • Ansari, H., Greco, G., and Luban, J. (2002) Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export. Mol. Cell. Biol. 22, 6993-7003
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6993-7003
    • Ansari, H.1    Greco, G.2    Luban, J.3
  • 51
    • 0036534404 scopus 로고    scopus 로고
    • Cyclophilin-A is involved in excitotoxin-induced caspase activation in rat neuronal B50 cells
    • Capano, M., Virji, S., and Crompton, M. (2002) Cyclophilin-A is involved in excitotoxin-induced caspase activation in rat neuronal B50 cells. Biochem. J. 363, 29-36
    • (2002) Biochem. J. , vol.363 , pp. 29-36
    • Capano, M.1    Virji, S.2    Crompton, M.3
  • 52
    • 2442460088 scopus 로고    scopus 로고
    • Role of mitochondrial membrane permeabilization in apoptosis and cancer
    • Henry-Mowatt, J., Dive, C., Martinou, J. C., and James, D. (2004) Role of mitochondrial membrane permeabilization in apoptosis and cancer. Oncogene 23, 2850-2860
    • (2004) Oncogene , vol.23 , pp. 2850-2860
    • Henry-Mowatt, J.1    Dive, C.2    Martinou, J.C.3    James, D.4
  • 53
    • 0034666290 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • Chen, J. W., Dodia, C., Feinstein, S. I., Jain, M. K., and Fisher, A. B. (2000) 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J. Biol. Chem. 275, 28421-28427
    • (2000) J. Biol. Chem. , vol.275 , pp. 28421-28427
    • Chen, J.W.1    Dodia, C.2    Feinstein, S.I.3    Jain, M.K.4    Fisher, A.B.5
  • 54
    • 0033301995 scopus 로고    scopus 로고
    • From cytoprotection to tumor suppression: The multifactorial role of peroxiredoxins
    • Butterfield, L. H., Merino, A., Golub, S. H., and Shau, H. (1999) From cytoprotection to tumor suppression: The multifactorial role of peroxiredoxins. Antioxid. Redox Signal 1, 385-402
    • (1999) Antioxid. Redox Signal , vol.1 , pp. 385-402
    • Butterfield, L.H.1    Merino, A.2    Golub, S.H.3    Shau, H.4
  • 56
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., and Lunardi, J. (2002) Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. J. Biol. Chem. 277, 19396-19401
    • (2002) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 57
    • 1342306819 scopus 로고    scopus 로고
    • Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3
    • Lin, B. Z., Kolluri, S. K., Lin, F., Liu, W., Han, Y. H., Cao, X., Dawson, M. I., Reed, J. C., and Zhang, X. K. (2004) Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Cell 116, 527-540
    • (2004) Cell , vol.116 , pp. 527-540
    • Lin, B.Z.1    Kolluri, S.K.2    Lin, F.3    Liu, W.4    Han, Y.H.5    Cao, X.6    Dawson, M.I.7    Reed, J.C.8    Zhang, X.K.9
  • 58
    • 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
    • Zheng, L., Roeder, R. G., and Luo, Y. (2003) S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114, 255-266
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 60
    • 0037058623 scopus 로고    scopus 로고
    • Tumor M2 pyruvate kinase - Determination in breast cancer patients receiving trastuzumab therapy
    • Hoopmann, M., Warm, M., Mallmann, P., Thomas, A., Gohring, U. J., and Schondorf, T. (2002) Tumor M2 pyruvate kinase - Determination in breast cancer patients receiving trastuzumab therapy. Cancer Lett. 187, 223-228
    • (2002) Cancer Lett. , vol.187 , pp. 223-228
    • Hoopmann, M.1    Warm, M.2    Mallmann, P.3    Thomas, A.4    Gohring, U.J.5    Schondorf, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.