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Volumn 11, Issue 8, 2004, Pages 842-852

Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: A cell biochemical and proteomic investigation

Author keywords

Apoptosis; Flow cytometric analysis; PDT; Protein carbonylation; Proteomic analysis

Indexed keywords

ALPHA TUBULIN; BETA ACTIN; CALRETICULIN; ENOLASE; ENOLASE ALPHA; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 71; ISOMERASE; PHOSPHATE DISULFIDE ISOMERASE; PURPURIN 18; PURPURIN DERIVATIVE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 4344604345     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401427     Document Type: Article
Times cited : (105)

References (60)
  • 1
    • 0028943734 scopus 로고
    • Apoptosis in pathogenesis and treatment of disease
    • Thompson C (1995) Apoptosis in pathogenesis and treatment of disease. Science 267: 1456-1461
    • (1995) Science , vol.267 , pp. 1456-1461
    • Thompson, C.1
  • 2
    • 0036889913 scopus 로고    scopus 로고
    • Apoptosis: Biochemical aspects and clinical implications
    • Kiechle FL and Zhang X (2002) Apoptosis: biochemical aspects and clinical implications. Clin. Chim. Acta 326: 27-45
    • (2002) Clin. Chim. Acta , vol.326 , pp. 27-45
    • Kiechle, F.L.1    Zhang, X.2
  • 3
    • 0032078217 scopus 로고    scopus 로고
    • Caspases: Key mediators of apoptosis
    • Thornberry NA (1998) Caspases: key mediators of apoptosis. Chem. Biol. 5: R97-103
    • (1998) Chem. Biol. , vol.5
    • Thornberry, N.A.1
  • 4
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO (2000) The biochemistry of apoptosis. Nature 407: 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 6
    • 0033805296 scopus 로고    scopus 로고
    • Triggering and modulation of apoptosis by oxidative stress
    • Chandra J, Samali A and Orrenius S (2000) Triggering and modulation of apoptosis by oxidative stress. Free Radic. Biol. Med. 29: 323-333
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 323-333
    • Chandra, J.1    Samali, A.2    Orrenius, S.3
  • 7
    • 0036176217 scopus 로고    scopus 로고
    • An update on photodynamic therapy applications
    • Dougherty TJ (2002) An update on photodynamic therapy applications. J. Clin. Laser Med. Surg. 20: 3-7
    • (2002) J. Clin. Laser Med. Surg. , vol.20 , pp. 3-7
    • Dougherty, T.J.1
  • 8
    • 0033937773 scopus 로고    scopus 로고
    • Mechanism of photodynamic therapy-induced cell death
    • Ahmad N and Mukhtar H (2000) Mechanism of photodynamic therapy-induced cell death. Methods Enzymol. 319: 342-358
    • (2000) Methods Enzymol. , vol.319 , pp. 342-358
    • Ahmad, N.1    Mukhtar, H.2
  • 9
    • 0035861589 scopus 로고    scopus 로고
    • Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization
    • Lam M, Oleinick NL and Nieminen AL (2001) Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization. J. Biol. Chem. 276: 47379-47386
    • (2001) J. Biol. Chem. , vol.276 , pp. 47379-47386
    • Lam, M.1    Oleinick, N.L.2    Nieminen, A.L.3
  • 10
    • 0035286178 scopus 로고    scopus 로고
    • Purpurin-18 in combination with light leads to apoptosis or necrosis in HL60 leukemia cells
    • Di Stefano A, Ettorre A, Sbrana S, Giovane C and Neri P (2001) Purpurin-18 in combination with light leads to apoptosis or necrosis in HL60 leukemia cells. Photochem. Photobiol. 73: 290-296
    • (2001) Photochem. Photobiol. , vol.73 , pp. 290-296
    • Di Stefano, A.1    Ettorre, A.2    Sbrana, S.3    Giovane, C.4    Neri, P.5
  • 11
    • 0035887462 scopus 로고    scopus 로고
    • Photosensitization with zinc (II) phthalocyanine as a switch in the decision between apoptosis and necrosis
    • Fabris C, Valduga G, Miotto G, Borsetto L, Jori G, Garbisa S and Reddi L (2001) Photosensitization with zinc (II) phthalocyanine as a switch in the decision between apoptosis and necrosis. Cancer Res. 61: 7495-7500
    • (2001) Cancer Res. , vol.61 , pp. 7495-7500
    • Fabris, C.1    Valduga, G.2    Miotto, G.3    Borsetto, L.4    Jori, G.5    Garbisa, S.6    Reddi, L.7
  • 12
    • 0036461958 scopus 로고    scopus 로고
    • The role of apoptosis in response to photodynamic therapy: What, where, why, and how
    • Oleinick NL, Morris RL and Belichenko I (2002) The role of apoptosis in response to photodynamic therapy: what, where, why, and how. Photochem. Photobiol. Sci. 1: 1-21
    • (2002) Photochem. Photobiol. Sci. , vol.1 , pp. 1-21
    • Oleinick, N.L.1    Morris, R.L.2    Belichenko, I.3
  • 13
    • 0027146422 scopus 로고
    • Phospholipase activation triggers apoptosis in photosensitized mouse lymphoma cells
    • Agarwal ML, Larkin HE, Zaidi SIA, Mukhtar H and Oleinick NL (1993) Phospholipase activation triggers apoptosis in photosensitized mouse lymphoma cells. Cancer Res. 53: 5897-5902
    • (1993) Cancer Res. , vol.53 , pp. 5897-5902
    • Agarwal, M.L.1    Larkin, H.E.2    Zaidi, S.I.A.3    Mukhtar, H.4    Oleinick, N.L.5
  • 14
    • 0032080377 scopus 로고    scopus 로고
    • Involvement of nitric oxide during phthalocyanine (Pc4) photodynamic therapy-mediated apoptosis
    • Gupta S, Ahmad N and Mukhtar H (1998) Involvement of nitric oxide during phthalocyanine (Pc4) photodynamic therapy-mediated apoptosis. Cancer Res. 58: 1785-1788
    • (1998) Cancer Res. , vol.58 , pp. 1785-1788
    • Gupta, S.1    Ahmad, N.2    Mukhtar, H.3
  • 16
    • 0028353883 scopus 로고
    • Photodynamic therapy-mediated oxidative stress as a molecular switch for the temporal expression of genes ligated to the human heat shock promoter
    • Luna MC, Wong S and Gomer CY (1994) Photodynamic therapy-mediated oxidative stress as a molecular switch for the temporal expression of genes ligated to the human heat shock promoter. Cancer Res. 54: 1374-1380
    • (1994) Cancer Res. , vol.54 , pp. 1374-1380
    • Luna, M.C.1    Wong, S.2    Gomer, C.Y.3
  • 17
    • 0029948740 scopus 로고    scopus 로고
    • Photodynamic therapy-mediated oxidative stress can induce expression of heat shock proteins
    • Gomer CJ, Ryter SW, Ferrario A, Rucker N, Wong S and Fisher AMR (1996) Photodynamic therapy-mediated oxidative stress can induce expression of heat shock proteins. Cancer Res. 56: 2355-2360
    • (1996) Cancer Res. , vol.56 , pp. 2355-2360
    • Gomer, C.J.1    Ryter, S.W.2    Ferrario, A.3    Rucker, N.4    Wong, S.5    Fisher, A.M.R.6
  • 18
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal FM (2002) Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32: 797-803
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, F.M.1
  • 19
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol E, Piulats E, Echave P, Herrero E and Ros J (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J. Biol. Chem. 275: 27393-27398
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 20
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J, Cabiscol E and Ros J (1998) Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273: 3027-3032
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 21
    • 0035890871 scopus 로고    scopus 로고
    • Selectivity of protein oxidative damage during aging in Drosophila melanogaster
    • Das N, Levine RL, Orr WC and Sohal RS (2001) Selectivity of protein oxidative damage during aging in Drosophila melanogaster, Biochem. J. 360 (Part 1): 209-216
    • (2001) Biochem. J. , vol.360 , Issue.PART 1 , pp. 209-216
    • Das, N.1    Levine, R.L.2    Orr, W.C.3    Sohal, R.S.4
  • 24
    • 0343294288 scopus 로고    scopus 로고
    • Adaptation of protein carbonyl detection to the requirements of proteome analysis demonstrated for hypoxia/reoxygenation in isolated rat liver mitochondria
    • Reinheckel T, Korn S, Mohring S, Augustin W, Halangk W and Shild L (2000) Adaptation of protein carbonyl detection to the requirements of proteome analysis demonstrated for hypoxia/reoxygenation in isolated rat liver mitochondria. Arch. Biochem. Biophys. 376: 59-65
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 59-65
    • Reinheckel, T.1    Korn, S.2    Mohring, S.3    Augustin, W.4    Halangk, W.5    Shild, L.6
  • 25
    • 0042122458 scopus 로고    scopus 로고
    • Involvement of oxidative stress in apoptosis induced by a mixture of isothiazolinones in normal human keratinocytes
    • Ettorre A, Andreassi M, Anselmi C, Neri P, Andreassi L and Di Stefano A (2003) Involvement of oxidative stress in apoptosis induced by a mixture of isothiazolinones in normal human keratinocytes. J. Invest. Dermatol. 121: 328-336
    • (2003) J. Invest. Dermatol. , vol.121 , pp. 328-336
    • Ettorre, A.1    Andreassi, M.2    Anselmi, C.3    Neri, P.4    Andreassi, L.5    Di Stefano, A.6
  • 26
    • 0033088957 scopus 로고    scopus 로고
    • The role of glutathione in the regulation of apoptosis
    • Hall AG (1999) The role of glutathione in the regulation of apoptosis. Eur. J. Clin. Invest. 29: 238-245
    • (1999) Eur. J. Clin. Invest. , vol.29 , pp. 238-245
    • Hall, A.G.1
  • 28
    • 0029033862 scopus 로고
    • Mitochondrial changes associated with glutathione deficiency
    • Meister A (1995) Mitochondrial changes associated with glutathione deficiency. Biochim. Biophys. Acta 1271: 35-42
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 35-42
    • Meister, A.1
  • 29
    • 0035797106 scopus 로고    scopus 로고
    • Mitochondria-based photodynamic anti-cancer therapy
    • Morgan J and Oseroff AR (2001) Mitochondria-based photodynamic anti-cancer therapy. Adv. Drug Deliv. Rev. 49: 71-86
    • (2001) Adv. Drug Deliv. Rev. , vol.49 , pp. 71-86
    • Morgan, J.1    Oseroff, A.R.2
  • 30
    • 4344593171 scopus 로고    scopus 로고
    • ROS production and alteration of mitochondrial transmembrane potential after PDT with Purpurin-18 in human leukemia cells
    • Ettorre A, Soldani P, Fabbrini M, Neri P and Di Stefano A (2002) ROS production and alteration of mitochondrial transmembrane potential after PDT with Purpurin-18 in human leukemia cells. Int. J. Biochem. 51: 86
    • (2002) Int. J. Biochem. , vol.51 , pp. 86
    • Ettorre, A.1    Soldani, P.2    Fabbrini, M.3    Neri, P.4    Di Stefano, A.5
  • 31
    • 0031149813 scopus 로고    scopus 로고
    • Mitofilin is a transmembrane protein of the inner mitochondrial membrane expressed as two isoforms
    • Gieffers C, Korioth F, Heimann P, Ungermann C and Frey J (1997) Mitofilin is a transmembrane protein of the inner mitochondrial membrane expressed as two isoforms. Exp. Cell Res. 232: 395-399
    • (1997) Exp. Cell Res. , vol.232 , pp. 395-399
    • Gieffers, C.1    Korioth, F.2    Heimann, P.3    Ungermann, C.4    Frey, J.5
  • 32
    • 0029815971 scopus 로고    scopus 로고
    • Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains
    • Odgren PR, Toukatly G, Bangs PL, Gilmore R and Fey EG (1996) Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains. J. Cell Sci. 109 (Part 9): 2253-2264
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 9 , pp. 2253-2264
    • Odgren, P.R.1    Toukatly, G.2    Bangs, P.L.3    Gilmore, R.4    Fey, E.G.5
  • 34
    • 20244373291 scopus 로고    scopus 로고
    • Protein changes in HL60 leukemia cells associated with 5-aminolevulinic acid-based photodynamic therapy. Early effects on endoplasmic reticulum chaperones
    • Grebenova D, Halada P, Stulik J, Havlicek V and Hrkal Z (2000) Protein changes in HL60 leukemia cells associated with 5-aminolevulinic acid-based photodynamic therapy. Early effects on endoplasmic reticulum chaperones. Photochem. Photobiol. 72: 16-22
    • (2000) Photochem. Photobiol. , vol.72 , pp. 16-22
    • Grebenova, D.1    Halada, P.2    Stulik, J.3    Havlicek, V.4    Hrkal, Z.5
  • 35
    • 4344619399 scopus 로고    scopus 로고
    • Analysis of the Candida albicans protein pattern in response to the photodynamic therapy by two-dimensional gel electrophoresis and mass-spectrometry
    • From Genome to Proteome: functional proteomics, fifth Siena Meeting Sept 2-5, Siena Italy
    • Raggiaschi R, Cocchi A, Liberatori S, Armini A, Fantetti L, Bini L and Roncucci G (2002) Analysis of the Candida albicans protein pattern in response to the photodynamic therapy by two-dimensional gel electrophoresis and mass-spectrometry. From Genome to Proteome: functional proteomics, fifth Siena Meeting Sept 2-5, Siena Italy pp 351
    • (2002) , pp. 351
    • Raggiaschi, R.1    Cocchi, A.2    Liberatori, S.3    Armini, A.4    Fantetti, L.5    Bini, L.6    Roncucci, G.7
  • 36
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease and oxidative stress
    • Berlett BS and Stadtman ER (1997) Protein oxidation in aging, disease and oxidative stress. J. Biol. Chem. 272: 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 37
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T and Holbrook NJ (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408: 239-247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 39
    • 0030805622 scopus 로고    scopus 로고
    • A generalised increase in protein carbonyls in the brain in Parkinson's but incidental lewy body disease
    • Alam ZI, Daniel SE, Lees AJ, Mardsen DC, Jenner P and Halliwell BA (1997) A generalised increase in protein carbonyls in the brain in Parkinson's but incidental lewy body disease. J. Neurochem. 69: 1326-1329
    • (1997) J. Neurochem. , vol.69 , pp. 1326-1329
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Mardsen, D.C.4    Jenner, P.5    Halliwell, B.A.6
  • 40
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 41
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Moser DD, Caron AW, Bourget L, Denis-Larose C and Massie B (2000) Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17: 5317-5327
    • (2000) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Moser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 42
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin KM, Lin B, Lian IY, Mestril R, Scheffler IE and Dillmann WH (2001) Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation 103: 1787-1792
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 47
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR and Butterfield DA (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71. J. Neurochem. 82: 1524-1532
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 49
    • 0002588647 scopus 로고    scopus 로고
    • Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin
    • Schüler H, Nyakern M, Schutt CE, Lindberg U and Karlssoon R (2000) Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin. Eur. J. Biochem. 267: 4054-4062
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4054-4062
    • Schüler, H.1    Nyakern, M.2    Schutt, C.E.3    Lindberg, U.4    Karlssoon, R.5
  • 50
    • 0038297002 scopus 로고    scopus 로고
    • The late increase in intracellular free radical oxygen species during apoptosis is associated with cytochrome c release, caspase activation, and mitochondrial dysfunction
    • Chen Q, Chai Y-C, Mazumder S, Jiang C, Macklis RM, Chisolm GM and Almasan A (2003) The late increase in intracellular free radical oxygen species during apoptosis is associated with cytochrome c release, caspase activation, and mitochondrial dysfunction. Cell Death Differ. 10: 323-334
    • (2003) Cell Death Differ. , vol.10 , pp. 323-334
    • Chen, Q.1    Chai, Y.-C.2    Mazumder, S.3    Jiang, C.4    Macklis, R.M.5    Chisolm, G.M.6    Almasan, A.7
  • 51
    • 0022481601 scopus 로고
    • Flow-cytometric determination of glutathione alterations in vital cells by o-phthadialdehyde (OPT) staining
    • Treumer J and Valet G (1986) Flow-cytometric determination of glutathione alterations in vital cells by o-phthadialdehyde (OPT) staining. Exp. Cell Res. 163: 518-524
    • (1986) Exp. Cell Res. , vol.163 , pp. 518-524
    • Treumer, J.1    Valet, G.2
  • 52
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 53
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale
    • Bjellqvist B, Pasquali C, Ravier F, Sanchez JC and Hochstrasser DF (1993) A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis 14: 1357-1365
    • (1993) Electrophoresis , vol.14 , pp. 1357-1365
    • Bjellqvist, B.1    Pasquali, C.2    Ravier, F.3    Sanchez, J.C.4    Hochstrasser, D.F.5
  • 54
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg A, Postel W and Gunther S (1988) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9: 531-546
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 56
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley BR, Kirsch DR and Morris R (1981) A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 106: 361-363
    • (1981) Anal. Biochem. , vol.106 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, R.3
  • 57
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehlin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 59
    • 0028983813 scopus 로고
    • Improvement of an 'In-Gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman U, Wernstedt C, Gonez J and Heldin CH (1995) Improvement of an 'In-Gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224: 451-455
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 60
    • 0039846981 scopus 로고    scopus 로고
    • Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor
    • Soskic V, Gorlach M, Poznanovic S, Boehmer FD and Godovac-Zimmermann J (1999) Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor. Biochemistry 38: 1757-1764
    • (1999) Biochemistry , vol.38 , pp. 1757-1764
    • Soskic, V.1    Gorlach, M.2    Poznanovic, S.3    Boehmer, F.D.4    Godovac-Zimmermann, J.5


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