메뉴 건너뛰기




Volumn 80, Issue 4, 2010, Pages 540-547

A toxicoproteomic study on cardioprotective effects of pre-administration of docetaxel in a mouse model of adriamycin-induced cardiotoxicity

Author keywords

Adriamycin induced cardiotoxicity; Docetaxel pre administration; Fluorogenic derivatization liquid chromatography tandem mass spectrometry; Toxicoproteomics

Indexed keywords

ACONITATE HYDRATASE; ACONITATE HYDRATASE 2; CREATINE KINASE; DIAZEPAM BINDING INHIBITOR; DOCETAXEL; DOXORUBICIN; ELECTRON TRANSFERRING FLAVOPROTEIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE ISOENZYME; LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASE ISOENZYME 5; SODIUM CHLORIDE; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG;

EID: 77953915996     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.04.037     Document Type: Article
Times cited : (17)

References (60)
  • 1
    • 0021878134 scopus 로고
    • Early and delayed clinical cardiotoxicity of doxorubicin
    • Buzdar A.U., Marcus C., Smith T.L., Blumenschein G.R. Early and delayed clinical cardiotoxicity of doxorubicin. Cancer 1985, 55:2761-2765.
    • (1985) Cancer , vol.55 , pp. 2761-2765
    • Buzdar, A.U.1    Marcus, C.2    Smith, T.L.3    Blumenschein, G.R.4
  • 2
    • 27244438750 scopus 로고    scopus 로고
    • Phase II to III study comparing doxorubicin and docetaxel with fluorouracil, doxorubicin, and cyclophosphamide as first-line chemotherapy in patients with metastatic breast cancer: results of a Dutch community setting trial for the clinical trial group of the comprehensive cancer center
    • Bontenbal M., Creemers G.-J., Braun H.J., de Boer A.C., Janssen J.Th, Leys R.B., et al. Phase II to III study comparing doxorubicin and docetaxel with fluorouracil, doxorubicin, and cyclophosphamide as first-line chemotherapy in patients with metastatic breast cancer: results of a Dutch community setting trial for the clinical trial group of the comprehensive cancer center. J Clin Oncol 2005, 23:7081-7088.
    • (2005) J Clin Oncol , vol.23 , pp. 7081-7088
    • Bontenbal, M.1    Creemers, G.-J.2    Braun, H.J.3    de Boer, A.C.4    Janssen, J.5    Leys, R.B.6
  • 3
    • 0037445247 scopus 로고    scopus 로고
    • Docetaxel and doxorubicin compared with doxorubicin and cyclophosphamide as first-line chemotherapy for metastatic breast cancer: results of a randomized, multicenter, phase III trial
    • Nabholtz J.M., Falkson C., Campos D., Szanto J., Martin M., Chan S., et al. Docetaxel and doxorubicin compared with doxorubicin and cyclophosphamide as first-line chemotherapy for metastatic breast cancer: results of a randomized, multicenter, phase III trial. J Clin Oncol 2003, 21:968-975.
    • (2003) J Clin Oncol , vol.21 , pp. 968-975
    • Nabholtz, J.M.1    Falkson, C.2    Campos, D.3    Szanto, J.4    Martin, M.5    Chan, S.6
  • 4
    • 6344280155 scopus 로고    scopus 로고
    • Long-survival in responding patients with metastatic breast cancer treated with doxorubicin-docetaxel combination. A multicenter phase II trial
    • Mattioli R., Lippe P., Massacesi C., Cappelletti C., Nacciarriti D., Bisonni R., et al. Long-survival in responding patients with metastatic breast cancer treated with doxorubicin-docetaxel combination. A multicenter phase II trial. Anticancer Res 2004, 24:3257-3262.
    • (2004) Anticancer Res , vol.24 , pp. 3257-3262
    • Mattioli, R.1    Lippe, P.2    Massacesi, C.3    Cappelletti, C.4    Nacciarriti, D.5    Bisonni, R.6
  • 5
    • 0041055512 scopus 로고    scopus 로고
    • Randomized multicenter trial of chronotherapy with oxaliplatin, fluorouracil, and folic acid in metastatic colorectal cancer. International Organization for Cancer Chronotherapy
    • Lévi F., Zidani R., Misset J. Randomized multicenter trial of chronotherapy with oxaliplatin, fluorouracil, and folic acid in metastatic colorectal cancer. International Organization for Cancer Chronotherapy. Lancet 1997, 350:681-686.
    • (1997) Lancet , vol.350 , pp. 681-686
    • Lévi, F.1    Zidani, R.2    Misset, J.3
  • 7
    • 17744399916 scopus 로고    scopus 로고
    • Time-dependent nephrotoxicity associated with daily administration of cisplatin in mice
    • To H., Kikuchi A., Tsuruoka S., Sugimoto K., Fujimura A., Higuchi S., et al. Time-dependent nephrotoxicity associated with daily administration of cisplatin in mice. J Pharm Pharmacol 2000, 52:1499-1504.
    • (2000) J Pharm Pharmacol , vol.52 , pp. 1499-1504
    • To, H.1    Kikuchi, A.2    Tsuruoka, S.3    Sugimoto, K.4    Fujimura, A.5    Higuchi, S.6
  • 8
    • 0021956173 scopus 로고
    • Circadian timing of cancer chemotherapy
    • Hrushesky W.J. Circadian timing of cancer chemotherapy. Science 1985, 228:73-75.
    • (1985) Science , vol.228 , pp. 73-75
    • Hrushesky, W.J.1
  • 10
    • 0037530384 scopus 로고    scopus 로고
    • Dosing-time dependency of adriamycin-induced cardiotoxicity and bone marrow toxicity in rats
    • To H., Ohdo S., Shin M., Uchimaru H., Yukawa E., Higuchi S., et al. Dosing-time dependency of adriamycin-induced cardiotoxicity and bone marrow toxicity in rats. J Pharm Pharmacol 2003, 55:803-810.
    • (2003) J Pharm Pharmacol , vol.55 , pp. 803-810
    • To, H.1    Ohdo, S.2    Shin, M.3    Uchimaru, H.4    Yukawa, E.5    Higuchi, S.6
  • 11
    • 0019120975 scopus 로고
    • Synthetic adrenocorticotropin for optimizing murine circadian chronotolerance for adriamycin
    • Lévi F., Halberg F., Haus E. Synthetic adrenocorticotropin for optimizing murine circadian chronotolerance for adriamycin. Chronobiologia 1980, 7:227-244.
    • (1980) Chronobiologia , vol.7 , pp. 227-244
    • Lévi, F.1    Halberg, F.2    Haus, E.3
  • 12
    • 0018855928 scopus 로고
    • Circadian bioperiodic response of mice bearing advanced L1210 leukemia to combination therapy with adriamycin and cyclophosphamide
    • Scheving L.E., Burns E.R., Pauly J.E., Halberg F. Circadian bioperiodic response of mice bearing advanced L1210 leukemia to combination therapy with adriamycin and cyclophosphamide. Cancer Res 1980, 40:1511-1515.
    • (1980) Cancer Res , vol.40 , pp. 1511-1515
    • Scheving, L.E.1    Burns, E.R.2    Pauly, J.E.3    Halberg, F.4
  • 13
    • 0027138165 scopus 로고
    • Circadian-timed combination doxorubicin-cisplatin chemotherapy for advanced endometrial carcinoma. A phase II study of the Gynecologic Oncology Group
    • Barrett R.J., Blessing J.A., Homesley H.D., Twiggs L., Webster K.D. Circadian-timed combination doxorubicin-cisplatin chemotherapy for advanced endometrial carcinoma. A phase II study of the Gynecologic Oncology Group. Am J Clin Oncol 1993, 16:494-496.
    • (1993) Am J Clin Oncol , vol.16 , pp. 494-496
    • Barrett, R.J.1    Blessing, J.A.2    Homesley, H.D.3    Twiggs, L.4    Webster, K.D.5
  • 14
    • 0842289261 scopus 로고    scopus 로고
    • Influence of dosing schedule on toxicity and antitumor effects of a combination of adriamycin and docetaxel in mice
    • To H., Shin M., Tabuchi M., Sakaguchi H., Takeuchi A., Matsunaga N., et al. Influence of dosing schedule on toxicity and antitumor effects of a combination of adriamycin and docetaxel in mice. Clin Cancer Res 2004, 10:762-769.
    • (2004) Clin Cancer Res , vol.10 , pp. 762-769
    • To, H.1    Shin, M.2    Tabuchi, M.3    Sakaguchi, H.4    Takeuchi, A.5    Matsunaga, N.6
  • 15
    • 24944470170 scopus 로고    scopus 로고
    • Therapeutic index by combination of adriamycin and docetaxel depends on dosing time in mice
    • Tabuchi M., To H., Sakaguchi H., Goto N., Takeuchi A., Higuchi S., et al. Therapeutic index by combination of adriamycin and docetaxel depends on dosing time in mice. Cancer Res 2005, 65:8448-8454.
    • (2005) Cancer Res , vol.65 , pp. 8448-8454
    • Tabuchi, M.1    To, H.2    Sakaguchi, H.3    Goto, N.4    Takeuchi, A.5    Higuchi, S.6
  • 16
  • 17
    • 38349099927 scopus 로고    scopus 로고
    • Toxicoproteomics and its application to human health risk assessment
    • Ge Y., Preston R.J., Owen R.D. Toxicoproteomics and its application to human health risk assessment. Proteomics Clin Appl 2007, 1:1613-1624.
    • (2007) Proteomics Clin Appl , vol.1 , pp. 1613-1624
    • Ge, Y.1    Preston, R.J.2    Owen, R.D.3
  • 18
    • 0036525708 scopus 로고    scopus 로고
    • Toxicoproteomics-a new preclinical tool
    • Bandara L.R., Kennedy S. Toxicoproteomics-a new preclinical tool. Drug Discov Today 2002, 7:411-418.
    • (2002) Drug Discov Today , vol.7 , pp. 411-418
    • Bandara, L.R.1    Kennedy, S.2
  • 19
    • 0043064080 scopus 로고    scopus 로고
    • An identification method for altered proteins in tissues utilizing fluorogenic derivatization, liquid chromatography, tandem mass spectrometry, and a database searching algorithm
    • Toriumi C., Imai K. An identification method for altered proteins in tissues utilizing fluorogenic derivatization, liquid chromatography, tandem mass spectrometry, and a database searching algorithm. Anal Chem 2003, 75:3725-3730.
    • (2003) Anal Chem , vol.75 , pp. 3725-3730
    • Toriumi, C.1    Imai, K.2
  • 20
    • 0842305702 scopus 로고    scopus 로고
    • Fluorogenic derivatization reagents suitable for isolation and identification of cystein-containing proteins utilizing high-performance liquid chromatography-tandem mass spectrometry
    • Masuda M., Toriumi C., Santa T., Imai K. Fluorogenic derivatization reagents suitable for isolation and identification of cystein-containing proteins utilizing high-performance liquid chromatography-tandem mass spectrometry. Anal Chem 2004, 76:728-735.
    • (2004) Anal Chem , vol.76 , pp. 728-735
    • Masuda, M.1    Toriumi, C.2    Santa, T.3    Imai, K.4
  • 21
    • 24944486228 scopus 로고    scopus 로고
    • An improved method for proteomic studies on C. elegans by fluorogenic derivatization, HPLC isolation, enzymatic digestion, and liquid chromatography-tandem mass spectrometric identification
    • Masuda M., Saimaru H., Takamura N., Imai K. An improved method for proteomic studies on C. elegans by fluorogenic derivatization, HPLC isolation, enzymatic digestion, and liquid chromatography-tandem mass spectrometric identification. Biomed Chromatogr 2005, 19:556-560.
    • (2005) Biomed Chromatogr , vol.19 , pp. 556-560
    • Masuda, M.1    Saimaru, H.2    Takamura, N.3    Imai, K.4
  • 22
    • 41549097831 scopus 로고    scopus 로고
    • Proteomics of Caenorhabditis elegans over-expressing human alpha-synuclein analyzed by fluorogenic derivatization-liquid chromatography/tandem mass spectrometry: identification of Actin and several ribosomal proteins as negative markers at early Parkinson's disease stages
    • Ichibangase T., Saimaru H., Takamura N., Kuwahara T., Koyama A., Iwatsubo T., et al. Proteomics of Caenorhabditis elegans over-expressing human alpha-synuclein analyzed by fluorogenic derivatization-liquid chromatography/tandem mass spectrometry: identification of Actin and several ribosomal proteins as negative markers at early Parkinson's disease stages. Biomed Chromatogr 2008, 22:232-234.
    • (2008) Biomed Chromatogr , vol.22 , pp. 232-234
    • Ichibangase, T.1    Saimaru, H.2    Takamura, N.3    Kuwahara, T.4    Koyama, A.5    Iwatsubo, T.6
  • 23
    • 34547149582 scopus 로고    scopus 로고
    • A proteomic method revealing disease-related proteins in livers of hepatitis-infected mouse model
    • Ichibangase T., Moriya K., Koike K., Imai K. A proteomic method revealing disease-related proteins in livers of hepatitis-infected mouse model. J Proteome Res 2007, 6:2841-2849.
    • (2007) J Proteome Res , vol.6 , pp. 2841-2849
    • Ichibangase, T.1    Moriya, K.2    Koike, K.3    Imai, K.4
  • 24
    • 65249187816 scopus 로고    scopus 로고
    • A proteomics study on human breast cancer cell lines by fluorogenic derivatization-liquid chromatography-tandem mass spectrometry
    • Imai K., Ichibangase T., Saitoh R., Horikawa Y. A proteomics study on human breast cancer cell lines by fluorogenic derivatization-liquid chromatography-tandem mass spectrometry. Biomed Chromatogr 2008, 22:1304-1314.
    • (2008) Biomed Chromatogr , vol.22 , pp. 1304-1314
    • Imai, K.1    Ichibangase, T.2    Saitoh, R.3    Horikawa, Y.4
  • 25
    • 53049092110 scopus 로고    scopus 로고
    • Application of an improved proteomics method, fluorogenic derivatization-liquid chromatography-tandem mass spectrometry, to differential analysis of proteins in small regions of mouse brain
    • Asamoto H., Ichibangase T., Uchikuro K., Imai K. Application of an improved proteomics method, fluorogenic derivatization-liquid chromatography-tandem mass spectrometry, to differential analysis of proteins in small regions of mouse brain. J Chromatogr A 2008, 1208:147-155.
    • (2008) J Chromatogr A , vol.1208 , pp. 147-155
    • Asamoto, H.1    Ichibangase, T.2    Uchikuro, K.3    Imai, K.4
  • 26
    • 65249112183 scopus 로고    scopus 로고
    • Application of fluorogenic derivatization-liquid chromatography-tandem mass spectrometric proteome method to skeletal muscle proteins in fast thoroughbred horses
    • Ichibangase T., Imai K. Application of fluorogenic derivatization-liquid chromatography-tandem mass spectrometric proteome method to skeletal muscle proteins in fast thoroughbred horses. J Proteome Res 2009, 8:2129-2134.
    • (2009) J Proteome Res , vol.8 , pp. 2129-2134
    • Ichibangase, T.1    Imai, K.2
  • 27
    • 8144229686 scopus 로고    scopus 로고
    • Modulation of doxorubicin-induced cardiac dysfunction in toll-like receptor-2-knockout mice
    • Nozaki N., Shishido T., Takeishi Y., Kubota I. Modulation of doxorubicin-induced cardiac dysfunction in toll-like receptor-2-knockout mice. Circulation 2004, 110:2869-2874.
    • (2004) Circulation , vol.110 , pp. 2869-2874
    • Nozaki, N.1    Shishido, T.2    Takeishi, Y.3    Kubota, I.4
  • 28
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • Wu W.W., Wang G., Baek S.J., Shen R.F. Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF. J Proteome Res 2006, 5:651-658.
    • (2006) J Proteome Res , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3    Shen, R.F.4
  • 29
    • 33745700428 scopus 로고    scopus 로고
    • Utility of cleavable isotope-coated affinity-tagged reagents for quantification of low-copy proteins induced by methylprednisolone using liquid chromatography/tandem mass spectrometry
    • Qu J., Jusko W.J., Straubinger R.M. Utility of cleavable isotope-coated affinity-tagged reagents for quantification of low-copy proteins induced by methylprednisolone using liquid chromatography/tandem mass spectrometry. Anal Chem 2006, 78:4543-4552.
    • (2006) Anal Chem , vol.78 , pp. 4543-4552
    • Qu, J.1    Jusko, W.J.2    Straubinger, R.M.3
  • 30
    • 0033861403 scopus 로고    scopus 로고
    • Relationship between the occurrence of cystein in proteins and the complexity of organism
    • Miseta A., Csutora P. Relationship between the occurrence of cystein in proteins and the complexity of organism. Mol Biol Evol 2000, 17:1232-1239.
    • (2000) Mol Biol Evol , vol.17 , pp. 1232-1239
    • Miseta, A.1    Csutora, P.2
  • 31
    • 21144438395 scopus 로고    scopus 로고
    • Proteomic identification of potential susceptibility factors in drug-induced liver disease
    • Welch K.D., Wen B., Goodlett D.R., Yi E., Lee H., Reilly T., et al. Proteomic identification of potential susceptibility factors in drug-induced liver disease. Chem Res Toxicol 2005, 18:924-933.
    • (2005) Chem Res Toxicol , vol.18 , pp. 924-933
    • Welch, K.D.1    Wen, B.2    Goodlett, D.R.3    Yi, E.4    Lee, H.5    Reilly, T.6
  • 32
    • 33745600548 scopus 로고    scopus 로고
    • Warm ischemia-induced alterations in oxidative and inflammatory proteins in hepatic kupffer cells in rats
    • Hirsch J., Hansen K.C., Choi S., Noh J., Hirose R., Roberts J., et al. Warm ischemia-induced alterations in oxidative and inflammatory proteins in hepatic kupffer cells in rats. Mol Cell Protemics 2006, 5:979-986.
    • (2006) Mol Cell Protemics , vol.5 , pp. 979-986
    • Hirsch, J.1    Hansen, K.C.2    Choi, S.3    Noh, J.4    Hirose, R.5    Roberts, J.6
  • 33
    • 36148985677 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiotoxicity: direct correlation of cardiac fibroblast and H9c2 cell survival and aconitase activity with heat shock protein 27
    • Turakhia S., Venkatakrishnan C.D., Dunsmore K., Wong H., Kuppusamy P., Zweier J.L., et al. Doxorubicin-induced cardiotoxicity: direct correlation of cardiac fibroblast and H9c2 cell survival and aconitase activity with heat shock protein 27. Am J Physiol Heart Circ Physiol 2007, 293:3111-3121.
    • (2007) Am J Physiol Heart Circ Physiol , vol.293 , pp. 3111-3121
    • Turakhia, S.1    Venkatakrishnan, C.D.2    Dunsmore, K.3    Wong, H.4    Kuppusamy, P.5    Zweier, J.L.6
  • 34
    • 10744224134 scopus 로고    scopus 로고
    • Chronic cardiotoxicity of anticancer anthracyclines in the rat: role of secondary metabolites and reduced toxicity by a novel anthracycline with impaired metabolite formation and reactivity
    • Sacco G., Giampietro R., Salvatorelli E., Menna P., Bertani N., Graiani G., et al. Chronic cardiotoxicity of anticancer anthracyclines in the rat: role of secondary metabolites and reduced toxicity by a novel anthracycline with impaired metabolite formation and reactivity. Br J Pharmacol 2003, 139:641-651.
    • (2003) Br J Pharmacol , vol.139 , pp. 641-651
    • Sacco, G.1    Giampietro, R.2    Salvatorelli, E.3    Menna, P.4    Bertani, N.5    Graiani, G.6
  • 36
    • 3342967512 scopus 로고    scopus 로고
    • Is the failing heart energy starved? On using chemical energy to support cardiac function
    • Ingwall J.S., Weiss R.G. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ Res 2004, 95:135-146.
    • (2004) Circ Res , vol.95 , pp. 135-146
    • Ingwall, J.S.1    Weiss, R.G.2
  • 38
    • 0043237846 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiac mitochondrionopathy
    • Wallace K.B. Doxorubicin-induced cardiac mitochondrionopathy. Pharmacol Toxicol 2003, 93:105-115.
    • (2003) Pharmacol Toxicol , vol.93 , pp. 105-115
    • Wallace, K.B.1
  • 39
    • 0031047983 scopus 로고    scopus 로고
    • Molecular mechanisms of doxorubicin-induced cardiomyopathy
    • Jeyaseelan R., Poizat C., Wu H.Y., Kedes L. Molecular mechanisms of doxorubicin-induced cardiomyopathy. J Biol Chem 1997, 272:5828-5832.
    • (1997) J Biol Chem , vol.272 , pp. 5828-5832
    • Jeyaseelan, R.1    Poizat, C.2    Wu, H.Y.3    Kedes, L.4
  • 40
    • 0035881024 scopus 로고    scopus 로고
    • Interference with calcium-dependent mitochondrial bioenergetics in cardiac myocytes isolated from doxorubicin-treated rats
    • Zhou S., Heller L.J., Wallace K.B. Interference with calcium-dependent mitochondrial bioenergetics in cardiac myocytes isolated from doxorubicin-treated rats. Toxicol Appl Pharmacol 2001, 175:60-67.
    • (2001) Toxicol Appl Pharmacol , vol.175 , pp. 60-67
    • Zhou, S.1    Heller, L.J.2    Wallace, K.B.3
  • 41
    • 33947354960 scopus 로고    scopus 로고
    • Anti-inflammatory agents and mono HER protect against DOX-induced cardiotoxicity and accumulation of CML in mice
    • Bruynzeel A., Abou El Hassan M.A., Schalkwijk C., Berkhof J., Bast A., Niessen H.W.M., et al. Anti-inflammatory agents and mono HER protect against DOX-induced cardiotoxicity and accumulation of CML in mice. Br J Cancer 2007, 96:937-943.
    • (2007) Br J Cancer , vol.96 , pp. 937-943
    • Bruynzeel, A.1    Abou El Hassan, M.A.2    Schalkwijk, C.3    Berkhof, J.4    Bast, A.5    Niessen, H.W.M.6
  • 42
    • 58349097915 scopus 로고    scopus 로고
    • Pretreatment with statin attenuates the cardiotoxicity of doxorubicin in mice
    • Riad A., Bien S., Westermann D., Becher P.M., Loya K., Landmesser U., et al. Pretreatment with statin attenuates the cardiotoxicity of doxorubicin in mice. Cancer Res 2009, 69:695-699.
    • (2009) Cancer Res , vol.69 , pp. 695-699
    • Riad, A.1    Bien, S.2    Westermann, D.3    Becher, P.M.4    Loya, K.5    Landmesser, U.6
  • 43
    • 0034320533 scopus 로고    scopus 로고
    • Myocardial high-energy phosphate metabolism is altered after treatment with anthracycline in childhood
    • Eidenschink A.B., Schroter G., Muller-Weihrich S., Stern H. Myocardial high-energy phosphate metabolism is altered after treatment with anthracycline in childhood. Cardiol Young 2000, 10:610-617.
    • (2000) Cardiol Young , vol.10 , pp. 610-617
    • Eidenschink, A.B.1    Schroter, G.2    Muller-Weihrich, S.3    Stern, H.4
  • 45
    • 70349330689 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase depletion induces cell cycle arrest and resistance to antimetabolites in human carcinoma cell lines
    • Phadke M.S., Krynetskaia N.F., Mishra A.K., Krynetskiy E. Glyceraldehyde 3-phosphate dehydrogenase depletion induces cell cycle arrest and resistance to antimetabolites in human carcinoma cell lines. J Pharmacol Exp Ther 2009, 331:77-86.
    • (2009) J Pharmacol Exp Ther , vol.331 , pp. 77-86
    • Phadke, M.S.1    Krynetskaia, N.F.2    Mishra, A.K.3    Krynetskiy, E.4
  • 46
    • 0031983180 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is regulated on a daily basis by the circadian clock
    • Shinohara M.L., Loros J.J., Dunlap J.C. Glyceraldehyde-3-phosphate dehydrogenase is regulated on a daily basis by the circadian clock. J Biol Chem 1998, 273:446-452.
    • (1998) J Biol Chem , vol.273 , pp. 446-452
    • Shinohara, M.L.1    Loros, J.J.2    Dunlap, J.C.3
  • 47
    • 0037454697 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase activity as an independent modifier of methylglyoxal levels in diabetes
    • Beisswenger P.J., Howell S.K., Smith K., Szwergold B.S. Glyceraldehyde-3-phosphate dehydrogenase activity as an independent modifier of methylglyoxal levels in diabetes. Biochim Biophys Acta Mol Basis Dis 2003, 1637:98-106.
    • (2003) Biochim Biophys Acta Mol Basis Dis , vol.1637 , pp. 98-106
    • Beisswenger, P.J.1    Howell, S.K.2    Smith, K.3    Szwergold, B.S.4
  • 48
    • 33644633955 scopus 로고    scopus 로고
    • The anti-cancer drug, doxorubicin, causes oxidant stress-induced endothelial dysfunction
    • Wolf M.B., Baynes J.W. The anti-cancer drug, doxorubicin, causes oxidant stress-induced endothelial dysfunction. Biochim Biophys Acta 2006, 1760:267-271.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 267-271
    • Wolf, M.B.1    Baynes, J.W.2
  • 49
    • 37549039041 scopus 로고    scopus 로고
    • Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase
    • Baek D., Jin Y., Jeong J.C., Lee H.J., Moon H., Lee J., et al. Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase. Phytochemstry 2008, 69:333-338.
    • (2008) Phytochemstry , vol.69 , pp. 333-338
    • Baek, D.1    Jin, Y.2    Jeong, J.C.3    Lee, H.J.4    Moon, H.5    Lee, J.6
  • 50
    • 0842313320 scopus 로고    scopus 로고
    • Mammalian Bax inhibitor-1 suppressing Bax-, hydrogen peroxide-, and salicylic acid-induced cell death
    • Kawai-Yamada M., Jin L., Yoshinaga K., Hirata A., Uchimiya H. Mammalian Bax inhibitor-1 suppressing Bax-, hydrogen peroxide-, and salicylic acid-induced cell death. Plant Cell 2004, 16:21-32.
    • (2004) Plant Cell , vol.16 , pp. 21-32
    • Kawai-Yamada, M.1    Jin, L.2    Yoshinaga, K.3    Hirata, A.4    Uchimiya, H.5
  • 51
    • 23844452781 scopus 로고    scopus 로고
    • New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover M.A. New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J Cell Biochem 2005, 95:45-52.
    • (2005) J Cell Biochem , vol.95 , pp. 45-52
    • Sirover, M.A.1
  • 52
    • 34249279169 scopus 로고    scopus 로고
    • GAPDH and autophagy preserve survival after apoptoic cytochrome c release in the absence of caspase activation
    • Colell A., Ricci J.E., Tait S., Milasta S., Maurer U., Bouchier-Hayes L., et al. GAPDH and autophagy preserve survival after apoptoic cytochrome c release in the absence of caspase activation. Cell 2007, 129:983-997.
    • (2007) Cell , vol.129 , pp. 983-997
    • Colell, A.1    Ricci, J.E.2    Tait, S.3    Milasta, S.4    Maurer, U.5    Bouchier-Hayes, L.6
  • 53
    • 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
    • Zhang L., Roeder R.G., Luo Y. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 2003, 114:255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zhang, L.1    Roeder, R.G.2    Luo, Y.3
  • 54
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptoic cell death by nuclear translocation following Siah1 binding
    • Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y., et al. S-nitrosylated GAPDH initiates apoptoic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 2005, 7:665-674.
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5    Ozeki, Y.6
  • 56
    • 33749049359 scopus 로고    scopus 로고
    • Redox proteomic identification of oxidized cardiac proteins in adriamycin-treated mice
    • Chen Y., Daosukho C., Opii W.O., Turner D.M., Pierce W.M., Klein J.B., et al. Redox proteomic identification of oxidized cardiac proteins in adriamycin-treated mice. Free Radic Biol Med 2006, 41:1470-1477.
    • (2006) Free Radic Biol Med , vol.41 , pp. 1470-1477
    • Chen, Y.1    Daosukho, C.2    Opii, W.O.3    Turner, D.M.4    Pierce, W.M.5    Klein, J.B.6
  • 57
    • 27744494443 scopus 로고    scopus 로고
    • Modulation of cytochrome c oxidase-Va is possibly involved in metallothionein protection from doxorubicin cardiotoxicity
    • Merten K.E., Feng W., Zhang L., Pierce W., Cai J., Klein J.B., et al. Modulation of cytochrome c oxidase-Va is possibly involved in metallothionein protection from doxorubicin cardiotoxicity. J Pharmacol Exp Ther 2005, 315:1314-1319.
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 1314-1319
    • Merten, K.E.1    Feng, W.2    Zhang, L.3    Pierce, W.4    Cai, J.5    Klein, J.B.6
  • 58
    • 0029781555 scopus 로고    scopus 로고
    • The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice
    • Yen H.C., Oberley T.D., Vichitbandha S., Ho Y.S., Clair DKSt. The protective role of manganese superoxide dismutase against adriamycin-induced acute cardiac toxicity in transgenic mice. J Clin Invest 1996, 98:1253-1260.
    • (1996) J Clin Invest , vol.98 , pp. 1253-1260
    • Yen, H.C.1    Oberley, T.D.2    Vichitbandha, S.3    Ho, Y.S.4    Clair, D.5
  • 59
    • 0036153830 scopus 로고    scopus 로고
    • Inhibition of doxorubicin chronic toxicity in catalase-overexpressing transgenic mouse heart
    • Kang Y.J., Sun X.H., Chen Y., Zhou Z.X. Inhibition of doxorubicin chronic toxicity in catalase-overexpressing transgenic mouse heart. Chem Res Toxicol 2002, 15:1-6.
    • (2002) Chem Res Toxicol , vol.15 , pp. 1-6
    • Kang, Y.J.1    Sun, X.H.2    Chen, Y.3    Zhou, Z.X.4
  • 60
    • 0035931561 scopus 로고    scopus 로고
    • + analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase
    • + analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase. Bioorg Med Chem Lett 2001, 11:95-98.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 95-98
    • Kennedy, K.J.1    Bressi, J.C.2    Gelb, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.