메뉴 건너뛰기




Volumn , Issue , 2014, Pages

Methyl jasmonate: Putative mechanisms of action on cancer cells cycle, metabolism, and apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

5 HYDROXYICOSATETRAENOIC ACID; ADENOSINE TRIPHOSPHATE; ALDO KETO REDUCTASE 1; ANTINEOPLASTIC AGENT; ARACHIDONATE 5 LIPOXYGENASE; CYTOCHROME C; HEXOKINASE; JASMONIC ACID METHYL ESTER; OXIDOREDUCTASE; PROTEIN P53; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84896852880     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2014/572097     Document Type: Review
Times cited : (79)

References (256)
  • 1
    • 33750996156 scopus 로고    scopus 로고
    • Pathway-specific differences between tumor cell lines and normal and tumor tissue cells
    • 2-s2.0-33750996156 10.1186/1476-4598-5-55
    • Ertel A., Verghese A., Byers S. W., Ochs M., Tozeren A., Pathway-specific differences between tumor cell lines and normal and tumor tissue cells. Molecular Cancer 2006 5, article 55 2-s2.0-33750996156 10.1186/1476-4598-5-55
    • (2006) Molecular Cancer , vol.555
    • Ertel, A.1    Verghese, A.2    Byers, S.W.3    Ochs, M.4    Tozeren, A.5
  • 3
    • 0037204996 scopus 로고    scopus 로고
    • The Jasmonate pathway
    • 2-s2.0-0037204996 10.1126/science.1071547
    • Liechti R., Farmer E. E., The Jasmonate pathway. Science 2002 296 5573 1649 1650 2-s2.0-0037204996 10.1126/science.1071547
    • (2002) Science , vol.296 , Issue.5573 , pp. 1649-1650
    • Liechti, R.1    Farmer, E.E.2
  • 4
    • 0036581314 scopus 로고    scopus 로고
    • Fatty acid-derived signals in plants
    • 2-s2.0-0036581314 10.1016/S1360-1385(02)02250-1
    • Weber H., Fatty acid-derived signals in plants. Trends in Plant Science 2002 7 5 217 224 2-s2.0-0036581314 10.1016/S1360-1385(02)02250-1
    • (2002) Trends in Plant Science , vol.7 , Issue.5 , pp. 217-224
    • Weber, H.1
  • 6
    • 0001596943 scopus 로고
    • The biochemistry and the physiological and molecular actions of jasmonates
    • 2-s2.0-0001596943
    • Sembdner G., Parthier B., The biochemistry and the physiological and molecular actions of jasmonates. Annual Review of Plant Physiology and Plant Molecular Biology 1993 44 1 569 589 2-s2.0-0001596943
    • (1993) Annual Review of Plant Physiology and Plant Molecular Biology , vol.44 , Issue.1 , pp. 569-589
    • Sembdner, G.1    Parthier, B.2
  • 8
    • 11944254202 scopus 로고
    • Interplant communication: Airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves
    • 2-s2.0-0025009188
    • Farmer E. E., Ryan C. A., Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proceedings of the National Academy of Sciences of the United States of America 1990 87 19 7713 7716 2-s2.0-0025009188
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.19 , pp. 7713-7716
    • Farmer, E.E.1    Ryan, C.A.2
  • 10
    • 33847749731 scopus 로고    scopus 로고
    • Solar ultraviolet-B radiation and insect herbivory trigger partially overlapping phenolic responses in Nicotiana attenuata and Nicotiana longiflora
    • 2-s2.0-33847749731 10.1093/aob/mcl226
    • Izaguirre M. M., Mazza C. A., Svatoš A., Baldwin I. T., Ballaré C. L., Solar ultraviolet-B radiation and insect herbivory trigger partially overlapping phenolic responses in Nicotiana attenuata and Nicotiana longiflora. Annals of Botany 2007 99 1 103 109 2-s2.0-33847749731 10.1093/aob/mcl226
    • (2007) Annals of Botany , vol.99 , Issue.1 , pp. 103-109
    • Izaguirre, M.M.1    Mazza, C.A.2    Svatoš, A.3    Baldwin, I.T.4    Ballaré, C.L.5
  • 11
    • 44649189101 scopus 로고    scopus 로고
    • Plant behaviour and communication
    • 2-s2.0-44649189101 10.1111/j.1461-0248.2008.01183.x
    • Karban R., Plant behaviour and communication. Ecology Letters 2008 11 7 727 739 2-s2.0-44649189101 10.1111/j.1461-0248.2008.01183.x
    • (2008) Ecology Letters , vol.11 , Issue.7 , pp. 727-739
    • Karban, R.1
  • 13
    • 0032709341 scopus 로고    scopus 로고
    • Ultraviolet-B-induced stress and changes in gene expression in Arabidopsis thaliana: Role of signalling pathways controlled by jasmonic acid, ethylene and reactive oxygen species
    • 2-s2.0-0032709341 10.1046/j.1365-3040.1999.00499.x
    • A.-H.-Mackerness S., Surplus S. L., Blake P., John C. F., Buchanan-Wollaston V., Jordan B. R., Thomas B., Ultraviolet-B-induced stress and changes in gene expression in Arabidopsis thaliana: role of signalling pathways controlled by jasmonic acid, ethylene and reactive oxygen species. Plant, Cell & Environment 1999 22 11 1413 1423 2-s2.0-0032709341 10.1046/j.1365-3040. 1999.00499.x
    • (1999) Plant, Cell & Environment , vol.22 , Issue.11 , pp. 1413-1423
    • Mackerness, S.A.H.1    Surplus, S.L.2    Blake, P.3    John, C.F.4    Buchanan-Wollaston, V.5    Jordan, B.R.6    Thomas, B.7
  • 14
    • 47249114779 scopus 로고    scopus 로고
    • Methyl jasmonate induces production of reactive oxygen species and alterations in mitochondrial dynamics that precede photosynthetic dysfunction and subsequent cell death
    • 2-s2.0-47249114779 10.1093/pcp/pcn086
    • Zhang L., Xing D., Methyl jasmonate induces production of reactive oxygen species and alterations in mitochondrial dynamics that precede photosynthetic dysfunction and subsequent cell death. Plant and Cell Physiology 2008 49 7 1092 1111 2-s2.0-47249114779 10.1093/pcp/pcn086
    • (2008) Plant and Cell Physiology , vol.49 , Issue.7 , pp. 1092-1111
    • Zhang, L.1    Xing, D.2
  • 15
    • 0036240569 scopus 로고    scopus 로고
    • Plant stress hormones suppress the proliferation and induce apoptosis in human cancer cells
    • 2-s2.0-0036240569 10.1038/sj/leu/2402419
    • Fingrut O., Flescher E., Plant stress hormones suppress the proliferation and induce apoptosis in human cancer cells. Leukemia 2002 16 4 608 616 2-s2.0-0036240569 10.1038/sj/leu/2402419
    • (2002) Leukemia , vol.16 , Issue.4 , pp. 608-616
    • Fingrut, O.1    Flescher, E.2
  • 16
    • 26244458767 scopus 로고    scopus 로고
    • Jasmonates - A new family of anti-cancer agents
    • 2-s2.0-26244458767 10.1097/01.cad.0000176501.63680.80
    • Flescher E., Jasmonates-a new family of anti-cancer agents. Anti-Cancer Drugs 2005 16 9 911 916 2-s2.0-26244458767 10.1097/01.cad.0000176501.63680.80
    • (2005) Anti-Cancer Drugs , vol.16 , Issue.9 , pp. 911-916
    • Flescher, E.1
  • 17
    • 27744487132 scopus 로고    scopus 로고
    • Jasmonates induce nonapoptotic death in high-resistance mutant p53-expressing B-lymphoma cells
    • 2-s2.0-27744487132 10.1038/sj.bjp.0706394
    • Fingrut O., Reischer D., Rotem R., Goldin N., Altboum I., Zan-Bar I., Flescher E., Jasmonates induce nonapoptotic death in high-resistance mutant p53-expressing B-lymphoma cells. British Journal of Pharmacology 2005 146 6 800 808 2-s2.0-27744487132 10.1038/sj.bjp.0706394
    • (2005) British Journal of Pharmacology , vol.146 , Issue.6 , pp. 800-808
    • Fingrut, O.1    Reischer, D.2    Rotem, R.3    Goldin, N.4    Altboum, I.5    Zan-Bar, I.6    Flescher, E.7
  • 18
    • 0242558937 scopus 로고    scopus 로고
    • The anticancer plant stress-protein methyl jasmonate induces activation of stress-regulated c-Jun N-terminal kinase and p38 protein kinase in human lymphoid cells
    • 2-s2.0-0242558937 10.1038/sj.leu.2403107
    • Rotem R., Fingrut O., Moskovitz J., Flescher E., The anticancer plant stress-protein methyl jasmonate induces activation of stress-regulated c-Jun N-terminal kinase and p38 protein kinase in human lymphoid cells. Leukemia 2003 17 11 2230 2234 2-s2.0-0242558937 10.1038/sj.leu.2403107
    • (2003) Leukemia , vol.17 , Issue.11 , pp. 2230-2234
    • Rotem, R.1    Fingrut, O.2    Moskovitz, J.3    Flescher, E.4
  • 19
    • 33845642967 scopus 로고    scopus 로고
    • Jasmonates in cancer therapy
    • 2-s2.0-33845642967 10.1016/j.canlet.2006.03.001
    • Flescher E., Jasmonates in cancer therapy. Cancer Letters 2007 245 1-2 1 10 2-s2.0-33845642967 10.1016/j.canlet.2006.03.001
    • (2007) Cancer Letters , vol.245 , Issue.1-2 , pp. 1-10
    • Flescher, E.1
  • 20
    • 34249934157 scopus 로고    scopus 로고
    • Mitochondria-mediated ATP depletion by anti-cancer agents of the jasmonate family
    • 2-s2.0-34249934157 10.1007/s10863-006-9061-y
    • Goldin N., Heyfets A., Reischer D., Flescher E., Mitochondria-mediated ATP depletion by anti-cancer agents of the jasmonate family. Journal of Bioenergetics and Biomembranes 2007 39 1 51 57 2-s2.0-34249934157 10.1007/s10863-006-9061-y
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.1 , pp. 51-57
    • Goldin, N.1    Heyfets, A.2    Reischer, D.3    Flescher, E.4
  • 21
    • 70350517590 scopus 로고    scopus 로고
    • Methyl jasmonate: A plant stress hormone as an anti-cancer drug
    • 2-s2.0-70350517590 10.1016/j.phytochem.2009.06.007
    • Cohen S., Flescher E., Methyl jasmonate: a plant stress hormone as an anti-cancer drug. Phytochemistry 2009 70 13-14 1600 1609 2-s2.0-70350517590 10.1016/j.phytochem.2009.06.007
    • (2009) Phytochemistry , vol.70 , Issue.13-14 , pp. 1600-1609
    • Cohen, S.1    Flescher, E.2
  • 23
    • 84875357754 scopus 로고    scopus 로고
    • Combined chemotherapy or biotherapy with jasmonates: Targeting energy metabolism for cancer treatment
    • Elia U., Flescher E., Combined chemotherapy or biotherapy with jasmonates: targeting energy metabolism for cancer treatment. Current Pharmaceutical Biotechnology 2013 14 3 331 341
    • (2013) Current Pharmaceutical Biotechnology , vol.14 , Issue.3 , pp. 331-341
    • Elia, U.1    Flescher, E.2
  • 25
    • 53749090929 scopus 로고    scopus 로고
    • Methyl jasmonate decreases membrane fluidity and induces apoptosis through tumor necrosis factor receptor 1 in breast cancer cells
    • 2-s2.0-53749090929 10.1097/CAD.0b013e32830b5894
    • Yeruva L., Elegbede J. A., Carper S. W., Methyl jasmonate decreases membrane fluidity and induces apoptosis through tumor necrosis factor receptor 1 in breast cancer cells. Anti-Cancer Drugs 2008 19 8 766 776 2-s2.0-53749090929 10.1097/CAD.0b013e32830b5894
    • (2008) Anti-Cancer Drugs , vol.19 , Issue.8 , pp. 766-776
    • Yeruva, L.1    Elegbede, J.A.2    Carper, S.W.3
  • 26
    • 53049089458 scopus 로고    scopus 로고
    • Methyl jasmonate induces cell death with mixed characteristics of apoptosis and necrosis in cervical cancer cells
    • 2-s2.0-53049089458 10.1016/j.canlet.2008.05.031
    • Kniazhanski T., Jackman A., Heyfets A., Gonen P., Flescher E., Sherman L., Methyl jasmonate induces cell death with mixed characteristics of apoptosis and necrosis in cervical cancer cells. Cancer Letters 2008 271 1 34 46 2-s2.0-53049089458 10.1016/j.canlet.2008.05.031
    • (2008) Cancer Letters , vol.271 , Issue.1 , pp. 34-46
    • Kniazhanski, T.1    Jackman, A.2    Heyfets, A.3    Gonen, P.4    Flescher, E.5    Sherman, L.6
  • 27
    • 77956307170 scopus 로고    scopus 로고
    • Apoptotic activity of a new jasmonate analogue is associated with its induction of DNA damage
    • 2-s2.0-77956307170 10.3892/or-00000920
    • Zhao J., Kang S., Zhang X., You S., Park J.-S., Jung J. H., Kim D.-K., Apoptotic activity of a new jasmonate analogue is associated with its induction of DNA damage. Oncology Reports 2010 24 3 771 777 2-s2.0-77956307170 10.3892/or-00000920
    • (2010) Oncology Reports , vol.24 , Issue.3 , pp. 771-777
    • Zhao, J.1    Kang, S.2    Zhang, X.3    You, S.4    Park, J.-S.5    Jung, J.H.6    Kim, D.-K.7
  • 28
    • 84858071650 scopus 로고    scopus 로고
    • Methyl jasmonate reduces the survival of cervical cancer cells and downregulates HPV E6 and E7, and survivin
    • 2-s2.0-84858071650 10.1016/j.canlet.2011.12.028
    • Milrot E., Jackman A., Kniazhanski T., Gonen P., Flescher E., Sherman L., Methyl jasmonate reduces the survival of cervical cancer cells and downregulates HPV E6 and E7, and survivin. Cancer Letters 2012 319 1 31 38 2-s2.0-84858071650 10.1016/j.canlet.2011.12.028
    • (2012) Cancer Letters , vol.319 , Issue.1 , pp. 31-38
    • Milrot, E.1    Jackman, A.2    Kniazhanski, T.3    Gonen, P.4    Flescher, E.5    Sherman, L.6
  • 29
    • 84879552332 scopus 로고    scopus 로고
    • Enhanced killing of cervical cancer cells by combinations of methyl jasmonate with cisplatin, X or alpha radiation
    • Milrot E., Jackman A., Flescher E., Gonen P., Kelson I., Keisari Y., Sherman L., Enhanced killing of cervical cancer cells by combinations of methyl jasmonate with cisplatin, X or alpha radiation. Investigational New Drugs 2013 31 2 333 344
    • (2013) Investigational New Drugs , vol.31 , Issue.2 , pp. 333-344
    • Milrot, E.1    Jackman, A.2    Flescher, E.3    Gonen, P.4    Kelson, I.5    Keisari, Y.6    Sherman, L.7
  • 32
    • 80054022978 scopus 로고    scopus 로고
    • Methyl jasmonate down-regulates survivin expression and sensitizes colon carcinoma cells towards TRAIL-induced cytotoxicity
    • 2-s2.0-80054022978 10.1111/j.1476-5381.2011.01419.x
    • Raviv Z., Zilberberg A., Cohen S., Reischer-Pelech D., Horrix C., Berger M. R., Rosin-Arbesfeld R., Flescher E., Methyl jasmonate down-regulates survivin expression and sensitizes colon carcinoma cells towards TRAIL-induced cytotoxicity. British Journal of Pharmacology 2011 164 5 1433 1444 2-s2.0-80054022978 10.1111/j.1476-5381.2011.01419.x
    • (2011) British Journal of Pharmacology , vol.164 , Issue.5 , pp. 1433-1444
    • Raviv, Z.1    Zilberberg, A.2    Cohen, S.3    Reischer-Pelech, D.4    Horrix, C.5    Berger, M.R.6    Rosin-Arbesfeld, R.7    Flescher, E.8
  • 33
    • 84873447008 scopus 로고    scopus 로고
    • Methyl jasmonate abolishes the migration, invasion and angiogenesis of gastric cancer cells through down-regulation of matrix metalloproteinase 14
    • Zheng L., Li D., Xiang X., Tong L., Qi M., Pu J., Huang K., Tong Q., Methyl jasmonate abolishes the migration, invasion and angiogenesis of gastric cancer cells through down-regulation of matrix metalloproteinase 14. BMC Cancer 2013 13, article 74
    • (2013) BMC Cancer , vol.1374
    • Zheng, L.1    Li, D.2    Xiang, X.3    Tong, L.4    Qi, M.5    Pu, J.6    Huang, K.7    Tong, Q.8
  • 34
    • 77957018959 scopus 로고    scopus 로고
    • A methyl jasmonate derivative, J-7, induces apoptosis in human hepatocarcinoma Hep3B cells in vitro
    • 2-s2.0-77957018959 10.1016/j.tiv.2010.08.001
    • Park C., Jin C.-Y., Kim G.-Y., Cheong J., Jung J. H., Yoo Y. H., Choi Y. H., A methyl jasmonate derivative, J-7, induces apoptosis in human hepatocarcinoma Hep3B cells in vitro. Toxicology in Vitro 2010 24 7 1920 1926 2-s2.0-77957018959 10.1016/j.tiv.2010.08.001
    • (2010) Toxicology in Vitro , vol.24 , Issue.7 , pp. 1920-1926
    • Park, C.1    Jin, C.-Y.2    Kim, G.-Y.3    Cheong, J.4    Jung, J.H.5    Yoo, Y.H.6    Choi, Y.H.7
  • 35
    • 84855353202 scopus 로고    scopus 로고
    • J7, a methyl jasmonate derivative, enhances TRAIL-mediated apoptosis through up-regulation of reactive oxygen species generation in human hepatoma HepG2 cells
    • 2-s2.0-84855353202 10.1016/j.tiv.2011.10.016
    • Park C., Jin C.-Y., Hwang H. J., Kim G.-Y., Jung J. H., Kim W.-J., Yoo Y. H., Choi Y. H., J7, a methyl jasmonate derivative, enhances TRAIL-mediated apoptosis through up-regulation of reactive oxygen species generation in human hepatoma HepG2 cells. Toxicology in Vitro 2012 26 1 86 93 2-s2.0-84855353202 10.1016/j.tiv.2011.10.016
    • (2012) Toxicology in Vitro , vol.26 , Issue.1 , pp. 86-93
    • Park, C.1    Jin, C.-Y.2    Hwang, H.J.3    Kim, G.-Y.4    Jung, J.H.5    Kim, W.-J.6    Yoo, Y.H.7    Choi, Y.H.8
  • 36
    • 16644392664 scopus 로고    scopus 로고
    • Methyl jasmonate induces apoptosis through induction of Bax/Bcl-XS and activation of caspase-3 via ROS production in A549 cells
    • 2-s2.0-16644392664
    • Kim J. H., Lee S. Y., Oh S. Y., Han S. I., Park H. G., Yoo M.-A., Kang H. S., Methyl jasmonate induces apoptosis through induction of Bax/Bcl-XS and activation of caspase-3 via ROS production in A549 cells. Oncology Reports 2004 12 6 1233 1238 2-s2.0-16644392664
    • (2004) Oncology Reports , vol.12 , Issue.6 , pp. 1233-1238
    • Kim, J.H.1    Lee, S.Y.2    Oh, S.Y.3    Han, S.I.4    Park, H.G.5    Yoo, M.-A.6    Kang, H.S.7
  • 37
    • 33845796924 scopus 로고    scopus 로고
    • Jasmonates induce apoptosis and cell cycle arrest in non-small cell lung cancer lines
    • 2-s2.0-33845796924 10.1080/01902140601059604
    • Yeruva L., Pierre K. J., Carper S. W., Elegbede J. A., Toy B. J., Wang R. C., Jasmonates induce apoptosis and cell cycle arrest in non-small cell lung cancer lines. Experimental Lung Research 2006 32 10 499 516 2-s2.0-33845796924 10.1080/01902140601059604
    • (2006) Experimental Lung Research , vol.32 , Issue.10 , pp. 499-516
    • Yeruva, L.1    Pierre, K.J.2    Carper, S.W.3    Elegbede, J.A.4    Toy, B.J.5    Wang, R.C.6
  • 38
    • 16444376422 scopus 로고    scopus 로고
    • Jasmonates: Novel anticancer agents acting directly and selectively on human cancer cell mitochondria
    • 2-s2.0-16444376422 10.1158/0008-5472.CAN-04-3091
    • Rotem R., Heyfets A., Fingrut O., Blickstein D., Shaklai M., Flescher E., Jasmonates: novel anticancer agents acting directly and selectively on human cancer cell mitochondria. Cancer Research 2005 65 5 1984 1993 2-s2.0-16444376422 10.1158/0008-5472.CAN-04-3091
    • (2005) Cancer Research , vol.65 , Issue.5 , pp. 1984-1993
    • Rotem, R.1    Heyfets, A.2    Fingrut, O.3    Blickstein, D.4    Shaklai, M.5    Flescher, E.6
  • 39
    • 33947320591 scopus 로고    scopus 로고
    • Effects of natural and novel synthetic jasmonates in experimental metastatic melanoma
    • 2-s2.0-33947320591 10.1038/sj.bjp.0707146
    • Reischer D., Heyfets A., Shimony S., Nordenberg J., Kashman Y., Flescher E., Effects of natural and novel synthetic jasmonates in experimental metastatic melanoma. British Journal of Pharmacology 2007 150 6 738 749 2-s2.0-33947320591 10.1038/sj.bjp.0707146
    • (2007) British Journal of Pharmacology , vol.150 , Issue.6 , pp. 738-749
    • Reischer, D.1    Heyfets, A.2    Shimony, S.3    Nordenberg, J.4    Kashman, Y.5    Flescher, E.6
  • 41
    • 4344686851 scopus 로고    scopus 로고
    • Induction of differentiation of human myeloid leukemia cells by jasmonates, plant hormones
    • 2-s2.0-4344686851 10.1038/sj.leu.2403421
    • Ishii Y., Kiyota H., Sakai S., Honma Y., Induction of differentiation of human myeloid leukemia cells by jasmonates, plant hormones. Leukemia 2004 18 8 1413 1419 2-s2.0-4344686851 10.1038/sj.leu.2403421
    • (2004) Leukemia , vol.18 , Issue.8 , pp. 1413-1419
    • Ishii, Y.1    Kiyota, H.2    Sakai, S.3    Honma, Y.4
  • 42
    • 64849100788 scopus 로고    scopus 로고
    • Gene expression profiles in differentiating leukemia cells induced by methyl jasmonate are similar to those of cytokinins and methyl jasmonate analogs induce the differentiation of human leukemia cells in primary culture
    • 2-s2.0-64849100788 10.1038/leu.2008.347
    • Tsumura H., Akimoto M., Kiyota H., Ishii Y., Ishikura H., Honma Y., Gene expression profiles in differentiating leukemia cells induced by methyl jasmonate are similar to those of cytokinins and methyl jasmonate analogs induce the differentiation of human leukemia cells in primary culture. Leukemia 2009 23 4 753 760 2-s2.0-64849100788 10.1038/leu.2008.347
    • (2009) Leukemia , vol.23 , Issue.4 , pp. 753-760
    • Tsumura, H.1    Akimoto, M.2    Kiyota, H.3    Ishii, Y.4    Ishikura, H.5    Honma, Y.6
  • 43
    • 49049118474 scopus 로고    scopus 로고
    • Methyl jasmonate induces apoptosis of human neuroblastoma cell line BE(2)-C and its mechanism
    • 2-s2.0-49049118474
    • Jiang G.-S., Tong Q.-S., Zeng F.-Q., Hu B., Zheng L.-D., Cai J.-B., Liu Y., Methyl jasmonate induces apoptosis of human neuroblastoma cell line BE(2)-C and its mechanism. Yaoxue Xuebao 2008 43 6 584 590 2-s2.0-49049118474
    • (2008) Yaoxue Xuebao , vol.43 , Issue.6 , pp. 584-590
    • Jiang, G.-S.1    Tong, Q.-S.2    Zeng, F.-Q.3    Hu, B.4    Zheng, L.-D.5    Cai, J.-B.6    Liu, Y.7
  • 44
    • 65849284657 scopus 로고    scopus 로고
    • Natural jasmonates of different structures suppress the growth of human neuroblastoma cell line SH-SY5Y and its mechanisms
    • 2-s2.0-65849284657 10.1111/j.1745-7254.2008.00814.x
    • Tong Q.-S., Jiang G.-S., Zheng L.-D., Tang S.-T., Cai J.-B., Liu Y., Zeng F.-Q., Dong J.-H., Natural jasmonates of different structures suppress the growth of human neuroblastoma cell line SH-SY5Y and its mechanisms. Acta Pharmacologica Sinica 2008 29 7 861 869 2-s2.0-65849284657 10.1111/j.1745-7254. 2008.00814.x
    • (2008) Acta Pharmacologica Sinica , vol.29 , Issue.7 , pp. 861-869
    • Tong, Q.-S.1    Jiang, G.-S.2    Zheng, L.-D.3    Tang, S.-T.4    Cai, J.-B.5    Liu, Y.6    Zeng, F.-Q.7    Dong, J.-H.8
  • 45
    • 53749096199 scopus 로고    scopus 로고
    • Methyl jasmonate downregulates expression of proliferating cell nuclear antigen and induces apoptosis in human neuroblastoma cell lines
    • 2-s2.0-53749096199 10.1097/CAD.0b013e3282fc46b0
    • Tong Q.-S., Jiang G.-S., Zheng L.-D., Tang S.-T., Cai J.-B., Liu Y., Zeng F.-Q., Dong J.-H., Methyl jasmonate downregulates expression of proliferating cell nuclear antigen and induces apoptosis in human neuroblastoma cell lines. Anti-Cancer Drugs 2008 19 6 573 581 2-s2.0-53749096199 10.1097/CAD. 0b013e3282fc46b0
    • (2008) Anti-Cancer Drugs , vol.19 , Issue.6 , pp. 573-581
    • Tong, Q.-S.1    Jiang, G.-S.2    Zheng, L.-D.3    Tang, S.-T.4    Cai, J.-B.5    Liu, Y.6    Zeng, F.-Q.7    Dong, J.-H.8
  • 47
    • 36148943488 scopus 로고    scopus 로고
    • Methyl jasmonate induced apoptosis in human prostate carcinoma cells via 5-lipoxygenase dependent pathway
    • 2-s2.0-36148943488
    • Ezekwudo D. E., Wang R. C., Elegbede J. A., Methyl jasmonate induced apoptosis in human prostate carcinoma cells via 5-lipoxygenase dependent pathway. Journal of Experimental Therapeutics and Oncology 2007 6 4 267 277 2-s2.0-36148943488
    • (2007) Journal of Experimental Therapeutics and Oncology , vol.6 , Issue.4 , pp. 267-277
    • Ezekwudo, D.E.1    Wang, R.C.2    Elegbede, J.A.3
  • 48
    • 57049178439 scopus 로고    scopus 로고
    • Delayed cytotoxic effects of methyl jasmonate and cis-jasmone induced apoptosis in prostate cancer cells
    • 2-s2.0-57049178439 10.1080/07357900801975272
    • Yeruva L., Pierre K. J., Bathina M., Elegbede A., Carper S. W., Delayed cytotoxic effects of methyl jasmonate and cis-jasmone induced apoptosis in prostate cancer cells. Cancer Investigation 2008 26 9 890 899 2-s2.0-57049178439 10.1080/07357900801975272
    • (2008) Cancer Investigation , vol.26 , Issue.9 , pp. 890-899
    • Yeruva, L.1    Pierre, K.J.2    Bathina, M.3    Elegbede, A.4    Carper, S.W.5
  • 49
    • 55849112650 scopus 로고    scopus 로고
    • PI3K/Akt pathway activation attenuates the cytotoxic effect of methyl jasmonate toward sarcoma cells
    • 2-s2.0-55849112650 10.1593/neo.08636
    • Elia U., Flescher E., PI3K/Akt pathway activation attenuates the cytotoxic effect of methyl jasmonate toward sarcoma cells. Neoplasia 2008 10 11 1303 1313 2-s2.0-55849112650 10.1593/neo.08636
    • (2008) Neoplasia , vol.10 , Issue.11 , pp. 1303-1313
    • Elia, U.1    Flescher, E.2
  • 50
    • 84866469996 scopus 로고    scopus 로고
    • Fragrance material review on methyl jasmonate
    • supplement 3 2-s2.0-84860596188 10.1016/j.fct.2012.03.035
    • Scognamiglio J., Jones L., Letizia C. S., Api A. M., Fragrance material review on methyl jasmonate. Food and Chemical Toxicology 2012 50 supplement 3 S572 S576 2-s2.0-84860596188 10.1016/j.fct.2012.03.035
    • (2012) Food and Chemical Toxicology , vol.50
    • Scognamiglio, J.1    Jones, L.2    Letizia, C.S.3    Api, A.M.4
  • 51
    • 79957990169 scopus 로고    scopus 로고
    • A preliminary study of the local treatment of preneoplastic and malignant skin lesions using methyl jasmonate
    • 2-s2.0-79957990169
    • Palmieri B., Iannitti T., Capone S., Flescher E., A preliminary study of the local treatment of preneoplastic and malignant skin lesions using methyl jasmonate. European Review for Medical and Pharmacological Sciences 2011 15 3 333 336 2-s2.0-79957990169
    • (2011) European Review for Medical and Pharmacological Sciences , vol.15 , Issue.3 , pp. 333-336
    • Palmieri, B.1    Iannitti, T.2    Capone, S.3    Flescher, E.4
  • 52
    • 84896861859 scopus 로고    scopus 로고
    • Methyl Jasmonate: Exemption from the requirement of a tolerance
    • Environmental Protection Agency (EPA)
    • Environmental Protection Agency (EPA), Methyl Jasmonate: exemption from the requirement of a tolerance. Federal Register 2013 78 74 22789 22794
    • (2013) Federal Register , vol.78 , Issue.74 , pp. 22789-22794
  • 53
    • 18144434267 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling: Cell cycle arrest versus apoptosis
    • 2-s2.0-18144434267 10.1016/S0300-483X(02)00460-2
    • Pietenpol J. A., Stewart Z. A., Cell cycle checkpoint signaling: cell cycle arrest versus apoptosis. Toxicology 2002 181-182 475 481 2-s2.0-18144434267 10.1016/S0300-483X(02)00460-2
    • (2002) Toxicology , vol.181-182 , pp. 475-481
    • Pietenpol, J.A.1    Stewart, Z.A.2
  • 54
    • 38549172149 scopus 로고    scopus 로고
    • Cell-cycle regulation
    • The C. elegans Research Community, WormBook 10.1895/wormbook.1.28.1
    • van den Heuvel S., Cell-cycle regulation. WormBook 2005 The C. elegans Research Community, WormBook 10.1895/wormbook.1.28.1
    • (2005) WormBook
    • Van Den Heuvel, S.1
  • 55
    • 0038052800 scopus 로고    scopus 로고
    • Cell cycle and apoptosis
    • 2-s2.0-0038052800 10.1046/j.1365-2184.2003.00267.x
    • Vermeulen K., Berneman Z. N., Van Bockstaele D. R., Cell cycle and apoptosis. Cell Proliferation 2003 36 3 165 175 2-s2.0-0038052800 10.1046/j.1365-2184.2003.00267.x
    • (2003) Cell Proliferation , vol.36 , Issue.3 , pp. 165-175
    • Vermeulen, K.1    Berneman, Z.N.2    Van Bockstaele, D.R.3
  • 56
    • 84864930500 scopus 로고    scopus 로고
    • Transcriptional regulation of the p53 tumor suppressor gene in S-phase of the cell-cycle and the cellular response to DNA damage
    • 808934 10.1155/2012/808934
    • Reisman D., Takahashi P., Polson A., Boggs K., Transcriptional regulation of the p53 tumor suppressor gene in S-phase of the cell-cycle and the cellular response to DNA damage. Biochemistry Research International 2012 2012 5 808934 10.1155/2012/808934
    • (2012) Biochemistry Research International , vol.2012 , pp. 5
    • Reisman, D.1    Takahashi, P.2    Polson, A.3    Boggs, K.4
  • 57
    • 84867659145 scopus 로고    scopus 로고
    • The influence of reactive oxygen species on cell cycle progression in mammalian cells
    • Verbon E. H., Post J. A., Boonstra J., The influence of reactive oxygen species on cell cycle progression in mammalian cells. Gene 2012 511 1 1 6
    • (2012) Gene , vol.511 , Issue.1 , pp. 1-6
    • Verbon, E.H.1    Post, J.A.2    Boonstra, J.3
  • 58
    • 84875181661 scopus 로고    scopus 로고
    • Oxidants, antioxidants and the current incurability of metastatic cancers
    • 120144
    • Watson J., Oxidants, antioxidants and the current incurability of metastatic cancers. Open Biology 2013 3 1 120144
    • (2013) Open Biology , vol.3 , Issue.1
    • Watson, J.1
  • 60
    • 84857483281 scopus 로고    scopus 로고
    • P53 regulates cell cycle and micrornas to promote differentiation of human embryonic stem cells
    • 2-s2.0-84857483281 10.1371/journal.pbio.1001268 e1001268
    • Jain A. K., Allton K., Iacovino M., Mahen E., Milczarek R. J., Zwaka T. P., Kyba M., Barton M. C., P53 regulates cell cycle and micrornas to promote differentiation of human embryonic stem cells. PLoS Biology 2012 10 2 2-s2.0-84857483281 10.1371/journal.pbio.1001268 e1001268
    • (2012) PLoS Biology , vol.10 , Issue.2
    • Jain, A.K.1    Allton, K.2    Iacovino, M.3    Mahen, E.4    Milczarek, R.J.5    Zwaka, T.P.6    Kyba, M.7    Barton, M.C.8
  • 63
    • 79960454735 scopus 로고    scopus 로고
    • The relative contribution of pro-apoptotic p53-target genes in the triggering of apoptosis following DNA damage in vitro and in vivo
    • 2-s2.0-79960454735 10.4161/cc.10.14.16588
    • Kuribayashi K., Finnberg N., Jeffers J. R., Zambetti G. P., El-Deiry W. S., The relative contribution of pro-apoptotic p53-target genes in the triggering of apoptosis following DNA damage in vitro and in vivo. Cell Cycle 2011 10 14 2380 2389 2-s2.0-79960454735 10.4161/cc.10.14.16588
    • (2011) Cell Cycle , vol.10 , Issue.14 , pp. 2380-2389
    • Kuribayashi, K.1    Finnberg, N.2    Jeffers, J.R.3    Zambetti, G.P.4    El-Deiry, W.S.5
  • 64
    • 80053036165 scopus 로고    scopus 로고
    • The role of p53 in metabolic regulation
    • 2-s2.0-80053036165 10.1177/1947601911409738
    • Puzio-Kuter A. M., The role of p53 in metabolic regulation. Genes and Cancer 2011 2 4 385 391 2-s2.0-80053036165 10.1177/1947601911409738
    • (2011) Genes and Cancer , vol.2 , Issue.4 , pp. 385-391
    • Puzio-Kuter, A.M.1
  • 65
    • 80052664208 scopus 로고    scopus 로고
    • Recent advances in p53 research and cancer treatment
    • 2-s2.0-80052664208 10.1155/2011/978312 978312
    • Suzuki K., Matsubara H., Recent advances in p53 research and cancer treatment. Journal of Biomedicine and Biotechnology 2011 2011 7 2-s2.0-80052664208 10.1155/2011/978312 978312
    • (2011) Journal of Biomedicine and Biotechnology , vol.2011 , pp. 7
    • Suzuki, K.1    Matsubara, H.2
  • 66
    • 32244441908 scopus 로고    scopus 로고
    • From cell cycle to differentiation: An expanding role for Cdk6
    • 2-s2.0-32244441908
    • Grossel M. J., Hinds P. W., From cell cycle to differentiation: an expanding role for Cdk6. Cell Cycle 2006 5 3 266 270 2-s2.0-32244441908
    • (2006) Cell Cycle , vol.5 , Issue.3 , pp. 266-270
    • Grossel, M.J.1    Hinds, P.W.2
  • 67
    • 61849135453 scopus 로고    scopus 로고
    • Tumor suppressors and cell metabolism: A recipe for cancer growth
    • 2-s2.0-61849135453 10.1101/gad.1756509
    • Jones R. G., Thompson C. B., Tumor suppressors and cell metabolism: a recipe for cancer growth. Genes and Development 2009 23 5 537 548 2-s2.0-61849135453 10.1101/gad.1756509
    • (2009) Genes and Development , vol.23 , Issue.5 , pp. 537-548
    • Jones, R.G.1    Thompson, C.B.2
  • 68
    • 77955363995 scopus 로고    scopus 로고
    • TP53 mutations in human cancers: Origins, consequences, and clinical use
    • a001008 2-s2.0-77955363995 10.1101/cshperspect.a001008
    • Olivier M., Hollstein M., Hainaut P., TP53 mutations in human cancers: origins, consequences, and clinical use. Cold Spring Harbor Perspectives in Biology 2010 2 1 a001008 2-s2.0-77955363995 10.1101/cshperspect.a001008
    • (2010) Cold Spring Harbor Perspectives in Biology , vol.2 , Issue.1
    • Olivier, M.1    Hollstein, M.2    Hainaut, P.3
  • 69
    • 84859855907 scopus 로고    scopus 로고
    • Redox regulation of p53, redox effectors regulated by p53: A subtle balance
    • 2-s2.0-84859855907 10.1089/ars.2011.4434
    • Maillet A., Pervaiz S., Redox regulation of p53, redox effectors regulated by p53: a subtle balance. Antioxidants and Redox Signaling 2012 16 11 1285 1294 2-s2.0-84859855907 10.1089/ars.2011.4434
    • (2012) Antioxidants and Redox Signaling , vol.16 , Issue.11 , pp. 1285-1294
    • Maillet, A.1    Pervaiz, S.2
  • 71
    • 77952192188 scopus 로고    scopus 로고
    • P53 regulation of metabolic pathways
    • a001040 2-s2.0-77952192188 10.1101/cshperspect.a001040
    • Gottlieb E., Vousden K. H., P53 regulation of metabolic pathways. Cold Spring Harbor Perspectives in Biology 2010 2 4 a001040 2-s2.0-77952192188 10.1101/cshperspect.a001040
    • (2010) Cold Spring Harbor Perspectives in Biology , vol.2 , Issue.4
    • Gottlieb, E.1    Vousden, K.H.2
  • 72
    • 0033229866 scopus 로고    scopus 로고
    • P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2
    • 2-s2.0-0033229866 10.1093/emboj/18.21.6027
    • Li P.-F., Dietz R., von Harsdorf R., P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2. EMBO Journal 1999 18 21 6027 6036 2-s2.0-0033229866 10.1093/emboj/18.21.6027
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 6027-6036
    • Li, P.-F.1    Dietz, R.2    Von Harsdorf, R.3
  • 74
    • 34250869019 scopus 로고    scopus 로고
    • MDA-MB-435 cells are derived from M14 Melanoma cells - A loss for breast cancer, but a boon for melanoma research
    • 2-s2.0-34250869019 10.1007/s10549-006-9392-8
    • Rae J. M., Creighton C. J., Meck J. M., Haddad B. R., Johnson M. D., MDA-MB-435 cells are derived from M14 Melanoma cells-a loss for breast cancer, but a boon for melanoma research. Breast Cancer Research and Treatment 2007 104 1 13 19 2-s2.0-34250869019 10.1007/s10549-006-9392-8
    • (2007) Breast Cancer Research and Treatment , vol.104 , Issue.1 , pp. 13-19
    • Rae, J.M.1    Creighton, C.J.2    Meck, J.M.3    Haddad, B.R.4    Johnson, M.D.5
  • 75
    • 45349097133 scopus 로고    scopus 로고
    • Analysis of p53 mutation status in human cancer cell lines: A paradigm for cell line cross-contamination
    • 2-s2.0-56149097419
    • Berglind H., Pawitan Y., Kato S., Ishioka C., Soussi T., Analysis of p53 mutation status in human cancer cell lines: a paradigm for cell line cross-contamination. Cancer Biology & Therapy 2008 7 5 699 708 2-s2.0-56149097419
    • (2008) Cancer Biology & Therapy , vol.7 , Issue.5 , pp. 699-708
    • Berglind, H.1    Pawitan, Y.2    Kato, S.3    Ishioka, C.4    Soussi, T.5
  • 76
    • 84871829780 scopus 로고    scopus 로고
    • Regulatory TGACG-motif may elicit the secondary metabolite production through inhibition of active Cyclin-dependent kinase/Cyclin complex
    • Nejad E. S., Askari H., Soltani S., Regulatory TGACG-motif may elicit the secondary metabolite production through inhibition of active Cyclin-dependent kinase/Cyclin complex. Plant Omics Journal 2012 5 6 553 558
    • (2012) Plant Omics Journal , vol.5 , Issue.6 , pp. 553-558
    • Nejad, E.S.1    Askari, H.2    Soltani, S.3
  • 78
    • 84859171807 scopus 로고    scopus 로고
    • MYC on the path to cancer
    • 2-s2.0-84859171807 10.1016/j.cell.2012.03.003
    • Dang C. V., MYC on the path to cancer. Cell 2012 149 1 22 35 2-s2.0-84859171807 10.1016/j.cell.2012.03.003
    • (2012) Cell , vol.149 , Issue.1 , pp. 22-35
    • Dang, C.V.1
  • 79
    • 79954462657 scopus 로고    scopus 로고
    • Survivin overexpression correlates with an apoptosis-resistant phenotype in chronic myeloid leukemia cells
    • 2-s2.0-79954462657 10.3892/or.2011.1224
    • Nestal de Moraes G., Silva K. L., Vasconcelos F. D. C., Maia R. C., Survivin overexpression correlates with an apoptosis-resistant phenotype in chronic myeloid leukemia cells. Oncology Reports 2011 25 6 1613 1619 2-s2.0-79954462657 10.3892/or.2011.1224
    • (2011) Oncology Reports , vol.25 , Issue.6 , pp. 1613-1619
    • Nestal De Moraes, G.1    Silva, K.L.2    Vasconcelos, F.D.C.3    Maia, R.C.4
  • 81
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • 2-s2.0-45349094984 10.1101/gad.1658508
    • Suen D.-F., Norris K. L., Youle R. J., Mitochondrial dynamics and apoptosis. Genes and Development 2008 22 12 1577 1590 2-s2.0-45349094984 10.1101/gad.1658508
    • (2008) Genes and Development , vol.22 , Issue.12 , pp. 1577-1590
    • Suen, D.-F.1    Norris, K.L.2    Youle, R.J.3
  • 82
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • 2-s2.0-33845977959 10.1152/physrev.00013.2006
    • Kroemer G., Galluzzi L., Brenner C., Mitochondrial membrane permeabilization in cell death. Physiological Reviews 2007 87 1 99 163 2-s2.0-33845977959 10.1152/physrev.00013.2006
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 83
    • 84872006971 scopus 로고    scopus 로고
    • Where killers meet - Permeabilization of the outer mitochondrial membrane during apoptosis
    • a011106
    • Bender T., Martinou G. C., Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis. Cold Spring Harbor Perspectives in Biology 2013 5 1 a011106
    • (2013) Cold Spring Harbor Perspectives in Biology , vol.5 , Issue.1
    • Bender, T.1    Martinou, G.C.2
  • 84
    • 63149129655 scopus 로고    scopus 로고
    • BcI-2 inhibitors: Targeting mitochondrial apoptotic pathways in cancer therapy
    • 2-s2.0-63149129655 10.1158/1078-0432.CCR-08-0144
    • Kang M. H., Reynolds C. P., BcI-2 inhibitors: targeting mitochondrial apoptotic pathways in cancer therapy. Clinical Cancer Research 2009 15 4 1126 1132 2-s2.0-63149129655 10.1158/1078-0432.CCR-08-0144
    • (2009) Clinical Cancer Research , vol.15 , Issue.4 , pp. 1126-1132
    • Kang, M.H.1    Reynolds, C.P.2
  • 85
    • 60249089101 scopus 로고    scopus 로고
    • Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?
    • 2-s2.0-60249089101 10.1016/j.mito.2008.10.003
    • Kumarswamy R., Chandna S., Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them? Mitochondrion 2009 9 1 1 8 2-s2.0-60249089101 10.1016/j.mito.2008.10.003
    • (2009) Mitochondrion , vol.9 , Issue.1 , pp. 1-8
    • Kumarswamy, R.1    Chandna, S.2
  • 87
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • 2-s2.0-0033519705 10.1038/20959
    • Shimizu S., Narita M., Tsujimoto Y., Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999 399 6735 483 487 2-s2.0-0033519705 10.1038/20959
    • (1999) Nature , vol.399 , Issue.6735 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 88
    • 0043204996 scopus 로고    scopus 로고
    • VDAC2 inhibits BAK activation and mitochondrial apoptosis
    • 2-s2.0-0043204996 10.1126/science.1083995
    • Cheng E. H.-Y., Sheiko T. V., Fisher J. K., Craigen W. J., Korsmeyer S. J., VDAC2 inhibits BAK activation and mitochondrial apoptosis. Science 2003 301 5632 513 517 2-s2.0-0043204996 10.1126/science.1083995
    • (2003) Science , vol.301 , Issue.5632 , pp. 513-517
    • Cheng, E.H.-Y.1    Sheiko, T.V.2    Fisher, J.K.3    Craigen, W.J.4    Korsmeyer, S.J.5
  • 89
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • 2-s2.0-34247895697 10.1038/ncb1575
    • Baines C. P., Kaiser R. A., Sheiko T., Craigen W. J., Molkentin J. D., Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nature Cell Biology 2007 9 5 550 555 2-s2.0-34247895697 10.1038/ncb1575
    • (2007) Nature Cell Biology , vol.9 , Issue.5 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 90
    • 84861532088 scopus 로고    scopus 로고
    • Killing a cancer: What are the alternatives?
    • Kreuzaler P., Watson C. J., Killing a cancer: what are the alternatives? Nature Reviews Cancer 2012 12 6 411 424
    • (2012) Nature Reviews Cancer , vol.12 , Issue.6 , pp. 411-424
    • Kreuzaler, P.1    Watson, C.J.2
  • 91
    • 80053039210 scopus 로고    scopus 로고
    • Mutations in the p53 tumor suppressor gene: Important milestones at the various steps of tumorigenesis
    • 2-s2.0-80053039210 10.1177/1947601911408889
    • Rivlin N., Brosh R., Oren M., Rotter V., Mutations in the p53 tumor suppressor gene: important milestones at the various steps of tumorigenesis. Genes and Cancer 2011 2 4 466 474 2-s2.0-80053039210 10.1177/1947601911408889
    • (2011) Genes and Cancer , vol.2 , Issue.4 , pp. 466-474
    • Rivlin, N.1    Brosh, R.2    Oren, M.3    Rotter, V.4
  • 92
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • 2-s2.0-65349103899 10.1016/j.cell.2009.04.037
    • Vousden K. H., Prives C., Blinded by the light: the growing complexity of p53. Cell 2009 137 3 413 431 2-s2.0-65349103899 10.1016/j.cell.2009.04.037
    • (2009) Cell , vol.137 , Issue.3 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 94
    • 79251534367 scopus 로고    scopus 로고
    • P53: The attractive tumor suppressor in the cancer research field
    • 2-s2.0-79251534367 10.1155/2011/603925 603925
    • Ozaki T., Nakagawara A., P53: the attractive tumor suppressor in the cancer research field. Journal of Biomedicine and Biotechnology 2011 2011 13 2-s2.0-79251534367 10.1155/2011/603925 603925
    • (2011) Journal of Biomedicine and Biotechnology , vol.2011 , pp. 13
    • Ozaki, T.1    Nakagawara, A.2
  • 96
    • 80155167845 scopus 로고    scopus 로고
    • Mitochondria as therapeutic targets for the treatment of malignant disease
    • 2-s2.0-80155167845 10.1089/ars.2011.4078
    • Fulda S., Kroemer G., Mitochondria as therapeutic targets for the treatment of malignant disease. Antioxidants and Redox Signaling 2011 15 12 2937 2949 2-s2.0-80155167845 10.1089/ars.2011.4078
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.12 , pp. 2937-2949
    • Fulda, S.1    Kroemer, G.2
  • 97
    • 84859833070 scopus 로고    scopus 로고
    • Antibody-induced nonapoptotic cell death in human lymphoma and leukemia cells is mediated through a novel reactive oxygen species-dependent pathway
    • 2-s2.0-84859833070 10.1182/blood-2011-12-395541
    • Honeychurch J., Alduaij W., Azizyan M., Cheadle E. J., Pelicano H., Ivanov A., Huang P., Cragg M. S., Illidge T. M., Antibody-induced nonapoptotic cell death in human lymphoma and leukemia cells is mediated through a novel reactive oxygen species-dependent pathway. Blood 2012 119 15 3523 3533 2-s2.0-84859833070 10.1182/blood-2011-12-395541
    • (2012) Blood , vol.119 , Issue.15 , pp. 3523-3533
    • Honeychurch, J.1    Alduaij, W.2    Azizyan, M.3    Cheadle, E.J.4    Pelicano, H.5    Ivanov, A.6    Huang, P.7    Cragg, M.S.8    Illidge, T.M.9
  • 98
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • 2-s2.0-1542406446
    • Lambeth J. D., NOX enzymes and the biology of reactive oxygen. Nature Reviews Immunology 2004 4 3 181 189 2-s2.0-1542406446
    • (2004) Nature Reviews Immunology , vol.4 , Issue.3 , pp. 181-189
    • Lambeth, J.D.1
  • 100
    • 80255125980 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate of cancer cells exposed to both standard and redox chemotherapeutic agents
    • 2-s2.0-80255125980 10.1016/j.bcp.2011.07.102
    • Verrax J., Dejeans N., Sid B., Glorieux C., Calderon P. B., Intracellular ATP levels determine cell death fate of cancer cells exposed to both standard and redox chemotherapeutic agents. Biochemical Pharmacology 2011 82 11 1540 1548 2-s2.0-80255125980 10.1016/j.bcp.2011.07.102
    • (2011) Biochemical Pharmacology , vol.82 , Issue.11 , pp. 1540-1548
    • Verrax, J.1    Dejeans, N.2    Sid, B.3    Glorieux, C.4    Calderon, P.B.5
  • 101
    • 33749178260 scopus 로고    scopus 로고
    • Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response
    • 2-s2.0-33749178260 10.1016/j.bbabio.2006.06.014
    • Festjens N., Vanden Berghe T., Vandenabeele P., Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response. Biochimica et Biophysica Acta 2006 1757 9-10 1371 1387 2-s2.0-33749178260 10.1016/j.bbabio.2006.06.014
    • (2006) Biochimica et Biophysica Acta , vol.1757 , Issue.9-10 , pp. 1371-1387
    • Festjens, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 103
    • 77957105977 scopus 로고    scopus 로고
    • Molecular mechanisms of necroptosis: An ordered cellular explosion
    • 2-s2.0-77957105977 10.1038/nrm2970
    • Vandenabeele P., Galluzzi L., Vanden Berghe T., Kroemer G., Molecular mechanisms of necroptosis: an ordered cellular explosion. Nature Reviews Molecular Cell Biology 2010 11 10 700 714 2-s2.0-77957105977 10.1038/nrm2970
    • (2010) Nature Reviews Molecular Cell Biology , vol.11 , Issue.10 , pp. 700-714
    • Vandenabeele, P.1    Galluzzi, L.2    Vanden Berghe, T.3    Kroemer, G.4
  • 104
    • 52449095786 scopus 로고    scopus 로고
    • Inhibition of expression of anti-apoptotic protein Bcl-2 and induction of cell death in radioresistant human prostate adenocarcinoma cell line (PC-3) by methyl jasmonate
    • 2-s2.0-52449095786 10.1016/j.canlet.2008.05.022
    • Ezekwudo D., Shashidharamurthy R., Devineni D., Bozeman E., Palaniappan R., Selvaraj P., Inhibition of expression of anti-apoptotic protein Bcl-2 and induction of cell death in radioresistant human prostate adenocarcinoma cell line (PC-3) by methyl jasmonate. Cancer Letters 2008 270 2 277 285 2-s2.0-52449095786 10.1016/j.canlet.2008.05.022
    • (2008) Cancer Letters , vol.270 , Issue.2 , pp. 277-285
    • Ezekwudo, D.1    Shashidharamurthy, R.2    Devineni, D.3    Bozeman, E.4    Palaniappan, R.5    Selvaraj, P.6
  • 105
    • 84867447062 scopus 로고    scopus 로고
    • Methyl jasmonate displays in vitro and in vivo activity against multiple myeloma cells
    • Klippel S., Jakubikova J., Delmore J., Methyl jasmonate displays in vitro and in vivo activity against multiple myeloma cells. British Journal of Haematology 2012 159 3 340 351
    • (2012) British Journal of Haematology , vol.159 , Issue.3 , pp. 340-351
    • Klippel, S.1    Jakubikova, J.2    Delmore, J.3
  • 106
    • 65549116046 scopus 로고    scopus 로고
    • Reactive oxygen species, cancer and anti-cancer therapies
    • 2-s2.0-65549116046
    • Manda G., Nechifor M. T., Neagu T.-M., Reactive oxygen species, cancer and anti-cancer therapies. Current Chemical Biology 2009 3 1 22 46 2-s2.0-65549116046
    • (2009) Current Chemical Biology , vol.3 , Issue.1 , pp. 22-46
    • Manda, G.1    Nechifor, M.T.2    Neagu, T.-M.3
  • 107
    • 22444433668 scopus 로고    scopus 로고
    • Oxidant and redox signaling in vascular oxygen sensing mechanisms: Basic concepts, current controversies, and potential importance of cytosolic NADPH
    • 2-s2.0-22444433668 10.1152/ajplung.00060.2005
    • Wolin M. S., Ahmad M., Gupte S. A., Oxidant and redox signaling in vascular oxygen sensing mechanisms: basic concepts, current controversies, and potential importance of cytosolic NADPH. American Journal of Physiology-Lung Cellular and Molecular Physiology 2005 289 2 L159 L173 2-s2.0-22444433668 10.1152/ajplung.00060.2005
    • (2005) American Journal of Physiology - Lung Cellular and Molecular Physiology , vol.289 , Issue.2
    • Wolin, M.S.1    Ahmad, M.2    Gupte, S.A.3
  • 108
    • 33749047437 scopus 로고    scopus 로고
    • Localizing NADPH oxidase-derived ROS
    • 2-s2.0-33749047437 10.1126/stke.3492006re8
    • Ushio-Fukai M., Localizing NADPH oxidase-derived ROS. Science's STKE 2006 2006 349, article re8 2-s2.0-33749047437 10.1126/stke.3492006re8
    • (2006) Science's STKE , vol.2006 , Issue.349 ARTICLE RE8
    • Ushio-Fukai, M.1
  • 109
    • 70349341899 scopus 로고    scopus 로고
    • Downstream targets and intracellular compartmentalization in Nox signaling
    • 2-s2.0-70349341899
    • Chen K., Craige S. E., Keaney J. F. Jr., Downstream targets and intracellular compartmentalization in Nox signaling. Antioxidants & Redox Signaling 2009 11 10 2467 2480 2-s2.0-70349341899
    • (2009) Antioxidants & Redox Signaling , vol.11 , Issue.10 , pp. 2467-2480
    • Chen, K.1    Craige, S.E.2    Keaney Jr., J.F.3
  • 110
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • 2-s2.0-75749123115 10.1021/cb900258z
    • Paulsen C. E., Carroll K. S., Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chemical Biology 2010 5 1 47 62 2-s2.0-75749123115 10.1021/cb900258z
    • (2010) ACS Chemical Biology , vol.5 , Issue.1 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 111
    • 84874853858 scopus 로고    scopus 로고
    • Cancer-produced metabolites of 5-lipoxygenase induce tumor-evoked regulatory B cells via peroxisome proliferator-activated receptor alpha
    • Wejksza K., Lee-Chang C., Bodogai M., Cancer-produced metabolites of 5-lipoxygenase induce tumor-evoked regulatory B cells via peroxisome proliferator-activated receptor alpha. The Journal of Immunology 2013 190 6 2575 2584
    • (2013) The Journal of Immunology , vol.190 , Issue.6 , pp. 2575-2584
    • Wejksza, K.1    Lee-Chang, C.2    Bodogai, M.3
  • 112
    • 70349769764 scopus 로고    scopus 로고
    • Reactive oxygen species production by mitochondria
    • 2-s2.0-70349769764 10.1007/978-1-59745-521-3-11
    • Lambert A. J., Brand M. D., Reactive oxygen species production by mitochondria. Methods in Molecular Biology 2009 554 165 181 2-s2.0-70349769764 10.1007/978-1-59745-521-3-11
    • (2009) Methods in Molecular Biology , vol.554 , pp. 165-181
    • Lambert, A.J.1    Brand, M.D.2
  • 113
    • 79251603273 scopus 로고    scopus 로고
    • Hydrogen peroxide probes directed to different cellular compartments
    • 2-s2.0-79251603273 10.1371/journal.pone.0014564 e14564
    • Malinouski M., Zhou Y., Belousov V. V., Hatfield D. L., Gladyshev V. N., Hydrogen peroxide probes directed to different cellular compartments. PLoS ONE 2011 6 1 2-s2.0-79251603273 10.1371/journal.pone.0014564 e14564
    • (2011) PLoS ONE , vol.6 , Issue.1
    • Malinouski, M.1    Zhou, Y.2    Belousov, V.V.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 114
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • 2-s2.0-0030729851 10.1016/S0014-5793(97)01159-9
    • Korshunov S. S., Skulachev V. P., Starkov A. A., High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Letters 1997 416 1 15 18 2-s2.0-0030729851 10.1016/S0014-5793(97)01159-9
    • (1997) FEBS Letters , vol.416 , Issue.1 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 115
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • 2-s2.0-0142150051 10.1113/jphysiol.2003.049478
    • Turrens J. F., Mitochondrial formation of reactive oxygen species. Journal of Physiology 2003 552 2 335 344 2-s2.0-0142150051 10.1113/jphysiol. 2003.049478
    • (2003) Journal of Physiology , vol.552 , Issue.2 , pp. 335-344
    • Turrens, J.F.1
  • 116
    • 11144303507 scopus 로고    scopus 로고
    • Reactive oxygen species and the mitochondrial signaling pathway of cell death
    • 2-s2.0-11144303507
    • Le Bras M., Clément M.-V., Pervaiz S., Brenner C., Reactive oxygen species and the mitochondrial signaling pathway of cell death. Histology and Histopathology 2005 20 1 205 219 2-s2.0-11144303507
    • (2005) Histology and Histopathology , vol.20 , Issue.1 , pp. 205-219
    • Le Bras, M.1    Clément, M.-V.2    Pervaiz, S.3    Brenner, C.4
  • 117
    • 79955835149 scopus 로고    scopus 로고
    • Mitochondrial subversion in cancer
    • 2-s2.0-79955835149 10.1158/1940-6207.CAPR-10-0326
    • Chatterjee A., Dasgupta S., Sidransky D., Mitochondrial subversion in cancer. Cancer Prevention Research 2011 4 5 638 654 2-s2.0-79955835149 10.1158/1940-6207.CAPR-10-0326
    • (2011) Cancer Prevention Research , vol.4 , Issue.5 , pp. 638-654
    • Chatterjee, A.1    Dasgupta, S.2    Sidransky, D.3
  • 118
    • 78049447695 scopus 로고    scopus 로고
    • A mitochondrial view of aging, reactive oxygen species and metastatic cancer
    • 2-s2.0-78049447695
    • Ladiges W., Wanagat J., Preston B., Loeb L., Rabinovitch P., A mitochondrial view of aging, reactive oxygen species and metastatic cancer. Aging Cell 2010 9 4 462 465 2-s2.0-78049447695
    • (2010) Aging Cell , vol.9 , Issue.4 , pp. 462-465
    • Ladiges, W.1    Wanagat, J.2    Preston, B.3    Loeb, L.4    Rabinovitch, P.5
  • 120
    • 77951432631 scopus 로고    scopus 로고
    • The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation - Why mitochondria are targets for cancer therapy
    • 2-s2.0-77951432631 10.1016/j.mam.2010.02.008
    • Ralph S. J., Rodríguez-Enríquez S., Neuzil J., Saavedra E., Moreno-Sánchez R., The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation-why mitochondria are targets for cancer therapy. Molecular Aspects of Medicine 2010 31 2 145 170 2-s2.0-77951432631 10.1016/j.mam.2010.02.008
    • (2010) Molecular Aspects of Medicine , vol.31 , Issue.2 , pp. 145-170
    • Ralph, S.J.1    Rodríguez-Enríquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sánchez, R.5
  • 121
    • 75149195862 scopus 로고    scopus 로고
    • Catalase protects tumor cells from apoptosis induction by intercellular ROS signaling
    • 2-s2.0-75149195862
    • Bechtel W., Bauer G., Catalase protects tumor cells from apoptosis induction by intercellular ROS signaling. Anticancer Research 2009 29 11 4541 4557 2-s2.0-75149195862
    • (2009) Anticancer Research , vol.29 , Issue.11 , pp. 4541-4557
    • Bechtel, W.1    Bauer, G.2
  • 122
    • 77649183649 scopus 로고    scopus 로고
    • Bioenergetic pathways in tumor mitochondria as targets for cancer therapy and the importance of the ROS-induced apoptotic trigger
    • 2-s2.0-77649183649 10.1016/j.mam.2009.12.006
    • Ralph S. J., Rodríguez-Enríquez S., Neuzil J., Moreno-Sánchez R., Bioenergetic pathways in tumor mitochondria as targets for cancer therapy and the importance of the ROS-induced apoptotic trigger. Molecular Aspects of Medicine 2010 31 1 29 59 2-s2.0-77649183649 10.1016/j.mam.2009.12.006
    • (2010) Molecular Aspects of Medicine , vol.31 , Issue.1 , pp. 29-59
    • Ralph, S.J.1    Rodríguez-Enríquez, S.2    Neuzil, J.3    Moreno-Sánchez, R.4
  • 123
    • 34748858784 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis: Impact on cancer therapy
    • 2-s2.0-34748858784 10.1002/jps.20874
    • Ozben T., Oxidative stress and apoptosis: impact on cancer therapy. Journal of Pharmaceutical Sciences 2007 96 9 2181 2196 2-s2.0-34748858784 10.1002/jps.20874
    • (2007) Journal of Pharmaceutical Sciences , vol.96 , Issue.9 , pp. 2181-2196
    • Ozben, T.1
  • 124
    • 84888769370 scopus 로고    scopus 로고
    • Reactive oxygen species reduction is a key underlying mechanism of drug resistance in cancer chemotherapy
    • Maiti A. K., Reactive oxygen species reduction is a key underlying mechanism of drug resistance in cancer chemotherapy. Chemotherapy 2012 1 104 108
    • (2012) Chemotherapy , vol.1 , pp. 104-108
    • Maiti, A.K.1
  • 126
    • 0035101409 scopus 로고    scopus 로고
    • Hydrogen peroxide acts as a second messenger for the induction of defense genes in tomato plants in response to wounding, systemin, and methyl jasmonate
    • 2-s2.0-0035101409 10.1105/tpc.13.1.179
    • Orozco-Cárdenas M. L., Narváez-Vásquez J., Ryan C. A., Hydrogen peroxide acts as a second messenger for the induction of defense genes in tomato plants in response to wounding, systemin, and methyl jasmonate. Plant Cell 2001 13 1 179 191 2-s2.0-0035101409 10.1105/tpc.13.1.179
    • (2001) Plant Cell , vol.13 , Issue.1 , pp. 179-191
    • Orozco-Cárdenas, M.L.1    Narváez-Vásquez, J.2    Ryan, C.A.3
  • 127
    • 33748564986 scopus 로고    scopus 로고
    • Membrane transport of hydrogen peroxide
    • 2-s2.0-33748564986 10.1016/j.bbamem.2006.02.015
    • Bienert G. P., Schjoerring J. K., Jahn T. P., Membrane transport of hydrogen peroxide. Biochimica et Biophysica Acta 2006 1758 8 994 1003 2-s2.0-33748564986 10.1016/j.bbamem.2006.02.015
    • (2006) Biochimica et Biophysica Acta , vol.1758 , Issue.8 , pp. 994-1003
    • Bienert, G.P.1    Schjoerring, J.K.2    Jahn, T.P.3
  • 128
    • 33744464485 scopus 로고    scopus 로고
    • Hydrogen peroxide is involved in methyl jasmonate-induced senescence of rice leaves
    • 2-s2.0-33744464485 10.1111/j.1399-3054.2006.00662.x
    • Hung K. T., Hsu Y. T., Kao C. H., Hydrogen peroxide is involved in methyl jasmonate-induced senescence of rice leaves. Physiologia Plantarum 2006 127 2 293 303 2-s2.0-33744464485 10.1111/j.1399-3054.2006.00662.x
    • (2006) Physiologia Plantarum , vol.127 , Issue.2 , pp. 293-303
    • Hung, K.T.1    Hsu, Y.T.2    Kao, C.H.3
  • 131
    • 34248396033 scopus 로고    scopus 로고
    • m produced either by a closure of the mitochondrial permeability transition pore or by inhibition of the ATP synthase
    • m produced either by a closure of the mitochondrial permeability transition pore or by inhibition of the ATP synthase. Cancer Letts 2007 252 1 8
    • (2007) Cancer Letts , vol.252 , pp. 1-8
    • López-Lázaro, M.1
  • 132
    • 66349108684 scopus 로고    scopus 로고
    • AKR1C isoforms represent a novel cellular target for jasmonates alongside their mitochondrial-mediated effects
    • 2-s2.0-66349108684 10.1158/0008-5472.CAN-08-4533
    • Davies N. J., Hayden R. E., Simpson P. J., Birtwistle J., Mayer K., Ride J. P., Bunce C. M., AKR1C isoforms represent a novel cellular target for jasmonates alongside their mitochondrial-mediated effects. Cancer Research 2009 69 11 4769 4775 2-s2.0-66349108684 10.1158/0008-5472.CAN-08-4533
    • (2009) Cancer Research , vol.69 , Issue.11 , pp. 4769-4775
    • Davies, N.J.1    Hayden, R.E.2    Simpson, P.J.3    Birtwistle, J.4    Mayer, K.5    Ride, J.P.6    Bunce, C.M.7
  • 133
    • 77955470822 scopus 로고    scopus 로고
    • Metabolism and proliferation share common regulatory pathways in cancer cells
    • 2-s2.0-77955470822 10.1038/onc.2010.182
    • Fritz V., Fajas L., Metabolism and proliferation share common regulatory pathways in cancer cells. Oncogene 2010 29 31 4369 4377 2-s2.0-77955470822 10.1038/onc.2010.182
    • (2010) Oncogene , vol.29 , Issue.31 , pp. 4369-4377
    • Fritz, V.1    Fajas, L.2
  • 134
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • 2-s2.0-0001221508
    • Warburg O., On respiratory impairment in cancer cells. Science 1956 124 3215 269 270 2-s2.0-0001221508
    • (1956) Science , vol.124 , Issue.3215 , pp. 269-270
    • Warburg, O.1
  • 135
    • 77953812468 scopus 로고    scopus 로고
    • The pivotal roles of mitochondria in cancer: Warburg and beyond and encouraging prospects for effective therapies
    • 2-s2.0-77953812468 10.1016/j.bbabio.2010.03.025
    • Mathupala S. P., Ko Y. H., Pedersen P. L., The pivotal roles of mitochondria in cancer: warburg and beyond and encouraging prospects for effective therapies. Biochimica et Biophysica Acta 2010 1797 6-7 1225 1230 2-s2.0-77953812468 10.1016/j.bbabio.2010.03.025
    • (2010) Biochimica et Biophysica Acta , vol.1797 , Issue.6-7 , pp. 1225-1230
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 136
    • 0037065972 scopus 로고    scopus 로고
    • Variation in mitochondrial function in hypoxia-sensitive and hypoxia-tolerant human glioma cells
    • 2-s2.0-0037065972 10.1038/sj.bjc.6600087
    • Turcotte M. L., Parliament H., Franko A., Allalunis-Turner J., Variation in mitochondrial function in hypoxia-sensitive and hypoxia-tolerant human glioma cells. British Journal of Cancer 2002 86 4 619 624 2-s2.0-0037065972 10.1038/sj.bjc.6600087
    • (2002) British Journal of Cancer , vol.86 , Issue.4 , pp. 619-624
    • Turcotte, M.L.1    Parliament, H.2    Franko, A.3    Allalunis-Turner, J.4
  • 137
    • 26944452745 scopus 로고    scopus 로고
    • Glucose metabolism heterogeneity in human and mouse malignant glioma cell lines
    • 2-s2.0-26944452745 10.1007/s11060-004-6404-6
    • Griguer C. E., Oliva C. R., Gillespie G. Y., Glucose metabolism heterogeneity in human and mouse malignant glioma cell lines. Journal of Neuro-Oncology 2005 74 2 123 133 2-s2.0-26944452745 10.1007/s11060-004-6404-6
    • (2005) Journal of Neuro-Oncology , vol.74 , Issue.2 , pp. 123-133
    • Griguer, C.E.1    Oliva, C.R.2    Gillespie, G.Y.3
  • 138
    • 79958015593 scopus 로고    scopus 로고
    • Targeting metabolic remodeling in glioblastoma multiforme
    • 2-s2.0-79958015593
    • Wolf A., Agnihotri S., Guha A., Targeting metabolic remodeling in glioblastoma multiforme. Oncotarget 2010 1 7 552 562 2-s2.0-79958015593
    • (2010) Oncotarget , vol.1 , Issue.7 , pp. 552-562
    • Wolf, A.1    Agnihotri, S.2    Guha, A.3
  • 139
    • 84867567280 scopus 로고    scopus 로고
    • Therapeutic targeting of cancer cell metabolism: Role of metabolic enzymes, oncogenes and tumor suppressor genes
    • Majeed R., Hamid A., Qurishi Y., Therapeutic targeting of cancer cell metabolism: role of metabolic enzymes, oncogenes and tumor suppressor genes. Journal of Cancer Science & Therapy 2012 4 9 281 291
    • (2012) Journal of Cancer Science & Therapy , vol.4 , Issue.9 , pp. 281-291
    • Majeed, R.1    Hamid, A.2    Qurishi, Y.3
  • 140
    • 0038714272 scopus 로고    scopus 로고
    • Isozymes of mammalian hexokinase: Structure, subcellular localization and metabolic function
    • 2-s2.0-0038714272 10.1242/jeb.00241
    • Wilson J. E., Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. Journal of Experimental Biology 2003 206 12 2049 2057 2-s2.0-0038714272 10.1242/jeb.00241
    • (2003) Journal of Experimental Biology , vol.206 , Issue.12 , pp. 2049-2057
    • Wilson, J.E.1
  • 141
    • 79952417296 scopus 로고    scopus 로고
    • Subcellular localization of hexokinases i and II directs the metabolic fate of glucose
    • 2-s2.0-79952417296 10.1371/journal.pone.0017674 e17674
    • John S., Weiss J. N., Ribalet B., Subcellular localization of hexokinases I and II directs the metabolic fate of glucose. PLoS ONE 2011 6 3 2-s2.0-79952417296 10.1371/journal.pone.0017674 e17674
    • (2011) PLoS ONE , vol.6 , Issue.3
    • John, S.1    Weiss, J.N.2    Ribalet, B.3
  • 142
    • 60249083822 scopus 로고    scopus 로고
    • Hexokinase-2 bound to mitochondria: Cancer's stygian link to the "warburg effect" and a pivotal target for effective therapy
    • 2-s2.0-60249083822 10.1016/j.semcancer.2008.11.006
    • Mathupala S. P., Ko Y. H., Pedersen P. L., Hexokinase-2 bound to mitochondria: cancer's stygian link to the "Warburg effect" and a pivotal target for effective therapy. Seminars in Cancer Biology 2009 19 1 17 24 2-s2.0-60249083822 10.1016/j.semcancer.2008.11.006
    • (2009) Seminars in Cancer Biology , vol.19 , Issue.1 , pp. 17-24
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 143
    • 0037056002 scopus 로고    scopus 로고
    • Mitochondrial bound type II hexokinase: A key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention
    • 2-s2.0-0037056002 10.1016/S0005-2728(02)00248-7
    • Pedersen P. L., Mathupala S., Rempel A., Geschwind J. F., Ko Y. H., Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention. Biochimica
    • (2002) Biochimica et Biophysica Acta , vol.1555 , Issue.1-3 , pp. 14-20
    • Pedersen, P.L.1    Mathupala, S.2    Rempel, A.3    Geschwind, J.F.4    Ko, Y.H.5
  • 144
    • 0022595453 scopus 로고
    • Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC
    • 2-s2.0-0022595453
    • Nakashima R. A., Mangan P. S., Colombini M., Pedersen P. L., Hexokinase receptor complex in hepatoma mitochondria: evidence from N,N′- dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 1986 25 5 1015 1021 2-s2.0-0022595453
    • (1986) Biochemistry , vol.25 , Issue.5 , pp. 1015-1021
    • Nakashima, R.A.1    Mangan, P.S.2    Colombini, M.3    Pedersen, P.L.4
  • 145
    • 52449089360 scopus 로고    scopus 로고
    • Voltage dependent anion channels (VDACs): A brief introduction with a focus on the outer mitochondrial compartment's roles together with hexokinase-2 in the "warburg effect" in cancer
    • 2-s2.0-52449089360 10.1007/s10863-008-9165-7
    • Pedersen P. L., Voltage dependent anion channels (VDACs): a brief introduction with a focus on the outer mitochondrial compartment's roles together with hexokinase-2 in the "Warburg effect" in cancer. Journal of Bioenergetics and Biomembranes 2008 40 3 123 126 2-s2.0-52449089360 10.1007/s10863-008-9165-7
    • (2008) Journal of Bioenergetics and Biomembranes , vol.40 , Issue.3 , pp. 123-126
    • Pedersen, P.L.1
  • 146
    • 52449086028 scopus 로고    scopus 로고
    • Mini review on the structure and supramolecular assembly of VDAC
    • 2-s2.0-52449086028 10.1007/s10863-008-9141-2
    • Gonçalves R. P., Buzhysnskyy N., Scheuring S., Mini review on the structure and supramolecular assembly of VDAC. Journal of Bioenergetics and Biomembranes 2008 40 3 133 138 2-s2.0-52449086028 10.1007/s10863-008-9141-2
    • (2008) Journal of Bioenergetics and Biomembranes , vol.40 , Issue.3 , pp. 133-138
    • Gonçalves, R.P.1    Buzhysnskyy, N.2    Scheuring, S.3
  • 148
    • 79551641146 scopus 로고    scopus 로고
    • Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer
    • 2-s2.0-79551641146 10.1371/journal.pone.0014635 e14635
    • Grills C., Jithesh P. V., Blayney J., Zhang S.-D., Fennell D. A., Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer. PLoS ONE 2011 6 1 2-s2.0-79551641146 10.1371/journal.pone.0014635 e14635
    • (2011) PLoS ONE , vol.6 , Issue.1
    • Grills, C.1    Jithesh, P.V.2    Blayney, J.3    Zhang, S.-D.4    Fennell, D.A.5
  • 149
    • 49149087268 scopus 로고    scopus 로고
    • Disruption of the hexokinase-VDAC complex for tumor therapy
    • 2-s2.0-49149087268 10.1038/onc.2008.114
    • Galluzzi L., Kepp O., Tajeddine N., Kroemer G., Disruption of the hexokinase-VDAC complex for tumor therapy. Oncogene 2008 27 34 4633 4635 2-s2.0-49149087268 10.1038/onc.2008.114
    • (2008) Oncogene , vol.27 , Issue.34 , pp. 4633-4635
    • Galluzzi, L.1    Kepp, O.2    Tajeddine, N.3    Kroemer, G.4
  • 150
    • 35448964610 scopus 로고    scopus 로고
    • Warburg, me and Hexokinase 2: Multiple discoveries of key molecular events underlying one of cancers' most common phenotypes, the "warburg Effect", i.e., elevated glycolysis in the presence of oxygen
    • 2-s2.0-35448964610 10.1007/s10863-007-9094-x
    • Pedersen P. L., Warburg, me and Hexokinase 2: multiple discoveries of key molecular events underlying one of cancers' most common phenotypes, the "Warburg Effect" i.e., elevated glycolysis in the presence of oxygen. Journal of Bioenergetics and Biomembranes 2007 39 3 211 222 2-s2.0-35448964610 10.1007/s10863-007-9094-x
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.3 , pp. 211-222
    • Pedersen, P.L.1
  • 151
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator - Thinking outside the box
    • 2-s2.0-29344468832 10.1016/j.bbadis.2005.10.006
    • Lemasters J. J., Holmuhamedov E., Voltage-dependent anion channel (VDAC) as mitochondrial governator-thinking outside the box. Biochimica et Biophysica Acta 2006 1762 2 181 190 2-s2.0-29344468832 10.1016/j.bbadis.2005.10.006
    • (2006) Biochimica et Biophysica Acta , vol.1762 , Issue.2 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 152
    • 79959716502 scopus 로고    scopus 로고
    • Hexokinase II acts through UCP3 to suppress mitochondrial reactive oxygen species production and maintain aerobic respiration
    • 2-s2.0-79959716502 10.1042/BJ20110571
    • Mailloux R. J., Dumouchel T., Aguer C., Dekemp R., Beanlands R., Harper M.-E., Hexokinase II acts through UCP3 to suppress mitochondrial reactive oxygen species production and maintain aerobic respiration. Biochemical Journal 2011 437 2 301 311 2-s2.0-79959716502 10.1042/BJ20110571
    • (2011) Biochemical Journal , vol.437 , Issue.2 , pp. 301-311
    • Mailloux, R.J.1    Dumouchel, T.2    Aguer, C.3    Dekemp, R.4    Beanlands, R.5    Harper, M.-E.6
  • 153
    • 68349143277 scopus 로고    scopus 로고
    • Enzymatic properties of the N-and C-terminal halves of human hexokinase II
    • 2-s2.0-68349143277
    • Ahn K. J., Kim J., Yun M., Park J. H., Lee J. D., Enzymatic properties of the N-and C-terminal halves of human hexokinase II. BMB Reports 2009 42 6 350 355 2-s2.0-68349143277
    • (2009) BMB Reports , vol.42 , Issue.6 , pp. 350-355
    • Ahn, K.J.1    Kim, J.2    Yun, M.3    Park, J.H.4    Lee, J.D.5
  • 154
    • 0347986675 scopus 로고    scopus 로고
    • Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases
    • 2-s2.0-0347986675 10.1128/MCB.24.2.730-740.2004
    • Majewski N., Nogueira V., Robey R. B., Hay N., Akt inhibits apoptosis downstream of BID cleavage via a glucose-dependent mechanism involving mitochondrial hexokinases. Molecular and Cellular Biology 2004 24 2 730 740 2-s2.0-0347986675 10.1128/MCB.24.2.730-740.2004
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.2 , pp. 730-740
    • Majewski, N.1    Nogueira, V.2    Robey, R.B.3    Hay, N.4
  • 156
    • 28544436922 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase 3 β disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity
    • 2-s2.0-28544436922 10.1158/0008-5472.CAN-05-1925
    • Pastorino J. G., Hoek J. B., Shulga N., Activation of glycogen synthase kinase 3 β disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity. Cancer Research 2005 65 22 10545 10554 2-s2.0-28544436922 10.1158/0008-5472.CAN-05-1925
    • (2005) Cancer Research , vol.65 , Issue.22 , pp. 10545-10554
    • Pastorino, J.G.1    Hoek, J.B.2    Shulga, N.3
  • 157
    • 84867699185 scopus 로고    scopus 로고
    • GSK3-mediated VDAC phosphorylation controls outer mitochondrial membrane permeability during lipid accumulation
    • Martel C., Allouche M., Esposti D. D., GSK3-mediated VDAC phosphorylation controls outer mitochondrial membrane permeability during lipid accumulation. Hepatology 2012 57 1 93 102
    • (2012) Hepatology , vol.57 , Issue.1 , pp. 93-102
    • Martel, C.1    Allouche, M.2    Esposti, D.D.3
  • 158
    • 84878248618 scopus 로고    scopus 로고
    • Akt inhibition promotes hexokinase 2 redistribution and glucose uptake in cancer cells
    • Neary C. L., Pastorino J. G., Akt inhibition promotes hexokinase 2 redistribution and glucose uptake in cancer cells. Journal of Cellular Physiology 2013 228 9 1943 1948
    • (2013) Journal of Cellular Physiology , vol.228 , Issue.9 , pp. 1943-1948
    • Neary, C.L.1    Pastorino, J.G.2
  • 159
    • 0041309460 scopus 로고    scopus 로고
    • Hexokinase II: The integration of energy metabolism and control of apoptosis
    • 2-s2.0-0041309460
    • Pastorino J. G., Hoek J. B., Hexokinase II: the integration of energy metabolism and control of apoptosis. Current Medicinal Chemistry 2003 10 16 1535 1551 2-s2.0-0041309460
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.16 , pp. 1535-1551
    • Pastorino, J.G.1    Hoek, J.B.2
  • 160
    • 33746924468 scopus 로고    scopus 로고
    • Hexokinase II: Cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria
    • 2-s2.0-33746924468 10.1038/sj.onc.1209603
    • Mathupala S. P., Ko Y. H., Pedersen P. L., Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria. Oncogene 2006 25 34 4777 4786 2-s2.0-33746924468 10.1038/sj.onc.1209603
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4777-4786
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 161
    • 67650245365 scopus 로고    scopus 로고
    • Regulation and pharmacology of the mitochondrial permeability transition pore
    • 2-s2.0-67650245365 10.1093/cvr/cvp151
    • Zorov D. B., Juhaszova M., Yaniv Y., Nuss H. B., Wang S., Sollott S. J., Regulation and pharmacology of the mitochondrial permeability transition pore. Cardiovascular Research 2009 83 2 213 225 2-s2.0-67650245365 10.1093/cvr/cvp151
    • (2009) Cardiovascular Research , vol.83 , Issue.2 , pp. 213-225
    • Zorov, D.B.1    Juhaszova, M.2    Yaniv, Y.3    Nuss, H.B.4    Wang, S.5    Sollott, S.J.6
  • 162
    • 44449147036 scopus 로고    scopus 로고
    • Tumor cell metabolism: Cancer's Achilles' heel
    • 2-s2.0-44449147036 10.1016/j.ccr.2008.05.005
    • Kroemer G., Pouyssegur J., Tumor cell metabolism: cancer's Achilles' heel. Cancer Cell 2008 13 6 472 482 2-s2.0-44449147036 10.1016/j.ccr.2008.05.005
    • (2008) Cancer Cell , vol.13 , Issue.6 , pp. 472-482
    • Kroemer, G.1    Pouyssegur, J.2
  • 163
    • 77953131908 scopus 로고    scopus 로고
    • Targeting mitochondria for cancer therapy
    • 2-s2.0-77953131908 10.1038/nrd3137
    • Fulda S., Galluzzi L., Kroemer G., Targeting mitochondria for cancer therapy. Nature Reviews Drug Discovery 2010 9 6 447 464 2-s2.0-77953131908 10.1038/nrd3137
    • (2010) Nature Reviews Drug Discovery , vol.9 , Issue.6 , pp. 447-464
    • Fulda, S.1    Galluzzi, L.2    Kroemer, G.3
  • 164
    • 79951699777 scopus 로고    scopus 로고
    • Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme
    • 2-s2.0-79951699777 10.1084/jem.20101470
    • Wolf A., Agnihotri S., Micallef J., Mukherjee J., Sabha N., Cairns R., Hawkins C., Guha A., Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme. Journal of Experimental Medicine 2011 208 2 313 326 2-s2.0-79951699777 10.1084/jem.20101470
    • (2011) Journal of Experimental Medicine , vol.208 , Issue.2 , pp. 313-326
    • Wolf, A.1    Agnihotri, S.2    Micallef, J.3    Mukherjee, J.4    Sabha, N.5    Cairns, R.6    Hawkins, C.7    Guha, A.8
  • 165
    • 84870918602 scopus 로고    scopus 로고
    • Mitochondrial localization of TIGAR under hypoxia stimulates HK2 and lowers ROS and cell death
    • Cheung E. C., Ludwig R. L., Vousden K. H., Mitochondrial localization of TIGAR under hypoxia stimulates HK2 and lowers ROS and cell death. Proceedings of the National Academy of Sciences 2012 109 50 20491 20496
    • (2012) Proceedings of the National Academy of Sciences , vol.109 , Issue.50 , pp. 20491-20496
    • Cheung, E.C.1    Ludwig, R.L.2    Vousden, K.H.3
  • 166
    • 34248142302 scopus 로고    scopus 로고
    • 2-Deoxy-D-glucose combined with cisplatin enhances cytotoxicity via metabolic oxidative stress in human head and neck cancer cells
    • 2-s2.0-34248142302 10.1158/0008-5472.CAN-06-3717
    • Simons A. L., Ahmad I. M., Mattson D. M., Dornfeld K. J., Spitz D. R., 2-Deoxy-D-glucose combined with cisplatin enhances cytotoxicity via metabolic oxidative stress in human head and neck cancer cells. Cancer Research 2007 67 7 3364 3370 2-s2.0-34248142302 10.1158/0008-5472.CAN-06-3717
    • (2007) Cancer Research , vol.67 , Issue.7 , pp. 3364-3370
    • Simons, A.L.1    Ahmad, I.M.2    Mattson, D.M.3    Dornfeld, K.J.4    Spitz, D.R.5
  • 167
    • 43649097186 scopus 로고    scopus 로고
    • 3-Bromopyruvate as inhibitor of tumour cell energy metabolism and chemopotentiator of platinum drugs
    • 2-s2.0-43649097186 10.1016/j.molonc.2008.01.003
    • Ihrlund L. S., Hernlund E., Khan O., Shoshan M. C., 3-Bromopyruvate as inhibitor of tumour cell energy metabolism and chemopotentiator of platinum drugs. Molecular Oncology 2008 2 1 94 101 2-s2.0-43649097186 10.1016/j.molonc.2008.01.003
    • (2008) Molecular Oncology , vol.2 , Issue.1 , pp. 94-101
    • Ihrlund, L.S.1    Hernlund, E.2    Khan, O.3    Shoshan, M.C.4
  • 168
    • 34748922322 scopus 로고    scopus 로고
    • Apoptosis-inducing antitumor efficacy of hexokinase II inhibitor in hepatocellular carcinoma
    • 2-s2.0-34748922322 10.1158/1535-7163.MCT-07-0115
    • Kim W., Yoon J.-H., Jeong J.-M., Cheon G.-J., Lee T.-S., Yang J.-I., Park S.-C., Lee H.-S., Apoptosis-inducing antitumor efficacy of hexokinase II inhibitor in hepatocellular carcinoma. Molecular Cancer Therapeutics 2007 6 9 2554 2562 2-s2.0-34748922322 10.1158/1535-7163.MCT-07-0115
    • (2007) Molecular Cancer Therapeutics , vol.6 , Issue.9 , pp. 2554-2562
    • Kim, W.1    Yoon, J.-H.2    Jeong, J.-M.3    Cheon, G.-J.4    Lee, T.-S.5    Yang, J.-I.6    Park, S.-C.7    Lee, H.-S.8
  • 169
    • 46649106720 scopus 로고    scopus 로고
    • Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels
    • 2-s2.0-46649106720 10.1371/journal.pone.0001852 e1852
    • Chiara F., Castellaro D., Marin O., Petronilli V., Brusilow W. S., Juhaszova M., Sollott S. J., Forte M., Bernardi P., Rasola A., Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. PLoS ONE 2008 3 3 2-s2.0-46649106720 10.1371/journal.pone.0001852 e1852
    • (2008) PLoS ONE , vol.3 , Issue.3
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6    Sollott, S.J.7    Forte, M.8    Bernardi, P.9    Rasola, A.10
  • 170
    • 34047168229 scopus 로고    scopus 로고
    • Cooperative cytotoxicity of methyl jasmonate with anti-cancer drugs and 2-deoxy-d-glucose
    • 2-s2.0-34047168229 10.1016/j.canlet.2006.10.013
    • Heyfets A., Flescher E., Cooperative cytotoxicity of methyl jasmonate with anti-cancer drugs and 2-deoxy-d-glucose. Cancer Letters 2007 250 2 300 310 2-s2.0-34047168229 10.1016/j.canlet.2006.10.013
    • (2007) Cancer Letters , vol.250 , Issue.2 , pp. 300-310
    • Heyfets, A.1    Flescher, E.2
  • 171
    • 43049158204 scopus 로고    scopus 로고
    • MAPKs and their relevance to arthritis and inflammation
    • 2-s2.0-43049158204 10.1093/rheumatology/kem297
    • Thalhamer T., McGrath M. A., Harnett M. M., MAPKs and their relevance to arthritis and inflammation. Rheumatology 2008 47 4 409 414 2-s2.0-43049158204 10.1093/rheumatology/kem297
    • (2008) Rheumatology , vol.47 , Issue.4 , pp. 409-414
    • Thalhamer, T.1    McGrath, M.A.2    Harnett, M.M.3
  • 172
    • 0036181363 scopus 로고    scopus 로고
    • Regulation of stress-activated protein kinase signaling pathways by protein phosphatases
    • 2-s2.0-0036181363 10.1046/j.0014-2956.2002.02754.x
    • Tamura S., Hanada M., Ohnishi M., Katsura K., Sasaki M., Kobayashi T., Regulation of stress-activated protein kinase signaling pathways by protein phosphatases. European Journal of Biochemistry 2002 269 4 1060 1066 2-s2.0-0036181363 10.1046/j.0014-2956.2002.02754.x
    • (2002) European Journal of Biochemistry , vol.269 , Issue.4 , pp. 1060-1066
    • Tamura, S.1    Hanada, M.2    Ohnishi, M.3    Katsura, K.4    Sasaki, M.5    Kobayashi, T.6
  • 173
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • 2-s2.0-14444281569 10.1126/science.275.5296.90
    • Ichijo H., Nishida E., Irie K., Ten Dijke P., Saitoh M., Moriguchi T., Takagi M., Matsumoto K., Miyazono K., Gotoh Y., Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997 275 5296 90 94 2-s2.0-14444281569 10.1126/science.275.5296.90
    • (1997) Science , vol.275 , Issue.5296 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3    Ten Dijke, P.4    Saitoh, M.5    Moriguchi, T.6    Takagi, M.7    Matsumoto, K.8    Miyazono, K.9    Gotoh, Y.10
  • 174
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK) - From inflammation to development
    • 2-s2.0-0032054723 10.1016/S0955-0674(98)80143-9
    • Ip Y. T., Davis R. J., Signal transduction by the c-Jun N-terminal kinase (JNK)-from inflammation to development. Current Opinion in Cell Biology 1998 10 2 205 219 2-s2.0-0032054723 10.1016/S0955-0674(98)80143-9
    • (1998) Current Opinion in Cell Biology , vol.10 , Issue.2 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 175
    • 0036803602 scopus 로고    scopus 로고
    • In the cellular garden of forking paths: How p38 MAPKs signal for downstream assistance
    • 2-s2.0-0036803602 10.1515/BC.2002.173
    • Shi Y., Gaestel M., In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance. Biological Chemistry 2002 383 10 1519 1536 2-s2.0-0036803602 10.1515/BC.2002.173
    • (2002) Biological Chemistry , vol.383 , Issue.10 , pp. 1519-1536
    • Shi, Y.1    Gaestel, M.2
  • 176
    • 51349109215 scopus 로고    scopus 로고
    • Multidrug resistance in acute myeloid leukemia: Potential new therapeutics
    • 2-s2.0-51349109215 10.2967/jnumed.107.050153
    • Weisburg J. H., Multidrug resistance in acute myeloid leukemia: potential new therapeutics. Journal of Nuclear Medicine 2008 49 9 1405 1407 2-s2.0-51349109215 10.2967/jnumed.107.050153
    • (2008) Journal of Nuclear Medicine , vol.49 , Issue.9 , pp. 1405-1407
    • Weisburg, J.H.1
  • 177
    • 79960091029 scopus 로고    scopus 로고
    • Innate inflammation and cancer: Is it time for cancer prevention?
    • 2-s2.0-79960091029 10.3410/M3-11
    • Trinchieri G., Innate inflammation and cancer: is it time for cancer prevention? F1000 Medicine Reports 2011 3 1, article 11 2-s2.0-79960091029 10.3410/M3-11
    • (2011) F1000 Medicine Reports , vol.3 , Issue.1 ARTICLE 11
    • Trinchieri, G.1
  • 178
    • 56349144702 scopus 로고    scopus 로고
    • New jasmonate analogues as potential anti-inflammatory agents
    • 2-s2.0-56349144702 10.1016/j.bmc.2008.10.050
    • Dang H. T., Lee H. J., Yoo E. S., Hong J., Bao B., Choi J. S., Jung J. H., New jasmonate analogues as potential anti-inflammatory agents. Bioorganic and Medicinal Chemistry 2008 16 24 10228 10235 2-s2.0-56349144702 10.1016/j.bmc.2008.10.050
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.24 , pp. 10228-10235
    • Dang, H.T.1    Lee, H.J.2    Yoo, E.S.3    Hong, J.4    Bao, B.5    Choi, J.S.6    Jung, J.H.7
  • 180
    • 59549104762 scopus 로고    scopus 로고
    • The role of leukotriene B4 in allergic diseases
    • 2-s2.0-59549104762 10.2332/allergolint.08-RAI-0019
    • Ohnishi H., Miyahara N., Gelfand E. W., The role of leukotriene B4 in allergic diseases. Allergology International 2008 57 4 291 298 2-s2.0-59549104762 10.2332/allergolint.08-RAI-0019
    • (2008) Allergology International , vol.57 , Issue.4 , pp. 291-298
    • Ohnishi, H.1    Miyahara, N.2    Gelfand, E.W.3
  • 182
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: From dissemination to organ-specific colonization
    • 2-s2.0-63049090100 10.1038/nrc2622
    • Nguyen D. X., Bos P. D., Massagué J., Metastasis: from dissemination to organ-specific colonization. Nature Reviews Cancer 2009 9 4 274 284 2-s2.0-63049090100 10.1038/nrc2622
    • (2009) Nature Reviews Cancer , vol.9 , Issue.4 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 183
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • 2-s2.0-33847021147 10.1146/annurev.pharmtox.47.120505.105337
    • Jin Y., Penning T. M., Aldo-keto reductases and bioactivation/ detoxication. Annual Review of Pharmacology and Toxicology 2007 47 263 292 2-s2.0-33847021147 10.1146/annurev.pharmtox.47.120505.105337
    • (2007) Annual Review of Pharmacology and Toxicology , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 184
    • 0031759084 scopus 로고    scopus 로고
    • Identification of a principal mRNA species for human 3 α -hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity
    • 2-s2.0-0031759084
    • Matsuura K., Shiraishi H., Hara A., Sato K., Deyashiki Y., Ninomiya M., Sakai S., Identification of a principal mRNA species for human 3 α -hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. Journal of Biochemistry 1998 124 5 940 946 2-s2.0-0031759084
    • (1998) Journal of Biochemistry , vol.124 , Issue.5 , pp. 940-946
    • Matsuura, K.1    Shiraishi, H.2    Hara, A.3    Sato, K.4    Deyashiki, Y.5    Ninomiya, M.6    Sakai, S.7
  • 185
    • 34547692874 scopus 로고    scopus 로고
    • Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms
    • 2-s2.0-34547692874 10.1016/j.abb.2007.04.024
    • Penning T. M., Drury J. E., Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Archives of Biochemistry and Biophysics 2007 464 2 241 250 2-s2.0-34547692874 10.1016/j.abb.2007.04.024
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.2 , pp. 241-250
    • Penning, T.M.1    Drury, J.E.2
  • 187
    • 0035866794 scopus 로고    scopus 로고
    • Overexpression of dihydrodiol dehydrogenase as a prognostic marker of non-small cell lung cancer
    • 2-s2.0-0035866794
    • Hsu N.-Y., Ho H.-C., Chow K.-C., Lin T.-Y., Shih C.-S., Wang L.-S., Tsai C.-M., Overexpression of dihydrodiol dehydrogenase as a prognostic marker of non-small cell lung cancer. Cancer Research 2001 61 6 2727 2731 2-s2.0-0035866794
    • (2001) Cancer Research , vol.61 , Issue.6 , pp. 2727-2731
    • Hsu, N.-Y.1    Ho, H.-C.2    Chow, K.-C.3    Lin, T.-Y.4    Shih, C.-S.5    Wang, L.-S.6    Tsai, C.-M.7
  • 189
    • 33947713276 scopus 로고    scopus 로고
    • Overexpression of aldo-keto reductase 1C2 as a high-risk factor in bladder cancer
    • 2-s2.0-33947713276
    • Tai H.-L., Lin T.-S., Huang H.-H., Lin T.-Y., Chou M.-C., Chiou S.-H., Chow K.-C., Overexpression of aldo-keto reductase 1C2 as a high-risk factor in bladder cancer. Oncology Reports 2007 17 2 305 311 2-s2.0-33947713276
    • (2007) Oncology Reports , vol.17 , Issue.2 , pp. 305-311
    • Tai, H.-L.1    Lin, T.-S.2    Huang, H.-H.3    Lin, T.-Y.4    Chou, M.-C.5    Chiou, S.-H.6    Chow, K.-C.7
  • 190
    • 0037177887 scopus 로고    scopus 로고
    • Increased expression of dihydrodiol dehydrogenase induces resistance to cisplatin in human ovarian carcinoma cells
    • 2-s2.0-0037177887 10.1074/jbc.M112028200
    • Deng H. B., Parekh H. K., Chow K.-C., Simpkins H., Increased expression of dihydrodiol dehydrogenase induces resistance to cisplatin in human ovarian carcinoma cells. The Journal of Biological Chemistry 2002 277 17 15035 15043 2-s2.0-0037177887 10.1074/jbc.M112028200
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 15035-15043
    • Deng, H.B.1    Parekh, H.K.2    Chow, K.-C.3    Simpkins, H.4
  • 191
    • 15544379141 scopus 로고    scopus 로고
    • Overexpression of dihydrodiol dehydrogenase is associated with cisplatin-based chemotherapy resistance in ovarian cancer patients
    • 2-s2.0-15544379141 10.1016/j.ygyno.2004.12.031
    • Chen Y.-J., Yuan C.-C., Chow K.-C., Wang P.-H., Lai C.-R., Yen M.-S., Wang L.-S., Overexpression of dihydrodiol dehydrogenase is associated with cisplatin-based chemotherapy resistance in ovarian cancer patients. Gynecologic Oncology 2005 97 1 110 117 2-s2.0-15544379141 10.1016/j.ygyno.2004.12.031
    • (2005) Gynecologic Oncology , vol.97 , Issue.1 , pp. 110-117
    • Chen, Y.-J.1    Yuan, C.-C.2    Chow, K.-C.3    Wang, P.-H.4    Lai, C.-R.5    Yen, M.-S.6    Wang, L.-S.7
  • 192
    • 84865982067 scopus 로고    scopus 로고
    • Regulation of aldo-keto reductases in human diseases
    • Chen W. D., Zhang Y., Regulation of aldo-keto reductases in human diseases. Frontiers in Pharmacology 2012 3, article 35
    • (2012) Frontiers in Pharmacology , vol.335
    • Chen, W.D.1    Zhang, Y.2
  • 193
    • 0033988708 scopus 로고    scopus 로고
    • Development of daunorubicin resistance in tumour cells by induction of carbonyl reduction
    • 2-s2.0-0033988708 10.1016/S0006-2952(99)00322-6
    • Ax W., Soldan M., Koch L., Maser E., Development of daunorubicin resistance in tumour cells by induction of carbonyl reduction. Biochemical Pharmacology 2000 59 3 293 300 2-s2.0-0033988708 10.1016/S0006-2952(99)00322-6
    • (2000) Biochemical Pharmacology , vol.59 , Issue.3 , pp. 293-300
    • Ax, W.1    Soldan, M.2    Koch, L.3    Maser, E.4
  • 194
    • 0036746965 scopus 로고    scopus 로고
    • Inhibition of aldose reductase enhances Hela cell sensitivity to chemotherapeutic drugs and involves activation of extracellular signal-regulated kinases
    • 2-s2.0-0036746965 10.1097/00001813-200209000-00012
    • Lee E. K., Regenold W. T., Shapiro P., Inhibition of aldose reductase enhances Hela cell sensitivity to chemotherapeutic drugs and involves activation of extracellular signal-regulated kinases. Anti-Cancer Drugs 2002 13 8 859 868 2-s2.0-0036746965 10.1097/00001813-200209000-00012
    • (2002) Anti-Cancer Drugs , vol.13 , Issue.8 , pp. 859-868
    • Lee, E.K.1    Regenold, W.T.2    Shapiro, P.3
  • 195
    • 84896869019 scopus 로고    scopus 로고
    • Lipoxygenases, apoptosis, and the role of antioxidants
    • Advances in Photosynthesis and Respiration
    • Maccarrone M., Lipoxygenases, apoptosis, and the role of antioxidants. Photoprotection, Photoinhibition, Gene Regulation, and Environment 2008 21 321 332 Advances in Photosynthesis and Respiration
    • (2008) Photoprotection, Photoinhibition, Gene Regulation, and Environment , vol.21 , pp. 321-332
    • Maccarrone, M.1
  • 196
    • 0033588022 scopus 로고    scopus 로고
    • Lipoxygenases: Occurrence, functions, catalysis, and acquisition of substrate
    • 2-s2.0-0033588022 10.1074/jbc.274.34.23679
    • Brash A. R., Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. The Journal of Biological Chemistry 1999 274 34 23679 23682 2-s2.0-0033588022 10.1074/jbc.274.34.23679
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.34 , pp. 23679-23682
    • Brash, A.R.1
  • 197
    • 16244389350 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors as potential anti-inflammatory agents
    • 2-s2.0-16244389350 10.2174/1381612053507521
    • Meyer M. C., Rastogi P., Beckett C. S., McHowat J., Phospholipase A2 inhibitors as potential anti-inflammatory agents. Current Pharmaceutical Design 2005 11 10 1301 1312 2-s2.0-16244389350 10.2174/1381612053507521
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.10 , pp. 1301-1312
    • Meyer, M.C.1    Rastogi, P.2    Beckett, C.S.3    McHowat, J.4
  • 198
    • 84859738661 scopus 로고    scopus 로고
    • Chronic inflammatory diseases are stimulated by current lifestyle: How diet, stress levels and medication prevent our body from recovering
    • 2-s2.0-84859738661 10.1186/1743-7075-9-32
    • Bosma-den Boer M. M., van Wetten M.-L., Pruimboom L., Chronic inflammatory diseases are stimulated by current lifestyle: how diet, stress levels and medication prevent our body from recovering. Nutrition & Metabolism 2012 9, article 32 2-s2.0-84859738661 10.1186/1743-7075-9-32
    • (2012) Nutrition & Metabolism , vol.932
    • Bosma-Den Boer, M.M.1    Van Wetten, M.-L.2    Pruimboom, L.3
  • 200
    • 0036728051 scopus 로고    scopus 로고
    • Lipoxygenase inhibitors attenuate growth of human pancreatic cancer xenografts and induce apoptosis through the mitochondrial pathway
    • 2-s2.0-0036728051
    • Tong W.-G., Ding X.-Z., Witt R. C., Adrian T. E., Lipoxygenase inhibitors attenuate growth of human pancreatic cancer xenografts and induce apoptosis through the mitochondrial pathway. Molecular Cancer Therapeutics 2002 1 11 929 935 2-s2.0-0036728051
    • (2002) Molecular Cancer Therapeutics , vol.1 , Issue.11 , pp. 929-935
    • Tong, W.-G.1    Ding, X.-Z.2    Witt, R.C.3    Adrian, T.E.4
  • 201
    • 0036384212 scopus 로고    scopus 로고
    • The mechanisms of lipoxygenase inhibitor-induced apoptosis in human breast cancer cells
    • 2-s2.0-0036384212 10.1016/S0006-291X(02)02014-4
    • Tong W.-G., Ding X.-Z., Adrian T. E., The mechanisms of lipoxygenase inhibitor-induced apoptosis in human breast cancer cells. Biochemical and Biophysical Research Communications 2002 296 4 942 948 2-s2.0-0036384212 10.1016/S0006-291X(02)02014-4
    • (2002) Biochemical and Biophysical Research Communications , vol.296 , Issue.4 , pp. 942-948
    • Tong, W.-G.1    Ding, X.-Z.2    Adrian, T.E.3
  • 202
    • 4444354992 scopus 로고    scopus 로고
    • Contributory role of 5-lipoxygenase and its association with angiogenesis in the promotion of inflammation-associated colonic tumorigenesis by cigarette smoking
    • 2-s2.0-4444354992 10.1016/j.tox.2004.06.004
    • Ye Y.-N., Liu E. S.-L., Shin V. Y., Wu W. K.-K., Cho C.-H., Contributory role of 5-lipoxygenase and its association with angiogenesis in the promotion of inflammation-associated colonic tumorigenesis by cigarette smoking. Toxicology 2004 203 1-3 179 188 2-s2.0-4444354992 10.1016/j.tox.2004.06.004
    • (2004) Toxicology , vol.203 , Issue.1-3 , pp. 179-188
    • Ye, Y.-N.1    Liu, E.S.-L.2    Shin, V.Y.3    Wu, W.K.-K.4    Cho, C.-H.5
  • 203
    • 23944483974 scopus 로고    scopus 로고
    • LTB4 stimulates growth of human pancreatic cancer cells via MAPK and PI-3 kinase pathways
    • 2-s2.0-23944483974 10.1016/j.bbrc.2005.07.166
    • Tong W.-G., Ding X.-Z., Talamonti M. S., Bell R. H., Adrian T. E., LTB4 stimulates growth of human pancreatic cancer cells via MAPK and PI-3 kinase pathways. Biochemical and Biophysical Research Communications 2005 335 3 949 956 2-s2.0-23944483974 10.1016/j.bbrc.2005.07.166
    • (2005) Biochemical and Biophysical Research Communications , vol.335 , Issue.3 , pp. 949-956
    • Tong, W.-G.1    Ding, X.-Z.2    Talamonti, M.S.3    Bell, R.H.4    Adrian, T.E.5
  • 204
    • 0031577170 scopus 로고    scopus 로고
    • Arachidonic acid stimulates prostate cancer cell growth: Critical role of 5-lipoxygenase
    • 2-s2.0-0031577170 10.1006/bbrc.1997.6799
    • Ghosh J., Myers C. E., Arachidonic acid stimulates prostate cancer cell growth: critical role of 5-lipoxygenase. Biochemical and Biophysical Research Communications 1997 235 2 418 423 2-s2.0-0031577170 10.1006/bbrc.1997.6799
    • (1997) Biochemical and Biophysical Research Communications , vol.235 , Issue.2 , pp. 418-423
    • Ghosh, J.1    Myers, C.E.2
  • 205
    • 0036896107 scopus 로고    scopus 로고
    • 5(S)-hydroxy-6,8,11,14-E,Z,Z,Z-eicosatetraenoate stimulates PC3 cell signaling and growth by a receptor-dependent mechanism
    • 2-s2.0-0036896107
    • O'Flaherty J. T., Rogers L. C., Chadwell B. A., Owen J. S., Rao A., Cramer S. D., Daniel L. W., 5(S)-hydroxy-6,8,11,14-E,Z,Z,Z-eicosatetraenoate stimulates PC3 cell signaling and growth by a receptor-dependent mechanism. Cancer Research 2002 62 23 6817 6819 2-s2.0-0036896107
    • (2002) Cancer Research , vol.62 , Issue.23 , pp. 6817-6819
    • O'Flaherty, J.T.1    Rogers, L.C.2    Chadwell, B.A.3    Owen, J.S.4    Rao, A.5    Cramer, S.D.6    Daniel, L.W.7
  • 206
    • 4444354992 scopus 로고    scopus 로고
    • Contributory role of 5-lipoxygenase and its association with angiogenesis in the promotion of inflammation-associated colonic tumorigenesis by cigarette smoking
    • 2-s2.0-4444354992 10.1016/j.tox.2004.06.004
    • Ye Y.-N., Liu E. S.-L., Shin V. Y., Wu W. K.-K., Cho C.-H., Contributory role of 5-lipoxygenase and its association with angiogenesis in the promotion of inflammation-associated colonic tumorigenesis by cigarette smoking. Toxicology 2004 203 1-3 179 188 2-s2.0-4444354992 10.1016/j.tox.2004.06.004
    • (2004) Toxicology , vol.203 , Issue.1-3 , pp. 179-188
    • Ye, Y.-N.1    Liu, E.S.-L.2    Shin, V.Y.3    Wu, W.K.-K.4    Cho, C.-H.5
  • 207
    • 0031737260 scopus 로고    scopus 로고
    • 5-Lipoxygenase inhibitors reduce PC-3 cell proliferation and initiate nonnecrotic cell death
    • Anderson K. M., Seed T., Vos M., Mulshine J., Meng J., Alrefai W., Ou D., Harris J. E., 5-Lipoxygenase inhibitors reduce PC-3 cell proliferation and initiate nonnecrotic cell death. Prostate 1998 37 3 161 173
    • (1998) Prostate , vol.37 , Issue.3 , pp. 161-173
    • Anderson, K.M.1    Seed, T.2    Vos, M.3    Mulshine, J.4    Meng, J.5    Alrefai, W.6    Ou, D.7    Harris, J.E.8
  • 208
    • 0035458615 scopus 로고    scopus 로고
    • Five-lipoxygenase inhibitors can mediate apoptosis in human breast cancer cell lines through complex eicosanoid interactions
    • 2-s2.0-0035458615
    • Avis I., Hong S. H., Martinez A., Moody T., Choi Y. H., Trepel J., Das R., Jett M., Mulshine J. L., Five-lipoxygenase inhibitors can mediate apoptosis in human breast cancer cell lines through complex eicosanoid interactions. The FASEB Journal 2001 15 11 2007 2009 2-s2.0-0035458615
    • (2001) The FASEB Journal , vol.15 , Issue.11 , pp. 2007-2009
    • Avis, I.1    Hong, S.H.2    Martinez, A.3    Moody, T.4    Choi, Y.H.5    Trepel, J.6    Das, R.7    Jett, M.8    Mulshine, J.L.9
  • 209
    • 9144224191 scopus 로고    scopus 로고
    • Five-lipoxygenase-activating protein inhibitor MK-886 induces apoptosis in gastric cancer through upregulation of p27kip1 and bax
    • 2-s2.0-9144224191 10.1111/j.1440-1746.2004.03194.x
    • Fan X. M., Tu S. P., Lam S. K., Wang W. P., Wu J., Wong W. M., Yuen M. F., Lin M. C. M., Kung H. F., Wong B. C.-Y., Five-lipoxygenase-activating protein inhibitor MK-886 induces apoptosis in gastric cancer through upregulation of p27kip1 and bax. Journal of Gastroenterology and Hepatology 2004 19 1 31 37 2-s2.0-9144224191 10.1111/j.1440-1746.2004.03194.x
    • (2004) Journal of Gastroenterology and Hepatology , vol.19 , Issue.1 , pp. 31-37
    • Fan, X.M.1    Tu, S.P.2    Lam, S.K.3    Wang, W.P.4    Wu, J.5    Wong, W.M.6    Yuen, M.F.7    Lin, M.C.M.8    Kung, H.F.9    Wong, B.C.-Y.10
  • 210
    • 7444227449 scopus 로고    scopus 로고
    • The effects of TNF-alpha and inhibitors of arachidonic acid metabolism on human colon HT-29 cells depend on differentiation status
    • Kovarikova M., Hofmanova J., Soucek K., Kozubik A., The effects of TNF-alpha and inhibitors of arachidonic acid metabolism on human colon HT-29 cells depend on differentiation status. Differentiation 2004 72 1 23 31
    • (2004) Differentiation , vol.72 , Issue.1 , pp. 23-31
    • Kovarikova, M.1    Hofmanova, J.2    Soucek, K.3    Kozubik, A.4
  • 211
    • 20244363504 scopus 로고    scopus 로고
    • Increased 5-lipoxygenase expression and induction of apoptosis by its inhibitors in esophageal cancer: A potential target for prevention
    • 2-s2.0-20244363504 10.1093/carcin/bgi026
    • Hoque A., Lippman S. M., Wu T.-T., Xu Y., Liang Z. D., Swisher S., Zhang H., Cao L., Ajani J. A., Xu X.-C., Increased 5-lipoxygenase expression and induction of apoptosis by its inhibitors in esophageal cancer: a potential target for prevention. Carcinogenesis 2005 26 4 785 791 2-s2.0-20244363504 10.1093/carcin/bgi026
    • (2005) Carcinogenesis , vol.26 , Issue.4 , pp. 785-791
    • Hoque, A.1    Lippman, S.M.2    Wu, T.-T.3    Xu, Y.4    Liang, Z.D.5    Swisher, S.6    Zhang, H.7    Cao, L.8    Ajani, J.A.9    Xu, X.-C.10
  • 212
    • 33750614657 scopus 로고    scopus 로고
    • Five-lipoxygenase pathway of arachidonic acid metabolism in carcinogenesis and cancer chemoprevention
    • 2-s2.0-33750614657 10.2174/156800906778742451
    • Chen X., Sood S., Yang C. S., Li N., Sun Z., Five-lipoxygenase pathway of arachidonic acid metabolism in carcinogenesis and cancer chemoprevention. Current Cancer Drug Targets 2006 6 7 613 622 2-s2.0-33750614657 10.2174/156800906778742451
    • (2006) Current Cancer Drug Targets , vol.6 , Issue.7 , pp. 613-622
    • Chen, X.1    Sood, S.2    Yang, C.S.3    Li, N.4    Sun, Z.5
  • 214
    • 0141988847 scopus 로고    scopus 로고
    • Expression of lipoxygenase in human bladder carcinoma and growth inhibition by its inhibitors
    • 2-s2.0-0141988847 10.1097/01.ju.0000080296.54262.c8
    • Yoshimura R., Matsuyama M., Tsuchida K., Kawahito Y., Sano H., Nakatani T., Expression of lipoxygenase in human bladder carcinoma and growth inhibition by its inhibitors. Journal of Urology 2003 170 5 1994 1999 2-s2.0-0141988847 10.1097/01.ju.0000080296.54262.c8
    • (2003) Journal of Urology , vol.170 , Issue.5 , pp. 1994-1999
    • Yoshimura, R.1    Matsuyama, M.2    Tsuchida, K.3    Kawahito, Y.4    Sano, H.5    Nakatani, T.6
  • 215
    • 0038167016 scopus 로고    scopus 로고
    • The deregulation of arachidonic acid metabolism-related genes in human esophageal squamous cell carcinoma
    • 2-s2.0-0038167016 10.1002/ijc.11225
    • Zhi H., Zhang J., Hu G., Lu J., Wang X., Zhou C., Wu M., Liu Z., The deregulation of arachidonic acid metabolism-related genes in human esophageal squamous cell carcinoma. International Journal of Cancer 2003 106 3 327 333 2-s2.0-0038167016 10.1002/ijc.11225
    • (2003) International Journal of Cancer , vol.106 , Issue.3 , pp. 327-333
    • Zhi, H.1    Zhang, J.2    Hu, G.3    Lu, J.4    Wang, X.5    Zhou, C.6    Wu, M.7    Liu, Z.8
  • 217
    • 84865209780 scopus 로고    scopus 로고
    • Tumor 5-lipoxygenase expression correlates with gastric cancer metastasis and its selective inhibitor induces cancer cell apoptosis
    • Zou L.-Y., Li J.-Y., Chen F.-L., Chen Z.-X., Wang X.-Z., Tumor 5-lipoxygenase expression correlates with gastric cancer metastasis and its selective inhibitor induces cancer cell apoptosis. Journal of Cancer Molecules 2006 2 6 227 233
    • (2006) Journal of Cancer Molecules , vol.2 , Issue.6 , pp. 227-233
    • Zou, L.-Y.1    Li, J.-Y.2    Chen, F.-L.3    Chen, Z.-X.4    Wang, X.-Z.5
  • 218
    • 0035162355 scopus 로고    scopus 로고
    • 5-Lipoxygenase regulates malignant mesothelial cell survival: Involvement of vascular endothelial growth factor
    • 2-s2.0-0035162355 10.1096/fj.01-0150com
    • Romano M., Catalano A., Nutini M., D'Urbano E., Crescenzi C., Claria J., Libner R., Davi G., Procopio A., 5-Lipoxygenase regulates malignant mesothelial cell survival: involvement of vascular endothelial growth factor. The FASEB Journal 2001 15 13 2326 2336 2-s2.0-0035162355 10.1096/fj.01-0150com
    • (2001) The FASEB Journal , vol.15 , Issue.13 , pp. 2326-2336
    • Romano, M.1    Catalano, A.2    Nutini, M.3    D'Urbano, E.4    Crescenzi, C.5    Claria, J.6    Libner, R.7    Davi, G.8    Procopio, A.9
  • 220
    • 0026702580 scopus 로고
    • Differential expression of arachidonate 5-lipoxygenase transcripts in human brain tumors: Evidence for the expression of a multitranscript family
    • 2-s2.0-0026702580 10.1073/pnas.89.19.9044
    • Boado R. J., Pardridge W. M., Vinters H. V., Black K. L., Differential expression of arachidonate 5-lipoxygenase transcripts in human brain tumors: evidence for the expression of a multitranscript family. Proceedings of the National Academy of Sciences of the United States of America 1992 89 19 9044 9048 2-s2.0-0026702580 10.1073/pnas.89.19.9044
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , Issue.19 , pp. 9044-9048
    • Boado, R.J.1    Pardridge, W.M.2    Vinters, H.V.3    Black, K.L.4
  • 221
    • 0028904461 scopus 로고
    • Chemoprevention of colon carcinogenesis by sulindac, a nonsteroidal anti- inflammatory agent
    • 2-s2.0-0028904461
    • Rao C. V., Rivenson A., Simi B., Zang E., Kelloff G., Steele V., Reddy B. S., Chemoprevention of colon carcinogenesis by sulindac, a nonsteroidal anti- inflammatory agent. Cancer Research 1995 55 7 1464 1472 2-s2.0-0028904461
    • (1995) Cancer Research , vol.55 , Issue.7 , pp. 1464-1472
    • Rao, C.V.1    Rivenson, A.2    Simi, B.3    Zang, E.4    Kelloff, G.5    Steele, V.6    Reddy, B.S.7
  • 222
    • 80053110423 scopus 로고    scopus 로고
    • 5-Lipoxygenase contributes to the progression of hepatocellular carcinoma
    • 2-s2.0-80053110423 10.3892/mmr.2011.547
    • Xu X.-M., Deng J.-J., Yuan G.-J., Yang F., Guo H.-T., Xiang M., Ge W., Wu Y.-G., 5-Lipoxygenase contributes to the progression of hepatocellular carcinoma. Molecular Medicine Reports 2011 4 6 1195 1200 2-s2.0-80053110423 10.3892/mmr.2011.547
    • (2011) Molecular Medicine Reports , vol.4 , Issue.6 , pp. 1195-1200
    • Xu, X.-M.1    Deng, J.-J.2    Yuan, G.-J.3    Yang, F.4    Guo, H.-T.5    Xiang, M.6    Ge, W.7    Wu, Y.-G.8
  • 223
    • 54049153617 scopus 로고    scopus 로고
    • Expression of enzymes and receptors of the leukotriene pathway in human neuroblastoma promotes tumor survival and provides a target for therapy
    • 2-s2.0-54049153617 10.1096/fj.07-103457
    • Sveinbjörnsson B., Rasmuson A., Baryawno N., Wan M., Pettersen I., Ponthan F., Orrego A., Haeggström J. Z., Johnsen J. I., Kogner P., Expression of enzymes and receptors of the leukotriene pathway in human neuroblastoma promotes tumor survival and provides a target for therapy. The FASEB Journal 2008 22 10 3525 3536 2-s2.0-54049153617 10.1096/fj.07-103457
    • (2008) The FASEB Journal , vol.22 , Issue.10 , pp. 3525-3536
    • Sveinbjörnsson, B.1    Rasmuson, A.2    Baryawno, N.3    Wan, M.4    Pettersen, I.5    Ponthan, F.6    Orrego, A.7    Haeggström, J.Z.8    Johnsen, J.I.9    Kogner, P.10
  • 225
    • 70549103224 scopus 로고    scopus 로고
    • 5-lipoxygenase pathway promotes cell proliferation in human glioma cell lines
    • 2-s2.0-70549103224
    • Ishii K., Zaitsu M., Yonemitsu N., Kan Y., Hamasaki Y., Matsuo M., 5-lipoxygenase pathway promotes cell proliferation in human glioma cell lines. Clinical Neuropathology 2009 28 6 445 452 2-s2.0-70549103224
    • (2009) Clinical Neuropathology , vol.28 , Issue.6 , pp. 445-452
    • Ishii, K.1    Zaitsu, M.2    Yonemitsu, N.3    Kan, Y.4    Hamasaki, Y.5    Matsuo, M.6
  • 226
    • 84865399705 scopus 로고    scopus 로고
    • Increased expression of the 5-lipoxygenase pathway and its cellular localization in Barrett's adenocarcinoma
    • Boger P. C., Shutt J. D., Neale J. R., Increased expression of the 5-lipoxygenase pathway and its cellular localization in Barrett's adenocarcinoma. Histopathology 2012 61 509 517
    • (2012) Histopathology , vol.61 , pp. 509-517
    • Boger, P.C.1    Shutt, J.D.2    Neale, J.R.3
  • 227
    • 33747875667 scopus 로고    scopus 로고
    • Involvement of the 5-lipoxygenase/leukotriene A4 hydrolase pathway in 7,12-dimethylbenz[a]anthracene (DMBA)-induced oral carcinogenesis in hamster cheek pouch, and inhibition of carcinogenesis by its inhibitors
    • 2-s2.0-33747875667 10.1093/carcin/bgl039
    • Sun Z., Sood S., Li N., Ramji D., Yang P., Newman R. A., Yang C. S., Chen X., Involvement of the 5-lipoxygenase/leukotriene A4 hydrolase pathway in 7,12-dimethylbenz[a]anthracene (DMBA)-induced oral carcinogenesis in hamster cheek pouch, and inhibition of carcinogenesis by its inhibitors. Carcinogenesis 2006 27 9 1902 1908 2-s2.0-33747875667 10.1093/carcin/bgl039
    • (2006) Carcinogenesis , vol.27 , Issue.9 , pp. 1902-1908
    • Sun, Z.1    Sood, S.2    Li, N.3    Ramji, D.4    Yang, P.5    Newman, R.A.6    Yang, C.S.7    Chen, X.8
  • 228
    • 84866412878 scopus 로고    scopus 로고
    • Prevalence of 5-lipoxygenase expression in canine osteosarcoma and the effects of a dual 5-lipoxygenase/cyclooxygenase inhibitor on osteosarcoma cells in vitro and in vivo
    • Goupil R. C., Bushey J. J., Peters-Kennedy J., Wakshlag J. J., Prevalence of 5-lipoxygenase expression in canine osteosarcoma and the effects of a dual 5-lipoxygenase/cyclooxygenase inhibitor on osteosarcoma cells in vitro and in vivo. Veterinary Pathology 2012 49 5 802 810
    • (2012) Veterinary Pathology , vol.49 , Issue.5 , pp. 802-810
    • Goupil, R.C.1    Bushey, J.J.2    Peters-Kennedy, J.3    Wakshlag, J.J.4
  • 229
    • 0029740056 scopus 로고    scopus 로고
    • Inhibition of tumour growth by lipoxygenase inhibitors
    • 2-s2.0-0029740056
    • Hussey H. J., Tisdale M. J., Inhibition of tumour growth by lipoxygenase inhibitors. British Journal of Cancer 1996 74 5 683 687 2-s2.0-0029740056
    • (1996) British Journal of Cancer , vol.74 , Issue.5 , pp. 683-687
    • Hussey, H.J.1    Tisdale, M.J.2
  • 231
    • 77957240474 scopus 로고    scopus 로고
    • 5-Lipoxygenase inhibitors induce potent anti-proliferative and cytotoxic effects in human tumour cells independently of suppression of 5-lipoxygenase activity
    • 2-s2.0-77957240474 10.1111/j.1476-5381.2010.00915.x
    • Fischer A. S., Metzner J., Steinbrink S. D., Ulrich S., Angioni C., Geisslinger G., Steinhilber D., Maier T. J., 5-Lipoxygenase inhibitors induce potent anti-proliferative and cytotoxic effects in human tumour cells independently of suppression of 5-lipoxygenase activity. British Journal of Pharmacology 2010 161 4 936 949 2-s2.0-77957240474 10.1111/j.1476-5381.2010. 00915.x
    • (2010) British Journal of Pharmacology , vol.161 , Issue.4 , pp. 936-949
    • Fischer, A.S.1    Metzner, J.2    Steinbrink, S.D.3    Ulrich, S.4    Angioni, C.5    Geisslinger, G.6    Steinhilber, D.7    Maier, T.J.8
  • 232
    • 0032573175 scopus 로고    scopus 로고
    • Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells
    • 2-s2.0-0032573175 10.1073/pnas.95.22.13182
    • Ghosh J., Myers C. E., Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells. Proceedings of the National Academy of Sciences of the United States of America 1998 95 22 13182 13187 2-s2.0-0032573175 10.1073/pnas.95.22.13182
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.22 , pp. 13182-13187
    • Ghosh, J.1    Myers, C.E.2
  • 233
    • 0034605252 scopus 로고    scopus 로고
    • 5-HETE congeners as modulators of cell proliferation
    • 2-s2.0-0034605252 10.1016/S0960-894X(00)00370-X
    • Miller T. A., Ghosh J., Myers C. E., Macdonald T. L., 5-HETE congeners as modulators of cell proliferation. Bioorganic and Medicinal Chemistry Letters 2000 10 17 1913 1916 2-s2.0-0034605252 10.1016/S0960-894X(00)00370-X
    • (2000) Bioorganic and Medicinal Chemistry Letters , vol.10 , Issue.17 , pp. 1913-1916
    • Miller, T.A.1    Ghosh, J.2    Myers, C.E.3    Macdonald, T.L.4
  • 234
    • 0038013796 scopus 로고    scopus 로고
    • Inhibition of arachidonate 5-lipoxygenase triggers prostate cancer cell death through rapid activation of c-Jun N-terminal kinase
    • 2-s2.0-0038013796 10.1016/S0006-291X(03)01201-4
    • Ghosh J., Inhibition of arachidonate 5-lipoxygenase triggers prostate cancer cell death through rapid activation of c-Jun N-terminal kinase. Biochemical and Biophysical Research Communications 2003 307 2 342 349 2-s2.0-0038013796 10.1016/S0006-291X(03)01201-4
    • (2003) Biochemical and Biophysical Research Communications , vol.307 , Issue.2 , pp. 342-349
    • Ghosh, J.1
  • 235
    • 0034904380 scopus 로고    scopus 로고
    • Lipoxygenases and their involvement in programmed cell death
    • 2-s2.0-0034904380 10.1038/sj.cdd.4400908
    • Maccarrone M., Melino G., Finazzi-Agrò A., Lipoxygenases and their involvement in programmed cell death. Cell Death and Differentiation 2001 8 8 776 784 2-s2.0-0034904380 10.1038/sj.cdd.4400908
    • (2001) Cell Death and Differentiation , vol.8 , Issue.8 , pp. 776-784
    • Maccarrone, M.1    Melino, G.2    Finazzi-Agrò, A.3
  • 236
    • 0037378120 scopus 로고    scopus 로고
    • Leukotriene synthesis by epithelial cells
    • 2-s2.0-0037378120
    • Luo M., Lee S., Brock T. G., Leukotriene synthesis by epithelial cells. Histology and Histopathology 2003 18 2 587 595 2-s2.0-0037378120
    • (2003) Histology and Histopathology , vol.18 , Issue.2 , pp. 587-595
    • Luo, M.1    Lee, S.2    Brock, T.G.3
  • 237
    • 27544516027 scopus 로고    scopus 로고
    • Stress-induced nuclear export of 5-lipoxygenase
    • 2-s2.0-27544516027 10.1016/j.bbrc.2005.09.001
    • Hanaka H., Shimizu T., Izumi T., Stress-induced nuclear export of 5-lipoxygenase. Biochemical and Biophysical Research Communications 2005 338 1 111 116 2-s2.0-27544516027 10.1016/j.bbrc.2005.09.001
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 111-116
    • Hanaka, H.1    Shimizu, T.2    Izumi, T.3
  • 238
    • 33750102847 scopus 로고    scopus 로고
    • Therapeutic options for 5-lipoxygenase inhibitors
    • 2-s2.0-33750102847 10.1016/j.pharmthera.2006.05.009
    • Werz O., Steinhilber D., Therapeutic options for 5-lipoxygenase inhibitors. Pharmacology and Therapeutics 2006 112 3 701 718 2-s2.0-33750102847 10.1016/j.pharmthera.2006.05.009
    • (2006) Pharmacology and Therapeutics , vol.112 , Issue.3 , pp. 701-718
    • Werz, O.1    Steinhilber, D.2
  • 239
    • 77957240474 scopus 로고    scopus 로고
    • 5-Lipoxygenase inhibitors induce potent anti-proliferative and cytotoxic effects in human tumour cells independently of suppression of 5-lipoxygenase activity
    • 2-s2.0-77957240474 10.1111/j.1476-5381.2010.00915.x
    • Fischer A. S., Metzner J., Steinbrink S. D., Ulrich S., Angioni C., Geisslinger G., Steinhilber D., Maier T. J., 5-Lipoxygenase inhibitors induce potent anti-proliferative and cytotoxic effects in human tumour cells independently of suppression of 5-lipoxygenase activity. British Journal of Pharmacology 2010 161 4 936 949 2-s2.0-77957240474 10.1111/j.1476-5381.2010. 00915.x
    • (2010) British Journal of Pharmacology , vol.161 , Issue.4 , pp. 936-949
    • Fischer, A.S.1    Metzner, J.2    Steinbrink, S.D.3    Ulrich, S.4    Angioni, C.5    Geisslinger, G.6    Steinhilber, D.7    Maier, T.J.8
  • 241
    • 84866880994 scopus 로고    scopus 로고
    • A new jasmonic acid stereoisomeric derivative induces apoptosis via reactive oxygen species in human prostate cancer cells
    • Russo A., Espinoza C. L., Caggia S., A new jasmonic acid stereoisomeric derivative induces apoptosis via reactive oxygen species in human prostate cancer cells. Cancer Letters 2012 326 2 199 205
    • (2012) Cancer Letters , vol.326 , Issue.2 , pp. 199-205
    • Russo, A.1    Espinoza, C.L.2    Caggia, S.3
  • 242
    • 84862546573 scopus 로고    scopus 로고
    • Inflammation and cancer: Chemical approaches to mechanisms, imaging, and treatment
    • Marnett L. J., Inflammation and cancer: chemical approaches to mechanisms, imaging, and treatment. The Journal of Organic Chemistry 2012 77 12 5224 5238
    • (2012) The Journal of Organic Chemistry , vol.77 , Issue.12 , pp. 5224-5238
    • Marnett, L.J.1
  • 243
    • 84870166894 scopus 로고    scopus 로고
    • Cancer prevention with promising natural products: Mechanisms of action and molecular targets
    • Pratheeshkumar P., Sreekala C., Zhang Z., Cancer prevention with promising natural products: mechanisms of action and molecular targets. Anti-Cancer Agents in Medicinal Chemistry 2012 12 10 1159 1184
    • (2012) Anti-Cancer Agents in Medicinal Chemistry , vol.12 , Issue.10 , pp. 1159-1184
    • Pratheeshkumar, P.1    Sreekala, C.2    Zhang, Z.3
  • 244
    • 34848871080 scopus 로고    scopus 로고
    • Targeted agents: The rules of combination
    • 2-s2.0-34848871080 10.1158/1078-0432.CCR-07-1385
    • Kwak E. L., Clark J. W., Chabner B., Targeted agents: the rules of combination. Clinical Cancer Research 2007 13 18 5232 5237 2-s2.0-34848871080 10.1158/1078-0432.CCR-07-1385
    • (2007) Clinical Cancer Research , vol.13 , Issue.18 , pp. 5232-5237
    • Kwak, E.L.1    Clark, J.W.2    Chabner, B.3
  • 245
    • 78650934857 scopus 로고    scopus 로고
    • Informatics of drug synergism in naturally occurring anticancer agents
    • 2-s2.0-78650934857 10.2174/157489211793980105
    • Ghavami G., Kazemali M. R., Sardari S., Informatics of drug synergism in naturally occurring anticancer agents. Recent Patents on Anti-Cancer Drug Discovery 2011 6 1 26 44 2-s2.0-78650934857 10.2174/157489211793980105
    • (2011) Recent Patents on Anti-Cancer Drug Discovery , vol.6 , Issue.1 , pp. 26-44
    • Ghavami, G.1    Kazemali, M.R.2    Sardari, S.3
  • 246
    • 84876129955 scopus 로고    scopus 로고
    • Combinations of plant polyphenols & anti-cancer molecules: A novel treatment strategy for cancer chemotherapy
    • Mohan A., Narayanan S., Sethuraman S., Krishnan U. M., Combinations of plant polyphenols & anti-cancer molecules: a novel treatment strategy for cancer chemotherapy. Anti-Cancer Agents in Medicinal Chemistry 2013 13 2 281 295
    • (2013) Anti-Cancer Agents in Medicinal Chemistry , vol.13 , Issue.2 , pp. 281-295
    • Mohan, A.1    Narayanan, S.2    Sethuraman, S.3    Krishnan, U.M.4
  • 248
    • 84874454497 scopus 로고    scopus 로고
    • Phytochemicals as chemosensitizers: From molecular mechanism to clinical significance
    • Vinod B. S., Maliekal T. T., Anto R. J., Phytochemicals as chemosensitizers: from molecular mechanism to clinical significance. Antioxidants & Redox Signaling 2013 18 11 1307 1348
    • (2013) Antioxidants & Redox Signaling , vol.18 , Issue.11 , pp. 1307-1348
    • Vinod, B.S.1    Maliekal, T.T.2    Anto, R.J.3
  • 249
    • 17144431814 scopus 로고    scopus 로고
    • Mitochondrial targeting of human O6-methylguanine DNA methyltransferase protects against cell killing by chemotherapeutic alkylating agents
    • 2-s2.0-17144431814
    • Cai S., Xu Y., Cooper R. J., Ferkowiez M. J., Hartwell J. R., Pollok K. E., Kelley M. R., Mitochondrial targeting of human O6-methylguanine DNA methyltransferase protects against cell killing by chemotherapeutic alkylating agents. Cancer Research 2005 65 8 3319 3327 2-s2.0-17144431814
    • (2005) Cancer Research , vol.65 , Issue.8 , pp. 3319-3327
    • Cai, S.1    Xu, Y.2    Cooper, R.J.3    Ferkowiez, M.J.4    Hartwell, J.R.5    Pollok, K.E.6    Kelley, M.R.7
  • 250
    • 0042705073 scopus 로고    scopus 로고
    • Reactive oxygen species mediate doxorubicin induced p53-independent apoptosis
    • 2-s2.0-0042705073 10.1016/S0024-3205(03)00566-6
    • Tsang W. P., Chau S. P. Y., Kong S. K., Fung K. P., Kwok T. T., Reactive oxygen species mediate doxorubicin induced p53-independent apoptosis. Life Sciences 2003 73 16 2047 2058 2-s2.0-0042705073 10.1016/S0024-3205(03)00566-6
    • (2003) Life Sciences , vol.73 , Issue.16 , pp. 2047-2058
    • Tsang, W.P.1    Chau, S.P.Y.2    Kong, S.K.3    Fung, K.P.4    Kwok, T.T.5
  • 251
    • 74349110044 scopus 로고    scopus 로고
    • Perillyl alcohol and methyl jasmonate sensitize cancer cells to cisplatin
    • 2-s2.0-74349110044 10.1097/CAD.0b013e32832a68ad
    • Yeruva L., Hall C., Elegbede J. A., Carper S. W., Perillyl alcohol and methyl jasmonate sensitize cancer cells to cisplatin. Anti-Cancer Drugs 2010 21 1 1 9 2-s2.0-74349110044 10.1097/CAD.0b013e32832a68ad
    • (2010) Anti-Cancer Drugs , vol.21 , Issue.1 , pp. 1-9
    • Yeruva, L.1    Hall, C.2    Elegbede, J.A.3    Carper, S.W.4
  • 252
    • 84881620320 scopus 로고    scopus 로고
    • Cisplatin: An old drug with a newfound efficacy - From mechanisms of action to cytotoxicity
    • 10.1517/14656566.2013.813934
    • Macciò A., Madeddu C., Cisplatin: an old drug with a newfound efficacy-from mechanisms of action to cytotoxicity. Expert Opinion on Pharmacotherapy 2013 14 13 1839 1857 10.1517/14656566.2013.813934
    • (2013) Expert Opinion on Pharmacotherapy , vol.14 , Issue.13 , pp. 1839-1857
    • Macciò, A.1    Madeddu, C.2
  • 253
    • 84869876935 scopus 로고    scopus 로고
    • Algae extracts and methyl jasmonate anti-cancer activities in prostate cancer: Choreographers of 'the dance macabre'
    • Farooqi A. A., Butt G., Razzaq Z., Algae extracts and methyl jasmonate anti-cancer activities in prostate cancer: choreographers of 'the dance macabre'. Cancer Cell International 2012 12, article 50
    • (2012) Cancer Cell International , vol.1250
    • Farooqi, A.A.1    Butt, G.2    Razzaq, Z.3
  • 254
    • 80052469706 scopus 로고    scopus 로고
    • Predominant enhancement of apoptosis induced by methyl jasmonate in bladder cancer cells: Therapeutic effect of the Antp-conjugated Smac peptide
    • 2-s2.0-80052469706 10.1097/CAD.0b013e3283482d40
    • Xiao X.-Y., Jiang G.-S., Wang L., Lv L., Zeng F.-Q., Predominant enhancement of apoptosis induced by methyl jasmonate in bladder cancer cells: therapeutic effect of the Antp-conjugated Smac peptide. Anti-Cancer Drugs 2011 22 9 853 863 2-s2.0-80052469706 10.1097/CAD.0b013e3283482d40
    • (2011) Anti-Cancer Drugs , vol.22 , Issue.9 , pp. 853-863
    • Xiao, X.-Y.1    Jiang, G.-S.2    Wang, L.3    Lv, L.4    Zeng, F.-Q.5
  • 255
    • 79251600082 scopus 로고    scopus 로고
    • AN N-terminal Smac peptide sensitizes human prostate carcinoma cells to methyl jasmonate-induced apoptosis
    • 2-s2.0-79251600082 10.1016/j.canlet.2010.12.009
    • Jiang G., Zhao J., Xiao X., Tao D., Gu C., Tong Q., Luo B., Wang L., Zeng F., AN N-terminal Smac peptide sensitizes human prostate carcinoma cells to methyl jasmonate-induced apoptosis. Cancer Letters 2011 302 1 37 46 2-s2.0-79251600082 10.1016/j.canlet.2010.12.009
    • (2011) Cancer Letters , vol.302 , Issue.1 , pp. 37-46
    • Jiang, G.1    Zhao, J.2    Xiao, X.3    Tao, D.4    Gu, C.5    Tong, Q.6    Luo, B.7    Wang, L.8    Zeng, F.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.