메뉴 건너뛰기




Volumn 14, Issue 2, 2009, Pages 191-202

Betulinic acid induces cytochrome c release and apoptosis in a Bax/Bak-independent, permeability transition pore dependent fashion

Author keywords

Bak; Bax; Bcl 2 family; Betulinic acid; Cell death; Cytochrome c release

Indexed keywords

BETULIC ACID; CYCLOSPORIN A; CYTOCHROME C; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL;

EID: 58849088375     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-008-0290-x     Document Type: Article
Times cited : (105)

References (47)
  • 1
    • 0028847024 scopus 로고
    • Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis
    • 10.1038/nm1095-1046
    • E Pisha H Chai IS Lee 1995 Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis Nat Med 1 1046 1051 10.1038/nm1095-1046
    • (1995) Nat Med , vol.1 , pp. 1046-1051
    • Pisha, E.1    Chai, H.2    Lee, I.S.3
  • 2
    • 0032969291 scopus 로고    scopus 로고
    • Betulinic acid: A new cytotoxic agent against malignant brain-tumor cells
    • 10.1002/(SICI)1097-0215(19990730)82:3<435::AID-IJC18>3.0.CO;2-1
    • S Fulda I Jeremias HH Steiner 1999 Betulinic acid: a new cytotoxic agent against malignant brain-tumor cells Int J Cancer 82 435 441 10.1002/(SICI)1097- 0215(19990730)82:3<435::AID-IJC18>3.0.CO;2-1
    • (1999) Int J Cancer , vol.82 , pp. 435-441
    • Fulda, S.1    Jeremias, I.2    Steiner, H.H.3
  • 3
    • 4344609047 scopus 로고    scopus 로고
    • Betulinic acid-induced apoptosis in leukemia cells
    • 10.1038/sj.leu.2403406
    • H Ehrhardt S Fulda M Fuhrer 2004 Betulinic acid-induced apoptosis in leukemia cells Leukemia 18 1406 1412 10.1038/sj.leu.2403406
    • (2004) Leukemia , vol.18 , pp. 1406-1412
    • Ehrhardt, H.1    Fulda, S.2    Fuhrer, M.3
  • 4
    • 3242810661 scopus 로고    scopus 로고
    • Betulinic acid: A promising anticancer candidate
    • DA Eiznhamer ZQ Xu 2004 Betulinic acid: a promising anticancer candidate IDrugs 7 359 373
    • (2004) IDrugs , vol.7 , pp. 359-373
    • Eiznhamer, D.A.1    Xu, Z.Q.2
  • 5
    • 34247120086 scopus 로고    scopus 로고
    • Broad in vitro efficacy of plant-derived betulinic acid against cell lines derived from the most prevalent human cancer types
    • 10.1016/j.canlet.2006.11.003
    • JH Kessler FB Mullauer GM de Roo 2007 Broad in vitro efficacy of plant-derived betulinic acid against cell lines derived from the most prevalent human cancer types Cancer Lett 251 132 145 10.1016/j.canlet.2006.11.003
    • (2007) Cancer Lett , vol.251 , pp. 132-145
    • Kessler, J.H.1    Mullauer, F.B.2    De Roo, G.M.3
  • 6
    • 36649016713 scopus 로고    scopus 로고
    • Effect of betulinic acid on anticancer drug-resistant colon cancer cells
    • 10.1111/j.1742-7843.2007.00115.x
    • GR Jung KJ Kim CH Choi 2007 Effect of betulinic acid on anticancer drug-resistant colon cancer cells Basic Clin Pharmacol Toxicol 101 277 285 10.1111/j.1742-7843.2007.00115.x
    • (2007) Basic Clin Pharmacol Toxicol , vol.101 , pp. 277-285
    • Jung, G.R.1    Kim, K.J.2    Choi, C.H.3
  • 7
    • 0037049876 scopus 로고    scopus 로고
    • Selective cytotoxicity of betulinic acid on tumor cell lines, but not on normal cells
    • 10.1016/S0304-3835(01)00718-2
    • V Zuco R Supino SC Righetti 2002 Selective cytotoxicity of betulinic acid on tumor cell lines, but not on normal cells Cancer Lett 175 17 25 10.1016/S0304-3835(01)00718-2
    • (2002) Cancer Lett , vol.175 , pp. 17-25
    • Zuco, V.1    Supino, R.2    Righetti, S.C.3
  • 8
    • 0034026724 scopus 로고    scopus 로고
    • Effects of betulinic acid alone and in combination with irradiation in human melanoma cells
    • 10.1046/j.1523-1747.2000.00972.x
    • E Selzer E Pimentel V Wacheck 2000 Effects of betulinic acid alone and in combination with irradiation in human melanoma cells J Invest Dermatol 114 935 940 10.1046/j.1523-1747.2000.00972.x
    • (2000) J Invest Dermatol , vol.114 , pp. 935-940
    • Selzer, E.1    Pimentel, E.2    Wacheck, V.3
  • 9
    • 0030815250 scopus 로고    scopus 로고
    • Betulinic acid triggers CD95 (APO-1/Fas)- and p53-independent apoptosis via activation of caspases in neuroectodermal tumors
    • S Fulda C Friesen M Los 1997 Betulinic acid triggers CD95 (APO-1/Fas)- and p53-independent apoptosis via activation of caspases in neuroectodermal tumors Cancer Res 57 4956 4964
    • (1997) Cancer Res , vol.57 , pp. 4956-4964
    • Fulda, S.1    Friesen, C.2    Los, M.3
  • 10
    • 0033023669 scopus 로고    scopus 로고
    • Betulinic acid-induced apoptosis in glioma cells: A sequential requirement for new protein synthesis, formation of reactive oxygen species, and caspase processing
    • W Wick C Grimmel B Wagenknecht 1999 Betulinic acid-induced apoptosis in glioma cells: a sequential requirement for new protein synthesis, formation of reactive oxygen species, and caspase processing J Pharmacol Exp Ther 289 1306 1312
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 1306-1312
    • Wick, W.1    Grimmel, C.2    Wagenknecht, B.3
  • 11
    • 0038492656 scopus 로고    scopus 로고
    • Betulinic acid-induced programmed cell death in human melanoma cells involves mitogen-activated protein kinase activation
    • Y Tan R Yu JM Pezzuto 2003 Betulinic acid-induced programmed cell death in human melanoma cells involves mitogen-activated protein kinase activation Clin Cancer Res 9 2866 2875
    • (2003) Clin Cancer Res , vol.9 , pp. 2866-2875
    • Tan, Y.1    Yu, R.2    Pezzuto, J.M.3
  • 12
    • 0032189535 scopus 로고    scopus 로고
    • Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells
    • S Fulda SA Susin G Kroemer 1998 Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells Cancer Res 58 4453 4460
    • (1998) Cancer Res , vol.58 , pp. 4453-4460
    • Fulda, S.1    Susin, S.A.2    Kroemer, G.3
  • 13
    • 0032545386 scopus 로고    scopus 로고
    • Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid
    • 10.1074/jbc.273.51.33942
    • S Fulda C Scaffidi SA Susin 1998 Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid J Biol Chem 273 33942 33948 10.1074/jbc.273.51.33942
    • (1998) J Biol Chem , vol.273 , pp. 33942-33948
    • Fulda, S.1    Scaffidi, C.2    Susin, S.A.3
  • 14
    • 0033646961 scopus 로고    scopus 로고
    • Betulinic acid induces apoptosis through a direct effect on mitochondria in neuroectodermal tumors
    • 10.1002/1096-911X(20001201)35:6<616::AID-MPO27>3.0.CO;2-N
    • S Fulda KM Debatin 2000 Betulinic acid induces apoptosis through a direct effect on mitochondria in neuroectodermal tumors Med Pediatr Oncol 35 616 618 10.1002/1096-911X(20001201)35:6<616::AID-MPO27>3.0.CO;2-N
    • (2000) Med Pediatr Oncol , vol.35 , pp. 616-618
    • Fulda, S.1    Debatin, K.M.2
  • 15
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • 10.1038/sj.onc.1210220
    • JM Adams S Cory 2007 The Bcl-2 apoptotic switch in cancer development and therapy Oncogene 26 1324 1337 10.1038/sj.onc.1210220
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 16
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • 10.1038/35085008
    • M Leist M Jaattela 2001 Four deaths and a funeral: from caspases to alternative mechanisms Nat Rev Mol Cell Biol 2 589 598 10.1038/35085008
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 17
    • 0141893342 scopus 로고    scopus 로고
    • A serine protease is involved in the initiation of DNA damage-induced apoptosis
    • 10.1038/sj.cdd.4401296
    • EC de Bruin D Meersma J de Wilde 2003 A serine protease is involved in the initiation of DNA damage-induced apoptosis Cell Death Differ 10 1204 1212 10.1038/sj.cdd.4401296
    • (2003) Cell Death Differ , vol.10 , pp. 1204-1212
    • De Bruin, E.C.1    Meersma, D.2    De Wilde, J.3
  • 18
    • 0032488664 scopus 로고    scopus 로고
    • Bcl-x(L) acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex
    • 10.1074/jbc.273.6.3388
    • JP Medema C Scaffidi PH Krammer 1998 Bcl-x(L) acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex J Biol Chem 273 3388 3393 10.1074/jbc.273.6.3388
    • (1998) J Biol Chem , vol.273 , pp. 3388-3393
    • Medema, J.P.1    Scaffidi, C.2    Krammer, P.H.3
  • 19
    • 0037817848 scopus 로고    scopus 로고
    • A new quantitative assay for cytochrome c release in apoptotic cells
    • 10.1038/sj.cdd.4401263
    • NJ Waterhouse JA Trapani 2003 A new quantitative assay for cytochrome c release in apoptotic cells Cell Death Differ 10 853 855 10.1038/sj.cdd.4401263
    • (2003) Cell Death Differ , vol.10 , pp. 853-855
    • Waterhouse, N.J.1    Trapani, J.A.2
  • 20
    • 0035720233 scopus 로고    scopus 로고
    • The Bax/Bcl-2 ratio determines the susceptibility of human melanoma cells to CD95/Fas-mediated apoptosis
    • 10.1046/j.0022-202x.2001.01409.x
    • M Raisova AM Hossini J Eberle 2001 The Bax/Bcl-2 ratio determines the susceptibility of human melanoma cells to CD95/Fas-mediated apoptosis J Invest Dermatol 117 333 340 10.1046/j.0022-202x.2001.01409.x
    • (2001) J Invest Dermatol , vol.117 , pp. 333-340
    • Raisova, M.1    Hossini, A.M.2    Eberle, J.3
  • 21
    • 0032607858 scopus 로고    scopus 로고
    • Alteration of caspase-3 (CPP32/Yama/apopain) in wild-type MCF-7, breast cancer cells
    • H Kurokawa K Nishio H Fukumoto 1999 Alteration of caspase-3 (CPP32/Yama/apopain) in wild-type MCF-7, breast cancer cells Oncol Rep 6 33 37
    • (1999) Oncol Rep , vol.6 , pp. 33-37
    • Kurokawa, H.1    Nishio, K.2    Fukumoto, H.3
  • 22
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3,-6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • 10.1074/jbc.M008363200
    • EA Slee C Adrain SJ Martin 2001 Executioner caspase-3,-6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis J Biol Chem 276 7320 7326 10.1074/jbc.M008363200
    • (2001) J Biol Chem , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 23
    • 0036097786 scopus 로고    scopus 로고
    • Keeping killers on a tight leash: Transcriptional and posttranslational control of the pro-apoptotic activity of BH3-only proteins
    • 10.1038/sj.cdd.4400998
    • H Puthalakath A Strasser 2002 Keeping killers on a tight leash: transcriptional and posttranslational control of the pro-apoptotic activity of BH3-only proteins Cell Death Differ 9 505 512 10.1038/sj.cdd.4400998
    • (2002) Cell Death Differ , vol.9 , pp. 505-512
    • Puthalakath, H.1    Strasser, A.2
  • 24
    • 19944432123 scopus 로고    scopus 로고
    • Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
    • 10.1016/j.molcel.2004.12.030
    • L Chen SN Willis A Wei 2005 Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function Mol Cell 17 393 403 10.1016/j.molcel.2004.12.030
    • (2005) Mol Cell , vol.17 , pp. 393-403
    • Chen, L.1    Willis, S.N.2    Wei, A.3
  • 25
    • 34748924281 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis: Mechanism and therapeutic potential
    • 10.1016/j.coi.2007.05.004
    • JM Adams S Cory 2007 Bcl-2-regulated apoptosis: mechanism and therapeutic potential Curr Opin Immunol 19 488 496 10.1016/j.coi.2007.05.004
    • (2007) Curr Opin Immunol , vol.19 , pp. 488-496
    • Adams, J.M.1    Cory, S.2
  • 26
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • 10.1126/science.1059108
    • MC Wei WX Zong EHY Cheng 2001 Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death Science 292 727 730 10.1126/science.1059108
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.Y.3
  • 27
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • 10.1126/science.290.5493.989
    • L Zhang J Yu BH Park 2000 Role of BAX in the apoptotic response to anticancer agents Science 290 989 992 10.1126/science.290.5493.989
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3
  • 28
    • 33750483637 scopus 로고    scopus 로고
    • Bak functionally complements for loss of Bax during p14(ARF)-induced mitochondrial apoptosis in human cancer cells
    • 10.1038/sj.onc.1209668
    • PG Hemmati D Guner B Gillissen 2006 Bak functionally complements for loss of Bax during p14(ARF)-induced mitochondrial apoptosis in human cancer cells Oncogene 25 6582 6594 10.1038/sj.onc.1209668
    • (2006) Oncogene , vol.25 , pp. 6582-6594
    • Hemmati, P.G.1    Guner, D.2    Gillissen, B.3
  • 29
    • 0035903220 scopus 로고    scopus 로고
    • Pro-apoptotic cleavage products of Bcl-x(L) form cytochrome c-conducting pores in pure lipid membranes
    • 10.1074/jbc.M103879200
    • G Basanez J Zhang BN Chau 2001 Pro-apoptotic cleavage products of Bcl-x(L) form cytochrome c-conducting pores in pure lipid membranes J Biol Chem 276 31083 31091 10.1074/jbc.M103879200
    • (2001) J Biol Chem , vol.276 , pp. 31083-31091
    • Basanez, G.1    Zhang, J.2    Chau, B.N.3
  • 30
    • 4544359229 scopus 로고    scopus 로고
    • Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals
    • 10.1073/pnas.0401372101
    • EA Jonas JA Hickman M Chachar 2004 Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals Proc Natl Acad Sci USA 101 13590 13595 10.1073/pnas.0401372101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13590-13595
    • Jonas, E.A.1    Hickman, J.A.2    Chachar, M.3
  • 31
    • 0033597785 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c
    • 10.1074/jbc.274.30.21155
    • DG Kirsch A Doseff BN Chau 1999 Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c J Biol Chem 274 21155 21161 10.1074/jbc.274.30.21155
    • (1999) J Biol Chem , vol.274 , pp. 21155-21161
    • Kirsch, D.G.1    Doseff, A.2    Chau, B.N.3
  • 32
    • 34247540380 scopus 로고    scopus 로고
    • The permeability transition pore in cell death
    • 10.1007/s10495-007-0747-3
    • S Grimm D Brdiczka 2007 The permeability transition pore in cell death Apoptosis 12 841 855 10.1007/s10495-007-0747-3
    • (2007) Apoptosis , vol.12 , pp. 841-855
    • Grimm, S.1    Brdiczka, D.2
  • 33
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • 10.1016/S0092-8674(03)00116-8
    • DD Newmeyer S Ferguson-Miller 2003 Mitochondria: releasing power for life and unleashing the machineries of death Cell 112 481 490 10.1016/S0092-8674(03) 00116-8
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 34
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • 10.1038/nature02229
    • JE Kokoszka KG Waymire SE Levy 2004 The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore Nature 427 461 465 10.1038/nature02229
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3
  • 35
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • 10.1038/ncb1575
    • CP Baines RA Kaiser T Sheiko 2007 Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat Cell Biol 9 550 555 10.1038/ncb1575
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3
  • 36
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • 10.1007/s10495-006-0525-7
    • Y Tsujimoto S Shimizu 2007 Role of the mitochondrial membrane permeability transition in cell death Apoptosis 12 835 840 10.1007/s10495-006- 0525-7
    • (2007) Apoptosis , vol.12 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 37
    • 48549085442 scopus 로고    scopus 로고
    • Curcumin decreases specificity protein expression in bladder cancer cells
    • 10.1158/0008-5472.CAN-07-6805
    • G Chadalapaka I Jutooru S Chintharlapani 2008 Curcumin decreases specificity protein expression in bladder cancer cells Cancer Res 68 5345 5354 10.1158/0008-5472.CAN-07-6805
    • (2008) Cancer Res , vol.68 , pp. 5345-5354
    • Chadalapaka, G.1    Jutooru, I.2    Chintharlapani, S.3
  • 38
    • 34047261665 scopus 로고    scopus 로고
    • Betulinic acid inhibits prostate cancer growth through inhibition of specificity protein transcription factors
    • 10.1158/0008-5472.CAN-06-3735
    • S Chintharlapalli S Papineni SK Ramaiah 2007 Betulinic acid inhibits prostate cancer growth through inhibition of specificity protein transcription factors Cancer Res 67 2816 2823 10.1158/0008-5472.CAN-06-3735
    • (2007) Cancer Res , vol.67 , pp. 2816-2823
    • Chintharlapalli, S.1    Papineni, S.2    Ramaiah, S.K.3
  • 39
    • 34447332823 scopus 로고    scopus 로고
    • Novel semisynthetic analogues of betulinic acid with diverse cytoprotective, antiproliferative, and proapoptotic activities
    • 10.1158/1535-7163.MCT-07-0180
    • K Liby T Honda CR Williams 2007 Novel semisynthetic analogues of betulinic acid with diverse cytoprotective, antiproliferative, and proapoptotic activities Mol Cancer Ther 6 2113 2119 10.1158/1535-7163.MCT-07-0180
    • (2007) Mol Cancer Ther , vol.6 , pp. 2113-2119
    • Liby, K.1    Honda, T.2    Williams, C.R.3
  • 40
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • 10.1038/20959
    • S Shimizu M Narita Y Tsujimoto 1999 Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC Nature 399 483 487 10.1038/20959
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 41
    • 0034618269 scopus 로고    scopus 로고
    • Bax and Bcl-x(L) independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator
    • 10.1038/sj.onc.1203788
    • S Shimizu Y Shinohara Y Tsujimoto 2000 Bax and Bcl-x(L) independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator Oncogene 19 4309 4318 10.1038/sj.onc.1203788
    • (2000) Oncogene , vol.19 , pp. 4309-4318
    • Shimizu, S.1    Shinohara, Y.2    Tsujimoto, Y.3
  • 42
    • 33845603436 scopus 로고    scopus 로고
    • Gossypol induces Bax/Bak-independent activation of apoptosis and cytochrome c release via a conformational change in Bcl-2
    • 10.1096/fj.05-5665fje
    • XB Lei YY Chen GH Du 2006 Gossypol induces Bax/Bak-independent activation of apoptosis and cytochrome c release via a conformational change in Bcl-2 FASEB J 20 2147 2149 10.1096/fj.05-5665fje
    • (2006) FASEB J , vol.20 , pp. 2147-2149
    • Lei, X.B.1    Chen, Y.Y.2    Du, G.H.3
  • 43
    • 34447516996 scopus 로고    scopus 로고
    • A Bax/Bak-independent mechanism of cytochrome c release
    • 10.1074/jbc.M611060200
    • T Mizuta S Shimizu Y Matsuoka 2007 A Bax/Bak-independent mechanism of cytochrome c release J Biol Chem 282 16623 16630 10.1074/jbc.M611060200
    • (2007) J Biol Chem , vol.282 , pp. 16623-16630
    • Mizuta, T.1    Shimizu, S.2    Matsuoka, Y.3
  • 44
    • 43749124428 scopus 로고    scopus 로고
    • Chelerythrine induces apoptosis through a Bax/Bak-independent mitochondrial mechanism
    • 10.1074/jbc.M707687200
    • KF Wan SL Chan SK Sukumaran 2008 Chelerythrine induces apoptosis through a Bax/Bak-independent mitochondrial mechanism J Biol Chem 283 8423 8433 10.1074/jbc.M707687200
    • (2008) J Biol Chem , vol.283 , pp. 8423-8433
    • Wan, K.F.1    Chan, S.L.2    Sukumaran, S.K.3
  • 45
    • 0034602536 scopus 로고    scopus 로고
    • Long-chain fatty acids promote opening of the reconstituted mitochondrial permeability transition pore
    • 10.1016/S0014-5793(00)02127-X
    • MR Wieckowski D Brdiczka L Wojtczak 2000 Long-chain fatty acids promote opening of the reconstituted mitochondrial permeability transition pore FEBS Lett 484 61 64 10.1016/S0014-5793(00)02127-X
    • (2000) FEBS Lett , vol.484 , pp. 61-64
    • Wieckowski, M.R.1    Brdiczka, D.2    Wojtczak, L.3
  • 46
    • 33746924468 scopus 로고    scopus 로고
    • Hexokinase II: Cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria
    • 10.1038/sj.onc.1209603
    • SP Mathupala YH Ko PL Pedersen 2006 Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria Oncogene 25 4777 4786 10.1038/sj.onc.1209603
    • (2006) Oncogene , vol.25 , pp. 4777-4786
    • Mathupala, S.P.1    Ko, Y.H.2    Pedersen, P.L.3
  • 47
    • 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
    • 10.1007/s10863-007-9094-x
    • PL Pedersen 2007 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 J Bioenerg Biomembr 39 211 222 10.1007/s10863-007-9094-x
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 211-222
    • Pedersen, P.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.