메뉴 건너뛰기




Volumn 148, Issue 5, 2012, Pages 988-1000

Sphingolipid metabolism cooperates with BAK and BAX to promote the mitochondrial pathway of apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; PROTEIN BAK; PROTEIN BAX; SPHINGOLIPID; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOSINE 1 PHOSPHATE;

EID: 84857873334     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2012.01.038     Document Type: Article
Times cited : (351)

References (68)
  • 1
    • 2342570298 scopus 로고    scopus 로고
    • Overcoming resistance to γ-rays in squamous carcinoma cells by poly-drug elevation of ceramide levels
    • DOI 10.1038/sj.onc.1207357
    • G. Alphonse, C. Bionda, M.T. Aloy, D. Ardail, R. Rousson, and C. Rodriguez-Lafrasse Overcoming resistance to gamma-rays in squamous carcinoma cells by poly-drug elevation of ceramide levels Oncogene 23 2004 2703 2715 (Pubitemid 38586324)
    • (2004) Oncogene , vol.23 , Issue.15 , pp. 2703-2715
    • Alphonse, G.1    Bionda, C.2    Aloy, M.-T.3    Ardail, D.4    Rousson, R.5    Rodriguez-Lafrasse, C.6
  • 2
    • 66349086742 scopus 로고    scopus 로고
    • Bioactive sphingolipids: Metabolism and function
    • N. Bartke, and Y.A. Hannun Bioactive sphingolipids: metabolism and function J. Lipid Res. 50 Suppl 2009 S91 S96
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Bartke, N.1    Hannun, Y.A.2
  • 3
    • 33947409221 scopus 로고    scopus 로고
    • TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax
    • DOI 10.1038/sj.cdd.4402055, PII 4402055
    • G. Bellot, P.F. Cartron, E. Er, L. Oliver, P. Juin, L.C. Armstrong, P. Bornstein, K. Mihara, S. Manon, and F.M. Vallette TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax Cell Death Differ. 14 2007 785 794 (Pubitemid 46444516)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 785-794
    • Bellot, G.1    Cartron, P.-F.2    Er, E.3    Oliver, L.4    Juin, P.5    Armstrong, L.C.6    Bornstein, P.7    Mihara, K.8    Manon, S.9    Vallette, F.M.10
  • 4
    • 0035199418 scopus 로고    scopus 로고
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis
    • DOI 10.1096/fj.01-0539com
    • H. Birbes, S. El Bawab, Y.A. Hannun, and L.M. Obeid Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis FASEB J. 15 2001 2669 2679 (Pubitemid 33131093)
    • (2001) FASEB Journal , vol.15 , Issue.14 , pp. 2669-2679
    • Birbes, H.1    El Bawab, S.2    Hannun, Y.A.3    Obeid, L.M.4
  • 5
    • 15944425766 scopus 로고    scopus 로고
    • A mitochondrial pool of sphingomyelin is involved in TNFα-induced Bax translocation to mitochondria
    • DOI 10.1042/BJ20041627
    • H. Birbes, C. Luberto, Y.T. Hsu, S. El Bawab, Y.A. Hannun, and L.M. Obeid A mitochondrial pool of sphingomyelin is involved in TNFalpha-induced Bax translocation to mitochondria Biochem. J. 386 2005 445 451 (Pubitemid 40445868)
    • (2005) Biochemical Journal , vol.386 , Issue.3 , pp. 445-451
    • Birbes, H.1    Luberto, C.2    Hsu, Y.-T.3    El Bawab, S.4    Hannun, Y.A.5    Obeid, L.M.6
  • 6
    • 38849099158 scopus 로고    scopus 로고
    • Chemical Inhibition of the Mitochondrial Division Dynamin Reveals Its Role in Bax/Bak-Dependent Mitochondrial Outer Membrane Permeabilization
    • DOI 10.1016/j.devcel.2007.11.019, PII S1534580707004753
    • A. Cassidy-Stone, J.E. Chipuk, E. Ingerman, C. Song, C. Yoo, T. Kuwana, M.J. Kurth, J.T. Shaw, J.E. Hinshaw, and D.R. Green Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer-membrane permeabilization Dev. Cell 14 2008 193 204 (Pubitemid 351189177)
    • (2008) Developmental Cell , vol.14 , Issue.2 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3    Song, C.4    Yoo, C.5    Kuwana, T.6    Kurth, M.J.7    Shaw, J.T.8    Hinshaw, J.E.9    Green, D.R.10    Nunnari, J.11
  • 9
    • 79953213300 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2 (nSMase2) is the primary neutral sphingomyelinase isoform activated by tumour necrosis factor-alpha in MCF-7 cells
    • C.J. Clarke, E.A. Cloessner, P.L. Roddy, and Y.A. Hannun Neutral sphingomyelinase 2 (nSMase2) is the primary neutral sphingomyelinase isoform activated by tumour necrosis factor-alpha in MCF-7 cells Biochem. J. 435 2011 381 390
    • (2011) Biochem. J. , vol.435 , pp. 381-390
    • Clarke, C.J.1    Cloessner, E.A.2    Roddy, P.L.3    Hannun, Y.A.4
  • 12
    • 2442711625 scopus 로고    scopus 로고
    • Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin
    • DOI 10.1038/sj.onc.1207430
    • Q. Dai, J. Liu, J. Chen, D. Durrant, T.M. McIntyre, and R.M. Lee Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin Oncogene 23 2004 3650 3658 (Pubitemid 38658432)
    • (2004) Oncogene , vol.23 , Issue.20 , pp. 3650-3658
    • Dai, Q.1    Liu, J.2    Chen, J.3    Durrant, D.4    McIntyre, T.M.5    Lee, R.M.6
  • 13
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • O.M. de Brito, and L. Scorrano Mitofusin 2 tethers endoplasmic reticulum to mitochondria Nature 456 2008 605 610
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 16
    • 43049105074 scopus 로고    scopus 로고
    • To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions
    • DOI 10.1016/j.molcel.2008.04.005, PII S1097276508002657
    • G. Dewson, T. Kratina, H.W. Sim, H. Puthalakath, J.M. Adams, P.M. Colman, and R.M. Kluck To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions Mol. Cell 30 2008 369 380 (Pubitemid 351626944)
    • (2008) Molecular Cell , vol.30 , Issue.3 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6    Kluck, R.M.7
  • 17
    • 77951665317 scopus 로고    scopus 로고
    • Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
    • V. Ganesan, M.N. Perera, D. Colombini, D. Datskovskiy, K. Chadha, and M. Colombini Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane Apoptosis 15 2010 553 562
    • (2010) Apoptosis , vol.15 , pp. 553-562
    • Ganesan, V.1    Perera, M.N.2    Colombini, D.3    Datskovskiy, D.4    Chadha, K.5    Colombini, M.6
  • 20
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • DOI 10.1038/nrm2329, PII NRM2329
    • Y.A. Hannun, and L.M. Obeid Principles of bioactive lipid signalling: lessons from sphingolipids Nat. Rev. Mol. Cell Biol. 9 2008 139 150 (Pubitemid 351158911)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 22
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • DOI 10.1074/jbc.272.21.13829
    • Y.T. Hsu, and R.J. Youle Nonionic detergents induce dimerization among members of the Bcl-2 family J. Biol. Chem. 272 1997 13829 13834 (Pubitemid 27224822)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13829-13834
    • Hsu, Y.-T.1    Youle, R.J.2
  • 24
    • 0141757451 scopus 로고    scopus 로고
    • Radiation and ceramide-induced apoptosis
    • DOI 10.1038/sj.onc.1206702
    • R. Kolesnick, and Z. Fuks Radiation and ceramide-induced apoptosis Oncogene 22 2003 5897 5906 (Pubitemid 37176710)
    • (2003) Oncogene , vol.22 , Issue.37 REV. ISS. 3 , pp. 5897-5906
    • Kolesnick, R.1    Fuks, Z.2
  • 25
    • 79954419484 scopus 로고    scopus 로고
    • The sphingolipid degradation product trans-2-hexadecenal induces cytoskeletal reorganization and apoptosis in a JNK-dependent manner
    • A. Kumar, H.S. Byun, R. Bittman, and J.D. Saba The sphingolipid degradation product trans-2-hexadecenal induces cytoskeletal reorganization and apoptosis in a JNK-dependent manner Cell. Signal. 23 2011 1144 1152
    • (2011) Cell. Signal. , vol.23 , pp. 1144-1152
    • Kumar, A.1    Byun, H.S.2    Bittman, R.3    Saba, J.D.4
  • 26
    • 79959958500 scopus 로고    scopus 로고
    • S1P lyase regulates DNA damage responses through a novel sphingolipid feedback mechanism
    • A. Kumar, B. Oskouian, H. Fyrst, M. Zhang, F. Paris, and J.D. Saba S1P lyase regulates DNA damage responses through a novel sphingolipid feedback mechanism Cell Death Dis 2 2011 e119
    • (2011) Cell Death Dis , vol.2 , pp. 119
    • Kumar, A.1    Oskouian, B.2    Fyrst, H.3    Zhang, M.4    Paris, F.5    Saba, J.D.6
  • 27
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • DOI 10.1016/j.molcel.2005.02.003
    • T. Kuwana, L. Bouchier-Hayes, J.E. Chipuk, C. Bonzon, B.A. Sullivan, D.R. Green, and D.D. Newmeyer BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly Mol. Cell 17 2005 525 535 (Pubitemid 40269117)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 28
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • DOI 10.1016/S0092-8674(02)01036-X
    • T. Kuwana, M.R. Mackey, G. Perkins, M.H. Ellisman, M. Latterich, R. Schneiter, D.R. Green, and D.D. Newmeyer Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane Cell 111 2002 331 342 (Pubitemid 35341388)
    • (2002) Cell , vol.111 , Issue.3 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6    Green, D.R.7    Newmeyer, D.D.8
  • 30
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • DOI 10.1016/S1535-6108(02)00127-7
    • A. Letai, M.C. Bassik, L.D. Walensky, M.D. Sorcinelli, S. Weiler, and S.J. Korsmeyer Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics Cancer Cell 2 2002 183 192 (Pubitemid 41043974)
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 32
    • 2142769665 scopus 로고    scopus 로고
    • Oligonucleotides blocking glucosylceramide synthase expression selectively reverse drug resistance in cancer cells
    • DOI 10.1194/jlr.M300486-JLR200
    • Y.Y. Liu, T.Y. Han, J.Y. Yu, A. Bitterman, A. Le, A.E. Giuliano, and M.C. Cabot Oligonucleotides blocking glucosylceramide synthase expression selectively reverse drug resistance in cancer cells J. Lipid Res. 45 2004 933 940 (Pubitemid 38552864)
    • (2004) Journal of Lipid Research , vol.45 , Issue.5 , pp. 933-940
    • Liu, Y.-Y.1    Han, T.Y.2    Yu, J.Y.3    Bitterman, A.4    Le, A.5    Giuliano, A.E.6    Cabot, M.C.7
  • 34
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • M. Lutter, M. Fang, X. Luo, M. Nishijima, X. Xie, and X. Wang Cardiolipin provides specificity for targeting of tBid to mitochondria Nat. Cell Biol. 2 2000 754 761
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 36
    • 77957938907 scopus 로고    scopus 로고
    • Anterograde and retrograde transport of neutral sphingomyelinase-2 between the Golgi and the plasma membrane
    • D. Milhas, C.J. Clarke, J. Idkowiak-Baldys, D. Canals, and Y.A. Hannun Anterograde and retrograde transport of neutral sphingomyelinase-2 between the Golgi and the plasma membrane Biochim. Biophys. Acta 1801 2010 1361 1374
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 1361-1374
    • Milhas, D.1    Clarke, C.J.2    Idkowiak-Baldys, J.3    Canals, D.4    Hannun, Y.A.5
  • 38
    • 0027511687 scopus 로고
    • Programmed cell death induced by ceramide
    • L.M. Obeid, C.M. Linardic, L.A. Karolak, and Y.A. Hannun Programmed cell death induced by ceramide Science 259 1993 1769 1771 (Pubitemid 23114667)
    • (1993) Science , vol.259 , Issue.5102 , pp. 1769-1771
    • Obeid, L.M.1    Linardic, C.M.2    Karolak, L.A.3    Hannun, Y.A.4
  • 40
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex?
    • M. Ott, E. Norberg, B. Zhivotovsky, and S. Orrenius Mitochondrial targeting of tBid/Bax: a role for the TOM complex? Cell Death Differ. 16 2009 1075 1082
    • (2009) Cell Death Differ. , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 43
    • 0037145310 scopus 로고    scopus 로고
    • Increasing endogenous ceramide using inhibitors of sphingolipid metabolism maximizes ionizing radiation-induced mitochondrial injury and apoptotic cell killing
    • C. Rodriguez-Lafrasse, G. Alphonse, M.T. Aloy, D. Ardail, J.P. Gerard, P. Louisot, and R. Rousson Increasing endogenous ceramide using inhibitors of sphingolipid metabolism maximizes ionizing radiation-induced mitochondrial injury and apoptotic cell killing Int. J. Cancer 101 2002 589 598
    • (2002) Int. J. Cancer , vol.101 , pp. 589-598
    • Rodriguez-Lafrasse, C.1    Alphonse, G.2    Aloy, M.T.3    Ardail, D.4    Gerard, J.P.5    Louisot, P.6    Rousson, R.7
  • 45
    • 0034670379 scopus 로고    scopus 로고
    • Identification of ISC1 (YERO19w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M007721200
    • H. Sawai, Y. Okamoto, C. Luberto, C. Mao, A. Bielawska, N. Domae, and Y.A. Hannun Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase c in Saccharomyces cerevisiae J. Biol. Chem. 275 2000 39793 39798 (Pubitemid 32059011)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39793-39798
    • Sawai, H.1    Okamoto, Y.2    Luberto, C.3    Mao, C.4    Bielawska, A.5    Domae, N.6    Hannun, Y.A.7
  • 46
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • DOI 10.1016/S1534-5807(01)00116-2
    • L. Scorrano, M. Ashiya, K. Buttle, S. Weiler, S.A. Oakes, C.A. Mannella, and S.J. Korsmeyer A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis Dev. Cell 2 2002 55 67 (Pubitemid 34065906)
    • (2002) Developmental Cell , vol.2 , Issue.1 , pp. 55-67
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3    Weiler, S.4    Oakes, S.A.5    Mannella, C.A.6    Korsmeyer, S.J.7
  • 48
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • DOI 10.1074/jbc.M200754200
    • L.J. Siskind, R.N. Kolesnick, and M. Colombini Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins J. Biol. Chem. 277 2002 26796 26803 (Pubitemid 34951684)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26796-26803
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 49
    • 33745037188 scopus 로고    scopus 로고
    • Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations
    • DOI 10.1016/j.mito.2006.03.002, PII S1567724906000365
    • L.J. Siskind, R.N. Kolesnick, and M. Colombini Ceramide forms channels in mitochondrial outer membranes at physiologically relevant concentrations Mitochondrion 6 2006 118 125 (Pubitemid 43872021)
    • (2006) Mitochondrion , vol.6 , Issue.3 , pp. 118-125
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 50
    • 42949105726 scopus 로고    scopus 로고
    • Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins
    • J. Stiban, L. Caputo, and M. Colombini Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins J. Lipid Res. 49 2008 625 634
    • (2008) J. Lipid Res. , vol.49 , pp. 625-634
    • Stiban, J.1    Caputo, L.2    Colombini, M.3
  • 51
    • 33645801577 scopus 로고    scopus 로고
    • Loss of sphingosine kinase-1 activates the intrinsic pathway of programmed cell death: Modulation of sphingolipid levels and the induction of apoptosis
    • DOI 10.1096/fj.05-4412fje
    • T.A. Taha, K. Kitatani, M. El-Alwani, J. Bielawski, Y.A. Hannun, and L.M. Obeid Loss of sphingosine kinase-1 activates the intrinsic pathway of programmed cell death: modulation of sphingolipid levels and the induction of apoptosis FASEB J. 20 2006 482 484 (Pubitemid 46671223)
    • (2006) FASEB Journal , vol.20 , Issue.3 , pp. 482-484
    • Taha, T.A.1    Kitatani, K.2    El-Alwani, M.3    Bielawski, J.4    Hannun, Y.A.5    Obeid, L.M.6
  • 52
    • 33845294390 scopus 로고    scopus 로고
    • A house divided: Ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death
    • DOI 10.1016/j.bbamem.2006.10.018, PII S0005273606004135, Sphingolipids, Apoptosis and Disease
    • T.A. Taha, T.D. Mullen, and L.M. Obeid A house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death Biochim. Biophys. Acta 1758 2006 2027 2036 (Pubitemid 44879375)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.12 , pp. 2027-2036
    • Taha, T.A.1    Mullen, T.D.2    Obeid, L.M.3
  • 53
    • 0017404306 scopus 로고
    • Biochemical properties of liver megamitochondria induced by chloramphenicol or cuprizone
    • T. Wagner, and J. Rafael Biochemical properties of liver megamitochondria induced by chloramphenicol or cuprizone Exp. Cell Res. 107 1977 1 13 (Pubitemid 8112708)
    • (1977) Experimental Cell Research , vol.107 , Issue.1 , pp. 1-13
    • Wagner, T.1    Rafael, J.2
  • 54
    • 26444593029 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: The lethal interorganelle cross-talk
    • DOI 10.1007/s10863-005-6600-x
    • L. Walter, and G. Hajnoczky Mitochondria and endoplasmic reticulum: the lethal interorganelle cross-talk J. Bioenerg. Biomembr. 37 2005 191 206 (Pubitemid 41420474)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.3 , pp. 191-206
    • Walter, L.1    Hajnoczky, G.2
  • 57
    • 77952937382 scopus 로고    scopus 로고
    • Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5
    • B.X. Wu, V. Rajagopalan, P.L. Roddy, C.J. Clarke, and Y.A. Hannun Identification and characterization of murine mitochondria-associated neutral sphingomyelinase (MA-nSMase), the mammalian sphingomyelin phosphodiesterase 5 J. Biol. Chem. 285 2010 17993 18002
    • (2010) J. Biol. Chem. , vol.285 , pp. 17993-18002
    • Wu, B.X.1    Rajagopalan, V.2    Roddy, P.L.3    Clarke, C.J.4    Hannun, Y.A.5
  • 58
    • 67749120148 scopus 로고    scopus 로고
    • A novel mitochondrial sphingomyelinase in zebrafish cells
    • T. Yabu, A. Shimuzu, and M. Yamashita A novel mitochondrial sphingomyelinase in zebrafish cells J. Biol. Chem. 284 2009 20349 20363
    • (2009) J. Biol. Chem. , vol.284 , pp. 20349-20363
    • Yabu, T.1    Shimuzu, A.2    Yamashita, M.3
  • 60
    • 33745883535 scopus 로고    scopus 로고
    • Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-mediated cell death in yeast
    • DOI 10.1111/j.1567-1364.2006.00052.x
    • Z. Yang, C. Khoury, G. Jean-Baptiste, and M.T. Greenwood Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-mediated cell death in yeast FEMS Yeast Res 6 2006 751 762 (Pubitemid 44049994)
    • (2006) FEMS Yeast Research , vol.6 , Issue.5 , pp. 751-762
    • Yang, Z.1    Khoury, C.2    Jean-Baptiste, G.3    Greenwood, M.T.4
  • 62
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • L. Zhang, J. Yu, B.H. Park, K.W. Kinzler, and B. Vogelstein Role of BAX in the apoptotic response to anticancer agents Science 290 2000 989 992
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 63
    • 33746271951 scopus 로고    scopus 로고
    • Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry
    • DOI 10.1016/j.ymeth.2006.05.004, PII S1046202306000727
    • Bielawski, J., Szulc, Z.M., Hannun, Y.A., and Bielawska, A. (2006). Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry. Methods 39, 82-91. (Pubitemid 44107706)
    • (2006) Methods , vol.39 , Issue.2 , pp. 82-91
    • Bielawski, J.1    Szulc, Z.M.2    Hannun, Y.A.3    Bielawska, A.4
  • 65
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • DOI 10.1016/S0092-8674(02)01036-X
    • Kuwana, T., Mackey, M.R., Perkins, G., Ellisman, M.H., Latterich, M., Schneiter, R., Green, D.R., and Newmeyer, D.D. (2002). Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111, 331-342. (Pubitemid 35341388)
    • (2002) Cell , vol.111 , Issue.3 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6    Green, D.R.7    Newmeyer, D.D.8
  • 66
    • 0032742647 scopus 로고    scopus 로고
    • Assaying sphingosine kinase activity
    • DOI 10.1016/S0076-6879(00)11084-5
    • Olivera, A., Barlow, K.D., and Spiegel, S. (2000). Assaying sphingosine kinase activity. Methods Enzymol. 311, 215-223. (Pubitemid 29512768)
    • (1999) Methods in Enzymology , vol.311 , pp. 215-223
    • Olivera, A.1    Barlow, K.D.2    Spiegel, S.3
  • 67
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R.J., and Tjandra, N. (2000). Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103, 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 68
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
    • von Ahsen, O., Renken, C., Perkins, G., Kluck, R.M., Bossy-Wetzel, E., and Newmeyer, D.D. (2000). Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. J. Cell Biol. 150, 1027-1036.
    • (2000) J. Cell Biol. , vol.150 , pp. 1027-1036
    • Von Ahsen, O.1    Renken, C.2    Perkins, G.3    Kluck, R.M.4    Bossy-Wetzel, E.5    Newmeyer, D.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.