메뉴 건너뛰기




Volumn 1788, Issue 3, 2009, Pages 623-631

How does the Bax-α1 targeting sequence interact with mitochondrial membranes? The role of cardiolipin

Author keywords

Apoptosis; Bax N terminal; Cardiolipin; Solid State NMR

Indexed keywords

CARDIOLIPIN; PROTEIN BAX; PROTEIN BAX ALPHA1; UNCLASSIFIED DRUG;

EID: 60849120099     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.12.014     Document Type: Article
Times cited : (41)

References (55)
  • 1
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • Okada H., and Mak T.W. Pathways of apoptotic and non-apoptotic death in tumour cells. Nat. Rev., Cancer 4 (2004) 592-603
    • (2004) Nat. Rev., Cancer , vol.4 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 2
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995) 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 3
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., and Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 4
    • 0036716281 scopus 로고    scopus 로고
    • The BCL2 family: regulators of the cellular life-or-death switch
    • Cory S., and Adams J.M. The BCL2 family: regulators of the cellular life-or-death switch. Nat. Rev., Cancer 2 (2002) 647-656
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 5
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 6
    • 0033288336 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: an overview
    • Kroemer G. Mitochondrial control of apoptosis: an overview. Biochem. Soc. Symp. 66 (1999) 1-15
    • (1999) Biochem. Soc. Symp. , vol.66 , pp. 1-15
    • Kroemer, G.1
  • 7
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane D.M., Bossy-Wetzel E., Waterhouse N.J., Cotter T.G., and Green D.R. Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J. Biol. Chem. 274 (1999) 2225-2233
    • (1999) J. Biol. Chem. , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 10
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X-L during apoptosis
    • Hsu Y.T., Wolter K.G., and Youle R.J. Cytosol-to-membrane redistribution of Bax and Bcl-X-L during apoptosis. Proc. Natl. Acad. Sci. U. S. A 94 (1997) 3668-3672
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 11
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., and Reed J.C. Mitochondrial control of cell death. Nat. Med. 6 (2000) 513-519
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 12
    • 0034869026 scopus 로고    scopus 로고
    • Conformational change of Bax: a question of life or death
    • Roucou X., and Martinou J.C. Conformational change of Bax: a question of life or death. Cell Death Differ. 8 (2001) 875-877
    • (2001) Cell Death Differ. , vol.8 , pp. 875-877
    • Roucou, X.1    Martinou, J.C.2
  • 13
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., and Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103 (2000) 645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 16
    • 47249105254 scopus 로고    scopus 로고
    • Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms
    • Valentijn A.J., Upton J.P., Bates N., and Gilmore A.P. Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms. Cell Death Differ. (2008)
    • (2008) Cell Death Differ.
    • Valentijn, A.J.1    Upton, J.P.2    Bates, N.3    Gilmore, A.P.4
  • 18
    • 42149094346 scopus 로고    scopus 로고
    • Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane
    • Lucken-Ardjomande S., Montessuit S., and Martinou J.C. Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane. Cell Death Differ. 15 (2008) 929-937
    • (2008) Cell Death Differ. , vol.15 , pp. 929-937
    • Lucken-Ardjomande, S.1    Montessuit, S.2    Martinou, J.C.3
  • 20
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M., Rua D., and Greenberg M.L. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39 (2000) 257-288
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 21
    • 33847146719 scopus 로고    scopus 로고
    • Pro-apoptotic bax-alpha1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes
    • Sani M.A., Loudet C., Grobner G., and Dufourc E.J. Pro-apoptotic bax-alpha1 synthesis and evidence for beta-sheet to alpha-helix conformational change as triggered by negatively charged lipid membranes. J. Pept. Sci. 13 (2006) 100-106
    • (2006) J. Pept. Sci. , vol.13 , pp. 100-106
    • Sani, M.A.1    Loudet, C.2    Grobner, G.3    Dufourc, E.J.4
  • 22
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N., and Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209 (1993) 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 23
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 24
    • 4244085403 scopus 로고    scopus 로고
    • Analysis of protein CD spectra: comparison of CONTIN, SELCON3, and CDSSTR methods in CDPro software
    • Sreerama N., and Woody R.W. Analysis of protein CD spectra: comparison of CONTIN, SELCON3, and CDSSTR methods in CDPro software. Biophys. J. 78 (2000) 334A
    • (2000) Biophys. J. , vol.78
    • Sreerama, N.1    Woody, R.W.2
  • 25
    • 18644365098 scopus 로고    scopus 로고
    • Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association
    • Lindstrom F., Williamson P.T., and Grobner G. Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association. J. Am. Chem. Soc. 127 (2005) 6610-6616
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6610-6616
    • Lindstrom, F.1    Williamson, P.T.2    Grobner, G.3
  • 26
    • 0018510430 scopus 로고
    • Deuterium magnetic resonance study of the gel and liquid crystalline phases of dipalmitoyl phosphatidylcholine
    • Davis J.H. Deuterium magnetic resonance study of the gel and liquid crystalline phases of dipalmitoyl phosphatidylcholine. Biophys. J. 27 (1979) 339-358
    • (1979) Biophys. J. , vol.27 , pp. 339-358
    • Davis, J.H.1
  • 27
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane-proteins by attenuated total reflection Fourier-transform infrared-spectroscopy on hydrated films
    • Goormaghtigh E., Cabiaux V., and Ruysschaert J.M. Secondary structure and dosage of soluble and membrane-proteins by attenuated total reflection Fourier-transform infrared-spectroscopy on hydrated films. Eur. J. Biochem. 193 (1990) 409-420
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 28
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh E., Raussens V., and Ruysschaert J.M. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1422 (1999) 105-185
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 29
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • Goormaghtigh E., Cabiaux V., and Ruysschaert J.M. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. Subcell. Biochem. 23 (1994) 329-450
    • (1994) Subcell. Biochem. , vol.23 , pp. 329-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 30
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm L.K., and Tatulian S.A. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30 (1997) 365-429
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 31
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist M., Lindstrom F., Watts A., and Grobner G. Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335 (2004) 1039-1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 32
    • 0026511937 scopus 로고
    • Dynamics of phosphate head groups in biomembranes - comprehensive analysis using P-31 nuclear-magnetic-resonance lineshape and relaxation-time measurements
    • Dufourc E.J., Mayer C., Stohrer J., Althoff G., and Kothe G. Dynamics of phosphate head groups in biomembranes - comprehensive analysis using P-31 nuclear-magnetic-resonance lineshape and relaxation-time measurements. Biophys. J. 61 (1992) 42-57
    • (1992) Biophys. J. , vol.61 , pp. 42-57
    • Dufourc, E.J.1    Mayer, C.2    Stohrer, J.3    Althoff, G.4    Kothe, G.5
  • 33
    • 0011179051 scopus 로고
    • P-31 and H-1-NMR pulse sequences to measure lineshapes, T1z and T2e relaxation-times in biological-membranes
    • Dufourc E.J., Mayer C., Stohrer J., and Kothe G. P-31 and H-1-NMR pulse sequences to measure lineshapes, T1z and T2e relaxation-times in biological-membranes. J. Chim. Phys. Pcb 89 (1992) 243-252
    • (1992) J. Chim. Phys. Pcb , vol.89 , pp. 243-252
    • Dufourc, E.J.1    Mayer, C.2    Stohrer, J.3    Kothe, G.4
  • 34
    • 33947380145 scopus 로고    scopus 로고
    • Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers
    • Pukala T.L., Boland M.P., Gehman J.D., Kuhn-Nentwig L., Separovic F., and Bowie J.H. Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers. Biochemistry 46 (2007) 3576-3585
    • (2007) Biochemistry , vol.46 , pp. 3576-3585
    • Pukala, T.L.1    Boland, M.P.2    Gehman, J.D.3    Kuhn-Nentwig, L.4    Separovic, F.5    Bowie, J.H.6
  • 35
    • 0034687122 scopus 로고    scopus 로고
    • Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study
    • Bonev B.B., Chan W.C., Bycroft B.W., Roberts G.C., and Watts A. Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study. Biochemistry 39 (2000) 11425-11433
    • (2000) Biochemistry , vol.39 , pp. 11425-11433
    • Bonev, B.B.1    Chan, W.C.2    Bycroft, B.W.3    Roberts, G.C.4    Watts, A.5
  • 36
    • 16644375466 scopus 로고    scopus 로고
    • Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers
    • Nomura K., Corzo G., Nakajima T., and Iwashita T. Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers. Biophys. J. 87 (2004) 2497-2507
    • (2004) Biophys. J. , vol.87 , pp. 2497-2507
    • Nomura, K.1    Corzo, G.2    Nakajima, T.3    Iwashita, T.4
  • 37
    • 24044479637 scopus 로고    scopus 로고
    • Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi- and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy
    • Castano S., and Desbat B. Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi- and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy. Biochim. Biophys. Acta 1715 (2005) 81-95
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 81-95
    • Castano, S.1    Desbat, B.2
  • 39
    • 33846562986 scopus 로고    scopus 로고
    • Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies
    • Ramamoorthy A., Kandasamy S.K., Lee D.K., Kidambi S., and Larson R.G. Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies. Biochemistry 46 (2007) 965-975
    • (2007) Biochemistry , vol.46 , pp. 965-975
    • Ramamoorthy, A.1    Kandasamy, S.K.2    Lee, D.K.3    Kidambi, S.4    Larson, R.G.5
  • 40
    • 33646231496 scopus 로고    scopus 로고
    • Cell selectivity correlates with membrane-specific interactions: a case study on the antimicrobial peptide G15 derived from granulysin
    • Ramamoorthy A., Thennarasu S., Tan A., Lee D.K., Clayberger C., and Krensky A.M. Cell selectivity correlates with membrane-specific interactions: a case study on the antimicrobial peptide G15 derived from granulysin. Biochim. Biophys. Acta 1758 (2006) 154-163
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 154-163
    • Ramamoorthy, A.1    Thennarasu, S.2    Tan, A.3    Lee, D.K.4    Clayberger, C.5    Krensky, A.M.6
  • 41
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian J.A. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta 1376 (1998) 401-415
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 42
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian J.A., Salemink I., de Planque M.R., Lindblom G., Koeppe Jr. R.E., and Greathouse D.V. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry 35 (1996) 1037-1045
    • (1996) Biochemistry , vol.35 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    de Planque, M.R.3    Lindblom, G.4    Koeppe Jr., R.E.5    Greathouse, D.V.6
  • 44
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • Baines C.P., Kaiser R.A., Sheiko T., Craigen W.J., and Molkentin J.D. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat. Cell Biol. 9 (2007) 550-555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 45
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G., Sharpe J.C., Galanis J., Brandt T.B., Hardwick J.M., and Zimmerberg J. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 277 (2002) 49360-49365
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 46
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S., Konishi A., Kodama T., and Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl. Acad. Sci. U. S. A 97 (2000) 3100-3105
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 47
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., Narita M., and Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 (1999) 483-487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 48
    • 0037070160 scopus 로고    scopus 로고
    • Involvement of the N-terminus of Bax in its intracellular localization and function
    • Cartron P.F., Moreau C., Oliver L., Mayat E., Meflah K., and Vallette F.M. Involvement of the N-terminus of Bax in its intracellular localization and function. FEBS Lett. 512 (2002) 95-100
    • (2002) FEBS Lett. , vol.512 , pp. 95-100
    • Cartron, P.F.1    Moreau, C.2    Oliver, L.3    Mayat, E.4    Meflah, K.5    Vallette, F.M.6
  • 49
    • 1542465184 scopus 로고    scopus 로고
    • Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis
    • Yethon J.A., Epand R.F., Leber B., Epand R.M., and Andrews D.W. Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J. Biol. Chem. 278 (2003) 48935-48941
    • (2003) J. Biol. Chem. , vol.278 , pp. 48935-48941
    • Yethon, J.A.1    Epand, R.F.2    Leber, B.3    Epand, R.M.4    Andrews, D.W.5
  • 51
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer lipid diffusion promoted by Bax: implications for apoptosis
    • Epand R.F., Martinou J.C., Montessuit S., and Epand R.M. Transbilayer lipid diffusion promoted by Bax: implications for apoptosis. Biochemistry 42 (2003) 14576-14582
    • (2003) Biochemistry , vol.42 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 52
    • 39149098440 scopus 로고    scopus 로고
    • Interplay between bax, reactive oxygen species production, and cardiolipin oxidation during apoptosis
    • Jiang J., Huang Z., Zhao Q., Feng W., Belikova N.A., and Kagan V.E. Interplay between bax, reactive oxygen species production, and cardiolipin oxidation during apoptosis. Biochem. Biophys. Res. Commun. 368 (2008) 145-150
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 145-150
    • Jiang, J.1    Huang, Z.2    Zhao, Q.3    Feng, W.4    Belikova, N.A.5    Kagan, V.E.6
  • 53
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber B., Lin J., and Andrews D.W. Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 12 (2007) 897-911
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 54
    • 33846287596 scopus 로고    scopus 로고
    • Phospholipid scramblase-3 regulates cardiolipin de novo biosynthesis and its resynthesis in growing HeLa cells
    • Van Q., Liu J., Lu B., Feingold K.R., Shi Y., Lee R.M., and Hatch G.M. Phospholipid scramblase-3 regulates cardiolipin de novo biosynthesis and its resynthesis in growing HeLa cells. Biochem. J. 401 (2007) 103-109
    • (2007) Biochem. J. , vol.401 , pp. 103-109
    • Van, Q.1    Liu, J.2    Lu, B.3    Feingold, K.R.4    Shi, Y.5    Lee, R.M.6    Hatch, G.M.7
  • 55
    • 10644224222 scopus 로고    scopus 로고
    • Studies of the interaction of substituted mutants of BAX with yeast mitochondria reveal that the C-terminal hydrophobic alpha-helix is a second ART sequence and plays a role in the interaction with anti-apoptotic BCL-x(L)
    • Arokium H., Camougrand N., Vallette F.M., and Manon S. Studies of the interaction of substituted mutants of BAX with yeast mitochondria reveal that the C-terminal hydrophobic alpha-helix is a second ART sequence and plays a role in the interaction with anti-apoptotic BCL-x(L). J. Biol. Chem. 279 (2004) 52566-52573
    • (2004) J. Biol. Chem. , vol.279 , pp. 52566-52573
    • Arokium, H.1    Camougrand, N.2    Vallette, F.M.3    Manon, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.