메뉴 건너뛰기




Volumn 99, Issue 9, 2010, Pages 2917-2925

Pores formed by Baxα5 relax to a smaller size and keep at equilibrium

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78349267221     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.08.068     Document Type: Article
Times cited : (72)

References (57)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature. 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 77955907520 scopus 로고    scopus 로고
    • Permeabilization of the outer mitochondrial membrane by Bcl-2 proteins
    • García-Sáez, A. J., G. Fuertes., J. Salgado. 2010. Permeabilization of the outer mitochondrial membrane by Bcl-2 proteins. Adv. Exp. Med. Biol. 677:91-105.
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 91-105
    • García-Sáez, A.J.1    Fuertes, G.2    Salgado, J.3
  • 3
    • 77955875669 scopus 로고    scopus 로고
    • Role of membrane lipids for the activity of pore forming peptides and proteins
    • Fuertes, G., D. Giménez., J. Salgado. 2010. Role of membrane lipids for the activity of pore forming peptides and proteins. Adv. Exp. Med. Biol. 677:31-55.
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 31-55
    • Fuertes, G.1    Giménez, D.2    Salgado, J.3
  • 4
    • 77949394595 scopus 로고    scopus 로고
    • Synthetic peptides derived from pro-and anti-apoptotic BCL-2 family members have distinct membrane behaviour reflecting functional divergence
    • Guillemin, Y., J. López., A. Aouacheria. 2010. Synthetic peptides derived from pro-and anti-apoptotic BCL-2 family members have distinct membrane behaviour reflecting functional divergence. PLoS ONE. 5: e9066.
    • (2010) PLoS ONE , vol.5
    • Guillemin, Y.1    López, J.2    Aouacheria, A.3
  • 5
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • García-Sáez, A. J., M. Coraiola., J. Salgado. 2005. Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins. Biophys. J. 88:3976-3990.
    • (2005) Biophys. J. , vol.88 , pp. 3976-3990
    • García-Sáez, A.J.1    Coraiola, M.2    Salgado, J.3
  • 6
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • García-Sáez, A. J., M. Coraiola., J. Salgado. 2006. Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores. FEBS J. 273:971-981.
    • (2006) FEBS J. , vol.273 , pp. 971-981
    • García-Sáez, A.J.1    Coraiola, M.2    Salgado, J.3
  • 7
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. 2000. Action of antimicrobial peptides: two-state model. Biochemistry. 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 8
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • Almeida, P. F., and A. Pokorny. 2009. Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry. 48:8083-8093.
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 9
    • 28544437689 scopus 로고    scopus 로고
    • Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability
    • Tamba, Y., and M. Yamazaki. 2005. Single giant unilamellar vesicle method reveals effect of antimicrobial peptide magainin 2 on membrane permeability. Biochemistry. 44:15823-15833.
    • (2005) Biochemistry , vol.44 , pp. 15823-15833
    • Tamba, Y.1    Yamazaki, M.2
  • 10
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • Lee, M. T., W. C. Hung., H. W. Huang. 2008. Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides. Proc. Natl. Acad. Sci. USA. 105:5087-5092.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5087-5092
    • Lee, M.T.1    Hung, W.C.2    Huang, H.W.3
  • 11
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K., O. Murase., K. Miyajima. 1996. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry. 35:11361-11368.
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 12
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., O. Murase., K. Miyajima. 1995. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry. 34:6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 13
    • 65249174105 scopus 로고    scopus 로고
    • Magainin 2-induced pore formation in the lipid membranes depends on its concentration in the membrane interface
    • Tamba, Y., and M. Yamazaki. 2009. Magainin 2-induced pore formation in the lipid membranes depends on its concentration in the membrane interface. J. Phys. Chem. B. 113:4846-4852.
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 4846-4852
    • Tamba, Y.1    Yamazaki, M.2
  • 14
    • 40149107726 scopus 로고    scopus 로고
    • A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A
    • Gregory, S. M., A. Cavenaugh., P. F. Almeida. 2008. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A. Biophys. J. 94:1667-1680.
    • (2008) Biophys. J. , vol.94 , pp. 1667-1680
    • Gregory, S.M.1    Cavenaugh, A.2    Almeida, P.F.3
  • 15
    • 0029904095 scopus 로고    scopus 로고
    • Membrane pores induced by magainin
    • Ludtke, S. J., K. He., H. W. Huang. 1996. Membrane pores induced by magainin. Biochemistry. 35:13723-13728.
    • (1996) Biochemistry , vol.35 , pp. 13723-13728
    • Ludtke, S.J.1    He, K.2    Huang, H.W.3
  • 16
    • 52049109183 scopus 로고    scopus 로고
    • Toroidal pores formed by antimicrobial peptides show significant disorder
    • Sengupta, D., H. Leontiadou., S. J. Marrink. 2008. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta. 1778:2308-2317.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2308-2317
    • Sengupta, D.1    Leontiadou, H.2    Marrink, S.J.3
  • 18
    • 77950860384 scopus 로고    scopus 로고
    • Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy
    • Fantner, G. E., R. J. Barbero., A. M. Belcher. 2010. Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy. Nat. Nanotechnol. 5:280-285.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 280-285
    • Fantner, G.E.1    Barbero, R.J.2    Belcher, A.M.3
  • 19
    • 48249157851 scopus 로고    scopus 로고
    • Biomolecular engineering by combinatorial design and high-throughput screening: Small, soluble peptides that permeabilize membranes
    • Rathinakumar, R., and W. C. Wimley. 2008. Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes. J. Am. Chem. Soc. 130:9849-9858.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 9849-9858
    • Rathinakumar, R.1    Wimley, W.C.2
  • 20
    • 58849140539 scopus 로고    scopus 로고
    • Magainin 2 revisited: A test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles
    • Gregory, S. M., A. Pokorny, and P. F. F. Almeida. 2009. Magainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles. Biophys. J. 96:116-131.
    • (2009) Biophys. J. , vol.96 , pp. 116-131
    • Gregory, S.M.1    Pokorny, A.2    Almeida, P.F.F.3
  • 21
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittininduced leakage mechanism of lipid vesicles
    • Rex, S., and G. Schwarz. 1998. Quantitative studies on the melittininduced leakage mechanism of lipid vesicles. Biochemistry. 37:2336-2345.
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 22
    • 0025042733 scopus 로고
    • Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA
    • Parente, R. A., S. Nir, and F. C. Szoka, Jr. 1990. Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA. Biochemistry. 29:8720-8728.
    • (1990) Biochemistry , vol.29 , pp. 8720-8728
    • Parente, R.A.1    Nir, S.2    Szoka Jr., F.C.3
  • 23
    • 58749085926 scopus 로고    scopus 로고
    • Magainin 2 in action: Distinct modes of membrane permeabilization in living bacterial and mammalian cells
    • Imura, Y., N. Choda, and K. Matsuzaki. 2008. Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells. Biophys. J. 95:5757-5765.
    • (2008) Biophys. J. , vol.95 , pp. 5757-5765
    • Imura, Y.1    Choda, N.2    Matsuzaki, K.3
  • 24
    • 3042743487 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli
    • Mangoni, M. L., N. Papo., A. C. Rinaldi. 2004. Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli. Biochem. J. 380:859-865.
    • (2004) Biochem. J. , vol.380 , pp. 859-865
    • Mangoni, M.L.1    Papo, N.2    Rinaldi, A.C.3
  • 25
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • Anderluh, G., and J. H. Lakey. 2008. Disparate proteins use similar architectures to damage membranes. Trends Biochem. Sci. 33:482-490.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 26
    • 67649396451 scopus 로고    scopus 로고
    • Free energies of molecular bound states in lipid bilayers: Lethal concentrations of antimicrobial peptides
    • Huang, H. W. 2009. Free energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptides. Biophys. J. 96:3263-3272.
    • (2009) Biophys. J. , vol.96 , pp. 3263-3272
    • Huang, H.W.1
  • 27
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • Matsuzaki, K., S. Yoneyama, and K. Miyajima. 1997. Pore formation and translocation of melittin. Biophys. J. 73:831-838.
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 28
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu, Y., H. W. Huang, and G. A. Olah. 1990. Method of oriented circular dichroism. Biophys. J. 57:797-806.
    • (1990) Biophys. J. , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 29
    • 17844363968 scopus 로고    scopus 로고
    • Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR
    • Glaser, R. W., C. Sachse., A. S. Ulrich. 2005. Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR. Biophys. J. 88:3392-3397.
    • (2005) Biophys. J. , vol.88 , pp. 3392-3397
    • Glaser, R.W.1    Sachse, C.2    Ulrich, A.S.3
  • 30
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke, S., K. He, and H. Huang. 1995. Membrane thinning caused by magainin 2. Biochemistry. 34:16764-16769.
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 31
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • Qian, S., W. Wang., H. W. Huang. 2008. Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores. Proc. Natl. Acad. Sci. USA. 105:17379-17383.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Huang, H.W.3
  • 32
    • 68949145453 scopus 로고    scopus 로고
    • Characterization of antibiotic peptide pores using cryo-EM and comparison to neutron scattering
    • Han, M., Y. Mei., S. J. Ludtke. 2009. Characterization of antibiotic peptide pores using cryo-EM and comparison to neutron scattering. Biophys. J. 97:164-172.
    • (2009) Biophys. J. , vol.97 , pp. 164-172
    • Han, M.1    Mei, Y.2    Ludtke, S.J.3
  • 33
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial, N. N., and S. J. Korsmeyer. 2004. Cell death: critical control points. Cell. 116:205-219.
    • (2004) Cell. , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 34
    • 0033545722 scopus 로고    scopus 로고
    • Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations
    • Basañez, G., A. Nechushtan., R. J. Youle. 1999. Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations. Proc. Natl. Acad. Sci. USA. 96:5492-5497.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5492-5497
    • Basañez, G.1    Nechushtan, A.2    Youle, R.J.3
  • 35
    • 3142746012 scopus 로고    scopus 로고
    • Lipidic pore formation by the concerted action of proapoptotic BAX and tBID
    • Terrones, O., B. Antonsson., G. Basañez. 2004. Lipidic pore formation by the concerted action of proapoptotic BAX and tBID. J. Biol. Chem. 279:30081-30091.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30081-30091
    • Terrones, O.1    Antonsson, B.2    Basañez, G.3
  • 36
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a Bax-derived peptide: Effect on the line tension of the membrane probed by AFM
    • García-Sáez, A. J., S. Chiantia., P. Schwille. 2007. Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM. Biophys. J. 93:103-112.
    • (2007) Biophys. J. , vol.93 , pp. 103-112
    • García-Sáez, A.J.1    Chiantia, S.2    Schwille, P.3
  • 37
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., R. J. Youle, and N. Tjandra. 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
  • 38
    • 0242317915 scopus 로고    scopus 로고
    • Liposomes in the study of pore-forming toxins
    • Dalla Serra, M., and G. Menestrina. 2003. Liposomes in the study of pore-forming toxins. Methods Enzymol. 372:99-124.
    • (2003) Methods Enzymol. , vol.372 , pp. 99-124
    • Serra, D.M.1    Menestrina, G.2
  • 39
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana, T., M. R. Mackey., D. D. Newmeyer. 2002. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell. 111:331-342.
    • (2002) Cell. , vol.111 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Newmeyer, D.D.3
  • 40
    • 0026328559 scopus 로고
    • Fluorescence assay for phospholipid membrane asymmetry
    • McIntyre, J. C., and R. G. Sleight. 1991. Fluorescence assay for phospholipid membrane asymmetry. Biochemistry. 30:11819-11827.
    • (1991) Biochemistry , vol.30 , pp. 11819-11827
    • McIntyre, J.C.1    Sleight, R.G.2
  • 41
    • 0242424071 scopus 로고
    • Lipid swelling and liposome formation mediated by electric fields
    • Dimitrov, D., and M. Angelova. 1988. Lipid swelling and liposome formation mediated by electric fields. Bioelectrochem. Bioenerg. 19:323-336.
    • (1988) Bioelectrochem. Bioenerg , vol.19 , pp. 323-336
    • Dimitrov, D.1    Angelova, M.2
  • 42
    • 1942454738 scopus 로고    scopus 로고
    • Lipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy
    • Kahya, N., D. Scherfeld., P. Schwille. 2004. Lipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy. J. Struct. Biol. 147:77-89.
    • (2004) J. Struct. Biol. , vol.147 , pp. 77-89
    • Kahya, N.1    Scherfeld, D.2    Schwille, P.3
  • 43
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • Schön, P., A. J. García-Sáez., P. Schwille. 2008. Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys. J. 95:691-698.
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schön, P.1    García-Sáez, A.J.2    Schwille, P.3
  • 44
    • 33746714404 scopus 로고    scopus 로고
    • Translocation of phospholipids and dithionite permeability in liquid-ordered and liquiddisordered membranes
    • Moreno, M. J., L. M. Estronca, and W. L. Vaz. 2006. Translocation of phospholipids and dithionite permeability in liquid-ordered and liquiddisordered membranes. Biophys. J. 91:873-881.
    • (2006) Biophys. J. , vol.91 , pp. 873-881
    • Moreno, M.J.1    Estronca, L.M.2    Vaz, W.L.3
  • 45
    • 0027161307 scopus 로고
    • Dithionite penetration through phospholipid bilayers as a measure of defects in lipid molecular packing
    • Langner, M., and S. W. Hui. 1993. Dithionite penetration through phospholipid bilayers as a measure of defects in lipid molecular packing. Chem. Phys. Lipids. 65:23-30.
    • (1993) Chem. Phys. Lipids , vol.65 , pp. 23-30
    • Langner, M.1    Hui, S.W.2
  • 46
    • 24144461618 scopus 로고    scopus 로고
    • Direct visualization of membrane leakage induced by the antibiotic peptides: Maculatin, citropin, and aurein
    • Ambroggio, E. E., F. Separovic., L. A. Bagatolli. 2005. Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein. Biophys. J. 89:1874-1881.
    • (2005) Biophys. J. , vol.89 , pp. 1874-1881
    • Ambroggio, E.E.1    Separovic, F.2    Bagatolli, L.A.3
  • 47
    • 0019871607 scopus 로고
    • Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins
    • Weinstein, J. N., R. D. Klausner., R. Blumenthal. 1981. Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins. Biochim. Biophys. Acta. 647:270-284.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 270-284
    • Weinstein, J.N.1    Klausner, R.D.2    Blumenthal, R.3
  • 48
    • 34047238809 scopus 로고    scopus 로고
    • Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers
    • Yandek, L. E., A. Pokorny., P. F. Almeida. 2007. Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers. Biophys. J. 92:2434-2444.
    • (2007) Biophys. J. , vol.92 , pp. 2434-2444
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.3
  • 49
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluorescence requenching
    • Ladokhin, A. S., W. C. Wimley, and S. H. White. 1995. Leakage of membrane vesicle contents: determination of mechanism using fluorescence requenching. Biophys. J. 69:1964-1971.
    • (1995) Biophys. J. , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 50
    • 0028784101 scopus 로고
    • Assessment of inflammatory events in epithelial permeability: A rapid screening method using fluorescein dextrans
    • Sanders, S. E., J. L. Madara., S. P. Colgan. 1995. Assessment of inflammatory events in epithelial permeability: a rapid screening method using fluorescein dextrans. Epithelial Cell Biol. 4:25-34.
    • (1995) Epithelial Cell. Biol. , vol.4 , pp. 25-34
    • Sanders, S.E.1    Madara, J.L.2    Colgan, S.P.3
  • 51
    • 37349082255 scopus 로고    scopus 로고
    • High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor
    • Mirkin, N., J. Jaconcic., A. Moreno. 2008. High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor. Proteins. 70:83-92.
    • (2008) Proteins , vol.70 , pp. 83-92
    • Mirkin, N.1    Jaconcic, J.2    Moreno, A.3
  • 52
    • 0037341542 scopus 로고    scopus 로고
    • Cascades of transient pores in giant vesicles: Line tension and transport
    • Karatekin, E., O. Sandre., F. Brochard-Wyart. 2003. Cascades of transient pores in giant vesicles: line tension and transport. Biophys. J. 84:1734-1749.
    • (2003) Biophys. J. , vol.84 , pp. 1734-1749
    • Karatekin, E.1    Sandre, O.2    Brochard-Wyart, F.3
  • 53
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang, H. W., F. Y. Chen, and M. T. Lee. 2004. Molecular mechanism of peptide-induced pores in membranes. Phys. Rev. Lett. 92:198304.
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 54
    • 70350315093 scopus 로고    scopus 로고
    • Stability of asymmetric lipid bilayers assessed by molecular dynamics simulations
    • Esteban-Martín, S., H. J. Risselada, J. Salgado, and S. J. Marrink. 2009. Stability of asymmetric lipid bilayers assessed by molecular dynamics simulations. J. Am. Chem. Soc. 131:15194-15202.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15194-15202
    • Esteban-Martín, S.1    Risselada, H.J.2    Salgado, J.3    Marrink, S.J.4
  • 55
    • 77949897877 scopus 로고    scopus 로고
    • Molecular details of Bax activation, oligomerization, and membrane insertion
    • Bleicken, S., M. Classen., E. Bordignon. 2010. Molecular details of Bax activation, oligomerization, and membrane insertion. J. Biol. Chem. 285:6636-6647.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6636-6647
    • Bleicken, S.1    Classen, M.2    Bordignon, E.3
  • 56
    • 65349136027 scopus 로고    scopus 로고
    • Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formation
    • Schafer, B., J. Quispe., T. Kuwana. 2009. Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formation. Mol. Biol. Cell. 20:2276-2285.
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 2276-2285
    • Schafer, B.1    Quispe, J.2    Kuwana, T.3
  • 57
    • 0036435610 scopus 로고    scopus 로고
    • Direct evidence for membrane pore formation by the apoptotic protein Bax
    • Epand, R. F., J. C. Martinou., C. M. Yip. 2002. Direct evidence for membrane pore formation by the apoptotic protein Bax. Biochem. Biophys. Res. Commun. 298:744-749.
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 744-749
    • Epand, R.F.1    Martinou, J.C.2    Yip, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.