메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

N-terminally glutamate-substituted analogue of gramicidin A as protonophore and selective mitochondrial uncoupler

Author keywords

[No Author keywords available]

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; CARBOXYLIC ACID; GLUTAMIC ACID; GRAMICIDIN A; GRAMICIDIN A DERIVATIVE; GRAMICIDIN DERIVATIVE; IONOPHORE; PROTONOPHORE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VALINE;

EID: 84864209699     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041919     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 0013942130 scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchell P, (1966) Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol Rev 41: 445-502.
    • (1966) Biol Rev , vol.41 , pp. 445-502
    • Mitchell, P.1
  • 2
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey TE, (2003) Voltage-gated proton channels and other proton transfer pathways. Physiol Rev 83: 475-579.
    • (2003) Physiol Rev , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 3
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: new approaches to an old problem of bioenergetics
    • S0005-2728(97)00091-1 [Pii]
    • Skulachev VP, (1998) Uncoupling: new approaches to an old problem of bioenergetics. Biochim Biophys Acta 1363: 100-124. S0005-2728(97)00091-1 [pii].
    • (1998) Biochim Biophys Acta , vol.1363 , pp. 100-124
    • Skulachev, V.P.1
  • 5
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov SS, Skulachev VP, Starkov AA, (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416: 15-18.
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 6
    • 0030726009 scopus 로고    scopus 로고
    • "Mild" uncoupling of mitochondria
    • Starkov AA, (1997) "Mild" uncoupling of mitochondria. Biosci Rep 17: 273-279.
    • (1997) Biosci Rep , vol.17 , pp. 273-279
    • Starkov, A.A.1
  • 7
    • 0042433242 scopus 로고    scopus 로고
    • Regulation of brain mitochondrial H2O2 production by membrane potential and NAD(P)H redox state
    • Starkov AA, Fiskum G, (2003) Regulation of brain mitochondrial H2O2 production by membrane potential and NAD(P)H redox state. J Neurochem 86: 1101-1107.
    • (2003) J Neurochem , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 8
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev VP, (1996) Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q Rev Biophys 29: 169-202.
    • (1996) Q Rev Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 9
    • 67649803093 scopus 로고    scopus 로고
    • The optimal dosage and window of opportunity to maintain mitochondrial homeostasis following traumatic brain injury using the uncoupler FCCP
    • Pandya JD, Pauly JR, Sullivan PG, (2009) The optimal dosage and window of opportunity to maintain mitochondrial homeostasis following traumatic brain injury using the uncoupler FCCP. Exp Neurol 218: 381-389.
    • (2009) Exp Neurol , vol.218 , pp. 381-389
    • Pandya, J.D.1    Pauly, J.R.2    Sullivan, P.G.3
  • 12
    • 0035502402 scopus 로고    scopus 로고
    • Mitochondrial uncoupling as a target for drug development for the treatment of obesity
    • Harper JA, Dickinson K, Brand MD, (2001) Mitochondrial uncoupling as a target for drug development for the treatment of obesity. Obes Rev 2: 255-265.
    • (2001) Obes Rev , vol.2 , pp. 255-265
    • Harper, J.A.1    Dickinson, K.2    Brand, M.D.3
  • 13
    • 79961167173 scopus 로고    scopus 로고
    • 2,4-dinitrophenol (DNP): a weight loss agent with significant acute toxicity and risk of death
    • 10.1007/s13181-011-0162-6 [Doi]
    • Grundlingh J, Dargan PI, El-Zanfaly M, Wood DM, (2011) 2,4-dinitrophenol (DNP): a weight loss agent with significant acute toxicity and risk of death. J Med Toxicol 7: 205-212. 10.1007/s13181-011-0162-6 [doi].
    • (2011) J Med Toxicol , vol.7 , pp. 205-212
    • Grundlingh, J.1    Dargan, P.I.2    El-Zanfaly, M.3    Wood, D.M.4
  • 14
    • 0034116371 scopus 로고    scopus 로고
    • Mitochondrial targets of drug toxicity
    • 10.1146/Annurev.Pharmtox.40.1.353 [Doi]
    • Wallace KB, Starkov AA, (2000) Mitochondrial targets of drug toxicity. Annu Rev Pharmacol Toxicol 40: 353-388. 10.1146/annurev.pharmtox.40.1.353 [doi].
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 353-388
    • Wallace, K.B.1    Starkov, A.A.2
  • 15
    • 33744952060 scopus 로고    scopus 로고
    • Simultaneous monitoring of ionophore- and inhibitor-mediated plasma and mitochondrial membrane potential changes in cultured neurons
    • M510916200 [Pii];10.1074/Jbc.M510916200 [Doi]
    • Nicholls DG, (2006) Simultaneous monitoring of ionophore- and inhibitor-mediated plasma and mitochondrial membrane potential changes in cultured neurons. J Biol Chem 281: 14864-14874. M510916200 [pii];10.1074/jbc.M510916200 [doi].
    • (2006) J Biol Chem , vol.281 , pp. 14864-14874
    • Nicholls, D.G.1
  • 16
    • 0019486604 scopus 로고
    • Kinetics for development of gramicidin-induced ion permeability in unilamellar phospholipid vesicles
    • Clement NR, Gould JM, (1981) Kinetics for development of gramicidin-induced ion permeability in unilamellar phospholipid vesicles. Biochemistry 20: 1544-1548.
    • (1981) Biochemistry , vol.20 , pp. 1544-1548
    • Clement, N.R.1    Gould, J.M.2
  • 17
    • 0023010783 scopus 로고
    • Temperature jump as a new technique to study the kinetics of fast transport of protons across membranes
    • Krishnamoorthy G, (1986) Temperature jump as a new technique to study the kinetics of fast transport of protons across membranes. Biochemistry 25: 6666-6671.
    • (1986) Biochemistry , vol.25 , pp. 6666-6671
    • Krishnamoorthy, G.1
  • 18
    • 0023429474 scopus 로고
    • Proton permeation of lipid bilayers
    • Deamer DW, (1987) Proton permeation of lipid bilayers. J Bioenerg Biomembr 19: 457-479.
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 457-479
    • Deamer, D.W.1
  • 19
    • 0030786782 scopus 로고    scopus 로고
    • Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers
    • Cukierman S, Quigley EP, Crumrine DS, (1997) Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers. Biophys J 73: 2489-2502.
    • (1997) Biophys J , vol.73 , pp. 2489-2502
    • Cukierman, S.1    Quigley, E.P.2    Crumrine, D.S.3
  • 20
    • 0036151798 scopus 로고    scopus 로고
    • Membrane dipole potential modulates proton conductance through gramicidin channel: movement of negative ionic defects inside the channel
    • Rokitskaya TI, Kotova EA, Antonenko YN, (2002) Membrane dipole potential modulates proton conductance through gramicidin channel: movement of negative ionic defects inside the channel. Biophys J 82: 865-873.
    • (2002) Biophys J , vol.82 , pp. 865-873
    • Rokitskaya, T.I.1    Kotova, E.A.2    Antonenko, Y.N.3
  • 21
    • 0035997479 scopus 로고    scopus 로고
    • The role of Trp side chains in tuning single proton conduction through gramicidin channels
    • Gowen JA, Markham JC, Morrison SE, Cross TA, Busath DD, et al. (2002) The role of Trp side chains in tuning single proton conduction through gramicidin channels. Biophys J 83: 880-898.
    • (2002) Biophys J , vol.83 , pp. 880-898
    • Gowen, J.A.1    Markham, J.C.2    Morrison, S.E.3    Cross, T.A.4    Busath, D.D.5
  • 22
    • 0037214584 scopus 로고    scopus 로고
    • Proton transfer in gramicidin channels is modulated by the thickness of monoglyceride bilayers
    • Chernyshev A, Armstrong KM, Cukierman S, (2003) Proton transfer in gramicidin channels is modulated by the thickness of monoglyceride bilayers. Biophys J 84: 238-250.
    • (2003) Biophys J , vol.84 , pp. 238-250
    • Chernyshev, A.1    Armstrong, K.M.2    Cukierman, S.3
  • 23
    • 0038652575 scopus 로고
    • Some toxicological and pharmacological properties of gramicidin, tyrocidine and tyrothricin
    • Robinson HJ, Molitor H, (1942) Some toxicological and pharmacological properties of gramicidin, tyrocidine and tyrothricin. J Pharmacol Exp Ther 74: 75-82.
    • (1942) J Pharmacol Exp Ther , vol.74 , pp. 75-82
    • Robinson, H.J.1    Molitor, H.2
  • 25
    • 0030132565 scopus 로고    scopus 로고
    • Structural polymorphism of gramicidin A channels: ion conductivity and spectral studies
    • Sychev SV, Sukhanov SV, Barsukov LI, Ivanov VT, (1996) Structural polymorphism of gramicidin A channels: ion conductivity and spectral studies. J Pept Sci 2: 141-156.
    • (1996) J Pept Sci , vol.2 , pp. 141-156
    • Sychev, S.V.1    Sukhanov, S.V.2    Barsukov, L.I.3    Ivanov, V.T.4
  • 26
    • 0030758516 scopus 로고    scopus 로고
    • The conformational preference of gramicidin channels is a function of lipid bilayer thickness
    • Mobashery N, Nielsen C, Andersen OS, (1997) The conformational preference of gramicidin channels is a function of lipid bilayer thickness. FEBS Lett 412: 15-20.
    • (1997) FEBS Lett , vol.412 , pp. 15-20
    • Mobashery, N.1    Nielsen, C.2    Andersen, O.S.3
  • 27
    • 0015156126 scopus 로고
    • Thickness dependence in the action of gramicidin A on lipid bilayers
    • Goodall MC, (1971) Thickness dependence in the action of gramicidin A on lipid bilayers. Arch Biochem Biophys 147: 129-135.
    • (1971) Arch Biochem Biophys , vol.147 , pp. 129-135
    • Goodall, M.C.1
  • 28
    • 0015027073 scopus 로고
    • The gramicidin A transmembrane channel: a proposed pi(L,D) helix
    • Urry DW, (1971) The gramicidin A transmembrane channel: a proposed pi(L,D) helix. Proc Natl Acad Sci USA 68: 672-676.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 672-676
    • Urry, D.W.1
  • 29
    • 0038059300 scopus 로고
    • Structure of the gramicidin A channel: discrimination between the piL,D and the beta helix by electrical measurements with lipid bilayer membranes
    • Bamberg E, Apell HJ, Alpes H, (1977) Structure of the gramicidin A channel: discrimination between the piL,D and the beta helix by electrical measurements with lipid bilayer membranes. Proc Natl Acad Sci USA 74: 2402-2406.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2402-2406
    • Bamberg, E.1    Apell, H.J.2    Alpes, H.3
  • 30
    • 0018700296 scopus 로고
    • Formation of ionic channels in black lipid membranes by succinic derivatives of gramicidin A
    • Bamberg E, Alpes H, Apell HJ, Bradley R, Harter B, et al. (1979) Formation of ionic channels in black lipid membranes by succinic derivatives of gramicidin A. J Membrane Biol 50: 257-270.
    • (1979) J Membrane Biol , vol.50 , pp. 257-270
    • Bamberg, E.1    Alpes, H.2    Apell, H.J.3    Bradley, R.4    Harter, B.5
  • 31
    • 0018801170 scopus 로고
    • Transmembrane channel activity of gramicidin A analogs: effects of modification and deletion of the amino-terminal residue
    • Morrow JS, Veatch WR, Stryer L, (1979) Transmembrane channel activity of gramicidin A analogs: effects of modification and deletion of the amino-terminal residue. Journal Of Molecular Biology 132: 733-738.
    • (1979) Journal Of Molecular Biology , vol.132 , pp. 733-738
    • Morrow, J.S.1    Veatch, W.R.2    Stryer, L.3
  • 32
    • 0018408288 scopus 로고
    • N-acetyl gramicidin: single-channel properties and implications for channel structure
    • Szabo G, Urry DW, (1979) N-acetyl gramicidin: single-channel properties and implications for channel structure. Science 203: 55-57.
    • (1979) Science , vol.203 , pp. 55-57
    • Szabo, G.1    Urry, D.W.2
  • 33
    • 0027420654 scopus 로고
    • Formamidinium-induced dimer stabilization and flicker block behavior in homo- and heterodimer channels formed by gramicidin A and N-acetyl gramicidin A
    • Seoh SA, Busath DD, (1993) Formamidinium-induced dimer stabilization and flicker block behavior in homo- and heterodimer channels formed by gramicidin A and N-acetyl gramicidin A. Biophys J 65: 1817-1827.
    • (1993) Biophys J , vol.65 , pp. 1817-1827
    • Seoh, S.A.1    Busath, D.D.2
  • 35
    • 0000011528 scopus 로고
    • Desformylgramicidin A proton selective channel
    • Bezrukov SM, Irkhin AI, Melnik EI, (1984) Desformylgramicidin A proton selective channel. Biol Mem 1: 659-665.
    • (1984) Biol Mem , vol.1 , pp. 659-665
    • Bezrukov, S.M.1    Irkhin, A.I.2    Melnik, E.I.3
  • 36
    • 0033737006 scopus 로고    scopus 로고
    • Desformylgramicidin: a model channel with an extremely high water permeability
    • Saparov SM, Antonenko YN, Koeppe RE, Pohl P, (2000) Desformylgramicidin: a model channel with an extremely high water permeability. Biophys J 79: 2526-2534.
    • (2000) Biophys J , vol.79 , pp. 2526-2534
    • Saparov, S.M.1    Antonenko, Y.N.2    Koeppe, R.E.3    Pohl, P.4
  • 37
    • 0024413497 scopus 로고
    • Mechanism of uncoupling of oxidative phosphorylation by gramicidin
    • Rottenberg H, Koeppe RE, (1989) Mechanism of uncoupling of oxidative phosphorylation by gramicidin. Biochemistry 28: 4355-4360.
    • (1989) Biochemistry , vol.28 , pp. 4355-4360
    • Rottenberg, H.1    Koeppe, R.E.2
  • 38
    • 0000438245 scopus 로고
    • Respiration-driven proton translocation in rat liver mitochondria
    • Mitchell P, Moyle J, (1967) Respiration-driven proton translocation in rat liver mitochondria. Biochem J 105: 1147-1162.
    • (1967) Biochem J , vol.105 , pp. 1147-1162
    • Mitchell, P.1    Moyle, J.2
  • 41
    • 0016632804 scopus 로고
    • Membrane potentials in mitochondrial preparations as measured by means of a cyanine dye
    • 0005-2728(75)90163-2 [Pii]
    • Laris PC, Bahr DP, Chaffee RR, (1975) Membrane potentials in mitochondrial preparations as measured by means of a cyanine dye. Biochim Biophys Acta 376: 415-425. 0005-2728(75)90163-2 [pii].
    • (1975) Biochim Biophys Acta , vol.376 , pp. 415-425
    • Laris, P.C.1    Bahr, D.P.2    Chaffee, R.R.3
  • 42
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • 0014-5793(76)80434-6 [Pii]
    • Akerman KE, Wikstrom MK, (1976) Safranine as a probe of the mitochondrial membrane potential. FEBS Lett 68: 191-197. 0014-5793(76)80434-6 [pii].
    • (1976) FEBS Lett , vol.68 , pp. 191-197
    • Akerman, K.E.1    Wikstrom, M.K.2
  • 43
    • 0018263815 scopus 로고
    • Proton electrochemical gradient and rate of controlled respiration in mitochondria
    • 0005-2728(78)90035-X [Pii]
    • Azzone GF, Pozzan T, Massari S, Bragadin M, (1978) Proton electrochemical gradient and rate of controlled respiration in mitochondria. Biochim Biophys Acta 501: 296-306. 0005-2728(78)90035-X [pii].
    • (1978) Biochim Biophys Acta , vol.501 , pp. 296-306
    • Azzone, G.F.1    Pozzan, T.2    Massari, S.3    Bragadin, M.4
  • 44
    • 0014674557 scopus 로고
    • Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria
    • Liberman EA, Topaly VP, Tsofina LM, Jasaitis AA, Skulachev VP, (1969) Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria. Nature 222: 1076-1078.
    • (1969) Nature , vol.222 , pp. 1076-1078
    • Liberman, E.A.1    Topaly, V.P.2    Tsofina, L.M.3    Jasaitis, A.A.4    Skulachev, V.P.5
  • 45
    • 0018337793 scopus 로고
    • Uncouplers of oxidative phosphorylation
    • Heytler PG, (1979) Uncouplers of oxidative phosphorylation. Methods Enzymol 55: 462-42.
    • (1979) Methods Enzymol , vol.55 , pp. 442-462
    • Heytler, P.G.1
  • 46
    • 0025046339 scopus 로고
    • Uncouplers of oxidative phosphorylation
    • Terada H, (1990) Uncouplers of oxidative phosphorylation. Environ Health Perspect 87: 213-218.
    • (1990) Environ Health Perspect , vol.87 , pp. 213-218
    • Terada, H.1
  • 47
    • 67650085500 scopus 로고    scopus 로고
    • Safranine O as a fluorescent probe for mitochondrial membrane potential studied on the single particle level and in suspension
    • Perevoshchikova IV, Sorochkina AI, Zorov DB, Antonenko YN, (2009) Safranine O as a fluorescent probe for mitochondrial membrane potential studied on the single particle level and in suspension. Biochemistry (Mosc) 74: 663-671.
    • (2009) Biochemistry (Mosc) , vol.74 , pp. 663-671
    • Perevoshchikova, I.V.1    Sorochkina, A.I.2    Zorov, D.B.3    Antonenko, Y.N.4
  • 48
    • 0028238446 scopus 로고
    • Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes
    • Nicolay K, Laterveer FD, van Heerde WL, (1994) Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes. J Bioenerg Biomembr 26: 327-334.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 327-334
    • Nicolay, K.1    Laterveer, F.D.2    van Heerde, W.L.3
  • 49
    • 0019883199 scopus 로고
    • Pyranine (8-hydroxy-1,3,6-pyrenetrisulfonate) as a probe of internal aqueous hydrogen ion concentration in phospholipid vesicles
    • Clement NR, Gould JM, (1981) Pyranine (8-hydroxy-1,3,6-pyrenetrisulfonate) as a probe of internal aqueous hydrogen ion concentration in phospholipid vesicles. Biochemistry 20: 1534-1538.
    • (1981) Biochemistry , vol.20 , pp. 1534-1538
    • Clement, N.R.1    Gould, J.M.2
  • 51
    • 0015748249 scopus 로고
    • Respiratory control and the proton electrochemical gradient in mitochondria
    • Padan E, Rottenberg H, (1973) Respiratory control and the proton electrochemical gradient in mitochondria. Eur J Biochem 40: 431-437.
    • (1973) Eur J Biochem , vol.40 , pp. 431-437
    • Padan, E.1    Rottenberg, H.2
  • 52
    • 0017148614 scopus 로고
    • Anthroyl stearate as a fluorescent probe of chloroplast membranes
    • Vandermeulen DL, Govindjee (1976) Anthroyl stearate as a fluorescent probe of chloroplast membranes. Biochim Biophys Acta 449: 340-356.
    • (1976) Biochim Biophys Acta , vol.449 , pp. 340-356
    • Vandermeulen, D.L.1    Govindjee2
  • 53
    • 0014667599 scopus 로고
    • Effects associated with permeability changes caused by gramicidin A in electroplax membrane
    • Podleski T, Changeux JP, (1969) Effects associated with permeability changes caused by gramicidin A in electroplax membrane. Nature 221: 541-545.
    • (1969) Nature , vol.221 , pp. 541-545
    • Podleski, T.1    Changeux, J.P.2
  • 54
    • 0015938929 scopus 로고
    • The effects of the antibiotics gramicidin A, amphotericin B, and nystatin on the electrical properties of frog skeletal muscle
    • 0005-2736(73)90088-6 [Pii]
    • Leung J, Eisenberg RS, (1973) The effects of the antibiotics gramicidin A, amphotericin B, and nystatin on the electrical properties of frog skeletal muscle. Biochim Biophys Acta 298: 718-723. 0005-2736(73)90088-6 [pii].
    • (1973) Biochim Biophys Acta , vol.298 , pp. 718-723
    • Leung, J.1    Eisenberg, R.S.2
  • 55
    • 0033494264 scopus 로고    scopus 로고
    • Gramicidin toxicity in NG108-15 cells: protective effects of acetamidine and guanidine
    • Doebler JA, (1999) Gramicidin toxicity in NG108-15 cells: protective effects of acetamidine and guanidine. Cell Biol Toxicol 15: 279-289.
    • (1999) Cell Biol Toxicol , vol.15 , pp. 279-289
    • Doebler, J.A.1
  • 56
    • 84857357887 scopus 로고    scopus 로고
    • The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A
    • 10.1007/s00249-011-0764-6 [Doi]
    • Rokitskaya TI, Sorochkina AI, Kovalchuk SI, Egorova NS, Kotova EA, et al. (2012) The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A. Eur Biophys J 41: 129-138. 10.1007/s00249-011-0764-6 [doi].
    • (2012) Eur Biophys J , vol.41 , pp. 129-138
    • Rokitskaya, T.I.1    Sorochkina, A.I.2    Kovalchuk, S.I.3    Egorova, N.S.4    Kotova, E.A.5
  • 58
    • 0031729363 scopus 로고    scopus 로고
    • Ion channels as tools to monitor lipid bilayer-membrane protein interactions: gramicidin channels as molecular force transducers
    • Andersen OS, Nielsen C, Maer AM, Lundbaek JA, Goulian M, et al. (1999) Ion channels as tools to monitor lipid bilayer-membrane protein interactions: gramicidin channels as molecular force transducers. Methods Enzymol 294: 208-224.
    • (1999) Methods Enzymol , vol.294 , pp. 208-224
    • Andersen, O.S.1    Nielsen, C.2    Maer, A.M.3    Lundbaek, J.A.4    Goulian, M.5
  • 60
    • 77957010110 scopus 로고
    • Isolation of liver or kidney mitochondria
    • Johnson D, Lardy H, (1967) Isolation of liver or kidney mitochondria. Methods Enzymol 10: 94-96.
    • (1967) Methods Enzymol , vol.10 , pp. 94-96
    • Johnson, D.1    Lardy, H.2
  • 62
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • Denizot F, Lang R, (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J Immunol Methods 89: 271-277.
    • (1986) J Immunol Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 63
    • 0033603586 scopus 로고    scopus 로고
    • A mechanism for tamoxifen-mediated inhibition of acidification
    • Chen Y, Schindler M, Simon SM, (1999) A mechanism for tamoxifen-mediated inhibition of acidification. J Biol Chem 274: 18364-18373.
    • (1999) J Biol Chem , vol.274 , pp. 18364-18373
    • Chen, Y.1    Schindler, M.2    Simon, S.M.3
  • 64
    • 33947480633 scopus 로고
    • Methods for the formation of single bimolecular lipid membranes in aqueous solution
    • Mueller P, Rudin DO, Tien HT, Wescott WC, (1963) Methods for the formation of single bimolecular lipid membranes in aqueous solution. J Phys Chem 67: 534-535.
    • (1963) J Phys Chem , vol.67 , pp. 534-535
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.