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Volumn 42, Issue 5, 2014, Pages 1460-1464

Lysosomotropic agents: Impact on lysosomal membrane permeabilization and cell death

Author keywords

Detergent; Lysosomal membrane; Lysosome; O methyl serine dodecylamine hydrochloride (MSDH); Permeabilization; Sphingosine

Indexed keywords

AMPHOPHILE; ANTINEOPLASTIC AGENT; DETERGENT; HYDROLASE; LYSOSOMOTROPIC DETERGENT; SPHINGOSINE; UNCLASSIFIED DRUG; AGENTS AFFECTING WATER, MOLECULE OR ION TRANSPORT; LIPID BILAYER;

EID: 84907188880     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140145     Document Type: Review
Times cited : (105)

References (47)
  • 1
    • 84881565288 scopus 로고    scopus 로고
    • The lysosome: From waste bag to potential therapeutic target
    • CrossRef PubMed
    • Appelqvist, H., Wäster, P., Ka˚gedal, K and Öllinger, K. (2013) The lysosome: from waste bag to potential therapeutic target. J. Mol. Cell Biol. 5, 214-226 CrossRef PubMed
    • (2013) J. Mol. Cell Biol. , vol.5 , pp. 214-226
    • Appelqvist, H.1    Wäster, P.2    Ka˚gedal, K.3    Öllinger, K.4
  • 2
    • 78649729542 scopus 로고    scopus 로고
    • Lysosomal membrane proteins: Life between acid and neutral conditions
    • CrossRef PubMed
    • Saftig, P., Schröder, B. and Blanz, J. (2010) Lysosomal membrane proteins: life between acid and neutral conditions. Biochem. Soc. Trans. 38, 1420-1423 CrossRef PubMed
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1420-1423
    • Saftig, P.1    Schröder, B.2    Blanz, J.3
  • 3
    • 63149196645 scopus 로고    scopus 로고
    • Principles of lysosomal membrane degradation: Cellular topology and biochemistry of lysosomal lipid degradation
    • CrossRef PubMed
    • Schulze, H., Kolter, T. and Sandhoff, K. (2009) Principles of lysosomal membrane degradation: cellular topology and biochemistry of lysosomal lipid degradation. Biochim. Biophys. Acta 1793, 674-683 CrossRef PubMed
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 674-683
    • Schulze, H.1    Kolter, T.2    Sandhoff, K.3
  • 4
    • 0025287536 scopus 로고
    • Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells
    • PubMed
    • Granger, B.L., Green, S.A., Gabel, C.A., Howe, C.L., Mellman, I. and Helenius, A. (1990) Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells. J. Biol. Chem. 265, 12036-12043 PubMed
    • (1990) J. Biol. Chem. , vol.265 , pp. 12036-12043
    • Granger, B.L.1    Green, S.A.2    Gabel, C.A.3    Howe, C.L.4    Mellman, I.5    Helenius, A.6
  • 7
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • CrossRef PubMed
    • Ka˚gedal, K., Zhao, M., Svensson, I. and Brunk, U.T. (2001) Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359, 335-343 CrossRef PubMed
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Ka˚gedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 8
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • PubMed
    • Roberg, K. and Öllinger, K. (1998) Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am. J. Pathol. 152, 1151-1156 PubMed
    • (1998) Am. J. Pathol. , vol.152 , pp. 1151-1156
    • Roberg, K.1    Öllinger, K.2
  • 10
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts
    • CrossRef PubMed
    • Roberg, K., Ka˚gedal, K. and Öllinger, K. (2002) Microinjection of cathepsin D induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161, 89-96 CrossRef PubMed
    • (2002) Am. J. Pathol. , vol.161 , pp. 89-96
    • Roberg, K.1    Ka˚gedal, K.2    Öllinger, K.3
  • 11
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • CrossRef PubMed
    • Cirman, T., Oresic, K., Mazovec, G.D., Turk, V., Reed, J.C. and Myers, R.M. (2004) Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem. 279, 3578-3587 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresic, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6
  • 12
    • 0032728949 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by a lysosomotropic agent, L-leucyl-L-leucine methyl ester
    • CrossRef PubMed
    • Uchimoto, T., Nohara, H., Kamehara, R., Iwamura, M., Watanabe, N. and Kobayashi, Y. (1999) Mechanism of apoptosis induced by a lysosomotropic agent, L-leucyl-L-leucine methyl ester. Apoptosis 4, 357-362 CrossRef PubMed
    • (1999) Apoptosis , vol.4 , pp. 357-362
    • Uchimoto, T.1    Nohara, H.2    Kamehara, R.3    Iwamura, M.4    Watanabe, N.5    Kobayashi, Y.6
  • 13
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen: Purification, distribution, intracellular localization and action on proteins
    • PubMed
    • Kirschke, H., Wiederanders, B., Bromme, D. and Rinne, A. (1989) Cathepsin S from bovine spleen: purification, distribution, intracellular localization and action on proteins. Biochem. J. 264, 467-473 PubMed
    • (1989) Biochem. J. , vol.264 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Bromme, D.3    Rinne, A.4
  • 15
    • 33745821268 scopus 로고    scopus 로고
    • Cytosolic acidification and lysosomal alkalinization during TNF-α induced apoptosis in U937 cells
    • CrossRef PubMed
    • Nilsson, C., Johansson, U., Johansson, A.C., Ka˚degal, K. and Öllinger, K. (2006) Cytosolic acidification and lysosomal alkalinization during TNF-α induced apoptosis in U937 cells. Apoptosis 11, 1149-1159 CrossRef PubMed
    • (2006) Apoptosis , vol.11 , pp. 1149-1159
    • Nilsson, C.1    Johansson, U.2    Johansson, A.C.3    Ka˚degal, K.4    Öllinger, K.5
  • 16
    • 29144446112 scopus 로고    scopus 로고
    • Sphingomyelins suppress the targeted disruption of lysosomes/endosomes by the photosensitizer NPe6 during photodynamic therapy
    • CrossRef PubMed
    • Caruso, J.A., Mathieu, P.A. and Reiners, Jr, J.J. (2005) Sphingomyelins suppress the targeted disruption of lysosomes/endosomes by the photosensitizer NPe6 during photodynamic therapy. Biochem. J. 392, 325-334 CrossRef PubMed
    • (2005) Biochem. J. , vol.392 , pp. 325-334
    • Caruso, J.A.1    Mathieu, P.A.2    Reiners, J.J.3
  • 19
    • 77951666702 scopus 로고    scopus 로고
    • Regulation of apoptosis-associated lysosomal membrane permeabilization
    • CrossRef PubMed
    • Johansson, A.C., Appelqvist, H., Nilsson, C., Ka˚degal, K., Roberg, K. and Öllinger, K. (2010) Regulation of apoptosis-associated lysosomal membrane permeabilization. Apoptosis 15, 527-540 CrossRef PubMed
    • (2010) Apoptosis , vol.15 , pp. 527-540
    • Johansson, A.C.1    Appelqvist, H.2    Nilsson, C.3    Ka˚degal, K.4    Roberg, K.5    Öllinger, K.6
  • 20
    • 0033756474 scopus 로고    scopus 로고
    • Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
    • CrossRef PubMed
    • Guicciardi, M.E., Deussing, J., Miyoshi, H., Bronk, S.F., Svingen, P.A., Peters, C., Kaufmann, S.H. and Gores, G.J. (2000) Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J. Clin. Invest. 106, 1127-1137 CrossRef PubMed
    • (2000) J. Clin. Invest. , vol.106 , pp. 1127-1137
    • Guicciardi, M.E.1    Deussing, J.2    Miyoshi, H.3    Bronk, S.F.4    Svingen, P.A.5    Peters, C.6    Kaufmann, S.H.7    Gores, G.J.8
  • 22
    • 0022869229 scopus 로고
    • Effects of weakly basic amines on proteolytic processing and terminal glycosylation of secretory proteins in cultured rat hepatocytes
    • PubMed
    • Oda, K., Koriyama, Y., Yamada, E. and Ikehara, Y. (1986) Effects of weakly basic amines on proteolytic processing and terminal glycosylation of secretory proteins in cultured rat hepatocytes. Biochem. J. 240, 739-745 PubMed
    • (1986) Biochem. J. , vol.240 , pp. 739-745
    • Oda, K.1    Koriyama, Y.2    Yamada, E.3    Ikehara, Y.4
  • 23
    • 79952037605 scopus 로고    scopus 로고
    • A high content screening assay for identifying lysosomotropic compounds
    • CrossRef PubMed
    • Nadanaciva, S., Lu, S., Gebhard, D.F., Jessen, B.A., Pennie, W.D. and Will, Y. (2011) A high content screening assay for identifying lysosomotropic compounds. Toxicol. In Vitro 25, 715-723 CrossRef PubMed
    • (2011) Toxicol. In Vitro , vol.25 , pp. 715-723
    • Nadanaciva, S.1    Lu, S.2    Gebhard, D.F.3    Jessen, B.A.4    Pennie, W.D.5    Will, Y.6
  • 25
    • 0025044550 scopus 로고
    • Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells
    • CrossRef PubMed
    • Thiele, D.L. and Lipsky, P.E. (1990) Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. Proc. Natl. Acad. Sci. U.S.A. 87, 83-87 CrossRef PubMed
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 83-87
    • Thiele, D.L.1    Lipsky, P.E.2
  • 26
    • 38349158920 scopus 로고    scopus 로고
    • Identification of new functional inhibitors of acid sphingomyelinase using a structure-property-activity relation model
    • CrossRef PubMed
    • Kornhuber, J., Tripal, P., Reichel, M., Terfloth, L., Bleich, S., Wiltfang, J. and Gulbins, E. (2008) Identification of new functional inhibitors of acid sphingomyelinase using a structure-property-activity relation model. J. Med. Chem. 51, 219-237 CrossRef PubMed
    • (2008) J. Med. Chem. , vol.51 , pp. 219-237
    • Kornhuber, J.1    Tripal, P.2    Reichel, M.3    Terfloth, L.4    Bleich, S.5    Wiltfang, J.6    Gulbins, E.7
  • 27
    • 0018656598 scopus 로고
    • Lysosomotropic agents. 1. Synthesis and cytotoxic action of lysosomotropic detergents
    • CrossRef PubMed
    • Firestone, R.A., Pisano, J.M. and Bonney, R.J. (1979) Lysosomotropic agents. 1. Synthesis and cytotoxic action of lysosomotropic detergents. J. Med. Chem. 22, 1130-1133 CrossRef PubMed
    • (1979) J. Med. Chem. , vol.22 , pp. 1130-1133
    • Firestone, R.A.1    Pisano, J.M.2    Bonney, R.J.3
  • 28
    • 0028957421 scopus 로고
    • The in vitro effects of three lysosomotropic detergents against three human tumor cell lines
    • CrossRef
    • Dubowchik, G.M., Gawlak, S.L. and Firestone, R.A. (1995) The in vitro effects of three lysosomotropic detergents against three human tumor cell lines. Bioorg. Med. Chem. Lett. 5, 893-898 CrossRef
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 893-898
    • Dubowchik, G.M.1    Gawlak, S.L.2    Firestone, R.A.3
  • 29
    • 0021069160 scopus 로고
    • Cell killing by lysosomotropic detergents
    • CrossRef PubMed
    • Miller, D.K., Griffiths, E., Lenard, J. and Firestone, R.A. (1983) Cell killing by lysosomotropic detergents. J. Cell Biol. 97, 1841-1851 CrossRef PubMed
    • (1983) J. Cell Biol. , vol.97 , pp. 1841-1851
    • Miller, D.K.1    Griffiths, E.2    Lenard, J.3    Firestone, R.A.4
  • 30
    • 0023224018 scopus 로고
    • The role of lysosomal enzymes in killing of mammalian cells by the lysosomotropic detergent N-dodecylimidazole
    • CrossRef PubMed
    • Wilson, P.D., Firestone, R.A. and Lenard, J. (1987) The role of lysosomal enzymes in killing of mammalian cells by the lysosomotropic detergent N-dodecylimidazole. J. Cell Biol. 104, 1223-1229 CrossRef PubMed
    • (1987) J. Cell Biol. , vol.104 , pp. 1223-1229
    • Wilson, P.D.1    Firestone, R.A.2    Lenard, J.3
  • 31
    • 79951829451 scopus 로고    scopus 로고
    • Attenuation of the lysosomal death pathway by lysosomal cholesterol accumulation
    • CrossRef PubMed
    • Appelqvist, H., Nilsson, C., Garner, B., Brown, A.J., Ka˚gedal, K. and Öllinger, K. (2011) Attenuation of the lysosomal death pathway by lysosomal cholesterol accumulation. Am. J. Pathol. 178, 629-639 CrossRef PubMed
    • (2011) Am. J. Pathol. , vol.178 , pp. 629-639
    • Appelqvist, H.1    Nilsson, C.2    Garner, B.3    Brown, A.J.4    Ka˚gedal, K.5    Öllinger, K.6
  • 33
    • 84887473756 scopus 로고    scopus 로고
    • Siramesine triggers cell death through destabilisation of mitochondria, but not lysosomes
    • CrossRef PubMed
    • Česen, M.H., Repnik, U., Turk, V. and Turk, B. (2013) Siramesine triggers cell death through destabilisation of mitochondria, but not lysosomes. Cell Death Dis. 4, e818 CrossRef PubMed
    • (2013) Cell Death Dis , vol.4 , pp. e818
    • Česen, M.H.1    Repnik, U.2    Turk, V.3    Turk, B.4
  • 34
    • 84861436735 scopus 로고    scopus 로고
    • Sphingosine mediates TNFα-induced lysosomal membrane permeabilization and ensuing programmed cell death in hepatoma cells
    • CrossRef PubMed
    • Ullio, C., Casas, J., Brunk, U.T., Sala, G., Fabriàs, G., Ghidoni, R., Bonelli, G., Baccino, F.M. and Autelli, R. (2012) Sphingosine mediates TNFα-induced lysosomal membrane permeabilization and ensuing programmed cell death in hepatoma cells. J. Lipid Res. 53, 1134-1143 CrossRef PubMed
    • (2012) J. Lipid Res. , vol.53 , pp. 1134-1143
    • Ullio, C.1    Casas, J.2    Brunk, U.T.3    Sala, G.4    Fabriàs, G.5    Ghidoni, R.6    Bonelli, G.7    Baccino, F.M.8    Autelli, R.9
  • 36
    • 20444506408 scopus 로고    scopus 로고
    • Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism
    • CrossRef PubMed
    • Taha, T.A., Kitatani, K., Bielawski, J., Cho, W., Hannun, Y.A. and Obeid, L.M. (2005) Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism. J. Biol. Chem. 280, 17196-17202 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 17196-17202
    • Taha, T.A.1    Kitatani, K.2    Bielawski, J.3    Cho, W.4    Hannun, Y.A.5    Obeid, L.M.6
  • 37
    • 0027973628 scopus 로고
    • A possible role of sphingosine in induction of apoptosis by tumor necrosis factor-α in human neutrophils
    • CrossRef PubMed
    • Ohta, H., Yatomi, Y., Sweeney, E.A., Hakomori, S. and Igarashi, Y. (1994) A possible role of sphingosine in induction of apoptosis by tumor necrosis factor-α in human neutrophils. FEBS Lett. 355, 267-270 CrossRef PubMed
    • (1994) FEBS Lett , vol.355 , pp. 267-270
    • Ohta, H.1    Yatomi, Y.2    Sweeney, E.A.3    Hakomori, S.4    Igarashi, Y.5
  • 38
    • 0035090339 scopus 로고    scopus 로고
    • Sphingosine generation, cytochrome c release, and activation of caspase-7 in doxorubicin-induced apoptosis of MCF7 breast adenocarcinoma cells
    • CrossRef PubMed
    • Cuvillier, O., Nava, V.E., Murthy, S.K., Edsall, L.C., Levade, T., Milstien, S. and Spiegel, S. (2001) Sphingosine generation, cytochrome c release, and activation of caspase-7 in doxorubicin-induced apoptosis of MCF7 breast adenocarcinoma cells. Cell Death Differ. 8, 162-171 CrossRef PubMed
    • (2001) Cell Death Differ , vol.8 , pp. 162-171
    • Cuvillier, O.1    Nava, V.E.2    Murthy, S.K.3    Edsall, L.C.4    Levade, T.5    Milstien, S.6    Spiegel, S.7
  • 39
    • 26444592307 scopus 로고    scopus 로고
    • Sphingosine forms channels in membranes that differ greatly from those formed by ceramide
    • CrossRef PubMed
    • Siskind, L.J., Fluss, S., Bui, M. and Colombini, M. (2005) Sphingosine forms channels in membranes that differ greatly from those formed by ceramide. J. Bioenerg. Biomembr. 37, 227-236 CrossRef PubMed
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 227-236
    • Siskind, L.J.1    Fluss, S.2    Bui, M.3    Colombini, M.4
  • 40
    • 4544261024 scopus 로고    scopus 로고
    • Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria?
    • CrossRef PubMed
    • Bionda, C., Portoukalian, J., Schmitt, D., Rodriguez-Lafrasse, C. and Ardail, D. (2004) Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria? Biochem. J. 382, 527-533 CrossRef PubMed
    • (2004) Biochem. J. , vol.382 , pp. 527-533
    • Bionda, C.1    Portoukalian, J.2    Schmitt, D.3    Rodriguez-Lafrasse, C.4    Ardail, D.5
  • 41
    • 84871720518 scopus 로고    scopus 로고
    • Ceramide-orchestrated signalling in cancer cells
    • CrossRef PubMed
    • Morad, S.A. and Cabot, M.C. (2013) Ceramide-orchestrated signalling in cancer cells. Nat. Rev. Cancer 13, 51-65 CrossRef PubMed
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 51-65
    • Morad, S.A.1    Cabot, M.C.2
  • 42
    • 67649386434 scopus 로고    scopus 로고
    • pH dependence of sphingosine aggregation
    • CrossRef PubMed
    • Sasaki, H., Arai, H., Cocco, M.J. and White, S.H. (2009) pH dependence of sphingosine aggregation. Biophys. J. 96, 2727-2733 CrossRef PubMed
    • (2009) Biophys. J. , vol.96 , pp. 2727-2733
    • Sasaki, H.1    Arai, H.2    Cocco, M.J.3    White, S.H.4
  • 43
    • 0024542958 scopus 로고
    • Structural requirements for long-chain (sphingoid) base inhibition of protein kinase C in vitro and for the cellular effects of these compounds
    • CrossRef PubMed
    • Merrill, Jr, A.H., Nimkar, S., Menaldino, D., Hannun, Y.A., Loomis, C., Bell, R.M., Tyagi, S.R., Lambeth, J.D., Stevens, V.L. and Hunter, R. (1989) Structural requirements for long-chain (sphingoid) base inhibition of protein kinase C in vitro and for the cellular effects of these compounds. Biochemistry 28, 3138-3145 CrossRef PubMed
    • (1989) Biochemistry , vol.28 , pp. 3138-3145
    • Merrill, A.H.1    Nimkar, S.2    Menaldino, D.3    Hannun, Y.A.4    Loomis, C.5    Bell, R.M.6    Tyagi, S.R.7    Lambeth, J.D.8    Stevens, V.L.9    Hunter, R.10
  • 44
    • 24044519647 scopus 로고    scopus 로고
    • Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules
    • CrossRef PubMed
    • Alanko, S.M., Halling, K.K., Maunula, S., Slotte, J.P. and Ramstedt, B. (2005) Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules. Biochim. Biophys. Acta 1715, 111-121 CrossRef PubMed
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 111-121
    • Alanko, S.M.1    Halling, K.K.2    Maunula, S.3    Slotte, J.P.4    Ramstedt, B.5
  • 45
    • 0027723066 scopus 로고
    • Influence of sphingosine on the thermal phase behaviour of neutral and acidic phospholipid liposomes
    • CrossRef PubMed
    • Kõiv, A., Mustonen, P. and Kinnunen, P.K. (1993) Influence of sphingosine on the thermal phase behaviour of neutral and acidic phospholipid liposomes. Chem. Phys. Lipids 66, 123-134 CrossRef PubMed
    • (1993) Chem. Phys. Lipids , vol.66 , pp. 123-134
    • Kõiv, A.1    Mustonen, P.2    Kinnunen, P.K.3
  • 46
    • 84900295816 scopus 로고    scopus 로고
    • Biophysical implications of sphingosine accumulation in membrane properties at neutral and acidic pH
    • CrossRef PubMed
    • Zupancic, E., Carreira, A.C., de Almeida, R.F. and Silva, L.C. (2014) Biophysical implications of sphingosine accumulation in membrane properties at neutral and acidic pH. J. Phys. Chem. B 118, 4858-4866 CrossRef PubMed
    • (2014) J. Phys. Chem. B , vol.118 , pp. 4858-4866
    • Zupancic, E.1    Carreira, A.C.2    De Almeida, R.F.3    Silva, L.C.4
  • 47
    • 33744924717 scopus 로고    scopus 로고
    • Sphingosine increases the permeability of model and cell membranes
    • CrossRef PubMed
    • Contreras, F.X., Sot, J., Alonso, A. and Goñi, F.M. (2006) Sphingosine increases the permeability of model and cell membranes. Biophys. J. 90, 4085-4092 CrossRef PubMed
    • (2006) Biophys. J. , vol.90 , pp. 4085-4092
    • Contreras, F.X.1    Sot, J.2    Alonso, A.3    Goñi, F.M.4


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