메뉴 건너뛰기




Volumn 1808, Issue 1, 2011, Pages 164-170

Multiple stages of detergent-erythrocyte membrane interaction-A spin label study

Author keywords

EPR; Erythrocyte; Hemolysis; Membrane; Solubilization; Triton X 100

Indexed keywords

DETERGENT; TRITON X 100;

EID: 78649794774     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.10.016     Document Type: Article
Times cited : (43)

References (63)
  • 3
    • 71549164295 scopus 로고    scopus 로고
    • Detergents: An overview
    • D. Linke Detergents: an overview Meth. Enzymol. 463 2009 603 617
    • (2009) Meth. Enzymol. , vol.463 , pp. 603-617
    • Linke, D.1
  • 4
    • 0034707091 scopus 로고    scopus 로고
    • Phase boundaries in mixtures of membrane-forming amphiphiles and micelle-forming amphiphiles
    • D. Lichtenberg, E. Opatowski, and M.M. Kozlov Phase boundaries in mixtures of membrane-forming amphiphiles and micelle-forming amphiphiles Biochim. Biophys. Acta 1508 2000 1 19
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 1-19
    • Lichtenberg, D.1    Opatowski, E.2    Kozlov, M.M.3
  • 5
    • 0029088548 scopus 로고
    • Interaction of detergents with lipid vesicles
    • J. Lasch Interaction of detergents with lipid vesicles Biochim. Biophys. Acta 1241 1995 269 292
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 269-292
    • Lasch, J.1
  • 6
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • M. Le Maire, P. Champeil, and J.V. Moller Interaction of membrane proteins and lipids with solubilizing detergents Biochim. Biophys. Acta 1508 2000 86 111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • D.A. Brown, and J.K. Rose Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface Cell 68 1992 533 544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 8
    • 0442276428 scopus 로고    scopus 로고
    • Detergents as tools for the purification and classification of lipid rafts
    • L.H. Chamberlain Detergents as tools for the purification and classification of lipid rafts FEBS Lett. 13 559 2004 1 5
    • (2004) FEBS Lett. , vol.13 , Issue.559 , pp. 1-5
    • Chamberlain, L.H.1
  • 9
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: Heterogeneity on the high seas
    • L.J. Pike Lipid rafts: heterogeneity on the high seas Biochem. J. 378 2004 281 292
    • (2004) Biochem. J. , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 10
    • 0035800734 scopus 로고    scopus 로고
    • The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection
    • B.U. Samuel, N. Mohandas, T. Harrison, H. McManus, W. Rosse, M. Reid, and K. Haldar The role of cholesterol and glycosylphosphatidylinositol-anchored proteins of erythrocyte rafts in regulating raft protein content and malarial infection J. Biol. Chem. 276 2001 29319 29329
    • (2001) J. Biol. Chem. , vol.276 , pp. 29319-29329
    • Samuel, B.U.1    Mohandas, N.2    Harrison, T.3    McManus, H.4    Rosse, W.5    Reid, M.6    Haldar, K.7
  • 11
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • U. Salzer, and R. Prohaska Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts Blood 97 2001 1141 1143
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 12
    • 0037274871 scopus 로고    scopus 로고
    • Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: An EPR spin label study
    • M.G. Rivas, and A.M. Gennaro Detergent resistant domains in erythrocyte membranes survive after cell cholesterol depletion: an EPR spin label study Chem. Phys. Lipids 122 2003 165 169
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 165-169
    • Rivas, M.G.1    Gennaro, A.M.2
  • 13
    • 22244473990 scopus 로고    scopus 로고
    • Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton
    • A. Ciana, C. Balduini, and G. Minetti Detergent-resistant membranes in human erythrocytes and their connection to the membrane-skeleton J. Biosci. 30 2005 317 328
    • (2005) J. Biosci. , vol.30 , pp. 317-328
    • Ciana, A.1    Balduini, C.2    Minetti, G.3
  • 14
    • 42949169913 scopus 로고    scopus 로고
    • Functional evidence for presence of lipid rafts in erythrocyte membranes: Gsα in rafts is essential for signal transduction
    • K. Kamata, S. Manno, M. Ozaki, and Y. Takakuwa Functional evidence for presence of lipid rafts in erythrocyte membranes: Gsα in rafts is essential for signal transduction Am. J. Hematol. 83 2008 371 375
    • (2008) Am. J. Hematol. , vol.83 , pp. 371-375
    • Kamata, K.1    Manno, S.2    Ozaki, M.3    Takakuwa, Y.4
  • 17
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • K. Simons, and R. Ehehalt Cholesterol, lipid rafts, and disease J. Clin. Invest. 110 2002 597 603
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 18
    • 33845586441 scopus 로고    scopus 로고
    • Characterization of Leishmania (Viannia) braziliensis membrane microdomains, and their role in macrophage infectivity
    • K.A.G. Yoneyama, A.K. Tanaka, T.G.V.H. Silveira, K. Takahashi, and A.H. Straus Characterization of Leishmania (Viannia) braziliensis membrane microdomains, and their role in macrophage infectivity J. Lipid Res. 47 2006 2171 2178
    • (2006) J. Lipid Res. , vol.47 , pp. 2171-2178
    • Yoneyama, K.A.G.1    Tanaka, A.K.2    Silveira, T.G.V.H.3    Takahashi, K.4    Straus, A.H.5
  • 19
    • 70449715103 scopus 로고    scopus 로고
    • The biological significance of detergent-resistant membranes in spermatozoa
    • B. Nixon, and R.J. Aitken The biological significance of detergent-resistant membranes in spermatozoa J. Reprod. Immunol. 83 2009 8 13
    • (2009) J. Reprod. Immunol. , vol.83 , pp. 8-13
    • Nixon, B.1    Aitken, R.J.2
  • 23
    • 0034691659 scopus 로고    scopus 로고
    • Binding of detergents and inhibitors to bovine complex I-A novel purification procedure for bovine complex i retaining full inhibitor sensitivity
    • J.G. Okun, V. Zickermann, K. Zwicker, and U. Brandt Binding of detergents and inhibitors to bovine complex I-a novel purification procedure for bovine complex I retaining full inhibitor sensitivity Biochim. Biophys. Acta 1459 2000 77 87
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 77-87
    • Okun, J.G.1    Zickermann, V.2    Zwicker, K.3    Brandt, U.4
  • 24
    • 0025063333 scopus 로고
    • Two types of haemolytic activity of detergents
    • J. Bielawski Two types of haemolytic activity of detergents Biochim. Biophys. Acta 1035 1990 214 217
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 214-217
    • Bielawski, J.1
  • 25
    • 0003017466 scopus 로고
    • Hemolytic activity of the non-ionic detergents Tween 80 and Triton X-100
    • J. Bielawski, L. Mrówczynska, and M. Konarczak Hemolytic activity of the non-ionic detergents Tween 80 and Triton X-100 Biol. Bull. Poznan 32 1995 27 41
    • (1995) Biol. Bull. Poznan , vol.32 , pp. 27-41
    • Bielawski, J.1    Mrówczynska, L.2    Konarczak, M.3
  • 26
    • 0023655059 scopus 로고
    • Biphasic interaction of Triton detergents with the erythrocyte membrane
    • D. Trägner, and A. Csordas Biphasic interaction of Triton detergents with the erythrocyte membrane Biochem. J. 244 1987 605 609
    • (1987) Biochem. J. , vol.244 , pp. 605-609
    • Trägner, D.1    Csordas, A.2
  • 27
    • 0026507081 scopus 로고
    • Effective detergent/lipid ratios in the solubilization of phosphatidylcholine vesicles by Triton X-100
    • M.A. Partearroyo, M.A. Urbaneja, and F.M. Goñi Effective detergent/lipid ratios in the solubilization of phosphatidylcholine vesicles by Triton X-100 FEBS Lett. 302 1992 138 140
    • (1992) FEBS Lett. , vol.302 , pp. 138-140
    • Partearroyo, M.A.1    Urbaneja, M.A.2    Goñi, F.M.3
  • 29
    • 0032968755 scopus 로고    scopus 로고
    • Surfactants in membrane solubilisation
    • M.N. Jones Surfactants in membrane solubilisation Int. J. Pharm. 177 1999 137 159
    • (1999) Int. J. Pharm. , vol.177 , pp. 137-159
    • Jones, M.N.1
  • 30
    • 0028816796 scopus 로고
    • Stability of protein formulations: Investigation of surfactant effects by a novel EPR spectroscopic technique
    • N.B. Bam, T.W. Randolph, and J.L. Cleland Stability of protein formulations: Investigation of surfactant effects by a novel EPR spectroscopic technique Pharm. Res. 122 1995 2 11
    • (1995) Pharm. Res. , vol.122 , pp. 2-11
    • Bam, N.B.1    Randolph, T.W.2    Cleland, J.L.3
  • 31
    • 0037162005 scopus 로고    scopus 로고
    • Quantitative assessment of human erythrocyte membrane solubilization by Triton X-100
    • P.S.C. Preté, S.V.P. Malheiros, N.C. Meirelles, and E. de Paula Quantitative assessment of human erythrocyte membrane solubilization by Triton X-100 Biophys. Chem. 97 2002 1 5
    • (2002) Biophys. Chem. , vol.97 , pp. 1-5
    • Preté, P.S.C.1    Malheiros, S.V.P.2    Meirelles, N.C.3    De Paula, E.4
  • 32
    • 0022348630 scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • D. Lichtenberg Characterization of the solubilization of lipid bilayers by surfactants Biochim. Biophys. Acta 821 1985 470 478
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 33
    • 0034707090 scopus 로고    scopus 로고
    • Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents
    • F.M. Goñi, and A. Alonso Spectroscopic techniques in the study of membrane solubilization, reconstitution and permeabilization by detergents Biochim. Biophys. Acta 1508 2000 51 68
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 51-68
    • Goñi, F.M.1    Alonso, A.2
  • 34
    • 0015241658 scopus 로고
    • Molecular motion in spin-labeled phospholipids and membranes
    • W.L. Hubbell, and H.M. McConnell Molecular motion in spin-labeled phospholipids and membranes J. Am. Chem. Soc. 93 1971 314 326
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 314-326
    • Hubbell, W.L.1    McConnell, H.M.2
  • 36
    • 0016634963 scopus 로고
    • Spectroscopic studies of membrane structure
    • D. Marsh Spectroscopic studies of membrane structure Essays Biochem. 11 1975 139 180
    • (1975) Essays Biochem. , vol.11 , pp. 139-180
    • Marsh, D.1
  • 37
    • 0001180501 scopus 로고
    • Spin label studies of structural and dynamic properties of detergent aggregates
    • S. Schreier, J.R. Ernandes, I.M. Cuccovia, and H. Chaimovich Spin label studies of structural and dynamic properties of detergent aggregates J. Magn. Reson. 30 1978 283 298
    • (1978) J. Magn. Reson. , vol.30 , pp. 283-298
    • Schreier, S.1    Ernandes, J.R.2    Cuccovia, I.M.3    Chaimovich, H.4
  • 38
    • 0021343046 scopus 로고
    • Effect of lipid membranes on the apparent pK of the local anesthetic tetracaine. Spin label and titration studies
    • S. Schreier, W.A. Frezzatti, P.S. Araujo, H. Chaimovich, and I.M. Cuccovia Effect of lipid membranes on the apparent pK of the local anesthetic tetracaine. Spin label and titration studies Biochim. Biophys. Acta 769 1984 231 237
    • (1984) Biochim. Biophys. Acta , vol.769 , pp. 231-237
    • Schreier, S.1    Frezzatti, W.A.2    Araujo, P.S.3    Chaimovich, H.4    Cuccovia, I.M.5
  • 39
    • 0025100904 scopus 로고
    • Methods for the determination of partition coefficients based on the effect of solutes upon membrane structure
    • E. Lissi, M.L. Bianconi, A.T. Amaral, E. de Paula, L.E.B. Blanch, and S. Schreier Methods for the determination of partition coefficients based on the effect of solutes upon membrane structure Biochim. Biophys. Acta 1021 1990 46 50
    • (1990) Biochim. Biophys. Acta , vol.1021 , pp. 46-50
    • Lissi, E.1    Bianconi, M.L.2    Amaral, A.T.3    De Paula, E.4    Blanch, L.E.B.5    Schreier, S.6
  • 40
    • 0028818451 scopus 로고
    • Use of a novel method for determination of partition coefficients to compare the effect of local anesthetics on membrane structure
    • E. de Paula, and S. Schreier Use of a novel method for determination of partition coefficients to compare the effect of local anesthetics on membrane structure Biochim. Biophys. Acta 1240 1995 25 33
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 25-33
    • De Paula, E.1    Schreier, S.2
  • 42
    • 0033047039 scopus 로고    scopus 로고
    • Investigation of protein-surfactant interactions by analytical ultracentrifugation and electron paramagnetic resonance: The use of recombinant human tissue factor as an example
    • L.S. Jones, D. Cipolla, J. Liu, S.J. Shire, and T.W. Randolph Investigation of protein-surfactant interactions by analytical ultracentrifugation and electron paramagnetic resonance: the use of recombinant human tissue factor as an example Pharm. Res. 16 1999 808 812
    • (1999) Pharm. Res. , vol.16 , pp. 808-812
    • Jones, L.S.1    Cipolla, D.2    Liu, J.3    Shire, S.J.4    Randolph, T.W.5
  • 43
    • 0024642298 scopus 로고
    • A spin label study of perturbation effects of N-(1-methyldodecyl)-N, N, N-trimethylammonium bromide and N-(1-methyldodecyl)-N, N-dimethylamine oxide on model membranes prepared from Escherichia coli-isolated lipids
    • F. Sersen, A. Leitmanová, F. Devínsky, I. Lacko, and P. Balgavy A spin label study of perturbation effects of N-(1-methyldodecyl)-N, N, N-trimethylammonium bromide and N-(1-methyldodecyl)-N, N-dimethylamine oxide on model membranes prepared from Escherichia coli-isolated lipids Gen. Physiol. Biophys. 8 1989 133 156
    • (1989) Gen. Physiol. Biophys. , vol.8 , pp. 133-156
    • Sersen, F.1    Leitmanová, A.2    Devínsky, F.3    Lacko, I.4    Balgavy, P.5
  • 44
    • 0032524729 scopus 로고    scopus 로고
    • Effects of polyoxyethylene chain length on erythrocyte hemolysis induced by poly[oxyethylene (n) nonylphenol] non-ionic surfactants
    • E. Galembeck, A. Alonso, and N.C. Meirelles Effects of polyoxyethylene chain length on erythrocyte hemolysis induced by poly[oxyethylene (n) nonylphenol] non-ionic surfactants Chem. Biol. Interact. 113 1998 91 103
    • (1998) Chem. Biol. Interact. , vol.113 , pp. 91-103
    • Galembeck, E.1    Alonso, A.2    Meirelles, N.C.3
  • 45
    • 0030927385 scopus 로고    scopus 로고
    • Electron resonance studies on the influence of anionic surfactants on human skin
    • Y. Kawasaki, D. Quan, K. Sakamoto, and H.I. Maibach Electron resonance studies on the influence of anionic surfactants on human skin Dermatology 194 1997 238 242
    • (1997) Dermatology , vol.194 , pp. 238-242
    • Kawasaki, Y.1    Quan, D.2    Sakamoto, K.3    Maibach, H.I.4
  • 46
    • 0025247787 scopus 로고
    • Interaction of surfactants with model and biological membranes. II. Effect of N-alkyl-N, N, N-trimethylammonium ions on phosphatidylcholine bilayers as studied by spin probe ESR
    • J. Gallová, F. Devínsky, and P. Balgavy Interaction of surfactants with model and biological membranes. II. Effect of N-alkyl-N, N, N-trimethylammonium ions on phosphatidylcholine bilayers as studied by spin probe ESR Chem. Phys. Lipids 53 1990 231 241
    • (1990) Chem. Phys. Lipids , vol.53 , pp. 231-241
    • Gallová, J.1    Devínsky, F.2    Balgavy, P.3
  • 47
    • 33745629303 scopus 로고    scopus 로고
    • Detergent solubilization of bovine erythrocytes: Comparison between the insoluble material and the intact membrane
    • P.M. Rodi, M.S. Cabeza, and A.M. Gennaro Detergent solubilization of bovine erythrocytes: comparison between the insoluble material and the intact membrane Biophys. Chem. 122 2006 114 122
    • (2006) Biophys. Chem. , vol.122 , pp. 114-122
    • Rodi, P.M.1    Cabeza, M.S.2    Gennaro, A.M.3
  • 48
    • 0032475507 scopus 로고    scopus 로고
    • Contribution of trifluoperazine/lipid ratio and drug ionization to hemolysis
    • S.V.P. Malheiros, E. de Paula, and N.C. Meirelles Contribution of trifluoperazine/lipid ratio and drug ionization to hemolysis Biochim. Biophys. Acta 1373 1998 332 340
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 332-340
    • Malheiros, S.V.P.1    De Paula, E.2    Meirelles, N.C.3
  • 50
    • 33847089082 scopus 로고
    • The size, shape and hydration of nonionic surfactant micelles of Triton X-100
    • R.J. Robson, and E.A. Dennis The size, shape and hydration of nonionic surfactant micelles of Triton X-100 J. Phys. Chem. 81 1977 1075 1078
    • (1977) J. Phys. Chem. , vol.81 , pp. 1075-1078
    • Robson, R.J.1    Dennis, E.A.2
  • 51
    • 0017479663 scopus 로고
    • Spin label study of detergents in the region of critical micelle concentration
    • J.R. Ernandes, H. Chaimovich, and S. Schreier Spin label study of detergents in the region of critical micelle concentration Chem. Phys. Lipids 18 1977 304 315
    • (1977) Chem. Phys. Lipids , vol.18 , pp. 304-315
    • Ernandes, J.R.1    Chaimovich, H.2    Schreier, S.3
  • 53
    • 0016657917 scopus 로고
    • Solubilizaton of membranes by detergents
    • A. Helenius, and K. Simons Solubilizaton of membranes by detergents Biochim. Biophys. Acta 415 1975 29 79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 54
    • 0021111186 scopus 로고
    • Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles
    • A. Prado, J.L.R. Arrondo, A. Villena, F.M. Goñi, and J.M. Macarulla Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles Biochim. Biophys. Acta 733 1983 163 171
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 163-171
    • Prado, A.1    Arrondo, J.L.R.2    Villena, A.3    Goñi, F.M.4    MacArulla, J.M.5
  • 55
    • 0027931816 scopus 로고
    • An assessment of the biochemical applications of the non-ionic surfactant Hecameg
    • M.B. Ruiz, A. Prado, F.M. Goñi, and A. Alonso An assessment of the biochemical applications of the non-ionic surfactant Hecameg Biochim. Biophys. Acta 1193 1994 301 306
    • (1994) Biochim. Biophys. Acta , vol.1193 , pp. 301-306
    • Ruiz, M.B.1    Prado, A.2    Goñi, F.M.3    Alonso, A.4
  • 56
    • 0026736107 scopus 로고
    • Structural perturbations of phospholipid bilayers induced by the neutral detergent octyl glucoside
    • J. Lasch, J. Hoffman, W. Richter, and H.W. Meyer Structural perturbations of phospholipid bilayers induced by the neutral detergent octyl glucoside J. Liposome Res. 2 1992 1 9
    • (1992) J. Liposome Res. , vol.2 , pp. 1-9
    • Lasch, J.1    Hoffman, J.2    Richter, W.3    Meyer, H.W.4
  • 57
    • 0031770290 scopus 로고    scopus 로고
    • The mechanism of detergent solubilization of liposomes and protein-containing membranes
    • U. Kragh-Hansen, M. Le Maire, and J.V. Moller The mechanism of detergent solubilization of liposomes and protein-containing membranes Biophys. J. 75 1998 2932 2946
    • (1998) Biophys. J. , vol.75 , pp. 2932-2946
    • Kragh-Hansen, U.1    Le Maire, M.2    Moller, J.V.3
  • 58
    • 0024281314 scopus 로고
    • Micelle-vesicle transition of egg phosphatidylcholine and octyl glucoside
    • M. Ollivon, O. Eidelman, R. Blumenthal, and A. Walter Micelle-vesicle transition of egg phosphatidylcholine and octyl glucoside Biochemistry 27 1988 1695 1703
    • (1988) Biochemistry , vol.27 , pp. 1695-1703
    • Ollivon, M.1    Eidelman, O.2    Blumenthal, R.3    Walter, A.4
  • 59
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside, and sodium cholate
    • M.T. Paternostre, M. Roux, and J. Rigaud Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside, and sodium cholate Biochemistry 27 1988 2668 2677
    • (1988) Biochemistry , vol.27 , pp. 2668-2677
    • Paternostre, M.T.1    Roux, M.2    Rigaud, J.3
  • 62
    • 76549165491 scopus 로고
    • The hemoglobin molecule
    • M.F. Perutz The hemoglobin molecule Sci. Am. 211 1964 64 76
    • (1964) Sci. Am. , vol.211 , pp. 64-76
    • Perutz, M.F.1
  • 63
    • 77952238679 scopus 로고    scopus 로고
    • Effect of cholesterol depletion and temperature on the isolation of detergent-resistant membranes from human erythrocytes
    • C.C. Domingues, A. Cianna, A. Buttafava, B.R. Casadei, C. Balduini, E. de Paula, and G. Minetti Effect of cholesterol depletion and temperature on the isolation of detergent-resistant membranes from human erythrocytes J. Membr. Biol. 234 2010 194 205
    • (2010) J. Membr. Biol. , vol.234 , pp. 194-205
    • Domingues, C.C.1    Cianna, A.2    Buttafava, A.3    Casadei, B.R.4    Balduini, C.5    De Paula, E.6    Minetti, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.