메뉴 건너뛰기




Volumn 31, Issue 36, 2015, Pages 9911-9923

The Presence of Sterols Favors Sticholysin I-Membrane Association and Pore Formation Regardless of Their Ability to Form Laterally Segregated Domains

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CHOLESTEROL; DIFFUSION IN LIQUIDS; FLUIDITY; LIPIDS; OLIGOMERIZATION; OLIGOMERS; PHASE SEPARATION; PHOSPHOLIPIDS; PORE SIZE; PROTEINS;

EID: 84941662529     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/acs.langmuir.5b01687     Document Type: Article
Times cited : (32)

References (62)
  • 1
    • 0024806978 scopus 로고
    • Effects of a high molecular weight toxin from Physalia physalis on glutamate responses
    • Mas, R.; Menéndez, R.; Garateix, A.; García, M.; Chávez, M. Effects of a high molecular weight toxin from Physalia physalis on glutamate responses Neuroscience 1989, 33, 269-273 10.1016/0306-4522(89)90206-6
    • (1989) Neuroscience , vol.33 , pp. 269-273
    • Mas, R.1    Menéndez, R.2    Garateix, A.3    García, M.4    Chávez, M.5
  • 2
    • 0028245287 scopus 로고
    • Positively charged amino acid residues located similarly in sea anemone and scorpion toxins
    • Loret, E. P.; Menéndez-Soto del Valle, R.; Mansuelle, P.; Sampieri, P.; Rochat, H. Positively charged amino acid residues located similarly in sea anemone and scorpion toxins J. Biol. Chem. 1994, 269, 16785-16788
    • (1994) J. Biol. Chem. , vol.269 , pp. 16785-16788
    • Loret, E.P.1    Menéndez-Soto Del Valle, R.2    Mansuelle, P.3    Sampieri, P.4    Rochat, H.5
  • 3
    • 70350617781 scopus 로고
    • Enzymatic characteristics of a fraction with phospholipase activity isolated from the anemone Stichodactyla helianthus
    • Pazos, F.; Gómez, T.; Tejuca, M.; Alvarez, C.; Lanio, M. E. Enzymatic characteristics of a fraction with phospholipase activity isolated from the anemone Stichodactyla helianthus Rev. Biol. 1993, 7, 115-123
    • (1993) Rev. Biol. , vol.7 , pp. 115-123
    • Pazos, F.1    Gómez, T.2    Tejuca, M.3    Alvarez, C.4    Lanio, M.E.5
  • 5
    • 0027968784 scopus 로고
    • Proteinase inhibitors from Stichodactyla helianthus: Purification, characterization and immobilization
    • Delfin, J.; González, Y.; Díaz, J.; Chávez, M. Proteinase inhibitors from Stichodactyla helianthus: purification, characterization and immobilization Arch. Med. Res. 1994, 25, 199-204
    • (1994) Arch. Med. Res. , vol.25 , pp. 199-204
    • Delfin, J.1    González, Y.2    Díaz, J.3    Chávez, M.4
  • 6
    • 0038883648 scopus 로고
    • Properties of a toxin from the sea anemone Stoichactis helianthus, including specific binding to sphingomyelin
    • Bernheimer, A. W.; Avigad, L. S. Properties of a toxin from the sea anemone Stoichactis helianthus, including specific binding to sphingomyelin Proc. Natl. Acad. Sci. U. S. A. 1976, 73, 467-471 10.1073/pnas.73.2.467
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 467-471
    • Bernheimer, A.W.1    Avigad, L.S.2
  • 7
    • 0024212323 scopus 로고
    • Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysin
    • Kem, W. R.; Dunn, B. M. Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysin Toxicon 1988, 26, 997-1008 10.1016/0041-0101(88)90198-5
    • (1988) Toxicon , vol.26 , pp. 997-1008
    • Kem, W.R.1    Dunn, B.M.2
  • 8
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • Anderluh, G.; Macek, P. Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria) Toxicon 2002, 40, 111-124 10.1016/S0041-0101(01)00191-X
    • (2002) Toxicon , vol.40 , pp. 111-124
    • Anderluh, G.1    Macek, P.2
  • 9
    • 0030865151 scopus 로고    scopus 로고
    • Channel-forming toxins: Tales of transformation
    • Gouaux, E. Channel-forming toxins: tales of transformation Curr. Opin. Struct. Biol. 1997, 7, 566-573 10.1016/S0959-440X(97)80123-6
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 566-573
    • Gouaux, E.1
  • 10
    • 33846829776 scopus 로고    scopus 로고
    • Pore-forming toxins and cellular non-immune defenses (CNIDs)
    • Aroian, R.; van der Goot, F. G. Pore-forming toxins and cellular non-immune defenses (CNIDs) Curr. Opin. Microbiol. 2007, 10, 57-61 10.1016/j.mib.2006.12.008
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 57-61
    • Aroian, R.1    Van Der Goot, F.G.2
  • 11
    • 0345643384 scopus 로고    scopus 로고
    • Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family
    • Anderluh, G.; Krizaj, I.; Strukelj, B.; Gubensek, F.; Macek, P.; Pungercar, J. Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family Toxicon 1999, 37, 1391-1401 10.1016/S0041-0101(99)00082-3
    • (1999) Toxicon , vol.37 , pp. 1391-1401
    • Anderluh, G.1    Krizaj, I.2    Strukelj, B.3    Gubensek, F.4    Macek, P.5    Pungercar, J.6
  • 12
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • Athanasiadis, A.; Anderluh, G.; Macek, P.; Turk, D. Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina Structure 2001, 9, 341-346 10.1016/S0969-2126(01)00592-5
    • (2001) Structure , vol.9 , pp. 341-346
    • Athanasiadis, A.1    Anderluh, G.2    Macek, P.3    Turk, D.4
  • 14
    • 68949150783 scopus 로고    scopus 로고
    • Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
    • Bellomio, A.; Morante, K.; Barlic, A.; Gutiérrez-Aguirre, I.; Viguera, A. R.; González-Mañas, J. M. Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea Toxicon 2009, 54, 869-880 10.1016/j.toxicon.2009.06.022
    • (2009) Toxicon , vol.54 , pp. 869-880
    • Bellomio, A.1    Morante, K.2    Barlic, A.3    Gutiérrez-Aguirre, I.4    Viguera, A.R.5    González-Mañas, J.M.6
  • 16
    • 39349103788 scopus 로고    scopus 로고
    • Sea Anemone Actinoporins: The transition from a folded soluble state to a functionally active membrane-bound oligomeric pore
    • Alegre-Cebollada, J.; Oñaderra, M.; Gavilanes, J. G.; Martínez del Pozo, A. Sea Anemone Actinoporins: The transition from a folded soluble state to a functionally active membrane-bound oligomeric pore Curr. Protein Pept. Sci. 2007, 8, 558-572 10.2174/138920307783018686
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 558-572
    • Alegre-Cebollada, J.1    Oñaderra, M.2    Gavilanes, J.G.3    Martínez Del Pozo, A.4
  • 17
    • 84923873558 scopus 로고    scopus 로고
    • Structural basis for self-assembly of a cytolytic pore lined by protein and lipid
    • Tanaka, R.; Caaveiro, J. M. M.; Morante, K.; González-Mañas, J. M.; Tsumoto, K. Structural basis for self-assembly of a cytolytic pore lined by protein and lipid Nat. Commun. 2015, 6, 6337 10.1038/ncomms7337
    • (2015) Nat. Commun. , vol.6 , pp. 6337
    • Tanaka, R.1    Caaveiro, J.M.M.2    Morante, K.3    González-Mañas, J.M.4    Tsumoto, K.5
  • 20
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II Permeabilizing Activity Depends on the presence of Sphingomyelin and Lipid Phase Coexistence
    • Schön, P.; García-Sáez, A. J.; Malovrh, P.; Bacia, K.; Anderluh, G.; Schwille, P. Equinatoxin II Permeabilizing Activity Depends on the presence of Sphingomyelin and Lipid Phase Coexistence Biophys. J. 2008, 95, 691-698 10.1529/biophysj.108.129981
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schön, P.1    García-Sáez, A.J.2    Malovrh, P.3    Bacia, K.4    Anderluh, G.5    Schwille, P.6
  • 21
    • 80054797440 scopus 로고    scopus 로고
    • Oligomerization and Pore Formation by Equinatoxin II Inhibit Endocytosis and Lead to Plasma Membrane Reorganization
    • García-Sáez, A. J.; Buschhorn, S. B.; Keller, H.; Anderluh, G.; Simons, K.; Schwille, P. Oligomerization and Pore Formation by Equinatoxin II Inhibit Endocytosis and Lead to Plasma Membrane Reorganization J. Biol. Chem. 2011, 286, 37768-37777 10.1074/jbc.M111.281592
    • (2011) J. Biol. Chem. , vol.286 , pp. 37768-37777
    • García-Sáez, A.J.1    Buschhorn, S.B.2    Keller, H.3    Anderluh, G.4    Simons, K.5    Schwille, P.6
  • 22
    • 84898862702 scopus 로고    scopus 로고
    • Imaging the Lipid-Phase-Dependent Pore Formation of Equinatoxin II in Droplet Interface Bilayers
    • Rojko, N.; Cronin, B.; Danial, J. S. H.; Baker, M. A. B.; Anderluh, G.; Wallace, M. I. Imaging the Lipid-Phase-Dependent Pore Formation of Equinatoxin II in Droplet Interface Bilayers Biophys. J. 2014, 106, 1630-1637 10.1016/j.bpj.2013.11.4507
    • (2014) Biophys. J. , vol.106 , pp. 1630-1637
    • Rojko, N.1    Cronin, B.2    Danial, J.S.H.3    Baker, M.A.B.4    Anderluh, G.5    Wallace, M.I.6
  • 23
    • 84928412952 scopus 로고    scopus 로고
    • The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface
    • García-Linares, S.; Alm, I.; Maula, T.; Gavilanes, J. G.; Slotte, J. P.; Martínez-del-Pozo, A. The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface Mar. Drugs 2015, 13, 1647-1665 10.3390/md13041647
    • (2015) Mar. Drugs , vol.13 , pp. 1647-1665
    • García-Linares, S.1    Alm, I.2    Maula, T.3    Gavilanes, J.G.4    Slotte, J.P.5    Martínez-Del-Pozo, A.6
  • 24
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/phosphatidylcholine/choleste rol phase diagram: Boundaries and composition of lipid rafts
    • de Almeida, R. F.; Fedorov, A.; Prieto, M. Sphingomyelin/phosphatidylcholine/choleste rol phase diagram: boundaries and composition of lipid rafts Biophys. J. 2003, 85, 2406-2416 10.1016/S0006-3495(03)74664-5
    • (2003) Biophys. J. , vol.85 , pp. 2406-2416
    • De Almeida, R.F.1    Fedorov, A.2    Prieto, M.3
  • 25
    • 84899041891 scopus 로고    scopus 로고
    • Sticholysin I-membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity
    • Pedrera, L.; Fanani, M. L.; Ros, U.; Lanio, M. E.; Maggio, B.; álvarez, C. Sticholysin I-membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity Biochim. Biophys. Acta, Biomembr. 2014, 1838, 1752-1759 10.1016/j.bbamem.2014.03.011
    • (2014) Biochim. Biophys. Acta, Biomembr. , vol.1838 , pp. 1752-1759
    • Pedrera, L.1    Fanani, M.L.2    Ros, U.3    Lanio, M.E.4    Maggio, B.5    Álvarez, C.6
  • 26
    • 24144500631 scopus 로고    scopus 로고
    • Sterol Structure Determines Miscibility versus Melting Transitions in Lipid Vesicles
    • Beattie, M. E.; Veatch, S. L.; Stottrup, B. L.; Keller, S. L. Sterol Structure Determines Miscibility versus Melting Transitions in Lipid Vesicles Biophys. J. 2005, 89, 1760-1768 10.1529/biophysj.104.049635
    • (2005) Biophys. J. , vol.89 , pp. 1760-1768
    • Beattie, M.E.1    Veatch, S.L.2    Stottrup, B.L.3    Keller, S.L.4
  • 27
    • 1642494863 scopus 로고    scopus 로고
    • Cholesterol oxidase senses subtle changes in lipid bilayer structure
    • Ahn, K. W.; Sampson, N. S. Cholesterol oxidase senses subtle changes in lipid bilayer structure Biochemistry 2004, 43, 827-836 10.1021/bi035697q
    • (2004) Biochemistry , vol.43 , pp. 827-836
    • Ahn, K.W.1    Sampson, N.S.2
  • 28
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the Structure of Natural Sterols and Sphingolipids on the Formation of Ordered Sphingolipid/Sterol Domains (Rafts)
    • Xu, X.; Bittman, R.; Duportail, G.; Heissler, D.; Vilcheze, C.; London, E. Effect of the Structure of Natural Sterols and Sphingolipids on the Formation of Ordered Sphingolipid/Sterol Domains (Rafts) J. Biol. Chem. 2001, 276, 33540-33546 10.1074/jbc.M104776200
    • (2001) J. Biol. Chem. , vol.276 , pp. 33540-33546
    • Xu, X.1    Bittman, R.2    Duportail, G.3    Heissler, D.4    Vilcheze, C.5    London, E.6
  • 29
    • 0024754221 scopus 로고
    • Interactions of neutral and anionic glycosphingolipids with dilauroylphosphatidylcholine and dilauroylphosphatidic acid in mixed monolayers
    • Bianco, I. D.; Maggio, B. Interactions of neutral and anionic glycosphingolipids with dilauroylphosphatidylcholine and dilauroylphosphatidic acid in mixed monolayers Colloids Surf. 1989, 40, 249-260 10.1016/0166-6622(89)80023-X
    • (1989) Colloids Surf. , vol.40 , pp. 249-260
    • Bianco, I.D.1    Maggio, B.2
  • 30
    • 0000729733 scopus 로고
    • Application of microcomputer-controlled film balance system to collection and analysis of data from mixed monolayers
    • Brockman, H. L.; Jones, C. M.; Schwebke, C. J.; Smaby, J. M.; Jarvis, D. E. Application of microcomputer-controlled film balance system to collection and analysis of data from mixed monolayers J. Colloid Interface Sci. 1980, 78, 502-512 10.1016/0021-9797(80)90588-3
    • (1980) J. Colloid Interface Sci. , vol.78 , pp. 502-512
    • Brockman, H.L.1    Jones, C.M.2    Schwebke, C.J.3    Smaby, J.M.4    Jarvis, D.E.5
  • 31
    • 70349289436 scopus 로고    scopus 로고
    • The influence of domain crowding on the lateral diffusion of Ceramide-enriched domains in a Sphingomyelin monolayer
    • Wilke, N.; Maggio, B. The influence of domain crowding on the lateral diffusion of Ceramide-enriched domains in a Sphingomyelin monolayer J. Phys. Chem. B 2009, 113, 12844-12851 10.1021/jp904378y
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12844-12851
    • Wilke, N.1    Maggio, B.2
  • 32
    • 77954258422 scopus 로고    scopus 로고
    • Rheological Properties of a Two Phase Lipid Monolayer at the Air/Water Interface: Effect of the Composition of the Mixture
    • Wilke, N.; Vega Mercado, F.; Maggio, B. Rheological Properties of a Two Phase Lipid Monolayer at the Air/Water Interface: Effect of the Composition of the Mixture Langmuir 2010, 26 (13) 11050-11059 10.1021/la100552j
    • (2010) Langmuir , vol.26 , Issue.13 , pp. 11050-11059
    • Wilke, N.1    Vega Mercado, F.2    Maggio, B.3
  • 33
    • 0019609427 scopus 로고
    • The translational and rotational drag on a cylinder moving in a membrane
    • Hughes, D.; Pailthorpe, B.; White, L. The translational and rotational drag on a cylinder moving in a membrane J. Fluid Mech. 1981, 110, 349-372 10.1017/S0022112081000785
    • (1981) J. Fluid Mech. , vol.110 , pp. 349-372
    • Hughes, D.1    Pailthorpe, B.2    White, L.3
  • 35
    • 84865271182 scopus 로고    scopus 로고
    • Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
    • Ale, E. C.; Maggio, B.; Fanani, M. L. Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase Biochim. Biophys. Acta, Biomembr. 2012, 1818, 2767-2776 10.1016/j.bbamem.2012.06.017
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 2767-2776
    • Ale, E.C.1    Maggio, B.2    Fanani, M.L.3
  • 36
    • 58149204198 scopus 로고    scopus 로고
    • Sphingomyelinase acts by an area-activated mechanism on the liquid-expanded phase of sphingomyelin monolayers
    • De Tullio, L.; Maggio, B.; Fanani, M. L. Sphingomyelinase acts by an area-activated mechanism on the liquid-expanded phase of sphingomyelin monolayers J. Lipid Res. 2008, 49, 2347-2355 10.1194/jlr.M800127-JLR200
    • (2008) J. Lipid Res. , vol.49 , pp. 2347-2355
    • De Tullio, L.1    Maggio, B.2    Fanani, M.L.3
  • 39
    • 11244261103 scopus 로고    scopus 로고
    • Miscibility of Ternary Mixtures of Phospholipids and Cholesterol in Monolayers, and Application to Bilayer Systems
    • Stottrup, B. L.; Stevens, D. S.; Keller, S. L. Miscibility of Ternary Mixtures of Phospholipids and Cholesterol in Monolayers, and Application to Bilayer Systems Biophys. J. 2005, 88, 269-276 10.1529/biophysj.104.048439
    • (2005) Biophys. J. , vol.88 , pp. 269-276
    • Stottrup, B.L.1    Stevens, D.S.2    Keller, S.L.3
  • 40
    • 78651260433 scopus 로고    scopus 로고
    • Liquid-liquid domain miscibility driven by composition and domain thickness mismatch in ternary lipid monolayers
    • Fanani, M. L.; Maggio, B. Liquid-liquid domain miscibility driven by composition and domain thickness mismatch in ternary lipid monolayers J. Phys. Chem. B 2011, 115, 41-49 10.1021/jp107344t
    • (2011) J. Phys. Chem. B , vol.115 , pp. 41-49
    • Fanani, M.L.1    Maggio, B.2
  • 41
    • 0032694324 scopus 로고    scopus 로고
    • The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes
    • Maget-Dana, R. The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes Biochim. Biophys. Acta, Biomembr. 1999, 1462, 109-140 10.1016/S0005-2736(99)00203-5
    • (1999) Biochim. Biophys. Acta, Biomembr. , vol.1462 , pp. 109-140
    • Maget-Dana, R.1
  • 42
    • 0033179620 scopus 로고    scopus 로고
    • Lipid monolayers: Why use half a membrane to characterize protein-membrane interactions?
    • Brockman, H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions? Curr. Opin. Struct. Biol. 1999, 9, 438-443 10.1016/S0959-440X(99)80061-X
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 438-443
    • Brockman, H.1
  • 43
    • 0016658645 scopus 로고
    • Lateral compressibility and penetration into phospholipid monolayers and bilayer membranes
    • Phillips, M. C.; Graham, D. E.; Hauser, H. Lateral compressibility and penetration into phospholipid monolayers and bilayer membranes Nature (London, U. K.) 1975, 254, 154-156 10.1038/254154a0
    • (1975) Nature (London, U. K.) , vol.254 , pp. 154-156
    • Phillips, M.C.1    Graham, D.E.2    Hauser, H.3
  • 44
    • 0030876951 scopus 로고    scopus 로고
    • Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol
    • Smaby, J. M.; Momsen, M. M.; Brockman, H. L.; Brown, R. E. Phosphatidylcholine acyl unsaturation modulates the decrease in interfacial elasticity induced by cholesterol Biophys. J. 1997, 73, 1492-1505 10.1016/S0006-3495(97)78181-5
    • (1997) Biophys. J. , vol.73 , pp. 1492-1505
    • Smaby, J.M.1    Momsen, M.M.2    Brockman, H.L.3    Brown, R.E.4
  • 45
    • 0030066744 scopus 로고    scopus 로고
    • The interfacial elastic packing interactions of galactosylceramides, sphingomyelins, and phosphatidylcholines
    • Smaby, J. M.; Kulkarni, V. S.; Momsen, M.; Brown, R. E. The interfacial elastic packing interactions of galactosylceramides, sphingomyelins, and phosphatidylcholines Biophys. J. 1996, 70, 868-877 10.1016/S0006-3495(96)79629-7
    • (1996) Biophys. J. , vol.70 , pp. 868-877
    • Smaby, J.M.1    Kulkarni, V.S.2    Momsen, M.3    Brown, R.E.4
  • 46
    • 0034069894 scopus 로고    scopus 로고
    • Sphingomyelin interfacial behavior: The impact of changing acyl chain composition
    • Li, X. M.; Smaby, J. M.; Momsen, M. M.; Brockman, H. L.; Brown, R. E. Sphingomyelin interfacial behavior: the impact of changing acyl chain composition Biophys. J. 2000, 78, 1921-1931 10.1016/S0006-3495(00)76740-3
    • (2000) Biophys. J. , vol.78 , pp. 1921-1931
    • Li, X.M.1    Smaby, J.M.2    Momsen, M.M.3    Brockman, H.L.4    Brown, R.E.5
  • 47
    • 33646147145 scopus 로고    scopus 로고
    • Phase behavior of lipid monolayers containing DPPC and cholesterol analogs
    • Stottrup, B. L.; Keller, S. L. Phase behavior of lipid monolayers containing DPPC and cholesterol analogs Biophys. J. 2006, 90, 3176-3183 10.1529/biophysj.105.072959
    • (2006) Biophys. J. , vol.90 , pp. 3176-3183
    • Stottrup, B.L.1    Keller, S.L.2
  • 48
    • 84883255628 scopus 로고    scopus 로고
    • Stiffness of Lipid Monolayers with Phase Coexistence
    • Caruso, B.; Mangiarotti, A.; Wilke, N. Stiffness of Lipid Monolayers with Phase Coexistence Langmuir 2013, 29, 10807-10816 10.1021/la4018322
    • (2013) Langmuir , vol.29 , pp. 10807-10816
    • Caruso, B.1    Mangiarotti, A.2    Wilke, N.3
  • 49
    • 0035883974 scopus 로고    scopus 로고
    • Sizing the radius of the pore formed in erytrocytes and lipid vesicles by the toxin sticholysin I from the sea anemone Stichodactyla helianthus
    • Tejuca, M.; Dalla Serra, M.; Potrich, C.; álvarez, C.; Menestrina, G. Sizing the radius of the pore formed in erytrocytes and lipid vesicles by the toxin sticholysin I from the sea anemone Stichodactyla helianthus J. Membr. Biol. 2001, 183, 125-135 10.1007/s00232-001-0060-y
    • (2001) J. Membr. Biol. , vol.183 , pp. 125-135
    • Tejuca, M.1    Dalla Serra, M.2    Potrich, C.3    Álvarez, C.4    Menestrina, G.5
  • 50
    • 0000576265 scopus 로고
    • Pore size distribution analysis of gel substances by size exclusion chromatography
    • Kuga, S. Pore size distribution analysis of gel substances by size exclusion chromatography J. Chromatogr. 1981, 206, 449-461 10.1016/S0021-9673(00)88914-1
    • (1981) J. Chromatogr. , vol.206 , pp. 449-461
    • Kuga, S.1
  • 51
    • 0000815976 scopus 로고
    • Determination of the effective hydrodynamic radii of small molecules by viscometry
    • Schultz, S. G.; Solomon, A. K. Determination of the effective hydrodynamic radii of small molecules by viscometry J. Gen. Physiol. 1961, 44, 1189-1199 10.1085/jgp.44.6.1189
    • (1961) J. Gen. Physiol. , vol.44 , pp. 1189-1199
    • Schultz, S.G.1    Solomon, A.K.2
  • 52
    • 34547143763 scopus 로고    scopus 로고
    • Transport of chloride and carboxyfluorescein through phospholipid vesicle membranes by heptapeptide amphiphiles
    • Ferdani, R.; Li, R.; Pajewski, R.; Pajewska, J.; Winter, R. K.; Gokel, G. W. Transport of chloride and carboxyfluorescein through phospholipid vesicle membranes by heptapeptide amphiphiles Org. Biomol. Chem. 2007, 5 (15) 2423-2432 10.1039/b705544g
    • (2007) Org. Biomol. Chem. , vol.5 , Issue.15 , pp. 2423-2432
    • Ferdani, R.1    Li, R.2    Pajewski, R.3    Pajewska, J.4    Winter, R.K.5    Gokel, G.W.6
  • 53
    • 84921033319 scopus 로고    scopus 로고
    • Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes
    • Alm, I.; García-Linares, S.; Gavilanes, J. G.; Martínez-del-Pozo, A.; Slotte, J. P. Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes Biochim. Biophys. Acta, Biomembr. 2015, 1848, 925-931 10.1016/j.bbamem.2014.12.017
    • (2015) Biochim. Biophys. Acta, Biomembr. , vol.1848 , pp. 925-931
    • Alm, I.1    García-Linares, S.2    Gavilanes, J.G.3    Martínez-Del-Pozo, A.4    Slotte, J.P.5
  • 54
    • 33847691929 scopus 로고    scopus 로고
    • Differential Effects of Cholesterol, Ergosterol and Lanosterol on a Dipalmitoyl Phosphatidylcholine Membrane: A Molecular Dynamics Simulation Study
    • Cournia, Z.; Ullmann, G. M.; Smith, J. C. Differential Effects of Cholesterol, Ergosterol and Lanosterol on a Dipalmitoyl Phosphatidylcholine Membrane: A Molecular Dynamics Simulation Study J. Phys. Chem. B 2007, 111, 1786-1801 10.1021/jp065172i
    • (2007) J. Phys. Chem. B , vol.111 , pp. 1786-1801
    • Cournia, Z.1    Ullmann, G.M.2    Smith, J.C.3
  • 55
    • 84930001051 scopus 로고    scopus 로고
    • Deuterium NMR of Raft Model Membranes Reveals Domain-Specific Order Profiles and Compositional Distribution
    • Yasuda, T.; Tsuchikawa, H.; Murata, M.; Matsumori, N. Deuterium NMR of Raft Model Membranes Reveals Domain-Specific Order Profiles and Compositional Distribution Biophys. J. 2015, 108, 2502-2506 10.1016/j.bpj.2015.04.008
    • (2015) Biophys. J. , vol.108 , pp. 2502-2506
    • Yasuda, T.1    Tsuchikawa, H.2    Murata, M.3    Matsumori, N.4
  • 56
    • 0035004910 scopus 로고    scopus 로고
    • Effects of Lipid Composition on Membrane Permeabilization by Sticholysin I and II, Two Cytolysins of the Sea Anemone Stichodactyla helianthus
    • Alvarez-Valcárcel, C.; Dalla Serra, M.; Potrich, C.; Bernhart, I.; Tejuca, M.; Martínez, D.; Pazos, F.; Lanio, M. E.; Menestrina, G. Effects of Lipid Composition on Membrane Permeabilization by Sticholysin I and II, Two Cytolysins of the Sea Anemone Stichodactyla helianthus Biophys. J. 2001, 80, 2761-2774 10.1016/S0006-3495(01)76244-3
    • (2001) Biophys. J. , vol.80 , pp. 2761-2774
    • Alvarez-Valcárcel, C.1    Dalla Serra, M.2    Potrich, C.3    Bernhart, I.4    Tejuca, M.5    Martínez, D.6    Pazos, F.7    Lanio, M.E.8    Menestrina, G.9
  • 57
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by Equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • Anderluh, G.; Dalla-Serra, M.; Viero, V.; Guella, G.; Macek, P.; Menestrina, G. Pore formation by Equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures J. Biol. Chem. 2003, 278, 45216-45223 10.1074/jbc.M305916200
    • (2003) J. Biol. Chem. , vol.278 , pp. 45216-45223
    • Anderluh, G.1    Dalla-Serra, M.2    Viero, V.3    Guella, G.4    Macek, P.5    Menestrina, G.6
  • 58
    • 0025134135 scopus 로고
    • Structure of the inverted hexagonal (HII) phase, and non-lamellar phase transitions of lipids
    • Seddon, J. M. Structure of the inverted hexagonal (HII) phase, and non-lamellar phase transitions of lipids Biochim. Biophys. Acta, Rev. Biomembr. 1990, 1031, 1-69 10.1016/0304-4157(90)90002-T
    • (1990) Biochim. Biophys. Acta, Rev. Biomembr. , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 59
    • 0019018524 scopus 로고
    • Physical principles of membrane organization
    • Israelachvili, J.; Marcelja, S.; Horn, R. Physical principles of membrane organization Q. Rev. Biophys. 1980, 13, 121-200 10.1017/S0033583500001645
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 121-200
    • Israelachvili, J.1    Marcelja, S.2    Horn, R.3
  • 61
    • 0026057849 scopus 로고
    • Complementary molecular shapes and additivity of the packing parameter of lipids
    • Kumar, V. V. Complementary molecular shapes and additivity of the packing parameter of lipids Proc. Natl. Acad. Sci. U. S. A. 1991, 88, 444-448 10.1073/pnas.88.2.444
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 444-448
    • Kumar, V.V.1
  • 62
    • 0020488323 scopus 로고
    • Correlation between molecular shape and hexagonal HII phase promoting ability of sterols
    • Gallay, J.; De Kruijff, B. Correlation between molecular shape and hexagonal HII phase promoting ability of sterols FEBS Lett. 1982, 143, 133-136 10.1016/0014-5793(82)80289-5
    • (1982) FEBS Lett. , vol.143 , pp. 133-136
    • Gallay, J.1    De Kruijff, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.