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Volumn 128, Issue 7, 2015, Pages 1422-1433

Complementary probes reveal that phosphatidylserine is required for the proper transbilayer distribution of cholesterol

Author keywords

Biosensor; Cholesterol; Phosphatidylserine; Plasma membrane

Indexed keywords

1 STEAROY 2 OLEOYL PHOSPHATIDYLSERINE; CHOLESTEROL; CHOLESTEROL OXIDASE; FILIPIN; FLOTILLIN 1; PHOSPHATIDYLSERINE; TOXIN; UNCLASSIFIED DRUG; LIPID BILAYER; MOLECULAR PROBE;

EID: 84928683537     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.164715     Document Type: Article
Times cited : (194)

References (58)
  • 1
  • 2
    • 69349085157 scopus 로고    scopus 로고
    • Molecular view of cholesterol flip-flop and chemical potential in different membrane environments
    • Bennett, W. F., MacCallum, J. L., Hinner, M. J., Marrink, S. J. and Tieleman, D. P. (2009). Molecular view of cholesterol flip-flop and chemical potential in different membrane environments. J. Am. Chem. Soc. 131, 12714-12720.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12714-12720
    • Bennett, W.F.1    MacCallum, J.L.2    Hinner, M.J.3    Marrink, S.J.4    Tieleman, D.P.5
  • 3
    • 0035807773 scopus 로고    scopus 로고
    • Mass spectrometric analysis reveals an increase in plasma membrane polyunsaturated phospholipid species upon cellular cholesterol loading
    • Blom, T. S., Koivusalo, M., Kuismanen, E., Kostiainen, R., Somerharju, P. and Ikonen, E. (2001). Mass spectrometric analysis reveals an increase in plasma membrane polyunsaturated phospholipid species upon cellular cholesterol loading. Biochemistry 40, 14635-14644.
    • (2001) Biochemistry , vol.40 , pp. 14635-14644
    • Blom, T.S.1    Koivusalo, M.2    Kuismanen, E.3    Kostiainen, R.4    Somerharju, P.5    Ikonen, E.6
  • 4
    • 0016275478 scopus 로고
    • Staining of cholesterol with the fluorescent antibiotic "filipin"
    • Börnig, H. and Geyer, G. (1974). Staining of cholesterol with the fluorescent antibiotic "filipin". Acta Histochem. 50, 110-115.
    • (1974) Acta Histochem. , vol.50 , pp. 110-115
    • Börnig, H.1    Geyer, G.2
  • 5
    • 34249090252 scopus 로고    scopus 로고
    • Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway
    • Chadda, R., Howes, M. T., Plowman, S. J., Hancock, J. F., Parton, R. G. and Mayor, S. (2007). Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Traffic 8, 702-717.
    • (2007) Traffic , vol.8 , pp. 702-717
    • Chadda, R.1    Howes, M.T.2    Plowman, S.J.3    Hancock, J.F.4    Parton, R.G.5    Mayor, S.6
  • 7
    • 84879533612 scopus 로고    scopus 로고
    • Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells
    • Das, A., Goldstein, J. L., Anderson, D. D., Brown, M. S. and Radhakrishnan, A. (2013). Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells. Proc. Natl. Acad. Sci. USA 110, 10580-10585.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 10580-10585
    • Das, A.1    Goldstein, J.L.2    Anderson, D.D.3    Brown, M.S.4    Radhakrishnan, A.5
  • 8
    • 84869217910 scopus 로고    scopus 로고
    • HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes
    • Dick, R. A., Goh, S. L., Feigenson, G. W. and Vogt, V. M. (2012). HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes. Proc. Natl. Acad. Sci. USA 109, 18761-18766.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 18761-18766
    • Dick, R.A.1    Goh, S.L.2    Feigenson, G.W.3    Vogt, V.M.4
  • 9
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • Dunstone, M. A. and Tweten, R. K. (2012). Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr. Opin. Struct. Biol. 22, 342-349.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 10
    • 66149142747 scopus 로고    scopus 로고
    • Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding
    • Flanagan, J. J., Tweten, R. K., Johnson, A. E. and Heuck, A. P. (2009). Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding. Biochemistry 48, 3977-3987.
    • (2009) Biochemistry , vol.48 , pp. 3977-3987
    • Flanagan, J.J.1    Tweten, R.K.2    Johnson, A.E.3    Heuck, A.P.4
  • 11
    • 84878752805 scopus 로고    scopus 로고
    • Sphingolipid domains in the plasma membranes of fibroblasts are not enriched with cholesterol
    • Frisz, J. F., Klitzing, H. A., Lou, K., Hutcheon, I. D., Weber, P. K., Zimmerberg, J. and Kraft, M. L. (2013). Sphingolipid domains in the plasma membranes of fibroblasts are not enriched with cholesterol. J. Biol. Chem. 288, 16855-16861.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16855-16861
    • Frisz, J.F.1    Klitzing, H.A.2    Lou, K.3    Hutcheon, I.D.4    Weber, P.K.5    Zimmerberg, J.6    Kraft, M.L.7
  • 12
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu, R., Demaurex, N., Parton, R. G., Hunziker, W., Huber, L. A. and Gruenberg, J. (2000). The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 11, 2775-2791.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 13
    • 0025174175 scopus 로고
    • Binding of human factor VIII to phospholipid vesicles
    • Gilbert, G. E., Furie, B. C. and Furie, B. (1990). Binding of human factor VIII to phospholipid vesicles. J. Biol. Chem. 265, 815-822.
    • (1990) J. Biol. Chem. , vol.265 , pp. 815-822
    • Gilbert, G.E.1    Furie, B.C.2    Furie, B.3
  • 14
    • 0037016677 scopus 로고    scopus 로고
    • Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle
    • Hao, M., Lin, S. X., Karylowski, O. J., Wüstner, D., McGraw, T. E. and Maxfield, F. R. (2002). Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle. J. Biol. Chem. 277, 609-617.
    • (2002) J. Biol. Chem. , vol.277 , pp. 609-617
    • Hao, M.1    Lin, S.X.2    Karylowski, O.J.3    Wüstner, D.4    McGraw, T.E.5    Maxfield, F.R.6
  • 16
    • 67849122725 scopus 로고    scopus 로고
    • Films of agarose enable rapid formation of giant liposomes in solutions of physiologic ionic strength
    • Horger, K. S., Estes, D. J., Capone, R. and Mayer, M. (2009). Films of agarose enable rapid formation of giant liposomes in solutions of physiologic ionic strength. J. Am. Chem. Soc. 131, 1810-1819.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1810-1819
    • Horger, K.S.1    Estes, D.J.2    Capone, R.3    Mayer, M.4
  • 17
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • Ikonen, E. (2008). Cellular cholesterol trafficking and compartmentalization. Nat. Rev. Mol. Cell Biol. 9, 125-138.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 125-138
    • Ikonen, E.1
  • 18
    • 40849120821 scopus 로고    scopus 로고
    • Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast
    • Jin, H., McCaffery, J. M. and Grote, E. (2008). Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast. J. Cell Biol. 180, 813-826.
    • (2008) J. Cell Biol. , vol.180 , pp. 813-826
    • Jin, H.1    McCaffery, J.M.2    Grote, E.3
  • 19
    • 84860126142 scopus 로고    scopus 로고
    • Modifications in perfringolysin O domain 4 alter the cholesterol concentration threshold required for binding
    • Johnson, B. B., Moe, P. C., Wang, D., Rossi, K., Trigatti, B. L. and Heuck, A. P. (2012). Modifications in perfringolysin O domain 4 alter the cholesterol concentration threshold required for binding. Biochemistry 51, 3373-3382.
    • (2012) Biochemistry , vol.51 , pp. 3373-3382
    • Johnson, B.B.1    Moe, P.C.2    Wang, D.3    Rossi, K.4    Trigatti, B.L.5    Heuck, A.P.6
  • 21
    • 84871715009 scopus 로고    scopus 로고
    • A human genome-wide screen for regulators of clathrin-coated vesicle formation reveals an unexpected role for the V-ATPase
    • Kozik, P., Hodson, N. A., Sahlender, D. A., Simecek, N., Soromani, C., Wu, J., Collinson, L. M. and Robinson, M. S. (2013). A human genome-wide screen for regulators of clathrin-coated vesicle formation reveals an unexpected role for the V-ATPase. Nat. Cell Biol. 15, 50-60.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 50-60
    • Kozik, P.1    Hodson, N.A.2    Sahlender, D.A.3    Simecek, N.4    Soromani, C.5    Wu, J.6    Collinson, L.M.7    Robinson, M.S.8
  • 22
    • 0034815625 scopus 로고    scopus 로고
    • Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol
    • Leventis, R. and Silvius, J. R. (2001). Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol. Biophys. J. 81, 2257-2267.
    • (2001) Biophys. J. , vol.81 , pp. 2257-2267
    • Leventis, R.1    Silvius, J.R.2
  • 24
    • 33644554780 scopus 로고    scopus 로고
    • First synthesis of free cholesterol-BODIPY conjugates
    • Li, Z., Mintzer, E. and Bittman, R. (2006). First synthesis of free cholesterol-BODIPY conjugates. J. Org. Chem. 71, 1718-1721.
    • (2006) J. Org. Chem. , vol.71 , pp. 1718-1721
    • Li, Z.1    Mintzer, E.2    Bittman, R.3
  • 25
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. and Simons, K. (2010). Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 26
    • 18144396107 scopus 로고    scopus 로고
    • The stomatin/prohibitin/flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes
    • Liu, J., Deyoung, S. M., Zhang, M., Dold, L. H. and Saltiel, A. R. (2005). The stomatin/prohibitin/flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes. J. Biol. Chem. 280, 16125-16134.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16125-16134
    • Liu, J.1    Deyoung, S.M.2    Zhang, M.3    Dold, L.H.4    Saltiel, A.R.5
  • 27
    • 34250663574 scopus 로고    scopus 로고
    • The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology
    • Lorenz, H., Hailey, D. W., Wunder, C. and Lippincott-Schwartz, J. (2006). The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology. Nat. Protoc. 1, 276-279.
    • (2006) Nat. Protoc. , vol.1 , pp. 276-279
    • Lorenz, H.1    Hailey, D.W.2    Wunder, C.3    Lippincott-Schwartz, J.4
  • 29
    • 84884210112 scopus 로고    scopus 로고
    • Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins
    • Maeda, K., Anand, K., Chiapparino, A., Kumar, A., Poletto, M., Kaksonen, M. and Gavin, A. C. (2013). Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501, 257-261.
    • (2013) Nature , vol.501 , pp. 257-261
    • Maeda, K.1    Anand, K.2    Chiapparino, A.3    Kumar, A.4    Poletto, M.5    Kaksonen, M.6    Gavin, A.C.7
  • 30
    • 84911978116 scopus 로고    scopus 로고
    • Molecular probes to visualize the location, organization and dynamics of lipids
    • Maekawa, M. and Fairn, G. D. (2014). Molecular probes to visualize the location, organization and dynamics of lipids. J. Cell Sci. 127, 4801-4812.
    • (2014) J. Cell Sci. , vol.127 , pp. 4801-4812
    • Maekawa, M.1    Fairn, G.D.2
  • 32
    • 0021459790 scopus 로고
    • The use and abuse of filipin to localize cholesterol in membranes
    • Miller, R. G. (1984). The use and abuse of filipin to localize cholesterol in membranes. Cell Biol. Int. Rep. 8, 519-535.
    • (1984) Cell Biol. Int. Rep. , vol.8 , pp. 519-535
    • Miller, R.G.1
  • 35
    • 61949446361 scopus 로고    scopus 로고
    • Sterols are mainly in the cytoplasmic leaflet of the plasma membrane and the endocytic recycling compartment in CHO cells
    • Mondal, M., Mesmin, B., Mukherjee, S. and Maxfield, F. R. (2009). Sterols are mainly in the cytoplasmic leaflet of the plasma membrane and the endocytic recycling compartment in CHO cells. Mol. Biol. Cell 20, 581-588.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 581-588
    • Mondal, M.1    Mesmin, B.2    Mukherjee, S.3    Maxfield, F.R.4
  • 36
    • 0036924163 scopus 로고    scopus 로고
    • Determination of membrane cholesterol partition coefficient using a lipid vesicle-cyclodextrin binary system: effect of phospholipid acyl chain unsaturation and headgroup composition
    • Niu, S. L. and Litman, B. J. (2002). Determination of membrane cholesterol partition coefficient using a lipid vesicle-cyclodextrin binary system: effect of phospholipid acyl chain unsaturation and headgroup composition. Biophys. J. 83,3408-3415.
    • (2002) Biophys. J. , vol.83 , pp. 3408-3415
    • Niu, S.L.1    Litman, B.J.2
  • 37
    • 84884293024 scopus 로고    scopus 로고
    • Oxysterol-binding proteins: sterol and phosphoinositide sensors coordinating transport, signaling and metabolism
    • Olkkonen, V. M. and Li, S. (2013). Oxysterol-binding proteins: sterol and phosphoinositide sensors coordinating transport, signaling and metabolism. Prog. Lipid Res. 52, 529-538.
    • (2013) Prog. Lipid Res. , vol.52 , pp. 529-538
    • Olkkonen, V.M.1    Li, S.2
  • 38
    • 0017882943 scopus 로고
    • Cholesterol oxidase as a probe for studying membrane organisation
    • Patzer, E. J. and Wagner, R. R. (1978). Cholesterol oxidase as a probe for studying membrane organisation. Nature 274, 394-395.
    • (1978) Nature , vol.274 , pp. 394-395
    • Patzer, E.J.1    Wagner, R.R.2
  • 39
    • 22844445240 scopus 로고    scopus 로고
    • Epidermal growth factor receptors are localized to lipid rafts that contain a balance of inner and outer leaflet lipids: a shotgun lipidomics study
    • Pike, L. J., Han, X. and Gross, R. W. (2005). Epidermal growth factor receptors are localized to lipid rafts that contain a balance of inner and outer leaflet lipids: a shotgun lipidomics study. J. Biol. Chem. 280, 26796-26804.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26796-26804
    • Pike, L.J.1    Han, X.2    Gross, R.W.3
  • 41
    • 0032479436 scopus 로고    scopus 로고
    • Genetic evidence that phosphatidylserine synthaseII catalyzestheconversion ofphosphatidylethanolaminetophosphatidylserine in Chinese hamster ovary cells
    • Saito, K., Nishijima, M. and Kuge, O. (1998). Genetic evidence that phosphatidylserine synthaseII catalyzestheconversion ofphosphatidylethanolaminetophosphatidylserine in Chinese hamster ovary cells. J. Biol. Chem. 273, 17199-17205.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17199-17205
    • Saito, K.1    Nishijima, M.2    Kuge, O.3
  • 42
    • 84904994558 scopus 로고    scopus 로고
    • Multi-protein assemblies underlie the mesoscale organization of the plasma membrane
    • Saka, S. K., Honigmann, A., Eggeling, C., Hell, S. W., Lang, T. and Rizzoli, S. O. (2014). Multi-protein assemblies underlie the mesoscale organization of the plasma membrane. Nat. Commun. 5, 4509.
    • (2014) Nat. Commun. , vol.5 , pp. 4509
    • Saka, S.K.1    Honigmann, A.2    Eggeling, C.3    Hell, S.W.4    Lang, T.5    Rizzoli, S.O.6
  • 43
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for poreforming toxins
    • Shatursky, O., Heuck, A. P., Shepard, L. A., Rossjohn, J., Parker, M. W., Johnson, A. E. and Tweten, R. K. (1999). The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for poreforming toxins. Cell 99, 293-299.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 44
    • 84871861963 scopus 로고    scopus 로고
    • Cholesterol modulates cell signaling and protein networking by specifically interacting with PDZ domain-containing scaffold proteins
    • Sheng, R., Chen, Y., Yung Gee, H., Stec, E., Melowic, H. R., Blatner, N. R., Tun, M. P., Kim, Y., Källberg, M., Fujiwara, T. K. et al. (2012). Cholesterol modulates cell signaling and protein networking by specifically interacting with PDZ domain-containing scaffold proteins. Nat. Commun. 3, 1249.
    • (2012) Nat. Commun. , vol.3 , pp. 1249
    • Sheng, R.1    Chen, Y.2    Yung Gee, H.3    Stec, E.4    Melowic, H.R.5    Blatner, N.R.6    Tun, M.P.7    Kim, Y.8    Källberg, M.9    Fujiwara, T.K.10
  • 45
    • 84904489367 scopus 로고    scopus 로고
    • Cholesterol selectively activates canonical Wnt signalling over non-canonical Wnt signalling
    • Sheng, R., Kim, H., Lee, H., Xin, Y., Chen, Y., Tian, W., Cui, Y., Choi, J. C., Doh, J., Han, J. K. et al. (2014). Cholesterol selectively activates canonical Wnt signalling over non-canonical Wnt signalling. Nat. Commun. 5, 4393.
    • (2014) Nat. Commun. , vol.5 , pp. 4393
    • Sheng, R.1    Kim, H.2    Lee, H.3    Xin, Y.4    Chen, Y.5    Tian, W.6    Cui, Y.7    Choi, J.C.8    Doh, J.9    Han, J.K.10
  • 46
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K. and Ehehalt, R. (2002). Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110, 597-603.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 47
  • 48
    • 77956511868 scopus 로고    scopus 로고
    • Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold
    • Sokolov, A. and Radhakrishnan, A. (2010). Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold. J. Biol. Chem. 285, 29480-29490.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29480-29490
    • Sokolov, A.1    Radhakrishnan, A.2
  • 50
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone, S. J. and Vance, J. E. (2000). Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J. Biol. Chem. 275, 34534-34540.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 51
    • 0023816534 scopus 로고
    • Cloning and expression in Escherichia coli of the perfringolysin O (theta-toxin) gene from Clostridium perfringens and characterization of the gene product
    • Tweten, R. K. (1988). Cloning and expression in Escherichia coli of the perfringolysin O (theta-toxin) gene from Clostridium perfringens and characterization of the gene product. Infect. Immun. 56, 3228-3234.
    • (1988) Infect. Immun. , vol.56 , pp. 3228-3234
    • Tweten, R.K.1
  • 54
    • 0037435608 scopus 로고    scopus 로고
    • Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains
    • Wanaski, S. P., Ng, B. K. and Glaser, M. (2003). Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains. Biochemistry 42, 42-56.
    • (2003) Biochemistry , vol.42 , pp. 42-56
    • Wanaski, S.P.1    Ng, B.K.2    Glaser, M.3
  • 55
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung, T., Gilbert, G. E., Shi, J., Silvius, J., Kapus, A. and Grinstein, S. (2008). Membrane phosphatidylserine regulates surface charge and protein localization. Science 319, 210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 56
    • 27844522310 scopus 로고    scopus 로고
    • Cytotoxicity of an anti-cancer lysophospholipid through selective modification of lipid raft composition
    • Zaremberg, V., Gajate, C., Cacharro, L. M., Mollinedo, F. and McMaster, C. R. (2005). Cytotoxicity of an anti-cancer lysophospholipid through selective modification of lipid raft composition. J. Biol. Chem. 280, 38047-38058.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38047-38058
    • Zaremberg, V.1    Gajate, C.2    Cacharro, L.M.3    Mollinedo, F.4    McMaster, C.R.5
  • 57
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou, M., Diwu, Z., Panchuk-Voloshina, N. and Haugland, R. P. (1997). A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal. Biochem. 253, 162-168.
    • (1997) Anal. Biochem. , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 58
    • 84893839471 scopus 로고    scopus 로고
    • Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters
    • Zhou, Y., Liang, H., Rodkey, T., Ariotti, N., Parton, R. G. and Hancock, J. F. (2014). Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters. Mol. Cell. Biol. 34, 862-876.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 862-876
    • Zhou, Y.1    Liang, H.2    Rodkey, T.3    Ariotti, N.4    Parton, R.G.5    Hancock, J.F.6


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