메뉴 건너뛰기




Volumn 149, Issue 6, 2000, Pages 1215-1224

An essential role for a membrane lipid in cytokinesis: Regulation of contractile ring disassembly by redistribution of phosphatidylethanolamine

Author keywords

Actin; Cell division; Chinese hamster ovary cell mutant; Hospholipid binding peptide; Phospholipid asymmetry

Indexed keywords

MEMBRANE PHOSPHOLIPID; MYOSIN; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID BINDING PROTEIN; RADIXIN;

EID: 0034640856     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.149.6.1215     Document Type: Article
Times cited : (209)

References (62)
  • 1
    • 0028101276 scopus 로고
    • A novel peptide probe for studying the transhilayer movement of phosphatidylethanolamine
    • Aoki, Y., T. Uenaka, J. Aoki, M. Umeda, and K. Inoue. 1994. A novel peptide probe for studying the transhilayer movement of phosphatidylethanolamine. J. Biochem. 116:291-297.
    • (1994) J. Biochem. , vol.116 , pp. 291-297
    • Aoki, Y.1    Uenaka, T.2    Aoki, J.3    Umeda, M.4    Inoue, K.5
  • 2
    • 0026525339 scopus 로고
    • Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes
    • Bazzi, M.D., M.A. Youakin, and G.L. Nelsestuen. 1992. Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes. Biochemistry. 31:1125-1134.
    • (1992) Biochemistry , vol.31 , pp. 1125-1134
    • Bazzi, M.D.1    Youakin, M.A.2    Nelsestuen, G.L.3
  • 3
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi, E., and J. Luthenhaus. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature. 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Luthenhaus, J.2
  • 4
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.G., and W.J. Dyer, 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 5
    • 0015854929 scopus 로고
    • New membrane formation during cytokinesis in normal and cytochalasin B-treated eggs of Xenopus laevis. I. Electron microscope observations
    • Bluemink, J.G., and S.W. deLaat. 1973. New membrane formation during cytokinesis in normal and cytochalasin B-treated eggs of Xenopus laevis. I. Electron microscope observations. J. Cell Biol. 59:89-108.
    • (1973) J. Cell Biol. , vol.59 , pp. 89-108
    • Bluemink, J.G.1    DeLaat, S.W.2
  • 6
    • 0033617356 scopus 로고    scopus 로고
    • Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone
    • Bogdanov, M., M. Umeda, and W. Dowhan. 1999. Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone. J. Biol. Chem. 274: 12339-12345.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12339-12345
    • Bogdanov, M.1    Umeda, M.2    Dowhan, W.3
  • 7
    • 0031771547 scopus 로고    scopus 로고
    • Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing premRNA processing factors
    • Boronenkov, I.V., J.C. Loijens, M. Umeda, and R.A. Anderson. 1998. Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing premRNA processing factors. Mol. Biol. Cell. 9:3547-3560.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3547-3560
    • Boronenkov, I.V.1    Loijens, J.C.2    Umeda, M.3    Anderson, R.A.4
  • 9
    • 0027978049 scopus 로고
    • Assembly of the prothrombinase complex on the lipid vesicles dependent on the stereochemical configuration of polar head group of phosphatidylserine
    • Comfurius, P., E.F. Smeets, G.M. Willems, E.M. Bevers, and R.F.A. Zwaal. 1994. Assembly of the prothrombinase complex on the lipid vesicles dependent on the stereochemical configuration of polar head group of phosphatidylserine. Biochemistry. 33:10319-10324.
    • (1994) Biochemistry , vol.33 , pp. 10319-10324
    • Comfurius, P.1    Smeets, E.F.2    Willems, G.M.3    Bevers, E.M.4    Zwaal, R.F.A.5
  • 10
    • 15844389625 scopus 로고    scopus 로고
    • A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells
    • Cui, Z., M. Houweling, M.H. Chen, M. Record, H. Chap, D.E. Vance, and F. Terce. 1996. A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells. J. Biol. Chem. 271:14668-14671.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14668-14671
    • Cui, Z.1    Houweling, M.2    Chen, M.H.3    Record, M.4    Chap, H.5    Vance, D.E.6    Terce, F.7
  • 11
    • 0018837810 scopus 로고
    • Lateral diffusion of membrane lipids and proteins during the cell cycle of neuroblastoma cells
    • deLaat, S.W., PT. van der Saag, E.L. Elson, and J. Schlessinger. 1980. Lateral diffusion of membrane lipids and proteins during the cell cycle of neuroblastoma cells. Proc. Natl. Acad. Sci. USA. 77:1526-1528.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1526-1528
    • DeLaat, S.W.1    Van Der Saag, P.T.2    Elson, E.L.3    Schlessinger, J.4
  • 12
    • 0025876649 scopus 로고
    • Static and dynamic lipid asymmetry in cell membranes
    • Devaux, P.F. 1991. Static and dynamic lipid asymmetry in cell membranes. Biochemistry. 30:1163-1173.
    • (1991) Biochemistry , vol.30 , pp. 1163-1173
    • Devaux, P.F.1
  • 13
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan, W. 1997. Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66:199-232.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 14
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • Drechsel, D.N., A.A. Hyman, A. Hall, and M. Glotzer. 1997. A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr. Biol. 7:12-23.
    • (1997) Curr. Biol. , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 16
    • 0029850318 scopus 로고    scopus 로고
    • Redistribution of phosphalidylethanolamine at the cleavage furrow of dividing cells during cytokinesis
    • Emoto, K., T. Kobayashi, A. Yamaji, H. Aizawa, I. Yahara, K. Inoue, and M. Umeda. 1996. Redistribution of phosphalidylethanolamine at the cleavage furrow of dividing cells during cytokinesis. Proc. Natl. Acad. Sci. USA. 93: 12867-12872.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12867-12872
    • Emoto, K.1    Kobayashi, T.2    Yamaji, A.3    Aizawa, H.4    Yahara, I.5    Inoue, K.6    Umeda, M.7
  • 18
    • 0033607230 scopus 로고    scopus 로고
    • Isolation of a Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine
    • Emoto, K., O. Kuge, M. Nishijima, and M. Umeda. 1999. Isolation of a Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine. Proc. Natl. Acad. Sci. USA. 96:12400-12405.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12400-12405
    • Emoto, K.1    Kuge, O.2    Nishijima, M.3    Umeda, M.4
  • 19
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophases
    • Fadok, V.A., D.R. Voelker, P.A. Campbell, J.J. Cohen, D.L. Bratton, and P.M. Henson. 1992. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophases. J. Immunol. 148:2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 20
    • 0033214990 scopus 로고    scopus 로고
    • Septins: Cytoskelelal polymers or signalling GTPase?
    • Field, C.M., and D. Kellogg. 1999. Septins: cytoskelelal polymers or signalling GTPase? Trends Cell Biol. 9:387-394.
    • (1999) Trends Cell Biol. , vol.9 , pp. 387-394
    • Field, C.M.1    Kellogg, D.2
  • 22
    • 0029969182 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling
    • Fujimoto, K., M. Umeda, and S. Fujimoto. 1996. Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling. J. Cell Sci. 109: 2453-2460.
    • (1996) J. Cell Sci. , vol.109 , pp. 2453-2460
    • Fujimoto, K.1    Umeda, M.2    Fujimoto, S.3
  • 23
    • 0030695874 scopus 로고    scopus 로고
    • The mechanism and control of cytokinesis
    • Glotzer, M. 1997. The mechanism and control of cytokinesis. Curr. Opin. Cell Biol. 9:815-823.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 815-823
    • Glotzer, M.1
  • 24
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPase and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPase and the actin cytoskeleton. Science. 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 25
    • 0032509553 scopus 로고    scopus 로고
    • Mammalian cell mulants resistant to a sphingomyelin-directed cytolysin
    • Hanada, K., T. Hara, M. Fukasawa, A. Yamaji, M. Umeda, and M. Nishijima. 1998. Mammalian cell mulants resistant to a sphingomyelin-directed cytolysin. J. Biol. Chem. 273:33787-33794.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33787-33794
    • Hanada, K.1    Hara, T.2    Fukasawa, M.3    Yamaji, A.4    Umeda, M.5    Nishijima, M.6
  • 26
    • 0028865692 scopus 로고
    • A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody: Localization of phosphatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarhoxylase
    • Igarashi, K., M. Kaneda, A. Yamaji, T.C. Saido, U. Kikkawa, Y. Ono, K. Inoue, and M. Umeda. 1995. A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody: localization of phosphatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarhoxylase. J. Biol. Chem. 270:29075-29078.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29075-29078
    • Igarashi, K.1    Kaneda, M.2    Yamaji, A.3    Saido, T.C.4    Kikkawa, U.5    Ono, Y.6    Inoue, K.7    Umeda, M.8
  • 28
    • 0029026637 scopus 로고
    • Eukaryotic phospholipid biosynthesis
    • Kent, C. 1995. Eukaryotic phospholipid biosynthesis. Ann. Rev. Biochem. 64: 315-343.
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 315-343
    • Kent, C.1
  • 29
    • 0030943556 scopus 로고    scopus 로고
    • Nedd5, a mammalian septin, is a novel cytoskelelal component interacting with actin-based structures
    • Kinoshita, M., S. Kumar, A. Mizoguchi, C. Ide, A. Kinoshita, T. Haraguchi, and M. Noda. 1997. Nedd5, a mammalian septin, is a novel cytoskelelal component interacting with actin-based structures. Genes Dev. 11:1535-1547.
    • (1997) Genes Dev. , vol.11 , pp. 1535-1547
    • Kinoshita, M.1    Kumar, S.2    Mizoguchi, A.3    Ide, C.4    Kinoshita, A.5    Haraguchi, T.6    Noda, M.7
  • 30
    • 0024550057 scopus 로고
    • Lipid transport during mitosis. Alternative pathways for delivery of newly synthesized lipids to cell surface
    • Kohayashi, T. and R.E. Pagano. 1989. Lipid transport during mitosis. Alternative pathways for delivery of newly synthesized lipids to cell surface. J. Biol. Chem. 264:5966-5973.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5966-5973
    • Kohayashi, T.1    Pagano, R.E.2
  • 31
    • 0027989808 scopus 로고
    • Annexin V for flow cytometric detection of phosphatidylserine expression on B cell undergoing apoptosis
    • Koopman, G., C.P.M. Reutelingsperger, G.A.M. Kuijlen, R.M.J. Keehne, S.T. Pals, and M.H.J. vanOers. 1994. Annexin V for flow cytometric detection of phosphatidylserine expression on B cell undergoing apoptosis. Blood. 84: 1415-1420.
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.M.2    Kuijlen, G.A.M.3    Keehne, R.M.J.4    Pals, S.T.5    VanOers, M.H.J.6
  • 33
    • 0023924910 scopus 로고    scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complex
    • Mann, K.G., R.J. Jenny, and S. Krishnaswamy. 1998. Cofactor proteins in the assembly and expression of blood clotting enzyme complex. Annu. Rev. Biochem. 57:915-956.
    • (1998) Annu. Rev. Biochem. , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 34
    • 0031856847 scopus 로고    scopus 로고
    • Localization and function of early cell division proteins in filamentous Escherichia coli cell lacking phosphatidylethanolamine
    • Mileykovskaya, E., O. Sun, W. Margolin, and W. Dowhan. 1998. Localization and function of early cell division proteins in filamentous Escherichia coli cell lacking phosphatidylethanolamine. J. Bacteriol. 180:4252-4257.
    • (1998) J. Bacteriol. , vol.180 , pp. 4252-4257
    • Mileykovskaya, E.1    Sun, O.2    Margolin, W.3    Dowhan, W.4
  • 35
    • 0023433971 scopus 로고
    • Visualization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells
    • Mittal, B., J.M. Sanger, and J.W. Sanger. 1987. Visualization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J. Cell Biol. 105:1753-1760.
    • (1987) J. Cell Biol. , vol.105 , pp. 1753-1760
    • Mittal, B.1    Sanger, J.M.2    Sanger, J.W.3
  • 36
    • 0023695737 scopus 로고
    • Production and characterization of monoclonal antibodies that bind to phosphatidylinositol 4,5-bisphosphate
    • Miyazawa, A., H. Inoue, T. Yoshioka, T. Horikoshi, K. Yanagisawa, M. Umeda, and K. Inoue. 1988. Production and characterization of monoclonal antibodies that bind to phosphatidylinositol 4,5-bisphosphate. Mol. Immunol. 25:1025-1031.
    • (1988) Mol. Immunol. , vol.25 , pp. 1025-1031
    • Miyazawa, A.1    Inoue, H.2    Yoshioka, T.3    Horikoshi, T.4    Yanagisawa, K.5    Umeda, M.6    Inoue, K.7
  • 38
    • 0025111567 scopus 로고
    • Production and characterization of monoclonal antibodies that specifically bind to phosphatidylcholine
    • Nam, K.S., K. Igarashi, M. Umeda, and K. Inoue. 1990. Production and characterization of monoclonal antibodies that specifically bind to phosphatidylcholine. Biochim. Biophys. Acta. 1046:89-96.
    • (1990) Biochim. Biophys. Acta , vol.1046 , pp. 89-96
    • Nam, K.S.1    Igarashi, K.2    Umeda, M.3    Inoue, K.4
  • 39
    • 0030807664 scopus 로고    scopus 로고
    • Mammalian cell mutants of membrane phospholipid biogenesis
    • Nishijima, M., O. Kuge, and K. Hanada. 1997. Mammalian cell mutants of membrane phospholipid biogenesis. Trends Cell Biol. 7:324-329.
    • (1997) Trends Cell Biol. , vol.7 , pp. 324-329
    • Nishijima, M.1    Kuge, O.2    Hanada, K.3
  • 40
    • 0025219143 scopus 로고
    • Scavenger receptor-mediated uptake and metabolism of lipid vesicles containing acidic phospholipids by mouse peritoneal macrophases
    • Nishikawa, K., H. Arai, and K. Inoue. 1990. Scavenger receptor-mediated uptake and metabolism of lipid vesicles containing acidic phospholipids by mouse peritoneal macrophases. J. Biol. Chem. 265:5226-5231.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5226-5231
    • Nishikawa, K.1    Arai, H.2    Inoue, K.3
  • 41
    • 0025736018 scopus 로고
    • Radixin, a barbed endo-capping actin-modulating protein, is concentrated at cleavage furrow during cytokinesis
    • Sato, N., S. Yonemura, T. Obinata, S. Tsukita, and S. Tsukita. 1991. Radixin, a barbed endo-capping actin-modulating protein, is concentrated at cleavage furrow during cytokinesis. J. Cell Biol. 113:321-330.
    • (1991) J. Cell Biol. , vol.113 , pp. 321-330
    • Sato, N.1    Yonemura, S.2    Obinata, T.3    Tsukita, S.4    Tsukita, S.5
  • 43
    • 0011014320 scopus 로고
    • Actin in dividing cells. Contractile ring filaments bind heavy meromyosin
    • Schroeder, T.E. 1973. Actin in dividing cells. Contractile ring filaments bind heavy meromyosin. Proc. Natl. Acad. Sci. USA. 70:1688-1693.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1688-1693
    • Schroeder, T.E.1
  • 44
    • 0025346732 scopus 로고
    • The contractile ring and furrowing in dividing cells
    • Schroeder, T. E. 1990. The contractile ring and furrowing in dividing cells. Ann. NY Acad. Sci. 582:78-87.
    • (1990) Ann. NY Acad. Sci. , vol.582 , pp. 78-87
    • Schroeder, T.E.1
  • 45
    • 0026423662 scopus 로고
    • Transbilayer movement of phospholipids in red cell and platelet membranes
    • Schroit, A.J., and R.F.A. Zwaal. 1991. Transbilayer movement of phospholipids in red cell and platelet membranes. Biochim. Biophys. Acta. 1071:313-329.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 313-329
    • Schroit, A.J.1    Zwaal, R.F.A.2
  • 47
    • 0032503947 scopus 로고    scopus 로고
    • Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes
    • Takei, K., V. Haucke, V. Slepnev, K. Farsad, M. Salazar, H. Chen, and P.D. Camilli. 1998. Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell 94:131-141.
    • (1998) Cell , vol.94 , pp. 131-141
    • Takei, K.1    Haucke, V.2    Slepnev, V.3    Farsad, K.4    Salazar, M.5    Chen, H.6    Camilli, P.D.7
  • 49
    • 0033792318 scopus 로고    scopus 로고
    • Cholesterol binds synaptophysin and is required for biogenesis of synaptic vesicles
    • Thiele, C., M.J. Hannah, F. Fahrenholz, and W.B. Muttner. 1999. Cholesterol binds synaptophysin and is required for biogenesis of synaptic vesicles. Nature Cell Biol. 2:42-49.
    • (1999) Nature Cell Biol. , vol.2 , pp. 42-49
    • Thiele, C.1    Hannah, M.J.2    Fahrenholz, F.3    Muttner, W.B.4
  • 50
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita, S., S. Yonemura, and S. Tsukita. 1997. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22:53-58.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 53-58
    • Tsukita, S.1    Yonemura, S.2    Tsukita, S.3
  • 51
    • 0024366194 scopus 로고
    • Effective production of monoclonal antibodies against phosphatidylserine: Stereo-specific recognition of phosphatidylserine by monoclonal antibody
    • Umeda, M., K. Igarashi, K.S. Nam, and K. Inoue. 1989. Effective production of monoclonal antibodies against phosphatidylserine: stereo-specific recognition of phosphatidylserine by monoclonal antibody. J. Immunol. 143:2273-2279.
    • (1989) J. Immunol. , vol.143 , pp. 2273-2279
    • Umeda, M.1    Igarashi, K.2    Nam, K.S.3    Inoue, K.4
  • 52
    • 0025917178 scopus 로고
    • Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites of synthesis to the cell surface
    • Vance, J.E., E.J. Aasman, and R. Szarka. 1991. Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites of synthesis to the cell surface. J. Biol. Chem. 266:8241-8247.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8241-8247
    • Vance, J.E.1    Aasman, E.J.2    Szarka, R.3
  • 54
    • 0031553041 scopus 로고    scopus 로고
    • Lipid transport pathways in mammalian cells
    • Voelker, D.R. 1997. Lipid transport pathways in mammalian cells. Biochem. Biophys. Acta. 1348:236-244.
    • (1997) Biochem. Biophys. Acta , vol.1348 , pp. 236-244
    • Voelker, D.R.1
  • 56
    • 0029845878 scopus 로고    scopus 로고
    • Midzone microtubules are continuously required for cytokinesis in cultured epithelial cells
    • Wgeatley, S.P., and Y.L. Wang. 1996. Midzone microtubules are continuously required for cytokinesis in cultured epithelial cells. J. Cell Biol. 135:981-989.
    • (1996) J. Cell Biol. , vol.135 , pp. 981-989
    • Wgeatley, S.P.1    Wang, Y.L.2
  • 58
    • 0024599261 scopus 로고
    • Lipid regulation of cell membrane structure and function
    • Yeagle, P.L. 1989. Lipid regulation of cell membrane structure and function. FASEB J. 3:1833-1842.
    • (1989) FASEB J. , vol.3 , pp. 1833-1842
    • Yeagle, P.L.1
  • 59
    • 0023052465 scopus 로고
    • Hydration and the lamellar to hexagonal II phase transition of phosphatidylethanolamine
    • Yeagle, P.L., and A. Sen. 1986. Hydration and the lamellar to hexagonal II phase transition of phosphatidylethanolamine. Biochemistry. 25:7518-7522.
    • (1986) Biochemistry , vol.25 , pp. 7518-7522
    • Yeagle, P.L.1    Sen, A.2
  • 60
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • Zachowski, A. 1993. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. J. 294:1-14.
    • (1993) Biochem. J. , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 61
    • 0026672292 scopus 로고
    • Improved procedures for determination of lipid phosphorus by malachite green
    • Zhou, X., and G. Arthur. 1992. Improved procedures for determination of lipid phosphorus by malachite green. J. Lipid Res. 33:1233-1236.
    • (1992) J. Lipid Res. , vol.33 , pp. 1233-1236
    • Zhou, X.1    Arthur, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.