메뉴 건너뛰기




Volumn 287, Issue 20, 2012, Pages 16073-16087

Structure-dependent pseudoreceptor intracellular traffic of adamantyl globotriaosyl ceramide mimics

Author keywords

[No Author keywords available]

Indexed keywords

ADAMANTANES; AMPHIPATHIC; CELL SURFACES; CERAMIDES; CHOLERA TOXIN; CYTOSOLIC; ENDOPLASMIC RETICULUM; ENDOSOMES; JURKAT CELL; MEMBRANE CHOLESTEROL; PHOSPHOLIPID LIPOSOMES; PROTEIN SYNTHESIS; SHIGA TOXIN; VACUOLAR MEMBRANES; VERO CELLS;

EID: 84860871097     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.318196     Document Type: Article
Times cited : (7)

References (89)
  • 1
    • 0028917379 scopus 로고
    • The P blood group system. Biochemical, serological, and clinical aspects
    • Spitalnik, P. F., and Spitalnik, S. L. (1995) The P blood group system. Biochemical, serological, and clinical aspects. Transfus. Med. Rev. 9, 110-122
    • (1995) Transfus. Med. Rev. , vol.9 , pp. 110-122
    • Spitalnik, P.F.1    Spitalnik, S.L.2
  • 2
    • 0025753758 scopus 로고
    • CD77. An antigen of germinal center B cells entering apoptosis
    • Mangeney, M., Richard, Y., Coulaud, D., Tursz, T., and Wiels, J. (1991) CD77. An antigen of germinal center B cells entering apoptosis. Eur. J. Immunol. 21, 1131-1140
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1131-1140
    • Mangeney, M.1    Richard, Y.2    Coulaud, D.3    Tursz, T.4    Wiels, J.5
  • 4
    • 73949159257 scopus 로고    scopus 로고
    • Verocytotoxin-producing Escherichia coli (VTEC)
    • Karmali, M. A., Gannon, V., and Sargeant, J. M. (2010) Verocytotoxin-producing Escherichia coli (VTEC). Vet. Microbiol. 140, 360-370
    • (2010) Vet. Microbiol. , vol.140 , pp. 360-370
    • Karmali, M.A.1    Gannon, V.2    Sargeant, J.M.3
  • 5
    • 0023787493 scopus 로고
    • The histopathology of the hemolytic uremic syndrome associated with vero-cytotoxin-producing Escherichia coli infections
    • Richardson, S. E., Karmali, M. A., Becker, L. E., and Smith, C. R. (1988) The histopathology of the hemolytic uremic syndrome associated with vero-cytotoxin-producing Escherichia coli infections. Hum. Pathol. 19, 1102-1108
    • (1988) Hum. Pathol. , vol.19 , pp. 1102-1108
    • Richardson, S.E.1    Karmali, M.A.2    Becker, L.E.3    Smith, C.R.4
  • 6
    • 62449181018 scopus 로고    scopus 로고
    • Shiga toxins, glycosphingolipid diversity, and endothelial cell injury
    • Müthing, J., Schweppe, C. H., Karch, H., and Friedrich, A. W. (2009) Shiga toxins, glycosphingolipid diversity, and endothelial cell injury. Thromb. Haemost. 101, 252-264
    • (2009) Thromb. Haemost. , vol.101 , pp. 252-264
    • Müthing, J.1    Schweppe, C.H.2    Karch, H.3    Friedrich, A.W.4
  • 7
    • 34547908163 scopus 로고    scopus 로고
    • Treatment and prevention of enterohemorrhagic Escherichia coli infection and hemolytic uremic syndrome
    • Goldwater, P. N. (2007) Treatment and prevention of enterohemorrhagic Escherichia coli infection and hemolytic uremic syndrome. Expert Rev. Anti Infect. Ther. 5, 653-663
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 653-663
    • Goldwater, P.N.1
  • 8
    • 80051804184 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany, 2011. A microbiological study
    • Bielaszewska, M., Mellmann, A., Zhang, W., Köck, R., Fruth, A., Bauwens, A., Peters, G., and Karch, H. (2011) Characterization of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany, 2011. A microbiological study. Lancet Infect. Dis. 11, 671-676
    • (2011) Lancet Infect. Dis. , vol.11 , pp. 671-676
    • Bielaszewska, M.1    Mellmann, A.2    Zhang, W.3    Köck, R.4    Fruth, A.5    Bauwens, A.6    Peters, G.7    Karch, H.8
  • 11
    • 41049117594 scopus 로고    scopus 로고
    • Relationship between pathogenicity for humans and stx genotype in Shiga toxin-producing Escherichia coli serotype O157
    • Kawano, K., Okada, M., Haga, T., Maeda, K., and Goto, Y. (2008) Relationship between pathogenicity for humans and stx genotype in Shiga toxin-producing Escherichia coli serotype O157. Eur. J. Clin. Microbiol. Infect. Dis. 27, 227-232
    • (2008) Eur. J. Clin. Microbiol. Infect. Dis. , vol.27 , pp. 227-232
    • Kawano, K.1    Okada, M.2    Haga, T.3    Maeda, K.4    Goto, Y.5
  • 12
    • 48749104439 scopus 로고    scopus 로고
    • Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies
    • Tam, P., Mahfoud, R., Nutikka, A., Khine, A. A., Binnington, B., Paroutis, P., and Lingwood, C. (2008) Differential intracellular transport and binding of verotoxin 1 and verotoxin 2 to globotriaosylceramide-containing lipid assemblies. J. Cell. Physiol. 216, 750-763
    • (2008) J. Cell. Physiol. , vol.216 , pp. 750-763
    • Tam, P.1    Mahfoud, R.2    Nutikka, A.3    Khine, A.A.4    Binnington, B.5    Paroutis, P.6    Lingwood, C.7
  • 13
    • 33744519950 scopus 로고    scopus 로고
    • Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion of globo-series glycosphingolipids and loss of sensitivity to verotoxins
    • DOI 10.1074/jbc.M600057200
    • Okuda, T., Tokuda, N., Numata, S., Ito, M., Ohta, M., Kawamura, K., Wiels, J., Urano, T., Tajima, O., and Furukawa, K. (2006) Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion of globo-series glycosphingolipids and loss of sensitivity to verotoxins. J. Biol. Chem. 281, 10230-10235 (Pubitemid 43864560)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10230-10235
    • Okuda, T.1    Tokuda, N.2    Numata, S.-I.3    Ito, M.4    Ohta, M.5    Kawamura, K.6    Wiels, J.7    Urano, T.8    Tajima, O.9    Furukawa, K.10    Furukawa, K.11
  • 14
    • 0030113327 scopus 로고    scopus 로고
    • Two distinct binding sites for globotriaosyl ceramide on verotoxins: Identification by molecular modelling and confirmation using deoxy analogues and a new glycolipid receptor for all verotoxins
    • Nyholm, P. G., Magnusson, G., Zheng, Z., Norel, R., Binnington-Boyd, B., and Lingwood, C. A. (1996) Two distinct binding sites for globotriaosyl ceramide on verotoxins. Identification by molecular modeling and confirmation using deoxy analogues and a new glycolipid receptor for all verotoxins. Chem. Biol. 3, 263-275 (Pubitemid 126663325)
    • (1996) Chemistry and Biology , vol.3 , Issue.4 , pp. 263-275
    • Nyholm, P.-G.1    Magnusson, G.2    Zheng, Z.3    Norel, R.4    Binnington-Boyd, B.5    Lingwood, C.A.6
  • 15
    • 1642439269 scopus 로고    scopus 로고
    • Differential carbohydrate epitope recognition of globotriaosyl ceramide by verotoxins and a monoclonal antibody: Role in human renal glomerular binding
    • DOI 10.1046/j.1432-1033.2003.03941.x
    • Chark, D., Nutikka, A., Trusevych, N., Kuzmina, J., and Lingwood, C. (2004) Differential carbohydrate epitope recognition of globotriaosyl ceramide by verotoxins and monoclonal antibody: Role in human renal glomerular binding. Eur. J. Biochem. 271, 405-417 (Pubitemid 38130468)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.2 , pp. 405-417
    • Chark, D.1    Nutikka, A.2    Trusevych, N.3    Kuzmina, J.4    Lingwood, C.5
  • 16
    • 70350389557 scopus 로고    scopus 로고
    • Fatty acid-dependent globotriaosyl ceramide receptor function in detergent-resistant model membranes
    • Mahfoud, R., Manis, A., and Lingwood, C. (2009) Fatty acid-dependent globotriaosyl ceramide receptor function in detergent-resistant model membranes. J. Lipid Res. 50, 1744-1755
    • (2009) J. Lipid Res. , vol.50 , pp. 1744-1755
    • Mahfoud, R.1    Manis, A.2    Lingwood, C.3
  • 17
    • 67349169490 scopus 로고    scopus 로고
    • Detergent-resistant globotriaosyl ceramide may define verotoxin/glomeruli-restricted hemolytic uremic syndrome pathology
    • Khan, F., Proulx, F., and Lingwood, C. A. (2009) Detergent-resistant globotriaosyl ceramide may define verotoxin/glomeruli-restricted hemolytic uremic syndrome pathology. Kidney Int. 75, 1209-1216
    • (2009) Kidney Int. , vol.75 , pp. 1209-1216
    • Khan, F.1    Proulx, F.2    Lingwood, C.A.3
  • 18
    • 77949360652 scopus 로고    scopus 로고
    • How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's β amyloid peptide (Aβ1-40)
    • Yahi, N., Aulas, A., and Fantini, J. (2010) How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's β amyloid peptide (Aβ1-40). PLoS One 5, e9079
    • (2010) PLoS One , vol.5
    • Yahi, N.1    Aulas, A.2    Fantini, J.3
  • 21
    • 78149233373 scopus 로고    scopus 로고
    • A major fraction of glycosphingolipids in model and cellular cholesterol-containing membranes is undetectable by their binding proteins
    • Mahfoud, R., Manis, A., Binnington, B., Ackerley, C., and Lingwood, C. A. (2010) A major fraction of glycosphingolipids in model and cellular cholesterol- containing membranes is undetectable by their binding proteins. J. Biol. Chem. 285, 36049-36059
    • (2010) J. Biol. Chem. , vol.285 , pp. 36049-36059
    • Mahfoud, R.1    Manis, A.2    Binnington, B.3    Ackerley, C.4    Lingwood, C.A.5
  • 23
    • 33644867725 scopus 로고    scopus 로고
    • The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect
    • DOI 10.1091/mbc.E05-11-1035
    • Smith, D. C., Sillence, D. J., Falguières, T., Jarvis, R. M., Johannes, L., Lord, J. M., Platt, F. M., and Roberts, L. M. (2006) The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect. Mol. Biol. Cell 17, 1375-1387 (Pubitemid 43376557)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.3 , pp. 1375-1387
    • Smith, D.C.1    Sillence, D.J.2    Falguieres, T.3    Jarvis, R.M.4    Johannes, L.5    Lord, J.M.6    Platt, F.M.7    Roberts, L.M.8
  • 24
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae
    • review
    • Hooper, N. (1999) Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review). Mol. Membr. Biol. 16, 145-156
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 145-156
    • Hooper, N.1
  • 26
    • 0024564286 scopus 로고
    • Endocytosis from coated pits of Shiga toxin: A glycolipid-binding protein from Shigella dysenteriae 1
    • DOI 10.1083/jcb.108.4.1331
    • Sandvig, K., Olsnes, S., Brown, J. E., Petersen, O. W., and van Deurs, B. (1989) Endocytosis from coated pits of Shiga toxin. A glycolipid-binding protein from Shigella dysenteriae 1. J. Cell Biol. 108, 1331-1343 (Pubitemid 19097041)
    • (1989) Journal of Cell Biology , vol.108 , Issue.4 , pp. 1331-1343
    • Sandvig, K.1    Olsnes, S.2    Brown, J.E.3    Petersen, O.W.4    Van Deurs, B.5
  • 28
    • 0026684124 scopus 로고
    • Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
    • Sandvig, K., Garred, O., Prydz, K., Kozlov, J. V., Hansen, S. H., and van Deurs, B. (1992) Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature 358, 510-512
    • (1992) Nature , vol.358 , pp. 510-512
    • Sandvig, K.1    Garred, O.2    Prydz, K.3    Kozlov, J.V.4    Hansen, S.H.5    Van Deurs, B.6
  • 29
    • 34547916885 scopus 로고    scopus 로고
    • 1 subunit in target cells
    • DOI 10.1099/mic.0.2007/006858-0
    • Tam, P. J., and Lingwood, C. A. (2007) Membrane cytosolic translocation of verotoxin A1 subunit in target cells. Microbiology 153, 2700-2710 (Pubitemid 47262059)
    • (2007) Microbiology , vol.153 , Issue.8 , pp. 2700-2710
    • Tam, P.J.1    Lingwood, C.A.2
  • 30
    • 0344375094 scopus 로고    scopus 로고
    • Verotoxin 1 binding to intestinal crypt epithelial cells results in localization to lysosomes and abrogation of toxicity
    • DOI 10.1046/j.1462-5822.2003.00254.x
    • Hoey, D. E., Sharp, L., Currie, C., Lingwood, C. A., Gally, D. L., and Smith, D. G. (2003) Verotoxin 1 binding to intestinal crypt epithelial cells results in localization to lysosomes and abrogation of toxicity. Cell. Microbiol. 5, 85-97 (Pubitemid 36395123)
    • (2003) Cellular Microbiology , vol.5 , Issue.2 , pp. 85-97
    • Hoey, D.E.E.1    Sharp, L.2    Currie, C.3    Lingwood, C.A.4    Gally, D.L.5    Smith, D.G.E.6
  • 31
    • 0034329025 scopus 로고    scopus 로고
    • Membrane traffic in sphingolipid storage diseases
    • Pagano, R. E., Puri, V., Dominguez, M., and Marks, D. L. (2000) Membrane traffic in sphingolipid storage diseases. Traffic 1, 807-815
    • (2000) Traffic , vol.1 , pp. 807-815
    • Pagano, R.E.1    Puri, V.2    Dominguez, M.3    Marks, D.L.4
  • 32
    • 0038632363 scopus 로고    scopus 로고
    • Effects of HIV-1 Nef on retrograde transport from the plasma membrane to the endoplasmic reticulum
    • Johannes, L., Pezo, V., Mallard, F., Tenza, D., Wiltz, A., Saint-Pol, A., Helft, J., Antony, C., and Benaroch, P. (2003) Effects of HIV-1 Nef on retrograde transport from the plasma membrane to the endoplasmic reticulum. Traffic 4, 323-332 (Pubitemid 36582634)
    • (2003) Traffic , vol.4 , Issue.5 , pp. 323-332
    • Johannes, L.1    Pezo, V.2    Mallard, F.3    Tenza, D.4    Wiltz, A.5    Saint-Pol, A.6    Helft, J.7    Antony, C.8    Benaroch, P.9
  • 33
    • 0028301437 scopus 로고
    • Glycosphingolipid receptor function is modified by fatty acid content. Verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues
    • Kiarash, A., Boyd, B., and Lingwood, C. A. (1994) Glycosphingolipid receptor function is modified by fatty acid content. Verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues. J. Biol. Chem. 269, 11138-11146
    • (1994) J. Biol. Chem. , vol.269 , pp. 11138-11146
    • Kiarash, A.1    Boyd, B.2    Lingwood, C.A.3
  • 34
    • 0027933527 scopus 로고
    • Lipid modulation of glycolipid receptor function Availability of Gal(α1-4)Gal disaccharide for verotoxin binding in natural and synthetic glycolipids
    • DOI 10.1111/j.1432-1033.1994.tb19064.x
    • Boyd, B., Magnusson, G., Zhiuyan, Z., and Lingwood, C. A. (1994) Lipid modulation of glycolipid receptor function. Availability of Gal(α1-4)Gal disaccharide for verotoxin binding in natural and synthetic glycolipids. Eur. J. Biochem. 223, 873-878 (Pubitemid 24263171)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.3 , pp. 873-878
    • Boyd, B.1    Magnusson, G.2    Zhiuyan, Z.3    Lingwood, C.A.4
  • 35
    • 0029923621 scopus 로고    scopus 로고
    • Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes: Comparison of a supported bilayer film and liposomes
    • DOI 10.1007/BF00731490
    • Arab, S., and Lingwood, C. A. (1996) Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes. Comparison of a supported bilayer film and liposomes. Glycoconj. J. 13, 159-166 (Pubitemid 26132723)
    • (1996) Glycoconjugate Journal , vol.13 , Issue.2 , pp. 159-166
    • Arab, S.1    Lingwood, C.A.2
  • 36
    • 0029760597 scopus 로고    scopus 로고
    • Aglycone modulation of glycolipid receptor function
    • Lingwood, C. A. (1996) Aglycone modulation of glycolipid receptor function. Glycoconj. J. 13, 495-503
    • (1996) Glycoconj. J. , vol.13 , pp. 495-503
    • Lingwood, C.A.1
  • 37
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • DOI 10.1016/S0014-5793(02)03182-4, PII S0014579302031824
    • Sandvig, K., and van Deurs, B. (2002) Transport of protein toxins into cells. Pathways used by ricin, cholera toxin, and Shiga toxin. FEBS Lett. 529, 49-53 (Pubitemid 35283911)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 49-53
    • Sandvig, K.1    Van Deurs, B.2
  • 38
    • 0345490781 scopus 로고    scopus 로고
    • The intracellular voyage of cholera toxin: Going retro
    • DOI 10.1016/j.tibs.2003.10.002
    • Lencer, W. I., and Tsai, B. (2003) The intracellular voyage of cholera toxin. Going retro. Trends Biochem. Sci. 28, 639-645 (Pubitemid 37500898)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 639-645
    • Lencer, W.I.1    Tsai, B.2
  • 39
    • 0034567169 scopus 로고    scopus 로고
    • Applications of BODIPY-sphingolipid analogs to study lipid traffic and metabolism in cells
    • Pagano, R. E., Watanabe, R., Wheatley, C., and Dominguez, M. (2000) Applications of BODIPY-sphingolipid analogs to study lipid traffic and metabolism in cells. Methods Enzymol. 312, 523-534
    • (2000) Methods Enzymol. , vol.312 , pp. 523-534
    • Pagano, R.E.1    Watanabe, R.2    Wheatley, C.3    Dominguez, M.4
  • 40
    • 0034628502 scopus 로고    scopus 로고
    • Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands
    • DOI 10.1038/35001095
    • Kitov, P. I., Sadowska, J. M., Mulvey, G., Armstrong, G. D., Ling, H., Pannu, N. S., Read, R. J., and Bundle, D. R. (2000) Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 403, 669-672 (Pubitemid 30104009)
    • (2000) Nature , vol.403 , Issue.6770 , pp. 669-672
    • Kitov, P.I.1    Sadowska, J.M.2    Mulvey, G.3    Armstrong, G.D.4    Ling, H.5    Pannu, N.S.6    Read, R.J.7    Bundle, D.R.8
  • 43
    • 0028596536 scopus 로고
    • Interaction of the Shiga-like toxin type 1 B-subunit with its carbohydrate receptor
    • St Hilaire, P. M., Boyd, M. K., and Toone, E. J. (1994) Interaction of the Shiga-like toxin type 1 B-subunit with its carbohydrate receptor. Biochemistry 33, 14452-14463
    • (1994) Biochemistry , vol.33 , pp. 14452-14463
    • St Hilaire, P.M.1    Boyd, M.K.2    Toone, E.J.3
  • 44
    • 0033551263 scopus 로고    scopus 로고
    • Adamantyl globotriaosyl ceramide: A monovalent soluble mimic which inhibits verotoxin binding to its glycolipid receptor
    • DOI 10.1006/bbrc.1999.0474
    • Mylvaganam, M., and Lingwood, C. (1999) Adamantyl globotriaosyl ceramide. A monovalent soluble mimic which inhibits verotoxin binding to its glycolipid receptor. Biochem. Biophys. Res. Commun. 257, 391-394 (Pubitemid 29301455)
    • (1999) Biochemical and Biophysical Research Communications , vol.257 , Issue.2 , pp. 391-394
    • Mylvaganam, M.1    Lingwood, C.A.2
  • 45
    • 16844367925 scopus 로고    scopus 로고
    • A preamble to aglycone reconstruction for membrane-presented glycolipids
    • Wong, C.-H., ed Wiley-VCH Press, Weinheim, Germany
    • Mylvaganam, M., and Lingwood, C. A. (2003) A preamble to aglycone reconstruction for membrane-presented glycolipids. in Carbohydrate-based Drug Discovery (Wong, C.-H., ed) pp. 761-780, Wiley-VCH Press, Weinheim, Germany
    • (2003) Carbohydrate-based Drug Discovery , pp. 761-780
    • Mylvaganam, M.1    Lingwood, C.A.2
  • 46
    • 0036419885 scopus 로고    scopus 로고
    • Differential tissue targeting and pathogenesis of verotoxins 1 and 2 in the mouse animal model
    • DOI 10.1046/j.1523-1755.2002.00502.x
    • Rutjes, N. W., Binnington, B. A., Smith, C. R., Maloney, M. D., and Lingwood, C. A. (2002) Differential tissue targeting and pathogenesis of verotoxins 1 and 2 in the mouse animal model. Kidney Int. 62, 832-845 (Pubitemid 35316712)
    • (2002) Kidney International , vol.62 , Issue.3 , pp. 832-845
    • Rutjes, N.W.P.1    Binnington, B.A.2    Smith, C.R.3    Maloney, M.D.4    Lingwood, C.A.5
  • 47
    • 0023101312 scopus 로고
    • Purification and biological properties of Escherichia coli verocytotoxin
    • DOI 10.1016/0378-1097(87)90284-9
    • Petric, M., Karmali, M. A., Richardson, S., and Cheung, R. (1987) Purification and biological properties of Escherichia coli verocytotoxin FEMS Microbiol. Lett. 41, 63-68 (Pubitemid 17030524)
    • (1987) FEMS Microbiology Letters , vol.41 , Issue.1 , pp. 63-68
    • Petric, M.1    Karmali, M.A.2    Richardson, S.3    Cheung, R.4
  • 48
    • 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
  • 49
    • 56049095508 scopus 로고    scopus 로고
    • Cholesterol interactions with fluid-phase phospholipids. Effect on the lateral organization of the bilayer
    • Halling, K. K., Ramstedt, B., Nyström, J. H., Slotte, J. P., and Nyholm, T. K. (2008) Cholesterol interactions with fluid-phase phospholipids. Effect on the lateral organization of the bilayer. Biophys. J. 95, 3861-3871
    • (2008) Biophys. J. , vol.95 , pp. 3861-3871
    • Halling, K.K.1    Ramstedt, B.2    Nyström, J.H.3    Slotte, J.P.4    Nyholm, T.K.5
  • 51
    • 4444271526 scopus 로고    scopus 로고
    • Brefeldin A and filipin distinguish two globotriaosyl ceramide/verotoxin-1 intracellular trafficking pathways involved in Vero cell cytotoxicity
    • DOI 10.1093/glycob/cwh085
    • Khine, A. A., Tam, P., Nutikka, A., and Lingwood, C. A. (2004) Brefeldin A and filipin distinguish two globotriaosyl ceramide/verotoxin-1 intracellular trafficking pathways involved in Vero cell cytotoxicity. Glycobiology 14, 701-712 (Pubitemid 39161977)
    • (2004) Glycobiology , vol.14 , Issue.8 , pp. 701-712
    • Khine, A.A.1    Tam, P.2    Nutikka, A.3    Lingwood, C.A.4
  • 52
    • 0028275814 scopus 로고
    • Endocytosis and intracellular sorting of ricin and Shiga toxin
    • DOI 10.1016/0014-5793(94)00281-9
    • Sandvig, K., and van Deurs, B. (1994) Endocytosis and intracellular sorting of ricin and Shiga toxin. FEBS Lett. 346, 99-102 (Pubitemid 24183836)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 99-102
    • Sandvig, K.1
  • 53
    • 0035957101 scopus 로고    scopus 로고
    • Interaction of cholesterol with sphingomyelin in mixed membranes containing phosphatidylcholine, studied by spin-label ESR and IR spectroscopies. A possible stabilization of gel-phase sphingolipid domains by cholesterol
    • DOI 10.1021/bi0019803
    • Veiga, M. P., Arrondo, J. L., Goñi, F. M., Alonso, A., and Marsh, D. (2001) Interaction of cholesterol with sphingomyelin in mixed membranes containing phosphatidylcholine, studied by spin-label ESR and IR spectroscopies. A possible stabilization of gel-phase sphingolipid domains by cholesterol. Biochemistry 40, 2614-2622 (Pubitemid 32171737)
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2614-2622
    • Veiga, M.P.1    Arrondo, J.L.R.2    Goni, F.M.3    Alonso, A.4    Marsh, D.5
  • 54
    • 0037084499 scopus 로고    scopus 로고
    • Differential expression of receptors for Shiga and Cholera toxin is regulated by the cell cycle
    • Majoul, I., Schmidt, T., Pomasanova, M., Boutkevich, E., Kozlov, Y., and Söling, H. D. (2002) Differential expression of receptors for Shiga and cholera toxin is regulated by the cell cycle. J. Cell Sci. 115, 817-826 (Pubitemid 34196341)
    • (2002) Journal of Cell Science , vol.115 , Issue.4 , pp. 817-826
    • Majoul, I.1    Schmidt, T.2    Pomasanova, M.3    Boutkevich, E.4    Kozlov, Y.5    Soling, H.-D.6
  • 55
    • 0000275401 scopus 로고    scopus 로고
    • Chinese hamster ovary cells lacking GM1 and GD1a synthesize gangliosides upon transfection with human GM2 synthase
    • DOI 10.1016/S0167-4781(97)00117-6, PII S0167478197001176
    • Rosales Fritz, V. M., Daniotti, J. L., and Maccioni, H. J. (1997) Chinese hamster ovary cells lacking GM1 and GD1a synthesize gangliosides upon transfection with human GM2 synthase. Biochim. Biophys. Acta 1354, 153-158 (Pubitemid 27513075)
    • (1997) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1354 , Issue.2 , pp. 153-158
    • Rosales, F.V.M.1    Daniotti, J.L.2    Maccioni, H.J.F.3
  • 56
    • 77951900305 scopus 로고    scopus 로고
    • Globotriaosyl ceramide receptor function. Where membrane structure and pathology intersect
    • Lingwood, C. A., Binnington, B., Manis, A., and Branch, D. R. (2010) Globotriaosyl ceramide receptor function. Where membrane structure and pathology intersect. FEBS Lett. 584, 1879-1886
    • (2010) FEBS Lett. , vol.584 , pp. 1879-1886
    • Lingwood, C.A.1    Binnington, B.2    Manis, A.3    Branch, D.R.4
  • 59
    • 0032603531 scopus 로고    scopus 로고
    • Verotoxin induces apoptosis and the complete, rapid, long-term elimination of human astrocytoma xenografts in nude mice
    • Arab, S., Rutka, J., and Lingwood, C. (1999) Verotoxin induces apoptosis and the complete, rapid, long-term elimination of human astrocytoma xenografts in nude mice. Oncol. Res. 11, 33-39
    • (1999) Oncol. Res. , vol.11 , pp. 33-39
    • Arab, S.1    Rutka, J.2    Lingwood, C.3
  • 60
    • 0036020196 scopus 로고    scopus 로고
    • The treatment of malignant meningioma with verotoxin
    • DOI 10.1038/sj.neo.7900243
    • Salhia, B., Rutka, J. T., Lingwood, C., Nutikka, A., and Van Furth, W. R. (2002) The treatment of malignant meningioma with verotoxin. Neoplasia 4, 304-311 (Pubitemid 34755840)
    • (2002) Neoplasia , vol.4 , Issue.4 , pp. 304-311
    • Salhia, B.1    Rutka, J.T.2    Lingwood, C.3    Nutikka, A.4    Van Furth, W.R.5
  • 64
    • 84655174997 scopus 로고    scopus 로고
    • Biochemical, pathological and oncological relevance of Gb3Cer receptor
    • Devenica, D., Čikeš Čulić, V., Vuica, A., and Markotić, A. (2011) Biochemical, pathological and oncological relevance of Gb3Cer receptor. Med. Oncol. 28, S675-S684
    • (2011) Med. Oncol. , vol.28
    • Devenica, D.1    Čikeš Čulić, V.2    Vuica, A.3    Markotić, A.4
  • 65
    • 0842311700 scopus 로고    scopus 로고
    • Verotoxin sensitivity of ECV304 cells in vitro and in vivo in a xenograft tumour model: VT1 as a tumour neovascular marker
    • DOI 10.1023/B:AGEN.0000011799.47529.fd
    • Heath-Engel, H. M., and Lingwood, C. A. (2003) Verotoxin sensitivity of ECV304 cells in vitro and in vivo in a xenograft tumor model. VT1 as a tumor neovascular marker. Angiogenesis 6, 129-141 (Pubitemid 38173864)
    • (2003) Angiogenesis , vol.6 , Issue.2 , pp. 129-141
    • Heath-Engel, H.M.1    Lingwood, C.A.2
  • 69
    • 44849128559 scopus 로고    scopus 로고
    • Transport through the Golgi Apparatus by Rapid Partitioning within a Two-Phase Membrane System
    • DOI 10.1016/j.cell.2008.04.044, PII S0092867408006181
    • Patterson, G. H., Hirschberg, K., Polishchuk, R. S., Gerlich, D., Phair, R. D., and Lippincott-Schwartz, J. (2008) Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system. Cell 133, 1055-1067 (Pubitemid 351795609)
    • (2008) Cell , vol.133 , Issue.6 , pp. 1055-1067
    • Patterson, G.H.1    Hirschberg, K.2    Polishchuk, R.S.3    Gerlich, D.4    Phair, R.D.5    Lippincott-Schwartz, J.6
  • 70
    • 80053562290 scopus 로고    scopus 로고
    • Apicobasal domain identities of expanding tubular membranes depend on glycosphingolipid biosynthesis
    • Zhang, H., Abraham, N., Khan, L. A., Hall, D. H., Fleming, J. T., and Göbel, V. (2011) Apicobasal domain identities of expanding tubular membranes depend on glycosphingolipid biosynthesis. Nat. Cell Biol. 13, 1189-1201
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1189-1201
    • Zhang, H.1    Abraham, N.2    Khan, L.A.3    Hall, D.H.4    Fleming, J.T.5    Göbel, V.6
  • 71
    • 39049193055 scopus 로고    scopus 로고
    • Soluble adamantyl glycosphingolipid analogs as probes of glycosphingolipid function
    • Braukhausen, I., ed Humana Press, Totowa, NJ
    • Lingwood, C. A., Sadacharan, S., Abul-Milh, A., Mylvaganam, M., and Peter, M. (2006) Soluble adamantyl glycosphingolipid analogs as probes of glycosphingolipid function. in Glycobiology Protocols (Braukhausen, I., ed) pp. 305-320, Humana Press, Totowa, NJ
    • (2006) Glycobiology Protocols , pp. 305-320
    • Lingwood, C.A.1    Sadacharan, S.2    Abul-Milh, A.3    Mylvaganam, M.4    Peter, M.5
  • 72
    • 79958729719 scopus 로고    scopus 로고
    • Adamantyl glycosphingolipids provide a new approach to the selective regulation of cellular glycosphingolipid metabolism
    • Kamani, M., Mylvaganam, M., Tian, R., Rigat, B., Binnington, B., and Lingwood, C. (2011) Adamantyl glycosphingolipids provide a new approach to the selective regulation of cellular glycosphingolipid metabolism. J. Biol. Chem. 286, 21413-21426
    • (2011) J. Biol. Chem. , vol.286 , pp. 21413-21426
    • Kamani, M.1    Mylvaganam, M.2    Tian, R.3    Rigat, B.4    Binnington, B.5    Lingwood, C.6
  • 73
    • 61349091063 scopus 로고    scopus 로고
    • Passage through the Golgi is necessary for Shiga toxin B subunit to reach the endoplasmic reticulum
    • McKenzie, J., Johannes, L., Taguchi, T., and Sheff, D. (2009) Passage through the Golgi is necessary for Shiga toxin B subunit to reach the endoplasmic reticulum. FEBS J. 276, 1581-1595
    • (2009) FEBS J. , vol.276 , pp. 1581-1595
    • McKenzie, J.1    Johannes, L.2    Taguchi, T.3    Sheff, D.4
  • 74
    • 48249097851 scopus 로고    scopus 로고
    • Plasma membranes are poised for activation of raft phase coalescence at physiological temperature
    • Lingwood, D., Ries, J., Schwille, P., and Simons, K. (2008) Plasma membranes are poised for activation of raft phase coalescence at physiological temperature. Proc. Natl. Acad. Sci. U.S.A. 105, 10005-10010
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10005-10010
    • Lingwood, D.1    Ries, J.2    Schwille, P.3    Simons, K.4
  • 75
    • 0035783078 scopus 로고    scopus 로고
    • Uptake and metabolism of exogenous glycosphingolipids by cultured cells
    • Schwarzmann, G. (2001) Uptake and metabolism of exogenous glycosphingolipids by cultured cells. Semin. Cell Dev. Biol. 12, 163-171
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 163-171
    • Schwarzmann, G.1
  • 78
    • 0031951703 scopus 로고    scopus 로고
    • PH-independent retrograde targeting of glycolipids to the Golgi complex
    • Schapiro, F. B., Lingwood, C., Furuya, W., and Grinstein, S. (1998) pH-independent retrograde targeting of glycolipids to the Golgi complex. Am. J. Physiol. 274, C319-C332
    • (1998) Am. J. Physiol. , vol.274
    • Schapiro, F.B.1    Lingwood, C.2    Furuya, W.3    Grinstein, S.4
  • 79
    • 3042639390 scopus 로고    scopus 로고
    • Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin
    • DOI 10.1242/jcs.01081
    • Lauvrak, S. U., Torgersen, M. L., and Sandvig, K. (2004) Efficient endosome- to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin. J. Cell Sci. 117, 2321-2331 (Pubitemid 38807499)
    • (2004) Journal of Cell Science , vol.117 , Issue.11 , pp. 2321-2331
    • Lauvrak, S.U.1    Torgersen, M.L.2    Sandvig, K.3
  • 81
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal, S. K., Skretting, G., Garred, O., van Deurs, B., and Sandvig, K. (1999) Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol. Biol. Cell 10, 961-974 (Pubitemid 29193724)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.4 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, O.3    Vilhardt, F.4    Van Deurs, B.5    Sandvig, K.6
  • 82
    • 0037444495 scopus 로고    scopus 로고
    • Distinct caveolae-mediated endocytic pathways target the Golgi apparatus and the endoplasmic reticulum
    • DOI 10.1242/jcs.00327
    • Le, P. U., and Nabi, I. R. (2003) Distinct caveolae-mediated endocytic pathways target the Golgi apparatus and the endoplasmic reticulum. J. Cell Sci. 116, 1059-1071 (Pubitemid 36395616)
    • (2003) Journal of Cell Science , vol.116 , Issue.6 , pp. 1059-1071
    • Le, P.U.1    Nabi, I.R.2
  • 83
    • 6044235526 scopus 로고    scopus 로고
    • M1 complex into Golgi and induction of toxicity depend on actin cytoskeleton
    • DOI 10.1152/ajpcell.00189.2004
    • Badizadegan, K., Wheeler, H. E., Fujinaga, Y., and Lencer, W. I. (2004) Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton. Am. J. Physiol. Cell Physiol. 287, C1453-C1462 (Pubitemid 39382907)
    • (2004) American Journal of Physiology - Cell Physiology , vol.287 , Issue.5
    • Badizadegan, K.1    Wheeler, H.E.2    Fujinaga, Y.3    Lencer, W.I.4
  • 84
    • 0042311010 scopus 로고    scopus 로고
    • Role of lipids in the retrograde pathway of ricin intoxication
    • Spilsberg, B., Van Meer, G., and Sandvig, K. (2003) Role of lipids in the retrograde pathway of ricin intoxication. Traffic 4, 544-552 (Pubitemid 36896546)
    • (2003) Traffic , vol.4 , Issue.8 , pp. 544-552
    • Spilsberg, B.1    Van Meer, G.2    Sandvig, K.3
  • 86
    • 0033203501 scopus 로고    scopus 로고
    • Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases
    • Puri, V., Watanabe, R., Dominguez, M., Sun, X., Wheatley, C. L., Marks, D. L., and Pagano, R. E. (1999) Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases. Nat. Cell Biol. 1, 386-388 (Pubitemid 129493583)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 386-388
    • Puri, V.1    Watanabe, R.2    Dominguez, M.3    Sun, X.4    Wheatley, C.L.5    Marks, D.L.6    Pagano, R.E.7
  • 87
    • 77953368751 scopus 로고    scopus 로고
    • Role of glycolipids in lipid rafts. A view through atomistic molecular dynamics simulations with galactosylceramide
    • Hall, A., Róg, T., Karttunen, M., and Vattulainen, I. (2010) Role of glycolipids in lipid rafts. A view through atomistic molecular dynamics simulations with galactosylceramide. J. Phys. Chem. B 114, 7797-7807
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7797-7807
    • Hall, A.1    Róg, T.2    Karttunen, M.3    Vattulainen, I.4
  • 88
    • 0027474954 scopus 로고
    • Orientation of the saccharide chains of glycolipids at the membrane surface. Conformational analysis of the glucose-ceramide and the glucose-glyceride linkages using molecular mechanics (MM3)
    • Nyholm, P. G., and Pascher, I. (1993) Orientation of the saccharide chains of glycolipids at the membrane surface. Conformational analysis of the glucose-ceramide and the glucose-glyceride linkages using molecular mechanics (MM3). Biochemistry 32, 1225-1234
    • (1993) Biochemistry , vol.32 , pp. 1225-1234
    • Nyholm, P.G.1    Pascher, I.2
  • 89
    • 0024119995 scopus 로고
    • On the dissection of binding epitopes on carbohydrate receptors for microbes using molecular modeling
    • Calander, N., Karlsson, K. A., Nyholm, P. G., and Pascher, I. (1988) On the dissection of binding epitopes on carbohydrate receptors for microbes using molecular modeling. Biochimie 70, 1673-1682
    • (1988) Biochimie , vol.70 , pp. 1673-1682
    • Calander, N.1    Karlsson, K.A.2    Nyholm, P.G.3    Pascher, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.