메뉴 건너뛰기




Volumn 30, Issue 2, 2010, Pages 258-269

Glycosylphosphatidylinositols are potential targets for the development of novel inhibitors for aerolysin-type of pore-forming bacterial toxins

Author keywords

Aerolysin; Carbohydrate; Glycolipid; GPI; Pore forming toxin; Toxin inhibitor

Indexed keywords

AEROLYSIN; BACTERIAL TOXIN; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL DERIVATIVE; PORE FORMING BACTERIAL TOXIN; UNCLASSIFIED DRUG;

EID: 77249145364     PISSN: 01986325     EISSN: 10981128     Source Type: Journal    
DOI: 10.1002/med.20167     Document Type: Review
Times cited : (12)

References (74)
  • 2
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco C, Papini E, Schiavo G. Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett 1994;346:92-98.
    • (1994) FEBS Lett , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 3
    • 0025940364 scopus 로고
    • Pore-forming bacterial protein hemolysins (cytolysins)
    • Braun V, Focareta T. Pore-forming bacterial protein hemolysins (cytolysins). Crit Rev Microbiol 1991;18:115-158.
    • (1991) Crit Rev Microbiol , vol.18 , pp. 115-158
    • Braun, V.1    Focareta, T.2
  • 5
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin-the ins and outs of a model channel-forming toxin
    • Parker MW, van der Goot FG, Buckley T. Aerolysin-the ins and outs of a model channel-forming toxin. Mol Microbiol 1996;19:205-212.
    • (1996) Mol Microbiol , vol.19 , pp. 205-212
    • Parker, M.W.1    van der Goot, F.G.2    Buckley, T.3
  • 6
    • 0034176550 scopus 로고    scopus 로고
    • Adventures of a pore-forming toxin at the target cell surface
    • Abrami L, Fivaz M, van der Goot FG. Adventures of a pore-forming toxin at the target cell surface. Trends Microbiol 2000;8:168-172.
    • (2000) Trends Microbiol , vol.8 , pp. 168-172
    • Abrami, L.1    Fivaz, M.2    van der Goot, F.G.3
  • 8
    • 0036076262 scopus 로고    scopus 로고
    • Clostridium septicum alpha-toxin is active against the parasitic protozoan Toxoplasma gondii and targets members of the SAG family of glycosylphosphatidylinositol-anchored surface proteins
    • Wichroski MJ, Melton JA, Donahue CG, Tweten RK, Ward GE. Clostridium septicum alpha-toxin is active against the parasitic protozoan Toxoplasma gondii and targets members of the SAG family of glycosylphosphatidylinositol-anchored surface proteins. Infect Immun 2002;70: 4353-4361.
    • (2002) Infect Immun , vol.70 , pp. 4353-4361
    • Wichroski, M.J.1    Melton, J.A.2    Donahue, C.G.3    Tweten, R.K.4    Ward, G.E.5
  • 10
    • 0036177096 scopus 로고    scopus 로고
    • Kre1p, the plasma membrane receptor for the yeast K1 viral toxin
    • Breinig F, Tipper DJ, Schmitt MJ. Kre1p, the plasma membrane receptor for the yeast K1 viral toxin. Cell 2002;108:395-405.
    • (2002) Cell , vol.108 , pp. 395-405
    • Breinig, F.1    Tipper, D.J.2    Schmitt, M.J.3
  • 11
    • 0032479373 scopus 로고    scopus 로고
    • Molecular cloning of a GPI-anchored aminopeptidase N from Bombyx mori midgut: A putative receptor for Bacillus thuringiensis CryIA toxin
    • Hua G, Tsukamoto K, Rasilo M-L, Ikezawa H. Molecular cloning of a GPI-anchored aminopeptidase N from Bombyx mori midgut: a putative receptor for Bacillus thuringiensis CryIA toxin. Gene 1998;214:177-185.
    • (1998) Gene , vol.214 , pp. 177-185
    • Hua, G.1    Tsukamoto, K.2    Rasilo, M.-L.3    Ikezawa, H.4
  • 12
    • 32944464814 scopus 로고    scopus 로고
    • A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae
    • Fernandez LE, Aimanova KG, Gill SS, Bravo A, Soberon M. A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem J 2006;394:77-84.
    • (2006) Biochem J , vol.394 , pp. 77-84
    • Fernandez, L.E.1    Aimanova, K.G.2    Gill, S.S.3    Bravo, A.4    Soberon, M.5
  • 14
    • 33846664997 scopus 로고    scopus 로고
    • Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins
    • Lang S, Xue J, Guo Z, Palmer M. Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins. Med Microbiol Immunol 2007;196:1-10.
    • (2007) Med Microbiol Immunol , vol.196 , pp. 1-10
    • Lang, S.1    Xue, J.2    Guo, Z.3    Palmer, M.4
  • 15
    • 0141755375 scopus 로고    scopus 로고
    • Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin
    • Lang S, Palmer M. Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. J Biol Chem 2003;278:38167-38173.
    • (2003) J Biol Chem , vol.278 , pp. 38167-38173
    • Lang, S.1    Palmer, M.2
  • 16
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosylphosphatidylinositol structure
    • Ferguson MAJ, Williams AF. Cell-surface anchoring of proteins via glycosylphosphatidylinositol structure. Ann Rev Biochem 1988;57:285-320.
    • (1988) Ann Rev Biochem , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 17
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund PT. The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Ann Rev Biochem 1993;62:121-138.
    • (1993) Ann Rev Biochem , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 18
    • 0023883979 scopus 로고
    • Glycosyl- phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
    • Ferguson MAJ, Homans SW, Dwek RA, Rademacher TW. Glycosyl- phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane. Science 1988;239:753-759.
    • (1988) Science , vol.239 , pp. 753-759
    • Ferguson, M.A.J.1    Homans, S.W.2    Dwek, R.A.3    Rademacher, T.W.4
  • 19
    • 0025303347 scopus 로고
    • Structure, biosynthesis, and function of glycosylphosphatidylinositols
    • Thomas JR, Dwek RA, Rademacher TW. Structure, biosynthesis, and function of glycosylphosphatidylinositols. Biochemistry 1990;29:5413-5422.
    • (1990) Biochemistry , vol.29 , pp. 5413-5422
    • Thomas, J.R.1    Dwek, R.A.2    Rademacher, T.W.3
  • 20
    • 84956491498 scopus 로고    scopus 로고
    • Functions of glycosyl phosphatidylinositols
    • Hart GW, Hart G, Sinaÿ P, Ernst B, Sinaikin P, editors, New York: Wiley-VCH;
    • Menon AK, Baumann NA, Rancour DM. Functions of glycosyl phosphatidylinositols. In: Hart GW, Hart G, Sinaÿ P, Ernst B, Sinaikin P, editors. Carbohydrates in chemistry and biology, Vol. 4. New York: Wiley-VCH; 2000. pp 757-769.
    • (2000) Carbohydrates in chemistry and biology , vol.4 , pp. 757-769
    • Menon, A.K.1    Baumann, N.A.2    Rancour, D.M.3
  • 21
    • 0023576304 scopus 로고
    • Biosynthesis, membrane association and release of N-CAM-120, a phosphatidylinositol-linked form of the neuron cell adhesion molecule
    • He H-T, Finne J, Goridis C. Biosynthesis, membrane association and release of N-CAM-120, a phosphatidylinositol-linked form of the neuron cell adhesion molecule. J Cell Biol 1987;105:2489-2500.
    • (1987) J Cell Biol , vol.105 , pp. 2489-2500
    • He, H.-T.1    Finne, J.2    Goridis, C.3
  • 22
    • 0026056244 scopus 로고
    • Signal transduction by GPI-anchored membrane proteins
    • Robinson PJ. Signal transduction by GPI-anchored membrane proteins. Cell Biol Intern Rep 1991;15:761-767.
    • (1991) Cell Biol Intern Rep , vol.15 , pp. 761-767
    • Robinson, P.J.1
  • 23
    • 0026020167 scopus 로고
    • Glycosylphosphatidylinositol: A candidate system for IL-2 signal transduction
    • Eardley DD, Koshland ME. Glycosylphosphatidylinositol: a candidate system for IL-2 signal transduction. Science 1991;251:78-81.
    • (1991) Science , vol.251 , pp. 78-81
    • Eardley, D.D.1    Koshland, M.E.2
  • 24
    • 0034951879 scopus 로고    scopus 로고
    • Glycosyl phosphatidylinositol-linked glycoconjugates: Structure, biosynthesis and function
    • Hwa K. Glycosyl phosphatidylinositol-linked glycoconjugates: structure, biosynthesis and function. Adv Exp Med Biol 2001;491:207-214.
    • (2001) Adv Exp Med Biol , vol.491 , pp. 207-214
    • Hwa, K.1
  • 25
    • 0024449097 scopus 로고
    • A glycosphospholipid anchor is required for Qa-2-mediated T cell activation
    • Robinson PJ, Millrain M, Antoniou J, Simpson E, Mellor AL. A glycosphospholipid anchor is required for Qa-2-mediated T cell activation. Nature 1989;342:85-87.
    • (1989) Nature , vol.342 , pp. 85-87
    • Robinson, P.J.1    Millrain, M.2    Antoniou, J.3    Simpson, E.4    Mellor, A.L.5
  • 26
    • 0034053612 scopus 로고    scopus 로고
    • Microdomains in lymphocyte signalling: Beyond GPI-anchored proteins
    • Ilangumaran S, He H-T, Hoessli DC. Microdomains in lymphocyte signalling: beyond GPI-anchored proteins. Immunol Today 2000;21:2-7.
    • (2000) Immunol Today , vol.21 , pp. 2-7
    • Ilangumaran, S.1    He, H.-T.2    Hoessli, D.C.3
  • 27
    • 0025231501 scopus 로고
    • Cellular and genetic aspects of antigenic variation in trypanosomes
    • Cross GAM. Cellular and genetic aspects of antigenic variation in trypanosomes. Ann Rev Immunol 1990;8:83-110.
    • (1990) Ann Rev Immunol , vol.8 , pp. 83-110
    • Cross, G.A.M.1
  • 28
    • 0030929760 scopus 로고    scopus 로고
    • Is there evidence for phospho-oligosaccharides as insulin mediators?
    • Field MC. Is there evidence for phospho-oligosaccharides as insulin mediators? Glycobiology 1997;7:161-168.
    • (1997) Glycobiology , vol.7 , pp. 161-168
    • Field, M.C.1
  • 29
    • 0028419123 scopus 로고
    • Glycosylated phosphatidylinositol molecules as second messengers
    • Gaulton GN, Pratt JC. Glycosylated phosphatidylinositol molecules as second messengers. Seminars Immunol 1994;6:97-104.
    • (1994) Seminars Immunol , vol.6 , pp. 97-104
    • Gaulton, G.N.1    Pratt, J.C.2
  • 31
    • 0342319235 scopus 로고    scopus 로고
    • Structure and assembly of the channel-forming Aeromonas toxin aerolysin
    • Parker MW, editor, New York: Springer;
    • Parker MW, Buckley JT, van Der Goot FG, Tsernoglou D. Structure and assembly of the channel-forming Aeromonas toxin aerolysin. In: Parker MW, editor. Protein toxin structure. New York: Springer; 1996. pp 79-95.
    • (1996) Protein toxin structure , pp. 79-95
    • Parker, M.W.1    Buckley, J.T.2    van Der Goot, F.G.3    Tsernoglou, D.4
  • 33
    • 0031756554 scopus 로고    scopus 로고
    • Secretion and properties of the large and small lobes of the channel-forming toxin aerolysin
    • Diep DB, Lawrence TS, Ausio J, Howard SP, Buckley JT. Secretion and properties of the large and small lobes of the channel-forming toxin aerolysin. Mol Microbiol 1998;30:341-352.
    • (1998) Mol Microbiol , vol.30 , pp. 341-352
    • Diep, D.B.1    Lawrence, T.S.2    Ausio, J.3    Howard, S.P.4    Buckley, J.T.5
  • 34
    • 0033621376 scopus 로고    scopus 로고
    • Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding
    • Fivaz M, Velluz M-C, van der Goot FG. Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding. J Biol Chem 1999;274:37705-37708.
    • (1999) J Biol Chem , vol.274 , pp. 37705-37708
    • Fivaz, M.1    Velluz, M.-C.2    van der Goot, F.G.3
  • 36
    • 0026721371 scopus 로고
    • The aerolysin membrane channel is formed by heptamerization of the monomer
    • Wilmsen HU, Leonard KR, Tichelaar W, Buckley JT, Pattus F. The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J 1992;11:2457-2463.
    • (1992) EMBO J , vol.11 , pp. 2457-2463
    • Wilmsen, H.U.1    Leonard, K.R.2    Tichelaar, W.3    Buckley, J.T.4    Pattus, F.5
  • 37
    • 0028077896 scopus 로고
    • The C-terminal peptide produced upon proteolytic activation of the cytolytic toxin aerolysin is not involved in channel formation
    • van der Goot FG, Hardie KR, Parker MW, Buckley JT. The C-terminal peptide produced upon proteolytic activation of the cytolytic toxin aerolysin is not involved in channel formation. J Biol Chem 1994;269:30496-30501.
    • (1994) J Biol Chem , vol.269 , pp. 30496-30501
    • van der Goot, F.G.1    Hardie, K.R.2    Parker, M.W.3    Buckley, J.T.4
  • 38
    • 0033157103 scopus 로고    scopus 로고
    • Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas
    • Nelson KL, Brodsky RA, Buckley JT. Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas. Cell Microbiol 1999;1:69-74.
    • (1999) Cell Microbiol , vol.1 , pp. 69-74
    • Nelson, K.L.1    Brodsky, R.A.2    Buckley, J.T.3
  • 39
    • 0032498627 scopus 로고    scopus 로고
    • A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum
    • Abrami L, Fivaz M, Glauser P-E, Parton RG, van Der Goot FG. A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J Cell Biol 1998;140:525-540.
    • (1998) J Cell Biol , vol.140 , pp. 525-540
    • Abrami, L.1    Fivaz, M.2    Glauser, P.-E.3    Parton, R.G.4    van Der Goot, F.G.5
  • 40
    • 0031936213 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin
    • Diep DB, Nelson KL, Raja SM, Pleshak EN, Buckley JT. Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin. J Biol Chem 1998;273:2355-2360.
    • (1998) J Biol Chem , vol.273 , pp. 2355-2360
    • Diep, D.B.1    Nelson, K.L.2    Raja, S.M.3    Pleshak, E.N.4    Buckley, J.T.5
  • 41
    • 0033529592 scopus 로고    scopus 로고
    • Analysis of receptor binding by the channel-forming toxin aerolysin using surface plasmon resonance
    • MacKenzie CR, Hirama T, Buckley JT. Analysis of receptor binding by the channel-forming toxin aerolysin using surface plasmon resonance. J Biol Chem 1999;274:22604-22609.
    • (1999) J Biol Chem , vol.274 , pp. 22604-22609
    • MacKenzie, C.R.1    Hirama, T.2    Buckley, J.T.3
  • 42
    • 0030789217 scopus 로고    scopus 로고
    • The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein
    • Cowell S, Aschauer W, Gruber HJ, Nelson KL, Buckley JT. The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein. Mol Microbiol 1997;25:343-350.
    • (1997) Mol Microbiol , vol.25 , pp. 343-350
    • Cowell, S.1    Aschauer, W.2    Gruber, H.J.3    Nelson, K.L.4    Buckley, J.T.5
  • 43
    • 0037070210 scopus 로고    scopus 로고
    • The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient: The polypeptide moiety is required for the toxin-receptor interaction
    • Abrami L, Velluz M-C, Hong Y, Ohishi K, Mehlert A, Ferguson M, Kinoshita T, van der Goot FG. The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient: the polypeptide moiety is required for the toxin-receptor interaction. FEBS Lett 2002;512:249-254.
    • (2002) FEBS Lett , vol.512 , pp. 249-254
    • Abrami, L.1    Velluz, M.-C.2    Hong, Y.3    Ohishi, K.4    Mehlert, A.5    Ferguson, M.6    Kinoshita, T.7    van der Goot, F.G.8
  • 44
    • 0036792614 scopus 로고    scopus 로고
    • Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin
    • Hong Y, Ohishi K, Inoue N, Kang J, Shime H, Horiguchi Y, van der Goot FG, Sugimoto N, Kinoshita T. Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin. EMBO J 2002;21:5047-5056.
    • (2002) EMBO J , vol.21 , pp. 5047-5056
    • Hong, Y.1    Ohishi, K.2    Inoue, N.3    Kang, J.4    Shime, H.5    Horiguchi, Y.6    van der Goot, F.G.7    Sugimoto, N.8    Kinoshita, T.9
  • 46
    • 0028878878 scopus 로고
    • The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin
    • Ballard J, Crabtree J, Roe BA, Tweten RK. The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin. Infect Immun 1995;63:340-344.
    • (1995) Infect Immun , vol.63 , pp. 340-344
    • Ballard, J.1    Crabtree, J.2    Roe, B.A.3    Tweten, R.K.4
  • 47
    • 0029136193 scopus 로고
    • Toxins as tools in neurochemistry
    • Hucho F. Toxins as tools in neurochemistry. Angew Chem Int Ed 1995;34:39-50.
    • (1995) Angew Chem Int Ed , vol.34 , pp. 39-50
    • Hucho, F.1
  • 48
    • 0028020468 scopus 로고
    • Triggers and switches in a self-assembling pore-forming protein
    • Bayley H. Triggers and switches in a self-assembling pore-forming protein. J Cell Biochem 1994;56:177-182.
    • (1994) J Cell Biochem , vol.56 , pp. 177-182
    • Bayley, H.1
  • 49
    • 4544374078 scopus 로고    scopus 로고
    • Chemical synthesis of GPIs and GPI-anchored glycopeptides
    • Guo Z, Bishop L. Chemical synthesis of GPIs and GPI-anchored glycopeptides. Eur J Org Chem 2004;3585-3596.
    • (2004) Eur J Org Chem , pp. 3585-3596
    • Guo, Z.1    Bishop, L.2
  • 50
    • 0025230748 scopus 로고
    • Synthetic studies on glycophosphatidyl inositol (GPI) anchor of Trypanosoma brucei: Glycoheptaosyl core
    • Murakata C, Ogawa T. Synthetic studies on glycophosphatidyl inositol (GPI) anchor of Trypanosoma brucei: glycoheptaosyl core. Tetrahedron Lett 1990;31:2439-2442.
    • (1990) Tetrahedron Lett , vol.31 , pp. 2439-2442
    • Murakata, C.1    Ogawa, T.2
  • 51
    • 0027111710 scopus 로고
    • Stereoselective total synthesis of the glycosylphosphatidylinositol (GPI) anchor of Trypanosoma brucei
    • Murakata C, Ogawa T. Stereoselective total synthesis of the glycosylphosphatidylinositol (GPI) anchor of Trypanosoma brucei. Carbohydr Res 1992;235:95-114.
    • (1992) Carbohydr Res , vol.235 , pp. 95-114
    • Murakata, C.1    Ogawa, T.2
  • 52
    • 0026067464 scopus 로고
    • A total synthesis of GPI anchor of Trypanosoma brucei
    • Murakata C, Ogawa T. A total synthesis of GPI anchor of Trypanosoma brucei. Tetrahedron Lett 1991;32:671-674.
    • (1991) Tetrahedron Lett , vol.32 , pp. 671-674
    • Murakata, C.1    Ogawa, T.2
  • 53
    • 0025959194 scopus 로고
    • Synthetic studies of glycophosphatidylinositol anchor: A highly efficient synthesis of glycobiosyl phosphatidylinositol through H-phosphonate approach
    • Murakata C, Ogawa T. Synthetic studies of glycophosphatidylinositol anchor: a highly efficient synthesis of glycobiosyl phosphatidylinositol through H-phosphonate approach. Tetrahedron Lett 1991;32:101.
    • (1991) Tetrahedron Lett , vol.32 , pp. 101
    • Murakata, C.1    Ogawa, T.2
  • 54
    • 0027116048 scopus 로고
    • Stereoselective synthesis of glycobiosyl phosphatidylinositol, a part structure of the glycosylphosphatidylinositol (GPI) anchor of Trypanosoma brucei
    • Murakata C, Ogawa T. Stereoselective synthesis of glycobiosyl phosphatidylinositol, a part structure of the glycosylphosphatidylinositol (GPI) anchor of Trypanosoma brucei. Carbohydr Res 1992;234:75-91.
    • (1992) Carbohydr Res , vol.234 , pp. 75-91
    • Murakata, C.1    Ogawa, T.2
  • 56
    • 0033985424 scopus 로고    scopus 로고
    • 1,2-Diacetals in synthesis: Total synthesis of a glycosylphosphatidylinositol anchor of Trypanosoma brucei
    • Baeschlin DK, Chaperon AR, Green LG, Hahn MG, Ince SJ, Ley SV. 1,2-Diacetals in synthesis: total synthesis of a glycosylphosphatidylinositol anchor of Trypanosoma brucei. Chem Eur J 2000;6:172-186.
    • (2000) Chem Eur J , vol.6 , pp. 172-186
    • Baeschlin, D.K.1    Chaperon, A.R.2    Green, L.G.3    Hahn, M.G.4    Ince, S.J.5    Ley, S.V.6
  • 57
    • 0346157341 scopus 로고    scopus 로고
    • First synthesis of a malarial prototype: A fully lipidated and phosphorylated GPI membrane anchor
    • Lu J, Jayaprakash KN, Fraser-Reid B. First synthesis of a malarial prototype: a fully lipidated and phosphorylated GPI membrane anchor. Tetrahedron Lett 2004;45:879-882.
    • (2004) Tetrahedron Lett , vol.45 , pp. 879-882
    • Lu, J.1    Jayaprakash, K.N.2    Fraser-Reid, B.3
  • 58
    • 2942691414 scopus 로고    scopus 로고
    • Synthesis of a malaria candidate glycosylphosphatidylinositol (GPI) structure: A strategy for fully inositol acylated and phosphory - lated GPIs
    • Lu J, Jayaprakash KN, Schlueter U, Fraser-Reid B. Synthesis of a malaria candidate glycosylphosphatidylinositol (GPI) structure: a strategy for fully inositol acylated and phosphory - lated GPIs. J Am Chem Soc 2004;126:7540-7547.
    • (2004) J Am Chem Soc , vol.126 , pp. 7540-7547
    • Lu, J.1    Jayaprakash, K.N.2    Schlueter, U.3    Fraser-Reid, B.4
  • 59
    • 0032811891 scopus 로고    scopus 로고
    • Glycosyl phosphatidylinositol (GPI) anchor synthesis based on versatile building blocks - total synthesis of a GPI anchor of Yeast
    • Mayer TG, Schmidt RR. Glycosyl phosphatidylinositol (GPI) anchor synthesis based on versatile building blocks - total synthesis of a GPI anchor of Yeast. Eur J Org Chem 1999: 1153-1165.
    • (1999) Eur J Org Chem , pp. 1153-1165
    • Mayer, T.G.1    Schmidt, R.R.2
  • 60
    • 33748244079 scopus 로고
    • Synthesis of a GPI anchor of yeast (Saccharomyces cerevisiae)
    • Mayer TG, Kratzer B, Schmidt RR. Synthesis of a GPI anchor of yeast (Saccharomyces cerevisiae). Angew Chem Int Ed 1994;33:2177-2181.
    • (1994) Angew Chem Int Ed , vol.33 , pp. 2177-2181
    • Mayer, T.G.1    Kratzer, B.2    Schmidt, R.R.3
  • 61
    • 0033593312 scopus 로고    scopus 로고
    • Synthesis of the glycosyl phosphatidyl inositol anchor of rat brain Thy-1
    • Tailler D, Ferrieres V, Pekari K, Schmidt RR. Synthesis of the glycosyl phosphatidyl inositol anchor of rat brain Thy-1. Tetrahedron Lett 1999;40:679-682.
    • (1999) Tetrahedron Lett , vol.40 , pp. 679-682
    • Tailler, D.1    Ferrieres, V.2    Pekari, K.3    Schmidt, R.R.4
  • 62
    • 0037458994 scopus 로고    scopus 로고
    • A variable concept for the preparation of branched glycosyl phosphatidyl inositol anchors
    • Pekari K, Schmidt RR. A variable concept for the preparation of branched glycosyl phosphatidyl inositol anchors. J Org Chem 2003;68:1295-1308.
    • (2003) J Org Chem , vol.68 , pp. 1295-1308
    • Pekari, K.1    Schmidt, R.R.2
  • 63
    • 0035798044 scopus 로고    scopus 로고
    • Synthesis of the fully phosphorylated GPI anchor pseudohexasaccharide of Toxoplasma gondii
    • Pekari K, Tailler D, Weingart R, Schmidt RR. Synthesis of the fully phosphorylated GPI anchor pseudohexasaccharide of Toxoplasma gondii. J Org Chem 2001;66:7432-7442.
    • (2001) J Org Chem , vol.66 , pp. 7432-7442
    • Pekari, K.1    Tailler, D.2    Weingart, R.3    Schmidt, R.R.4
  • 64
    • 0037073195 scopus 로고    scopus 로고
    • Rapid synthesis of a glycosylphosphatidylinositol-based malaria vaccine using automated solid-phase oligosaccharide synthesis
    • Hewitt MC, Snyder DA, Seeberger PH. Rapid synthesis of a glycosylphosphatidylinositol-based malaria vaccine using automated solid-phase oligosaccharide synthesis. J Am Chem Soc 2002;124:13434-13436.
    • (2002) J Am Chem Soc , vol.124 , pp. 13434-13436
    • Hewitt, M.C.1    Snyder, D.A.2    Seeberger, P.H.3
  • 67
    • 17744411431 scopus 로고    scopus 로고
    • A practical solid-phase synthesis of glycosylphosphatidylinositol precursors
    • Reichardt N-C, Martin-Lomas M. A practical solid-phase synthesis of glycosylphosphatidylinositol precursors. Angew Chem Int Ed 2003;42:4674-4677.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 4674-4677
    • Reichardt, N.-C.1    Martin-Lomas, M.2
  • 68
    • 0346434113 scopus 로고    scopus 로고
    • Convergent synthesis of a GPI containing an acylated inositol
    • Xue J, Guo Z. Convergent synthesis of a GPI containing an acylated inositol. J Am Chem Soc 2003;125:16334-16339.
    • (2003) J Am Chem Soc , vol.125 , pp. 16334-16339
    • Xue, J.1    Guo, Z.2
  • 69
    • 13244298180 scopus 로고    scopus 로고
    • A new approach to construct full-length glycosylphosphatidylinositols of parasitic protozoa and [4-deoxy-Man-III]-GPI analogues
    • Ali A, Gowda DC, Vishwakarma RA. A new approach to construct full-length glycosylphosphatidylinositols of parasitic protozoa and [4-deoxy-Man-III]-GPI analogues. Chem Commun 2005;519-521.
    • (2005) Chem Commun , pp. 519-521
    • Ali, A.1    Gowda, D.C.2    Vishwakarma, R.A.3
  • 70
    • 30444457876 scopus 로고    scopus 로고
    • The chemical synthesis of bioactive glycosylphosphatidylinositols from Trypanosoma cruzi containing an unsaturated fatty acid in the lipid
    • Yashunsky DV, Borodkin VS, Ferguson MAJ, Nikolaev AV. The chemical synthesis of bioactive glycosylphosphatidylinositols from Trypanosoma cruzi containing an unsaturated fatty acid in the lipid. Angew Chem Int Ed 2006;45:468-474.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 468-474
    • Yashunsky, D.V.1    Borodkin, V.S.2    Ferguson, M.A.J.3    Nikolaev, A.V.4
  • 71
    • 35548966321 scopus 로고    scopus 로고
    • Convergent synthesis of a fully phosphorylated GPI anchor of the CD52 antigen
    • Wu X, Guo Z. Convergent synthesis of a fully phosphorylated GPI anchor of the CD52 antigen. Org Lett 2007;9:4311-4313.
    • (2007) Org Lett , vol.9 , pp. 4311-4313
    • Wu, X.1    Guo, Z.2
  • 72
    • 46549090131 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of sperm CD52 GPI anchor and related derivatives as binding receptors of pore-forming CAMP factor
    • Wu X, Shen Z, Zeng X, Lang S, Palmer M, Guo Z. Synthesis and biological evaluation of sperm CD52 GPI anchor and related derivatives as binding receptors of pore-forming CAMP factor. Carbohydr Res 2008;343:1718-1729.
    • (2008) Carbohydr Res , vol.343 , pp. 1718-1729
    • Wu, X.1    Shen, Z.2    Zeng, X.3    Lang, S.4    Palmer, M.5    Guo, Z.6
  • 73
    • 11744318388 scopus 로고
    • Measurement of interfacial processes at electrode surfaces with the electrochemical quartz crystal microbalance
    • Buttry DA, Ward MD. Measurement of interfacial processes at electrode surfaces with the electrochemical quartz crystal microbalance. Chem Rev 1992;92:1355-1379.
    • (1992) Chem Rev , vol.92 , pp. 1355-1379
    • Buttry, D.A.1    Ward, M.D.2
  • 74
    • 28844508563 scopus 로고    scopus 로고
    • Heat-stabilized phospholipid films: Film characterization and the production of protein-resistant surfaces
    • Stine R, Pishko MV. Heat-stabilized phospholipid films: film characterization and the production of protein-resistant surfaces. Langmuir 2005;21:11352-11356.
    • (2005) Langmuir , vol.21 , pp. 11352-11356
    • Stine, R.1    Pishko, M.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.