메뉴 건너뛰기




Volumn 47, Issue 3, 2009, Pages 197-204

Trypanosome glycosylphosphatidylinositol biosynthesis

Author keywords

Biosynthesis; Glycoprotein; Glycosylphosphatidylinositol; Trypanosoma brucei; Trypanosome

Indexed keywords

ACYLTRANSFERASE; ETHANOLAMINE PHOSPHOTRANSFERASE; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; MANNOSE; MANNOSYLTRANSFERASE;

EID: 70349212401     PISSN: 00234001     EISSN: 17380006     Source Type: Journal    
DOI: 10.3347/kjp.2009.47.3.197     Document Type: Short Survey
Times cited : (22)

References (69)
  • 1
    • 0030131182 scopus 로고    scopus 로고
    • Antigenic variation in trypanosomes: Secrets surface slowly
    • Cross GA. Antigenic variation in trypanosomes: secrets surface slowly. Bioessays 1996; 18: 283-291.
    • (1996) Bioessays , vol.18 , pp. 283-291
    • Cross, G.A.1
  • 2
  • 3
    • 0023883979 scopus 로고
    • Glycosylphosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
    • Ferguson MA, Homans SW, Dwek RA, Rademacher TW. Glycosylphosphatidylinositol 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.1    Homans, S.W.2    Dwek, R.A.3    Rademacher, T.W.4
  • 4
    • 0024291704 scopus 로고
    • Complete structure of the glycosyl phosphatidylinositol membrane anchor of rat brain Thy-1 glycoprotein
    • Homans SW, Ferguson MA, Dwek RA, Rademacher TW, Anand R, Williams AF. Complete structure of the glycosyl phosphatidylinositol membrane anchor of rat brain Thy-1 glycoprotein. Nature 1988; 333: 269-272.
    • (1988) Nature , vol.333 , pp. 269-272
    • Homans, S.W.1    Ferguson, M.A.2    Dwek, R.A.3    Rademacher, T.W.4    Anand, R.5    Williams, A.F.6
  • 5
    • 0025737738 scopus 로고
    • A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei: Lipid structure and biosynthesis
    • Field MC, Menon AK, Cross GA. A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei: lipid structure and biosynthesis. EMBO J 1991; 10: 2731-2739.
    • (1991) EMBO J , vol.10 , pp. 2731-2739
    • Field, M.C.1    Menon, A.K.2    Cross, G.A.3
  • 6
    • 0026755131 scopus 로고
    • Site of palmitoylation of a phospholipase C-resistant glycosyl-phosphatidylinositol membrane anchor
    • Ferguson MAJ. Site of palmitoylation of a phospholipase C-resistant glycosyl-phosphatidylinositol membrane anchor. Biochem J 1992; 284: 297-300.
    • (1992) Biochem J , vol.284 , pp. 297-300
    • Ferguson, M.A.J.1
  • 7
    • 0027405470 scopus 로고
    • A simple purification of procyclic acidic repetitive protein and demonstration of a sialylated glycosyl-phosphatidylinositol membrane anchor
    • Ferguson MAJ, Murray P, Rutherford H, McConville MJ. A simple purification of procyclic acidic repetitive protein and demonstration of a sialylated glycosyl-phosphatidylinositol membrane anchor. Biochem J 1993; 291: 51-55.
    • (1993) Biochem J , vol.291 , pp. 51-55
    • Ferguson, M.A.J.1    Murray, P.2    Rutherford, H.3    McConville, M.J.4
  • 8
    • 0016809286 scopus 로고
    • Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei
    • Cross GA. Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. Parasitology 1975; 71: 393-417.
    • (1975) Parasitology , vol.71 , pp. 393-417
    • Cross, G.A.1
  • 9
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville MJ, Ferguson MAJ. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem J 1993; 294: 305-324.
    • (1993) Biochem J , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.J.2
  • 10
    • 0032029245 scopus 로고    scopus 로고
    • Expression and function of surface proteins in Trypanosoma brucei
    • Pays E, Nolan DP. Expression and function of surface proteins in Trypanosoma brucei. Mol Biochem Parasitol 1998; 91: 3-36.
    • (1998) Mol Biochem Parasitol , vol.91 , pp. 3-36
    • Pays, E.1    Nolan, D.P.2
  • 11
    • 0024441847 scopus 로고
    • The procyclic acidic repetitive proteins of Trypanosoma brucei. Purification and post-translational modification
    • Clayton CE, Mowatt MR. The procyclic acidic repetitive proteins of Trypanosoma brucei. Purification and post-translational modification. J Biol Chem 1989; 264: 15088-15093.
    • (1989) J Biol Chem , vol.264 , pp. 15088-15093
    • Clayton, C.E.1    Mowatt, M.R.2
  • 12
    • 0027405470 scopus 로고
    • A simple purification of procyclic acidic repetitive protein and demonstration of a sialylated glycosyl-phosphatidylinositol membrane anchor
    • Ferguson MA, Murray P, Rutherford H, McConville MJ. A simple purification of procyclic acidic repetitive protein and demonstration of a sialylated glycosyl-phosphatidylinositol membrane anchor. Biochem J 1993; 291(Pt 1): 51-55.
    • (1993) Biochem J , vol.291 , Issue.PART 1 , pp. 51-55
    • Ferguson, M.A.1    Murray, P.2    Rutherford, H.3    McConville, M.J.4
  • 13
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson MA. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J Cell Sci 1999; 112: 2799-2809.
    • (1999) J Cell Sci , vol.112 , pp. 2799-2809
    • Ferguson, M.A.1
  • 14
    • 0034091742 scopus 로고    scopus 로고
    • Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids
    • McConville MJ, Menon AK. Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids. Mol Membr Biol 2000; 17: 1-16.
    • (2000) Mol Membr Biol , vol.17 , pp. 1-16
    • McConville, M.J.1    Menon, A.K.2
  • 15
    • 0028981209 scopus 로고
    • How glycosylphosphatidylinositol-anchored membrane proteins are made
    • Udenfriend S, Kodukula K. How glycosylphosphatidylinositol-anchored membrane proteins are made. Annu Rev Biochem 1995; 64: 563-591.
    • (1995) Annu Rev Biochem , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 16
    • 0032996466 scopus 로고    scopus 로고
    • Biosynthesis of glycosylphosphatidylinositols in mammalian and unicellular microbes
    • Tiede A, Bastisch I, Schubert J, Orlean P, Schmidt RE. Biosynthesis of glycosylphosphatidylinositols in mammalian and unicellular microbes. Biol Chem 1999; 380: 503-523.
    • (1999) Biol Chem , vol.380 , pp. 503-523
    • Tiede, A.1    Bastisch, I.2    Schubert, J.3    Orlean, P.4    Schmidt, R.E.5
  • 17
    • 0036547672 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol (GPI)-anchored proteins
    • Ikezawa H. Glycosylphosphatidylinositol (GPI)-anchored proteins. Biol Pharm Bull 2002; 25: 409-417.
    • (2002) Biol Pharm Bull , vol.25 , pp. 409-417
    • Ikezawa, H.1
  • 18
    • 0032481318 scopus 로고    scopus 로고
    • The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
    • Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T. The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J 1998; 17: 877-885.
    • (1998) EMBO J , vol.17 , pp. 877-885
    • Watanabe, R.1    Inoue, N.2    Westfall, B.3    Taron, C.H.4    Orlean, P.5    Takeda, J.6    Kinoshita, T.7
  • 20
    • 27644514673 scopus 로고    scopus 로고
    • The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component
    • Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T. The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell 2005; 16: 5236-5246.
    • (2005) Mol Biol Cell , vol.16 , pp. 5236-5246
    • Murakami, Y.1    Siripanyaphinyo, U.2    Hong, Y.3    Tashima, Y.4    Maeda, Y.5    Kinoshita, T.6
  • 21
    • 0028046590 scopus 로고
    • Molecular cloning of murine Pig-a, a gene for GPI-anchor biosynthesis, and demonstration of interspecies conservation of its structure, function and gene locus
    • Kawagoe K, Takeda J, Endo Y, Kinoshita T. Molecular cloning of murine Pig-a, a gene for GPI-anchor biosynthesis, and demonstration of interspecies conservation of its structure, function and gene locus. Genomics 1994; 23: 566-574.
    • (1994) Genomics , vol.23 , pp. 566-574
    • Kawagoe, K.1    Takeda, J.2    Endo, Y.3    Kinoshita, T.4
  • 23
    • 0037147257 scopus 로고    scopus 로고
    • Cloning of Trypanosoma brucei and Leishmania major genes encoding the GlcNAc-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis that is essential to the African sleeping sickness parasite
    • Chang T, Milne KG, Guther ML, Smith TK, Ferguson MA. Cloning of Trypanosoma brucei and Leishmania major genes encoding the GlcNAc-phosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis that is essential to the African sleeping sickness parasite. J Biol Chem 2002; 277: 50176-50182.
    • (2002) J Biol Chem , vol.277 , pp. 50176-50182
    • Chang, T.1    Milne, K.G.2    Guther, M.L.3    Smith, T.K.4    Ferguson, M.A.5
  • 24
    • 20744458018 scopus 로고    scopus 로고
    • The N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzyme
    • Urbaniak MD, Crossman A, Chang T, Smith TK, van Aalten DM, Ferguson MA. The N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzyme. J Biol Chem 2005; 280: 22831-22838.
    • (2005) J Biol Chem , vol.280 , pp. 22831-22838
    • Urbaniak, M.D.1    Crossman, A.2    Chang, T.3    Smith, T.K.4    van Aalten, D.M.5    Ferguson, M.A.6
  • 25
    • 0032932124 scopus 로고    scopus 로고
    • Differences between the trypanosomal and human GlcNAc-PI de-N-acetylases of glycosylphosphatidylinositol membrane anchor biosynthesis
    • Sharma DK, Smith TK, Weller CT, Crossman A, Brimacombe JS, Ferguson MAJ. Differences between the trypanosomal and human GlcNAc-PI de-N-acetylases of glycosylphosphatidylinositol membrane anchor biosynthesis. Glycobiology 1999; 9: 415-422.
    • (1999) Glycobiology , vol.9 , pp. 415-422
    • Sharma, D.K.1    Smith, T.K.2    Weller, C.T.3    Crossman, A.4    Brimacombe, J.S.5    Ferguson, M.A.J.6
  • 26
    • 0035796558 scopus 로고    scopus 로고
    • Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors
    • Smith TK, Crossman A, Borissow CN, Paterson MJ, Dix A, Brimacombe JS, Ferguson MA. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. EMBO J 2001; 20: 3322-3332.
    • (2001) EMBO J , vol.20 , pp. 3322-3332
    • Smith, T.K.1    Crossman, A.2    Borissow, C.N.3    Paterson, M.J.4    Dix, A.5    Brimacombe, J.S.6    Ferguson, M.A.7
  • 29
    • 0029043758 scopus 로고
    • The role of inositol acylation and inositol deacylation in GPI biosynthesis in Trypanosoma brucei
    • Güther ML, Ferguson MA. The role of inositol acylation and inositol deacylation in GPI biosynthesis in Trypanosoma brucei. EMBO J 1995; 14: 3080-3093.
    • (1995) EMBO J , vol.14 , pp. 3080-3093
    • Güther, M.L.1    Ferguson, M.A.2
  • 30
    • 58149164667 scopus 로고    scopus 로고
    • Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. ACS
    • Urbaniak MD, Yashunsky DV, Crossman A, Nikolaev AV, Ferguson MA. Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. ACS Chem Biol 2008; 3: 625-634.
    • (2008) Chem Biol , vol.3 , pp. 625-634
    • Urbaniak, M.D.1    Yashunsky, D.V.2    Crossman, A.3    Nikolaev, A.V.4    Ferguson, M.A.5
  • 31
    • 0028358821 scopus 로고
    • The effects of phenylmethylsulfonyl fluoride on inositol-acylation and fatty acid remodeling in African trypanosomes
    • Güther ML, Masterson WJ, Ferguson MA. The effects of phenylmethylsulfonyl fluoride on inositol-acylation and fatty acid remodeling in African trypanosomes. J Biol Chem 1994; 269: 18694-18701.
    • (1994) J Biol Chem , vol.269 , pp. 18694-18701
    • Güther, M.L.1    Masterson, W.J.2    Ferguson, M.A.3
  • 32
    • 0029043758 scopus 로고
    • The role of inositol acylation and inositol deacylation in GPI biosynthesis in Trypanosoma brucei
    • Guther ML, Ferguson MA. The role of inositol acylation and inositol deacylation in GPI biosynthesis in Trypanosoma brucei. EMBO J 1995; 14: 3080-3093.
    • (1995) EMBO J , vol.14 , pp. 3080-3093
    • Guther, M.L.1    Ferguson, M.A.2
  • 33
    • 0028373211 scopus 로고
    • The role of glycolipid C in the GPI biosynthetic pathway in Trypanosoma brucei blood-stream forms
    • Güther ML, Masterson WJ, Ferguson MA. The role of glycolipid C in the GPI biosynthetic pathway in Trypanosoma brucei blood-stream forms. Braz J Med Biol Res 1994; 27: 121-126.
    • (1994) Braz J Med Biol Res , vol.27 , pp. 121-126
    • Güther, M.L.1    Masterson, W.J.2    Ferguson, M.A.3
  • 34
    • 47149083740 scopus 로고    scopus 로고
    • Yeast ARV1 is required for efficient delivery of an early GPI intermediate to the first mannosyltransferase during GPI assembly and controls lipid flow from the endoplasmic reticulum
    • Kajiwara K, Watanabe R, Pichler H, Ihara K, Murakami S, Riezman H, Funato K. Yeast ARV1 is required for efficient delivery of an early GPI intermediate to the first mannosyltransferase during GPI assembly and controls lipid flow from the endoplasmic reticulum. Mol Biol Cell 2008; 19: 2069-2082.
    • (2008) Mol Biol Cell , vol.19 , pp. 2069-2082
    • Kajiwara, K.1    Watanabe, R.2    Pichler, H.3    Ihara, K.4    Murakami, S.5    Riezman, H.6    Funato, K.7
  • 35
    • 0035863209 scopus 로고    scopus 로고
    • PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER
    • Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T. PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J 2001; 20: 250-261.
    • (2001) EMBO J , vol.20 , pp. 250-261
    • Maeda, Y.1    Watanabe, R.2    Harris, C.L.3    Hong, Y.4    Ohishi, K.5    Kinoshita, K.6    Kinoshita, T.7
  • 36
    • 14844325758 scopus 로고    scopus 로고
    • Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I
    • Ashida H, Hong Y, Murakami Y, Shishioh N, Sugimoto N, Kim YU, Maeda Y, Kinoshita T. Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I. Mol Biol Cell 2005; 16: 1439-1448.
    • (2005) Mol Biol Cell , vol.16 , pp. 1439-1448
    • Ashida, H.1    Hong, Y.2    Murakami, Y.3    Shishioh, N.4    Sugimoto, N.5    Kim, Y.U.6    Maeda, Y.7    Kinoshita, T.8
  • 37
    • 0033229883 scopus 로고    scopus 로고
    • Selective inhibitors of the glycosylphosphatidylinositol biosynthetic pathway of Trypanosoma brucei
    • Smith TK, Sharma DK, Crossman A, Brimacombe JS, Ferguson MA. Selective inhibitors of the glycosylphosphatidylinositol biosynthetic pathway of Trypanosoma brucei. EMBO J 1999; 18: 5922-5930.
    • (1999) EMBO J , vol.18 , pp. 5922-5930
    • Smith, T.K.1    Sharma, D.K.2    Crossman, A.3    Brimacombe, J.S.4    Ferguson, M.A.5
  • 39
    • 0029782178 scopus 로고    scopus 로고
    • Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T. PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J 1996; 15: 4254-4261.
    • Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T. PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J 1996; 15: 4254-4261.
  • 41
    • 0034617298 scopus 로고    scopus 로고
    • Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the third mannose in glycosylphosphatidylinositol
    • Hong Y, Maeda Y, Watanabe R, Inoue N, Ohishi K, Kinoshita T. Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the third mannose in glycosylphosphatidylinositol. J Biol Chem 2000; 275: 20911-20919.
    • (2000) J Biol Chem , vol.275 , pp. 20911-20919
    • Hong, Y.1    Maeda, Y.2    Watanabe, R.3    Inoue, N.4    Ohishi, K.5    Kinoshita, T.6
  • 42
    • 0033521023 scopus 로고    scopus 로고
    • Hong Y, Maeda Y, Watanabe R, Ohishi K, Mishkind M, Riezman H, Kinoshita T. Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol. J Biol Chem 1999; 274: 35099-35106.
    • Hong Y, Maeda Y, Watanabe R, Ohishi K, Mishkind M, Riezman H, Kinoshita T. Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring phosphoethanolamine to the first mannose of the glycosylphosphatidylinositol. J Biol Chem 1999; 274: 35099-35106.
  • 43
    • 15744391942 scopus 로고    scopus 로고
    • GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol
    • Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T. GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem 2005; 280: 9728-9734.
    • (2005) J Biol Chem , vol.280 , pp. 9728-9734
    • Shishioh, N.1    Hong, Y.2    Ohishi, K.3    Ashida, H.4    Maeda, Y.5    Kinoshita, T.6
  • 44
    • 0025359435 scopus 로고
    • Cell-free synthesis of glycosyl-phosphatidylinositol precursors for the glycolipid membrane anchor of Trypanosoma brucei variant surface glycoproteins. Structural characterization of putative biosynthetic intermediates
    • Menon AK, Schwarz RT, Mayor S, Cross GA. Cell-free synthesis of glycosyl-phosphatidylinositol precursors for the glycolipid membrane anchor of Trypanosoma brucei variant surface glycoproteins. Structural characterization of putative biosynthetic intermediates. J Biol Chem 1990; 265: 9033-9042.
    • (1990) J Biol Chem , vol.265 , pp. 9033-9042
    • Menon, A.K.1    Schwarz, R.T.2    Mayor, S.3    Cross, G.A.4
  • 45
    • 1842790673 scopus 로고    scopus 로고
    • Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p
    • Tanaka S, Maeda Y, Tashima Y, Kinoshita T. Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. J Biol Chem 2004; 279: 14256-14263.
    • (2004) J Biol Chem , vol.279 , pp. 14256-14263
    • Tanaka, S.1    Maeda, Y.2    Tashima, Y.3    Kinoshita, T.4
  • 46
    • 0035801644 scopus 로고    scopus 로고
    • Purification, cloning and characterization of a GPI inositol deacylase from Trypanosoma brucei
    • Guther ML, Leal S, Morrice NA, Cross GA, Ferguson MA. Purification, cloning and characterization of a GPI inositol deacylase from Trypanosoma brucei. EMBO J 2001; 20: 4923-4934.
    • (2001) EMBO J , vol.20 , pp. 4923-4934
    • Guther, M.L.1    Leal, S.2    Morrice, N.A.3    Cross, G.A.4    Ferguson, M.A.5
  • 47
    • 0348111212 scopus 로고    scopus 로고
    • Deletion of the GPIdeAc gene alters the location and fate of glycosylphosphatidylinositol precursors in Trypanosoma brucei
    • Guther ML, Prescott AR, Ferguson MA. Deletion of the GPIdeAc gene alters the location and fate of glycosylphosphatidylinositol precursors in Trypanosoma brucei. Biochemistry 2003; 42: 14532-14540.
    • (2003) Biochemistry , vol.42 , pp. 14532-14540
    • Guther, M.L.1    Prescott, A.R.2    Ferguson, M.A.3
  • 48
    • 33744953579 scopus 로고    scopus 로고
    • Removal or maintenance of inositol-linked acyl chain in GPI is critical in trypanosome life cycle
    • Hong Y, Nagamune K, Morita YS, Nakatani F, Ashida H, Maeda Y, Kinoshita T. Removal or maintenance of inositol-linked acyl chain in GPI is critical in trypanosome life cycle. J Biol Chem 2006; 281: 11595-11602.
    • (2006) J Biol Chem , vol.281 , pp. 11595-11602
    • Hong, Y.1    Nagamune, K.2    Morita, Y.S.3    Nakatani, F.4    Ashida, H.5    Maeda, Y.6    Kinoshita, T.7
  • 49
    • 0029981161 scopus 로고    scopus 로고
    • Acylation of glucosaminyl phosphatidylinositol revisited
    • Doerrler WT, Ye J, Falck JR, Lehrman MA. Acylation of glucosaminyl phosphatidylinositol revisited. J Biol Chem 1996; 271: 27031-27038.
    • (1996) J Biol Chem , vol.271 , pp. 27031-27038
    • Doerrler, W.T.1    Ye, J.2    Falck, J.R.3    Lehrman, M.A.4
  • 50
    • 0028358821 scopus 로고
    • The effects of phenylmethylsulfonyl fluoride on inositol-acylation and fatty acid remodeling in African trypanosomes
    • Guther ML, Masterson WJ, Ferguson MA. The effects of phenylmethylsulfonyl fluoride on inositol-acylation and fatty acid remodeling in African trypanosomes. J Biol Chem 1994; 269: 18694-18701.
    • (1994) J Biol Chem , vol.269 , pp. 18694-18701
    • Guther, M.L.1    Masterson, W.J.2    Ferguson, M.A.3
  • 51
    • 0028373211 scopus 로고
    • The role of glycolipid C n the GPI biosynthetic pathway in Trypanosoma brucei bloodstream forms
    • Guther ML, Masterson WJ, Ferguson MA. The role of glycolipid C n the GPI biosynthetic pathway in Trypanosoma brucei bloodstream forms. Braz J Med Biol Res 1994; 27: 121-126.
    • (1994) Braz J Med Biol Res , vol.27 , pp. 121-126
    • Guther, M.L.1    Masterson, W.J.2    Ferguson, M.A.3
  • 53
    • 40749160804 scopus 로고    scopus 로고
    • Lipid remodeling of GPI-anchored proteins and its function
    • Fujita M, Jigami Y. Lipid remodeling of GPI-anchored proteins and its function. Biochim Biophys Acta 2008; 1780: 410-420.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 410-420
    • Fujita, M.1    Jigami, Y.2
  • 54
    • 33644853935 scopus 로고    scopus 로고
    • PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
    • Tashima Y, Taguchi R, Murata C, Ashida H, Kinoshita T, Maeda Y. PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins. Mol Biol Cell 2006; 17: 1410-1420.
    • (2006) Mol Biol Cell , vol.17 , pp. 1410-1420
    • Tashima, Y.1    Taguchi, R.2    Murata, C.3    Ashida, H.4    Kinoshita, T.5    Maeda, Y.6
  • 55
    • 0035421238 scopus 로고    scopus 로고
    • PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
    • Ohishi K, Inoue N, Kinoshita T. PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J 2001; 20: 4088-4098.
    • (2001) EMBO J , vol.20 , pp. 4088-4098
    • Ohishi, K.1    Inoue, N.2    Kinoshita, T.3
  • 56
    • 0038247909 scopus 로고    scopus 로고
    • Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins
    • Hong Y, Ohishi K, Kang JY, Tanaka S, Inoue N, Nishimura J, Maeda Y, Kinoshita T. Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol Biol Cell 2003; 14: 1780-1789.
    • (2003) Mol Biol Cell , vol.14 , pp. 1780-1789
    • Hong, Y.1    Ohishi, K.2    Kang, J.Y.3    Tanaka, S.4    Inoue, N.5    Nishimura, J.6    Maeda, Y.7    Kinoshita, T.8
  • 57
    • 0141814703 scopus 로고    scopus 로고
    • GPI transamidase of Trypanosoma brucei has two previously uncharacterized (trypanosomatid transamidase 1 and 2) and three common subunits
    • Nagamune K, Ohishi K, Ashida H, Hong Y, Hino J, Kangawa K, Inoue N, Maeda Y, Kinoshita T. GPI transamidase of Trypanosoma brucei has two previously uncharacterized (trypanosomatid transamidase 1 and 2) and three common subunits. Proc Natl Acad Sci USA 2003; 100: 10682-10687.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10682-10687
    • Nagamune, K.1    Ohishi, K.2    Ashida, H.3    Hong, Y.4    Hino, J.5    Kangawa, K.6    Inoue, N.7    Maeda, Y.8    Kinoshita, T.9
  • 58
    • 0037853150 scopus 로고    scopus 로고
    • Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge
    • Ohishi K, Nagamune K, Maeda Y, Kinoshita T. Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J Biol Chem 2003; 278: 13959-13967.
    • (2003) J Biol Chem , vol.278 , pp. 13959-13967
    • Ohishi, K.1    Nagamune, K.2    Maeda, Y.3    Kinoshita, T.4
  • 59
    • 0034108088 scopus 로고    scopus 로고
    • Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins
    • Ohishi K, Inoue N, Maeda Y, Takeda J, Riezman H, Kinoshita T. Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. Mol Biol Cell 2000; 11: 1523-1533.
    • (2000) Mol Biol Cell , vol.11 , pp. 1523-1533
    • Ohishi, K.1    Inoue, N.2    Maeda, Y.3    Takeda, J.4    Riezman, H.5    Kinoshita, T.6
  • 60
    • 0034724159 scopus 로고    scopus 로고
    • Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins
    • Meyer U, Benghezal M, Imhof I, Conzelmann A. Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins. Biochemistry 2000; 39: 3461-3471.
    • (2000) Biochemistry , vol.39 , pp. 3461-3471
    • Meyer, U.1    Benghezal, M.2    Imhof, I.3    Conzelmann, A.4
  • 61
    • 0035003079 scopus 로고    scopus 로고
    • Endoplasmic reticulum proteins involved in glycosylphosphatidylinositol-anchor attachment: Photocrosslinking studies in a cell-free system
    • Vidugiriene J, Vainauskas S, Johnson AE, Menon AK. Endoplasmic reticulum proteins involved in glycosylphosphatidylinositol-anchor attachment: photocrosslinking studies in a cell-free system. Eur J Biochem 2001; 268: 2290-2300.
    • (2001) Eur J Biochem , vol.268 , pp. 2290-2300
    • Vidugiriene, J.1    Vainauskas, S.2    Johnson, A.E.3    Menon, A.K.4
  • 62
    • 0035844125 scopus 로고    scopus 로고
    • Early events in glycosylphosphatidylinositol anchor addition: Substrate proteins associates with the transamidase subunit Gpi8p
    • Spurway TD, Dalley JA, High S, Bulleid NJ. Early events in glycosylphosphatidylinositol anchor addition: substrate proteins associates with the transamidase subunit Gpi8p. J Biol Chem 2001; 276: 15975-15982.
    • (2001) J Biol Chem , vol.276 , pp. 15975-15982
    • Spurway, T.D.1    Dalley, J.A.2    High, S.3    Bulleid, N.J.4
  • 63
    • 0037096165 scopus 로고    scopus 로고
    • GPI anchor transamidase of Trypanosoma brucei: In vitro assay of the recombinant protein and VSG anchor exchange
    • Kang X, Szallies A, Rawer M, Echner H, Duszenko M. GPI anchor transamidase of Trypanosoma brucei: in vitro assay of the recombinant protein and VSG anchor exchange. J Cell Sci 2002; 115: 2529-2539.
    • (2002) J Cell Sci , vol.115 , pp. 2529-2539
    • Kang, X.1    Szallies, A.2    Rawer, M.3    Echner, H.4    Duszenko, M.5
  • 64
    • 0037346805 scopus 로고    scopus 로고
    • Essential roles for GPI-anchored proteins in African trypanosomes revealed using mutants deficient in GPI8
    • Lillico S, Field MC, Blundell P, Coombs GH, Mottram JC. Essential roles for GPI-anchored proteins in African trypanosomes revealed using mutants deficient in GPI8. Mol Biol Cell 2003; 14: 1182-1194.
    • (2003) Mol Biol Cell , vol.14 , pp. 1182-1194
    • Lillico, S.1    Field, M.C.2    Blundell, P.3    Coombs, G.H.4    Mottram, J.C.5
  • 65
    • 0029827249 scopus 로고    scopus 로고
    • Yeast Gpi8p is essential for GPI anchor attachment onto proteins
    • Benghezal M, Benachour A, Rusconi S, Aebi M, Conzelmann A. Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J 1996; 15: 6575-6583.
    • (1996) EMBO J , vol.15 , pp. 6575-6583
    • Benghezal, M.1    Benachour, A.2    Rusconi, S.3    Aebi, M.4    Conzelmann, A.5
  • 67
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low MG. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim Biophys Acta 1989; 988: 427-454.
    • (1989) Biochim Biophys Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 68
    • 0028802581 scopus 로고
    • Defective glycosyl phosphatidylinositol anchor synthesis and paroxysmal nocturnal hemoglobinuria
    • Kinoshita T, Inoue N, Takeda J. Defective glycosyl phosphatidylinositol anchor synthesis and paroxysmal nocturnal hemoglobinuria. Adv Immunol 1995; 60: 57-103.
    • (1995) Adv Immunol , vol.60 , pp. 57-103
    • Kinoshita, T.1    Inoue, N.2    Takeda, J.3
  • 69
    • 0028327126 scopus 로고
    • Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa
    • Moran P, Caras IW. Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa. J Cell Biol 1994; 125: 333-343.
    • (1994) J Cell Biol , vol.125 , pp. 333-343
    • Moran, P.1    Caras, I.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.