메뉴 건너뛰기




Volumn 48, Issue 3, 2009, Pages 191-202

Inositols and phosphoinositides in Tetrahymena

Author keywords

Inositol isomers; Myo inositol; Phosphatidyl scyllo inositol; Phosphoinositide signaling; Phosphoinositides; Scyllo inositol; Tetrahymena

Indexed keywords

EUKARYOTA; PROTISTA; TETRAHYMENA;

EID: 75349109667     PISSN: 00651583     EISSN: 16890027     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (5)

References (76)
  • 1
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • Berridge M. J. (1993) Inositol trisphosphate and calcium signaling. Nature 361: 315-325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 2
    • 0027331022 scopus 로고
    • Myo-Inositol transport and metabolism in fetal-bovine aortic endothelial cells
    • Berry G. T., Johanson R. A., Prantner J. E., States B., Yandrasitz J. R. (1993) myo-Inositol transport and metabolism in fetal-bovine aortic endothelial cells. Biochem. J. 295: 863-869
    • (1993) Biochem. J. , vol.295 , pp. 863-869
    • Berry, G.T.1    Johanson, R.A.2    Prantner, J.E.3    States, B.4    Yandrasitz, J.R.5
  • 3
    • 0022495752 scopus 로고
    • Active transport of myo-inositol in rat pancreatic islets
    • Biden T. J., Wollheim C. B. (1986) Active transport of myo-inositol in rat pancreatic islets. Biochem. J. 295: 889-893
    • (1986) Biochem. J. , vol.295 , pp. 889-893
    • Biden, T.J.1    Wollheim, C.B.2
  • 5
    • 0002899373 scopus 로고
    • History, taxonomy, ecology, and evolution of species of Tetrahymena
    • (Ed. A. M. Elliott), Dowden, Hutchinson & Ross Inc., Stroudsburg, PA
    • Corliss J. O. (1973) History, taxonomy, ecology, and evolution of species of Tetrahymena. In: Biology of Tetrahymena, (Ed. A. M. Elliott), Dowden, Hutchinson & Ross Inc., Stroudsburg, PA, 1-55
    • (1973) Biology of Tetrahymena , pp. 1-55
    • Corliss, J.O.1
  • 7
    • 46749124321 scopus 로고    scopus 로고
    • Deficiency in lysosomal enzyme secretion is associated with up-regulation of phosphatidylinositol 4-phosphate in Tetrahymena
    • Deli D., Leondaritis G., Tiedtke A., Galanopoulou D. (2008) Deficiency in lysosomal enzyme secretion is associated with up-regulation of phosphatidylinositol 4-phosphate in Tetrahymena. J. Eukaryot. Microbiol. 55: 343-350
    • (2008) J. Eukaryot. Microbiol. , vol.55 , pp. 343-350
    • Deli, D.1    Leondaritis, G.2    Tiedtke, A.3    Galanopoulou, D.4
  • 9
    • 0035172107 scopus 로고    scopus 로고
    • Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidyl 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology
    • Foti M., Audhya A., Emr S. D. (2001) Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidyl 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol. Biol. Cell 12: 2396-2411
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2396-2411
    • Foti, M.1    Audhya, A.2    Emr, S.D.3
  • 10
    • 0026725101 scopus 로고
    • Metabolism of inositol phosphates in the protozoan Paramecium. Characterization of a novel inositol-hexakisphosphate-dephosphorylating enzyme
    • Freund W. D., Mayr G. W., Tietz C., Schultz J. E. (1992) Metabolism of inositol phosphates in the protozoan Paramecium. Characterization of a novel inositol-hexakisphosphate-dephosphorylating enzyme. Eur. J. Biochem. 207: 359-367
    • (1992) Eur. J. Biochem. , vol.207 , pp. 359-367
    • Freund, W.D.1    Mayr, G.W.2    Tietz, C.3    Schultz, J.E.4
  • 12
    • 0023664866 scopus 로고
    • Phytic acid. A natural antioxidant
    • Graf E., Empson K.L., Eaton J.W. (1987) Phytic acid. A natural antioxidant. J. Biol. Chem. 262: 11647-11650
    • (1987) J. Biol. Chem. , vol.262 , pp. 11647-11650
    • Graf, E.1    Empson, K.L.2    Eaton, J.W.3
  • 13
    • 0020430520 scopus 로고
    • Inositol-epimerase inosose reductase from bovine brain
    • Hipps P. P., Ackermann K. E., Sherman W. R. (1982) Inositol-epimerase inosose reductase from bovine brain. Meth. Enzymol. 89: 593-598
    • (1982) Meth. Enzymol. , vol.89 , pp. 593-598
    • Hipps, P.P.1    Ackermann, K.E.2    Sherman, W.R.3
  • 14
    • 0017389874 scopus 로고
    • Interconversion of myo-and scyllo-inositol with simultaneous formation of neoinositol by an NADP-dependent epimerase from bovine brain
    • Hipps P. P., Holland W. H., Sherman W. R. (1977) Interconversion of myo-and scyllo-inositol with simultaneous formation of neoinositol by an NADP-dependent epimerase from bovine brain. Biochem. Biophys. Res. Commun. 77: 340-346
    • (1977) Biochem. Biophys. Res. Commun. , vol.77 , pp. 340-346
    • Hipps, P.P.1    Holland, W.H.2    Sherman, W.R.3
  • 15
    • 0015916311 scopus 로고
    • epimerase and inosose:NAD(P)H reductase from the fat body of the American cockroach, Periplaneta americanum L
    • epimerase and inosose:NAD(P)H reductase from the fat body of the American cockroach, Periplaneta americanum L. Biochemistry 12: 4705-4712
    • (1973) Biochemistry , vol.12 , pp. 4705-4712
    • Hipps, P.P.1    Sehgal, R.K.2    Holland, W.H.3    Sherman, W.R.4
  • 16
    • 0028926207 scopus 로고
    • Temperature-induced alteration of inositolphosphorylceramides in the putative glycosylated lipid precursors of Tetrahymena mimbres glycosylphosphatidylinositol-anchored proteins
    • Hung C. Y., Ko Y. G., Thompson G. A. Jr. (1995) Temperature-induced alteration of inositolphosphorylceramides in the putative glycosylated lipid precursors of Tetrahymena mimbres glycosylphosphatidylinositol-anchored proteins. Biochem. J. 307: 107-113
    • (1995) Biochem. J. , vol.307 , pp. 107-113
    • Hung, C.Y.1    Ko, Y.G.2    Thompson Jr., G.A.3
  • 17
    • 0033953431 scopus 로고    scopus 로고
    • Uptake and incorporation of myo-inositol by bovine preimplantation embryos from two-cell to early blastocyte stages
    • Hynes A. C., Streenan J. M., Kane M. T. (2000) Uptake and incorporation of myo-inositol by bovine preimplantation embryos from two-cell to early blastocyte stages. Mol. Reprod. Dev. 55: 265-269
    • (2000) Mol. Reprod. Dev. , vol.55 , pp. 265-269
    • Hynes, A.C.1    Streenan, J.M.2    Kane, M.T.3
  • 21
    • 75349106100 scopus 로고    scopus 로고
    • Uptake of inositol isomers by Tetrahymena
    • Kersting M. C., Ryals P. E. (2009) Uptake of inositol isomers by Tetrahymena. Florida Scient. 72: 1-10
    • (2009) Florida Scient , vol.72 , pp. 1-10
    • Kersting, M.C.1    Ryals, P.E.2
  • 23
    • 0026948470 scopus 로고
    • Immobilization antigens from Tetrahymena thermophila are glycosyl-phosphatidylinositollinked proteins
    • Ko Y. G., Thompson G. A. Jr. (1992) Immobilization antigens from Tetrahymena thermophila are glycosyl-phosphatidylinositollinked proteins. J. Protozool. 39: 719-723
    • (1992) J. Protozool. , vol.39 , pp. 719-723
    • Ko, Y.G.1    Thompson Jr., G.A.2
  • 24
    • 0028913978 scopus 로고
    • Temperature regulation of the Tetrahymena mimbres glycosylphosphatidylinositolanchored protein lipid composition
    • Ko Y. G., Hung C. Y., Thompson G. A. Jr. (1995) Temperature regulation of the Tetrahymena mimbres glycosylphosphatidylinositolanchored protein lipid composition. Biochem. J. 307: 115-121
    • (1995) Biochem. J. , vol.307 , pp. 115-121
    • Ko, Y.G.1    Hung, C.Y.2    Thompson Jr., G.A.3
  • 25
    • 0028869863 scopus 로고
    • Purification of glycosylphosphatidylinositol-anchored proteins by modified Triton X-114 partitioning and preparative gel electrophoresis
    • Ko Y. G., Thompson G. A. Jr. (1995) Purification of glycosylphosphatidylinositol-anchored proteins by modified Triton X-114 partitioning and preparative gel electrophoresis. Anal. Biochem. 224: 166-172
    • (1995) Anal. Biochem. , vol.224 , pp. 166-172
    • Ko, Y.G.1    Thompson Jr., G.A.2
  • 26
    • 0025145861 scopus 로고
    • Involvement of the phosphoinositol (PI) system in the mechanism of hormonal imprinting
    • Kovács P., Csaba G. (1990) Involvement of the phosphoinositol (PI) system in the mechanism of hormonal imprinting. Biochem. Biophys. Res. Commun. 170: 119-126
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 119-126
    • Kovács, P.1    Csaba, G.2
  • 27
    • 0028618630 scopus 로고
    • Effect of insulin on the incorporation of 3H-inositol into the inositol phospholipids (PI, PIP, PIP2) and glycosyl-phosphatidylinositols (GPIs) of Tetrahymena pyriformis
    • Kovács P., Csaba G. (1994) Effect of insulin on the incorporation of 3H-inositol into the inositol phospholipids (PI, PIP, PIP2) and glycosyl-phosphatidylinositols (GPIs) of Tetrahymena pyriformis. Biosci. Rep. 14: 215-219
    • (1994) Biosci. Rep. , vol.14 , pp. 215-219
    • Kovács, P.1    Csaba, G.2
  • 28
    • 0028936584 scopus 로고
    • Effects of choline and ethanolamine on the synthesis and breakdown of the inositol phospholipid (PI) system in Tetrahymena
    • Kovács P., Csaba G. (1995a) Effects of choline and ethanolamine on the synthesis and breakdown of the inositol phospholipid (PI) system in Tetrahymena. Cell Biochem. Funct. 13: 61-67
    • (1995) Cell Biochem. Funct. , vol.13 , pp. 61-67
    • Kovács, P.1    Csaba, G.2
  • 29
    • 0029062693 scopus 로고
    • Effect of phorbol 12-myristate 13-acetate (PMA) on the phosphoinositol (PI) system in Tetrahymena. Study of the 32P-incorporation and breakdown of phospholipids
    • Kovács P., Csaba G. (1995b) Effect of phorbol 12-myristate 13-acetate (PMA) on the phosphoinositol (PI) system in Tetrahymena. Study of the 32P-incorporation and breakdown of phospholipids. Cell Biochem. Funct. 13: 85-89
    • (1995) Cell Biochem. Funct. , vol.13 , pp. 85-89
    • Kovács, P.1    Csaba, G.2
  • 30
    • 0030346434 scopus 로고    scopus 로고
    • Effects of local anesthetics and phenothiazines on 32P-incorporation into the inositol phospholipids and glycosyl phosphatidylinositol of Tetrahymena pyriformis GL
    • Kovács P., Csaba G. (1996a) Effects of local anesthetics and phenothiazines on 32P-incorporation into the inositol phospholipids and glycosyl phosphatidylinositol of Tetrahymena pyriformis GL. Microbios 87: 149-159
    • (1996) Microbios , vol.87 , pp. 149-159
    • Kovács, P.1    Csaba, G.2
  • 31
    • 0029682381 scopus 로고    scopus 로고
    • Effect of neomycin on glycosyl-phosphatidylinositol and phosphatidylinositol system of Tetrahymena
    • Kovács P., Csaba G. (1996b) Effect of neomycin on glycosyl-phosphatidylinositol and phosphatidylinositol system of Tetrahymena. Microbios 85: 7-18
    • (1996) Microbios , vol.85 , pp. 7-18
    • Kovács, P.1    Csaba, G.2
  • 32
    • 0343924403 scopus 로고    scopus 로고
    • Indomethacin alters phospholipid and arachidonate metabolism in Tetrahymena pyriformis
    • Kovács P., Csaba G. (1997a) Indomethacin alters phospholipid and arachidonate metabolism in Tetrahymena pyriformis. Comp. Biochem. Physiol. 117C: 311-315
    • (1997) Comp. Biochem. Physiol. , vol.117 C , pp. 311-315
    • Kovács, P.1    Csaba, G.2
  • 33
    • 0030625957 scopus 로고    scopus 로고
    • Effects of the amino sugars, glucosamine, mannosamine, or the fluorinated derivative 2-deoxy-fluoroglucose on the phosphatidylinositol and glycosyl phosphatidyl inositol systems of Tetrahymena
    • Kovács P., Csaba G. (1997b) Effects of the amino sugars, glucosamine, mannosamine, or the fluorinated derivative 2-deoxy-fluoroglucose on the phosphatidylinositol and glycosyl phosphatidyl inositol systems of Tetrahymena. Microbios 89: 91-104
    • (1997) Microbios , vol.89 , pp. 91-104
    • Kovács, P.1    Csaba, G.2
  • 34
    • 0343052594 scopus 로고    scopus 로고
    • Effect of 3-amino-1-propanol on the phosphatidylinositol (PI) and glycosyl phosphatidylinositol (GPI) systems of Tetrahymena
    • Kovács P., Köhidai L., Csaba G. (1997) Effect of 3-amino-1-propanol on the phosphatidylinositol (PI) and glycosyl phosphatidylinositol (GPI) systems of Tetrahymena. Comp. Biochem. Physiol. C 118: 83-87
    • (1997) Comp. Biochem. Physiol. C , vol.118 , pp. 83-87
    • Kovács, P.1    Köhidai, L.2    Csaba, G.3
  • 35
    • 0031799764 scopus 로고    scopus 로고
    • Effects of tumor necrosis factor alpha (TNF alpha) on the phospholipid metabolism of Tetrahymena pyriformis
    • Kovács P., Köhidai L., Csaba G. (1998) Effects of tumor necrosis factor alpha (TNF alpha) on the phospholipid metabolism of Tetrahymena pyriformis. Cell Biochem. Funct. 16: 87-97
    • (1998) Cell Biochem. Funct. , vol.16 , pp. 87-97
    • Kovács, P.1    Köhidai, L.2    Csaba, G.3
  • 37
    • 0034490583 scopus 로고    scopus 로고
    • Effect of glucosphingolipid synthesis inhibitor (PPMP and PDMP) treatment on Tetrahymena pyriformis: Data on the evolution of the signaling system
    • Kovács P., Pinter M., Csaba G. (2000) Effect of glucosphingolipid synthesis inhibitor (PPMP and PDMP) treatment on Tetrahymena pyriformis: data on the evolution of the signaling system. Cell Biochem. Funct. 18: 269-280
    • (2000) Cell Biochem. Funct. , vol.18 , pp. 269-280
    • Kovács, P.1    Pinter, M.2    Csaba, G.3
  • 38
    • 0348173562 scopus 로고    scopus 로고
    • Phosphatidyl 3-kinase-like activity in Tetrahymena. Effects of wortmannin and LY294002
    • Kovács P., Pállinger E. (2003) Phosphatidyl 3-kinase-like activity in Tetrahymena. Effects of wortmannin and LY294002. Acta Protozool. 42: 277-285
    • (2003) Acta Protozool , vol.42 , pp. 277-285
    • Kovács, P.1    Pállinger, E.2
  • 39
    • 0037123420 scopus 로고    scopus 로고
    • Facile synthesis of all possible diastereomers of conduritol and various derivatives of inositol stereoisomers in high enantiopurity from myo-inositol
    • Kwon Y.-U., Lee C., Chung S.-K. (2002) Facile synthesis of all possible diastereomers of conduritol and various derivatives of inositol stereoisomers in high enantiopurity from myo-inositol. J. Org. Chem. 67: 3327-3338.
    • (2002) J. Org. Chem. , vol.67 , pp. 3327-3338
    • Kwon, Y.-U.1    Lee, C.2    Chung, S.-K.3
  • 40
    • 0029189223 scopus 로고
    • The effect of vasopressin on the phosphoinositides of Tetrahymena pyriformis. Relationship with glycogen content
    • László V., Csaba G. (1995) The effect of vasopressin on the phosphoinositides of Tetrahymena pyriformis. Relationship with glycogen content. Acta Microbiol. Immunol. Hung. 42: 209-213
    • (1995) Acta Microbiol. Immunol. Hung. , vol.42 , pp. 209-213
    • László, V.1    Csaba, G.2
  • 41
    • 0034047410 scopus 로고    scopus 로고
    • Characterization of inositol phospholipids and identification of a mastoparan-induced polyphosphoinositide response in Tetrahymena pyriformis
    • Leondaritis G., Galanopoulou D. (2000) Characterization of inositol phospholipids and identification of a mastoparan-induced polyphosphoinositide response in Tetrahymena pyriformis. Lipids 35: 525-532
    • (2000) Lipids , vol.35 , pp. 525-532
    • Leondaritis, G.1    Galanopoulou, D.2
  • 42
    • 24944474829 scopus 로고    scopus 로고
    • D-3 phosphoinositides of the ciliate Tetrahymena: Characterization and study of their regulatory role in lysosomal enzyme secretion
    • Leondaritis G., Tiedtke A., Galanopoulou D. (2005) D-3 phosphoinositides of the ciliate Tetrahymena: Characterization and study of their regulatory role in lysosomal enzyme secretion. Biochim. Biophys. Acta 1745: 330-341
    • (2005) Biochim. Biophys. Acta , vol.1745 , pp. 330-341
    • Leondaritis, G.1    Tiedtke, A.2    Galanopoulou, D.3
  • 43
    • 0028586130 scopus 로고
    • The inositol high-polyphosphate series blocks synaptic transmission by preventing vesicular fusion: A giant squid synapse study
    • Llinás R., Sugimori M., Lang E. J., Moeir M., Fukuda M., Niinobe M., Mikoshiba K. (1994) The inositol high-polyphosphate series blocks synaptic transmission by preventing vesicular fusion: a giant squid synapse study. Proc. Natl. Acad. Sci. USA 91: 12990-12993
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12990-12993
    • Llinás, R.1    Sugimori, M.2    Lang, E.J.3    Moeir, M.4    Fukuda, M.5    Niinobe, M.6    Mikoshiba, K.7
  • 45
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • Martin T. F. (1998) Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14: 231-264
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231-264
    • Martin, T.F.1
  • 46
    • 0000076196 scopus 로고
    • A complete intracellular unit for incorporation of amino acid into storage protein utilizing adenosine triphosphate generated from phytic acid
    • Morton R. K., Raison J. K. (1963) A complete intracellular unit for incorporation of amino acid into storage protein utilizing adenosine triphosphate generated from phytic acid. Nature 200: 429-433
    • (1963) Nature , vol.200 , pp. 429-433
    • Morton, R.K.1    Raison, J.K.2
  • 48
    • 0028643566 scopus 로고
    • Synaptogamin is an inositol polyphosphate binding protein: Isolation and characterization as an Ins 1,3,4,5-P4 binding protein
    • Niinobe A. U., Yamaguchi Y., Fukuda M., Mikoshiba K. (1994) Synaptogamin is an inositol polyphosphate binding protein: isolation and characterization as an Ins 1,3,4,5-P4 binding protein. Biochem. Biophys. Res. Commun. 205: 1036-1042
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1036-1042
    • Niinobe, A.U.1    Yamaguchi, Y.2    Fukuda, M.3    Mikoshiba, K.4
  • 49
    • 0028842364 scopus 로고
    • Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP3/AP180) and inhibits clathrin cage assembly in vitro
    • Norris F. A., Ungewickell E., Majerus P. W. (1995) Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP3/AP180) and inhibits clathrin cage assembly in vitro. J. Biol. Chem. 270: 214-217
    • (1995) J. Biol. Chem. , vol.270 , pp. 214-217
    • Norris, F.A.1    Ungewickell, E.2    Majerus, P.W.3
  • 50
    • 0025312233 scopus 로고
    • Competitive inhibition by glucose of myo-inositol incorporation into cultured porcine aortic endothelial cells
    • Olgemoller B. S., Schwaabe S., Schleicher E. D., Gerbitz K. D. (1990) Competitive inhibition by glucose of myo-inositol incorporation into cultured porcine aortic endothelial cells. Biochim. Biophys. Acta 1052: 47-52
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 47-52
    • Olgemoller, B.S.1    Schwaabe, S.2    Schleicher, E.D.3    Gerbitz, K.D.4
  • 52
    • 0025896167 scopus 로고
    • Phosphatidylinositol glycan formation and utilization by the ciliate Tetrahymena mimbres
    • Pak Y., Ryals P. E., Thompson G. A. Jr. (1991) Phosphatidylinositol glycan formation and utilization by the ciliate Tetrahymena mimbres. J. Biol. Chem. 266: 15054-15059
    • (1991) J. Biol. Chem. , vol.266 , pp. 15054-15059
    • Pak, Y.1    Ryals, P.E.2    Thompson Jr., G.A.3
  • 54
    • 34047117816 scopus 로고    scopus 로고
    • Phosphatidylinositol synthase of Tetrahymena: Inositol isomers as substrates in phosphatidylinositol biosynthesis and headgroup exchange reactions
    • Riggs B. M., Lansley T. A., Ryals P. E. (2007) Phosphatidylinositol synthase of Tetrahymena: Inositol isomers as substrates in phosphatidylinositol biosynthesis and headgroup exchange reactions. J. Eukaryot. Microbiol. 54: 119-124
    • (2007) J. Eukaryot. Microbiol. , vol.54 , pp. 119-124
    • Riggs, B.M.1    Lansley, T.A.2    Ryals, P.E.3
  • 55
    • 0026890747 scopus 로고
    • The immobilization antigens of Tetrahymena thermophila are glycoproteins
    • Ron A., Williams N. E., Doerder F. P. (1992) The immobilization antigens of Tetrahymena thermophila are glycoproteins. J. Protozool. 39: 508-510
    • (1992) J. Protozool. , vol.39 , pp. 508-510
    • Ron, A.1    Williams, N.E.2    Doerder, F.P.3
  • 56
    • 0032996227 scopus 로고    scopus 로고
    • Evidence for early signaling events in stomatin-induced differentiation of Tetrahymena vorax
    • Ryals P. E., Bae S., Patterson C. E. (1999) Evidence for early signaling events in stomatin-induced differentiation of Tetrahymena vorax. J. Eukaryot. Microbiol. 46: 77-83
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 77-83
    • Ryals, P.E.1    Bae, S.2    Patterson, C.E.3
  • 57
    • 75349097674 scopus 로고    scopus 로고
    • The signaling ligand stomatin triggers a rapid rise in intracellular calcium concentration in Tetrahymena vorax
    • Ryals P. E., Damaso R. M., Jones J. B., Steinmetz C. A. (2008) The signaling ligand stomatin triggers a rapid rise in intracellular calcium concentration in Tetrahymena vorax. Florida Scient. 71: 287-292
    • (2008) Florida Scient , vol.71 , pp. 287-292
    • Ryals, P.E.1    Damaso, R.M.2    Jones, J.B.3    Steinmetz, C.A.4
  • 58
    • 0033563810 scopus 로고    scopus 로고
    • 3H]scyllo-inositol by Tetrahymena. Incorporation into phosphatidylinositol, phosphatidylinositol-linked glycans, and polyphosphoinositols
    • 3H]scyllo-inositol by Tetrahymena. Incorporation into phosphatidylinositol, phosphatidylinositol-linked glycans, and polyphosphoinositols. Arch. Biochem. Biophys. 366: 261-266
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 261-266
    • Ryals, P.E.1    Kersting, M.C.2
  • 59
    • 0025788927 scopus 로고
    • Phosphatidylinositollinked glycans and phosphatidylinositol-anchored proteins of Tetrahymena mimbres
    • Ryals P. E., Pak Y., Thompson G. A. Jr. (1991) Phosphatidylinositollinked glycans and phosphatidylinositol-anchored proteins of Tetrahymena mimbres. J. Biol. Chem. 266: 15048-15053.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15048-15053
    • Ryals, P.E.1    Pak, Y.2    Thompson Jr., G.A.3
  • 60
    • 0036142204 scopus 로고    scopus 로고
    • Phenotype switching in polymorphic Tetrahymena. A single cell Jekyll and Hyde
    • Ryals P. E., Smith-Somerville H. E., Buhse H. E. Jr. (2002) Phenotype switching in polymorphic Tetrahymena. A single cell Jekyll and Hyde. Int. Rev. Cytol. 212: 209-238
    • (2002) Int. Rev. Cytol. , vol.212 , pp. 209-238
    • Ryals, P.E.1    Smith-Somerville, H.E.2    Buhse Jr., H.E.3
  • 61
    • 0029036869 scopus 로고
    • Metabolism and biological activities of inositol pentakisphosphate and inositol hexkisphosphate
    • Sasakawa N., Sharif M., Hanley M. R. (1995) Metabolism and biological activities of inositol pentakisphosphate and inositol hexkisphosphate. Biochem. Pharmacol. 50: 137146
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 137146
    • Sasakawa, N.1    Sharif, M.2    Hanley, M.R.3
  • 62
    • 0005614201 scopus 로고
    • Ueber eine neue, aus dem Muskelfleische, gewonnene Zuckerart
    • Scherer J. (1850) Ueber eine neue, aus dem Muskelfleische, gewonnene Zuckerart. Ann. Chem. 73: 322-328
    • (1850) Ann. Chem. , vol.73 , pp. 322-328
    • Scherer, J.1
  • 63
  • 64
    • 34547203204 scopus 로고    scopus 로고
    • Phosphoinositide signaling in unicellular eukaryotes
    • Shemarova I. V. (2007) Phosphoinositide signaling in unicellular eukaryotes. Crit. Rev. Microbiol. 33: 141-156
    • (2007) Crit. Rev. Microbiol. , vol.33 , pp. 141-156
    • Shemarova, I.V.1
  • 66
    • 0033992160 scopus 로고    scopus 로고
    • Role of exogenous inositol and phosphatidylinositol in glycosylphosphatidylinositol anchor synthesis of GP49 by Giardia lamblia
    • Subramanian A. B., Navarro S., Carrasco R. A., Marti M., Das S. (2000) Role of exogenous inositol and phosphatidylinositol in glycosylphosphatidylinositol anchor synthesis of GP49 by Giardia lamblia. Biochem. Biophys. Acta 1483: 69-80
    • (2000) Biochem. Biophys. Acta , vol.1483 , pp. 69-80
    • Subramanian, A.B.1    Navarro, S.2    Carrasco, R.A.3    Marti, M.4    Das, S.5
  • 67
    • 0036297327 scopus 로고    scopus 로고
    • Both myo-inositol to chiro-inositol epimerase activities and chiro-inositol to myo-inositol ratios are decreased in tissues of GK type 2 diabetic rats compared to Wistar controls
    • Sun T., Heimark D. B., Ngugyen T., Nadler J. L., Larner J. (2002) Both myo-inositol to chiro-inositol epimerase activities and chiro-inositol to myo-inositol ratios are decreased in tissues of GK type 2 diabetic rats compared to Wistar controls. Biochem. Biophys. Res. Commun. 293: 1092-1098
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1092-1098
    • Sun, T.1    Heimark, D.B.2    Ngugyen, T.3    Nadler, J.L.4    Larner, J.5
  • 68
    • 0036138203 scopus 로고    scopus 로고
    • Functional genomics: The coming of age for Tetrahymena pyriformis
    • Turkewitz A. P., Orias E., Kapler G. (2002) Functional genomics: the coming of age for Tetrahymena pyriformis. Trends in Genetics 18: 35-40
    • (2002) Trends in Genetics , vol.18 , pp. 35-40
    • Turkewitz, A.P.1    Orias, E.2    Kapler, G.3
  • 70
    • 75349088749 scopus 로고    scopus 로고
    • Growth of the vacuoleless mutant of Tetrahymena thermophila NP1 in phytate
    • Webb S., Smith-Somerville H. E. (2005) Growth of the vacuoleless mutant of Tetrahymena thermophila NP1 in phytate. J. Eukaryot. Microbiol. 52: 26S
    • (2005) J. Eukaryot. Microbiol. , vol.52
    • Webb, S.1    Smith-Somerville, H.E.2
  • 71
    • 0025992449 scopus 로고
    • Structural characterization of a novel glycosyl-phosphatidylinositol from the protozoan Tetrahymena mimbres
    • Weinhart U., Thomas J. R., Pak Y. B., Thompson G. A. Jr. (1991) Structural characterization of a novel glycosyl-phosphatidylinositol from the protozoan Tetrahymena mimbres. Biochem. J. 279: 605-608
    • (1991) Biochem. J. , vol.279 , pp. 605-608
    • Weinhart, U.1    Thomas, J.R.2    Pak, Y.B.3    Thompson Jr., G.A.4
  • 72
    • 5044242512 scopus 로고    scopus 로고
    • The effect of phosphoinositide 3-kinase inhibitors on programmed nuclear degradation in Tetrahymena and fate of surviving nuclei
    • Yakisich J. S., Kapler G. M. (2004) The effect of phosphoinositide 3-kinase inhibitors on programmed nuclear degradation in Tetrahymena and fate of surviving nuclei. Cell Death Differ. 11: 1146-1149
    • (2004) Cell Death Differ , vol.11 , pp. 1146-1149
    • Yakisich, J.S.1    Kapler, G.M.2
  • 73
    • 0028297066 scopus 로고
    • Cytodifferentiation in Tetrahymena vorax is linked to glycosyl-phosphatidylinositol-anchored protein assembly
    • Yang X., Ryals P. E. (1994) Cytodifferentiation in Tetrahymena vorax is linked to glycosyl-phosphatidylinositol-anchored protein assembly. Biochem. J. 298: 697-703
    • (1994) Biochem. J. , vol.298 , pp. 697-703
    • Yang, X.1    Ryals, P.E.2
  • 74
    • 0030958119 scopus 로고    scopus 로고
    • An apparent association between glycosylphosphatidylinositol-anchored proteins and a sphingolipid in Tetrahymena mimbres
    • Zhang X., Thompson G. A. Jr. (1997) An apparent association between glycosylphosphatidylinositol-anchored proteins and a sphingolipid in Tetrahymena mimbres. Biochem. J. 323: 197-206
    • (1997) Biochem. J. , vol.323 , pp. 197-206
    • Zhang, X.1    Thompson Jr., G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.