메뉴 건너뛰기




Volumn 63, Issue 5, 2006, Pages 552-564

Inositol pyrophosphates: Metabolism and signaling

Author keywords

Inositol pyrophosphates; Kinase; Metabolism; Phosphorylation; Phytic acid; Signaling

Indexed keywords

INOSITOL PHOSPHATE;

EID: 33645088429     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5446-z     Document Type: Review
Times cited : (153)

References (106)
  • 2
    • 0038464637 scopus 로고    scopus 로고
    • 20 Years of Ins(1,4,5)P3, and 40 years before
    • Irvine R. F. (2003) 20 years of Ins(1,4,5)P3, and 40 years before. Nat. Rev. Mol. Cell. Biol. 4: 586-590
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 586-590
    • Irvine, R.F.1
  • 3
    • 0024415927 scopus 로고
    • Mass changes in inositol tetrakis- and pentakisphosphate isomers induced by chemotactic peptide stimulation in HL-60 cells
    • Pittet D., Schlegel W., Lew D. P., Monod A. and Mayr G. W. (1989) Mass changes in inositol tetrakis- and pentakisphosphate isomers induced by chemotactic peptide stimulation in HL-60 cells. J. Biol. Chem. 264: 18489-18493
    • (1989) J. Biol. Chem. , vol.264 , pp. 18489-18493
    • Pittet, D.1    Schlegel, W.2    Lew, D.P.3    Monod, A.4    Mayr, G.W.5
  • 4
    • 0023669698 scopus 로고
    • Observation of inositol pentakis- and hexakis-phosphates in mammalian tissues by 31P NMR
    • Szwergold B. S., Graham R. A. and Brown T. R. (1987) Observation of inositol pentakis- and hexakis-phosphates in mammalian tissues by 31P NMR. Biochem. Biophys. Res. Commun. 149: 874-881
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 874-881
    • Szwergold, B.S.1    Graham, R.A.2    Brown, T.R.3
  • 5
    • 0023662588 scopus 로고
    • Identification of inositol hexaphosphate in 31P-NMR spectra of Dictyostelium discoideum amoebae. Relevance to intracellular pH determination
    • Martin J. B., Foray M. F., Klein G. and Satre M. (1987) Identification of inositol hexaphosphate in 31P-NMR spectra of Dictyostelium discoideum amoebae. Relevance to intracellular pH determination. Biochim. Biophys. Acta. 931: 16-25
    • (1987) Biochim. Biophys. Acta. , vol.931 , pp. 16-25
    • Martin, J.B.1    Foray, M.F.2    Klein, G.3    Satre, M.4
  • 6
    • 0142026184 scopus 로고    scopus 로고
    • myo-Inositol-1,2,3,4,5,6-hexakisphosphate
    • Raboy V. (2003) myo-Inositol-1,2,3,4,5,6-hexakisphosphate. Phytochemistry 64: 1033-1043
    • (2003) Phytochemistry , vol.64 , pp. 1033-1043
    • Raboy, V.1
  • 7
    • 0035087311 scopus 로고    scopus 로고
    • Assessing the omnipotence of inositol hexakisphosphate
    • Shears S. B. (2001) Assessing the omnipotence of inositol hexakisphosphate. Cell Signal. 13: 151-158
    • (2001) Cell Signal. , vol.13 , pp. 151-158
    • Shears, S.B.1
  • 8
    • 0034664805 scopus 로고    scopus 로고
    • Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair
    • Hanakahi L. A., Bartlet-Jones M., Chappell C., Pappin D. and West S. C. (2000) Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair. Cell 102: 721-729
    • (2000) Cell , vol.102 , pp. 721-729
    • Hanakahi, L.A.1    Bartlet-Jones, M.2    Chappell, C.3    Pappin, D.4    West, S.C.5
  • 9
    • 24644519954 scopus 로고    scopus 로고
    • Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • Macbeth M. R., Schubert H. L., Vandemark A. P., Lingam A. T., Hill C. P. and Bass B. L. (2005) Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309: 1534-1539
    • (2005) Science , vol.309 , pp. 1534-1539
    • Macbeth, M.R.1    Schubert, H.L.2    Vandemark, A.P.3    Lingam, A.T.4    Hill, C.P.5    Bass, B.L.6
  • 10
    • 0033516604 scopus 로고    scopus 로고
    • A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
    • York J. D., Odom A. R., Murphy R., Ives E. B. and Wente S. R. (1999) A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285: 96-100
    • (1999) Science , vol.285 , pp. 96-100
    • York, J.D.1    Odom, A.R.2    Murphy, R.3    Ives, E.B.4    Wente, S.R.5
  • 11
    • 0027456498 scopus 로고
    • Turnover of inositol polyphosphate pyrophosphates in pancreatoma cells
    • Menniti F. S., Miller R. N., Putney J. W. Jr and Shears S. B. (1993) Turnover of inositol polyphosphate pyrophosphates in pancreatoma cells. J. Biol. Chem. 268: 3850-3856
    • (1993) J. Biol. Chem. , vol.268 , pp. 3850-3856
    • Menniti, F.S.1    Miller, R.N.2    Putney Jr., J.W.3    Shears, S.B.4
  • 12
    • 0027536427 scopus 로고
    • The detection, purification, structural characterization and metabolism of diphosphoinositol pentakisphosphate(s) and bisdiphosphoinositol tetrakisphosphate(s)
    • Stephens L., Radenberg T., Thiel U., Vogel G., Khoo K. H., Dell A. et al. (1993) The detection, purification, structural characterization and metabolism of diphosphoinositol pentakisphosphate(s) and bisdiphosphoinositol tetrakisphosphate(s). J. Biol. Chem. 268: 4009-4015
    • (1993) J. Biol. Chem. , vol.268 , pp. 4009-4015
    • Stephens, L.1    Radenberg, T.2    Thiel, U.3    Vogel, G.4    Khoo, K.H.5    Dell, A.6
  • 13
    • 0027225842 scopus 로고
    • Turnover of inositol pentakisphosphates, inositol hexakisphosphate and diphosphoinositol polyphosphates in primary cultured hepatocytes
    • Glennon M. C. and Shears S. B. (1993) Turnover of inositol pentakisphosphates, inositol hexakisphosphate and diphosphoinositol polyphosphates in primary cultured hepatocytes. Biochem. J. 293 (Pt 2): 583-590
    • (1993) Biochem. J. , vol.293 , Issue.2 PART , pp. 583-590
    • Glennon, M.C.1    Shears, S.B.2
  • 14
    • 0028902735 scopus 로고
    • Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo
    • Shears S. B., Ali N., Craxton A. and Bembenek M. E. (1995) Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo. J. Biol. Chem. 270: 10489-10497
    • (1995) J. Biol. Chem. , vol.270 , pp. 10489-10497
    • Shears, S.B.1    Ali, N.2    Craxton, A.3    Bembenek, M.E.4
  • 15
    • 0942290439 scopus 로고    scopus 로고
    • How versatile are inositol phosphate kinases?
    • Shears S. B. (2004) How versatile are inositol phosphate kinases? Biochem. J. 377: 265-280
    • (2004) Biochem. J. , vol.377 , pp. 265-280
    • Shears, S.B.1
  • 16
    • 0033055446 scopus 로고    scopus 로고
    • Pathways for phosphoinositide synthesis
    • Tolias K. F. and Cantley L. C. (1999) Pathways for phosphoinositide synthesis. Chem. Phys. Lipids. 98: 69-77
    • (1999) Chem. Phys. Lipids , vol.98 , pp. 69-77
    • Tolias, K.F.1    Cantley, L.C.2
  • 17
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine R. F. and Schell M. J. (2001) Back in the water: the return of the inositol phosphates. Nat. Rev. Mol. Cell. Biol. 2: 327-338
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 18
    • 0026357317 scopus 로고
    • Accumulation of [3H]-inositol into inositol polyphosphates during development of Dictyostelium
    • Europe-Finner G. N., Gammon B. and Newell P. C. (1991) Accumulation of [3H]-inositol into inositol polyphosphates during development of Dictyostelium. Biochem. Biophys. Res. Commun. 181: 191-196
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 191-196
    • Europe-Finner, G.N.1    Gammon, B.2    Newell, P.C.3
  • 19
    • 0025762374 scopus 로고
    • myo-inositol pentakisphosphates. Structure, biological occurrence and phosphorylation to myo-inositol hexakisphosphate
    • Stephens L. R., Hawkins P. T., Stanley A. F., Moore T., Poyner D. R., Morris P. J. et al. (1991) myo-inositol pentakisphosphates. Structure, biological occurrence and phosphorylation to myo-inositol hexakisphosphate. Biochem. J. 275 (Pt 2): 485-499
    • (1991) Biochem. J. , vol.275 , Issue.2 PART , pp. 485-499
    • Stephens, L.R.1    Hawkins, P.T.2    Stanley, A.F.3    Moore, T.4    Poyner, D.R.5    Morris, P.J.6
  • 20
    • 0025310679 scopus 로고
    • Stepwise phosphorylation of myo-inositol leading to myo-inositol hexakisphosphate in Dictyostelium
    • Stephens L. R. and Irvine R. F. (1990) Stepwise phosphorylation of myo-inositol leading to myo-inositol hexakisphosphate in Dictyostelium. Nature 346: 580-583
    • (1990) Nature , vol.346 , pp. 580-583
    • Stephens, L.R.1    Irvine, R.F.2
  • 21
    • 23044476605 scopus 로고    scopus 로고
    • Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae
    • Seeds A. M., Bastidas R. J. and York J. D. (2005) Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae. J. Biol. Chem. 280: 27654-27661
    • (2005) J. Biol. Chem. , vol.280 , pp. 27654-27661
    • Seeds, A.M.1    Bastidas, R.J.2    York, J.D.3
  • 22
    • 0034010804 scopus 로고    scopus 로고
    • Diphospho-myo-inositol phosphates during the life cycle of Dictyostelium and Polysphondylium
    • Laussmann T., Pikzack C., Thiel U., Mayr G. W. and Vogel G. (2000) Diphospho-myo-inositol phosphates during the life cycle of Dictyostelium and Polysphondylium. Eur. J. Biochem. 267: 2447-2451
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2447-2451
    • Laussmann, T.1    Pikzack, C.2    Thiel, U.3    Mayr, G.W.4    Vogel, G.5
  • 23
    • 0029997459 scopus 로고    scopus 로고
    • Structures of diphospho-myo-inositol pentakisphosphate and bisdiphospho-myo-inositol tetrakisphosphate from Dictyostelium resolved by NMR analysis
    • Laussmann T., Eujen R., Weisshuhn C. M., Thiel U. and Vogel G. (1996) Structures of diphospho-myo-inositol pentakisphosphate and bisdiphospho-myo- inositol tetrakisphosphate from Dictyostelium resolved by NMR analysis. Biochem. J. 315 (Pt 3): 715-720
    • (1996) Biochem. J. , vol.315 , Issue.3 PART , pp. 715-720
    • Laussmann, T.1    Eujen, R.2    Weisshuhn, C.M.3    Thiel, U.4    Vogel, G.5
  • 24
    • 0031057586 scopus 로고    scopus 로고
    • Diphospho-myo-inositol phosphates from Dictyostelium identified as D-6-diphospho-myo-inositol pentakisphosphate and D-5,6-bisdiphospho-myo-inositol tetrakisphosphate
    • Laussmann T., Reddy K. M., Reddy K. K., Falck J. R. and Vogel G. (1997) Diphospho-myo-inositol phosphates from Dictyostelium identified as D-6-diphospho-myo-inositol pentakisphosphate and D-5,6-bisdiphospho-myo-inositol tetrakisphosphate. Biochem. J. 322 (Pt 1): 31-33
    • (1997) Biochem. J. , vol.322 , Issue.1 PART , pp. 31-33
    • Laussmann, T.1    Reddy, K.M.2    Reddy, K.K.3    Falck, J.R.4    Vogel, G.5
  • 25
    • 0030668774 scopus 로고    scopus 로고
    • Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells
    • Albert C., Safrany S. T., Bembenek M. E., Reddy K. M., Reddy K., Falck J. et al. (1997) Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (Pt 2): 553-560
    • (1997) Biochem. J. , vol.327 , Issue.2 PART , pp. 553-560
    • Albert, C.1    Safrany, S.T.2    Bembenek, M.E.3    Reddy, K.M.4    Reddy, K.5    Falck, J.6
  • 26
    • 0032502941 scopus 로고    scopus 로고
    • Diphospho-myo-inositol phosphates in Dictyostelium and Polysphondylium: Identification of a new bisdiphospho-myo-inositol tetrakisphosphate
    • Laussmann T., Hansen A., Reddy K. M., Reddy K. K., Falck J. R. and Vogel G. (1998) Diphospho-myo-inositol phosphates in Dictyostelium and Polysphondylium: identification of a new bisdiphospho-myo-inositol tetrakisphosphate. FEBS Lett. 426: 145-150
    • (1998) FEBS Lett. , vol.426 , pp. 145-150
    • Laussmann, T.1    Hansen, A.2    Reddy, K.M.3    Reddy, K.K.4    Falck, J.R.5    Vogel, G.6
  • 28
    • 9444295986 scopus 로고    scopus 로고
    • Protocols for regulation and study of diphosphoinositol polyphosphates
    • Safrany S. T. (2004) Protocols for regulation and study of diphosphoinositol polyphosphates. Mol. Pharmacol. 66: 1585-1591
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1585-1591
    • Safrany, S.T.1
  • 29
    • 2942748149 scopus 로고    scopus 로고
    • Complex changes in cellular inositol phosphate complement accompany transit through the cell cycle
    • Barker C. J., Wright J., Hughes P. J., Kirk C. J. and Michell R. H. (2004) Complex changes in cellular inositol phosphate complement accompany transit through the cell cycle. Biochem. J. 380: 465-473
    • (2004) Biochem. J. , vol.380 , pp. 465-473
    • Barker, C.J.1    Wright, J.2    Hughes, P.J.3    Kirk, C.J.4    Michell, R.H.5
  • 30
    • 0141540848 scopus 로고    scopus 로고
    • Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-Pt-dIns(3,4,5)P3 interactions
    • Luo H. R., Huang Y. E., Chen J. C., Saiardi A., Iijima M., Ye K. et al. (2003) Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-Pt-dIns(3,4,5)P3 interactions. Cell 114: 559-572
    • (2003) Cell , vol.114 , pp. 559-572
    • Luo, H.R.1    Huang, Y.E.2    Chen, J.C.3    Saiardi, A.4    Iijima, M.5    Ye, K.6
  • 31
    • 0029975911 scopus 로고    scopus 로고
    • Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor
    • USA
    • Voglmaier S. M., Bembenek M. E., Kaplin A. I., Dorman G., Olszewski J. D., Prestwich G. D. et al. (1996) Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor. Proc. Natl. Acad. Sci. USA 93: 4305-4310
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 4305-4310
    • Voglmaier, S.M.1    Bembenek, M.E.2    Kaplin, A.I.3    Dorman, G.4    Olszewski, J.D.5    Prestwich, G.D.6
  • 32
    • 0033581832 scopus 로고    scopus 로고
    • Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
    • Saiardi A., Erdjument-Bromage H., Snowman A. M., Tempst P. and Snyder S. H. (1999) Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9: 1323-1326
    • (1999) Curr. Biol. , vol.9 , pp. 1323-1326
    • Saiardi, A.1    Erdjument-Bromage, H.2    Snowman, A.M.3    Tempst, P.4    Snyder, S.H.5
  • 34
    • 0035914367 scopus 로고    scopus 로고
    • Identification and characterization of a novel inositol hexakisphosphate kinase
    • Saiardi A., Nagata E., Luo H. R., Snowman A. M. and Snyder S. H. (2001) Identification and characterization of a novel inositol hexakisphosphate kinase. J. Biol. Chem. 276: 39179-39185
    • (2001) J. Biol. Chem. , vol.276 , pp. 39179-39185
    • Saiardi, A.1    Nagata, E.2    Luo, H.R.3    Snowman, A.M.4    Snyder, S.H.5
  • 35
    • 0034637548 scopus 로고    scopus 로고
    • The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis
    • Saiardi A., Caffrey J. J., Snyder S. H. and Shears S. B. (2000) The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis. J. Biol. Chem. 275: 24686-24692
    • (2000) J. Biol. Chem. , vol.275 , pp. 24686-24692
    • Saiardi, A.1    Caffrey, J.J.2    Snyder, S.H.3    Shears, S.B.4
  • 36
    • 0034677903 scopus 로고    scopus 로고
    • A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control
    • Odom A. R., Stahlberg A., Wente S. R. and York J. D. (2000) A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287: 2026-2029
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 37
    • 0033975636 scopus 로고    scopus 로고
    • Inositol polyphosphate multikinase (ArgRIII) determines nuclear mRNA export in Saccharomyces cerevisiae
    • Saiardi A., Caffrey J. J., Snyder S. H. and Shears S. B. (2000) Inositol polyphosphate multikinase (ArgRIII) determines nuclear mRNA export in Saccharomyces cerevisiae. FEBS Lett. 468: 28-32
    • (2000) FEBS Lett. , vol.468 , pp. 28-32
    • Saiardi, A.1    Caffrey, J.J.2    Snyder, S.H.3    Shears, S.B.4
  • 38
    • 0036711574 scopus 로고    scopus 로고
    • The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
    • Nalaskowski M. M., Deschermeier C., Fanick W. and Mayr G. W. (2002) The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. Biochem. J. 366: 549-556
    • (2002) Biochem. J. , vol.366 , pp. 549-556
    • Nalaskowski, M.M.1    Deschermeier, C.2    Fanick, W.3    Mayr, G.W.4
  • 39
    • 0037044795 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases
    • Stevenson-Paulik J., Odom A. R. and York J. D. (2002) Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases. J. Biol. Chem. 277: 42711-42718
    • (2002) J. Biol. Chem. , vol.277 , pp. 42711-42718
    • Stevenson-Paulik, J.1    Odom, A.R.2    York, J.D.3
  • 40
    • 0242684549 scopus 로고    scopus 로고
    • Arabidopsis inositol polyphosphate 6-/3-kinase is a nuclear protein that complements a yeast mutant lacking a functional ArgR-Mcm1 transcription complex
    • Xia H. J., Brearley C., Elge S., Kaplan B., Fromm H. and Mueller-Roeber B. (2003) Arabidopsis inositol polyphosphate 6-/3-kinase is a nuclear protein that complements a yeast mutant lacking a functional ArgR-Mcm1 transcription complex. Plant Cell 15: 449-463
    • (2003) Plant Cell , vol.15 , pp. 449-463
    • Xia, H.J.1    Brearley, C.2    Elge, S.3    Kaplan, B.4    Fromm, H.5    Mueller-Roeber, B.6
  • 41
    • 0035956860 scopus 로고    scopus 로고
    • Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate
    • USA
    • Saiardi A., Nagata E., Luo H. R., Sawa A., Luo X., Snowman A. M. et al. (2001) Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate. Proc. Natl. Acad. Sci. USA 98: 2306-2311
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 2306-2311
    • Saiardi, A.1    Nagata, E.2    Luo, H.R.3    Sawa, A.4    Luo, X.5    Snowman, A.M.6
  • 42
    • 0035853450 scopus 로고    scopus 로고
    • The transcriptional regulator, Arg82, is a hybrid kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activity
    • Zhang T., Caffrey J. J. and Shears S. B. (2001) The transcriptional regulator, Arg82, is a hybrid kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activity. FEBS Lett. 494: 208-212
    • (2001) FEBS Lett. , vol.494 , pp. 208-212
    • Zhang, T.1    Caffrey, J.J.2    Shears, S.B.3
  • 43
    • 17144366551 scopus 로고    scopus 로고
    • Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase
    • Mayr G. W., Windhorst S. and Hillemeier K. (2005) Antiproliferative plant and synthetic polyphenolics are specific inhibitors of vertebrate inositol-1,4,5-trisphosphate 3-kinases and inositol polyphosphate multikinase. J. Biol. Chem. 280: 13229-13240
    • (2005) J. Biol. Chem. , vol.280 , pp. 13229-13240
    • Mayr, G.W.1    Windhorst, S.2    Hillemeier, K.3
  • 44
    • 4444223742 scopus 로고    scopus 로고
    • Structure of a human inositol 1,4,5-trisphosphate 3-kinase: Substrate binding reveals why it is not a phosphoinositide 3-kinase
    • Gonzalez B., Schell M. J., Letcher A. J., Veprintsev D. B., Irvine R. F. and Williams R. L. (2004) Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. Mol. Cell 15: 689-701
    • (2004) Mol. Cell , vol.15 , pp. 689-701
    • Gonzalez, B.1    Schell, M.J.2    Letcher, A.J.3    Veprintsev, D.B.4    Irvine, R.F.5    Williams, R.L.6
  • 45
    • 4444230351 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase
    • Miller G. J. and Hurley J. H. (2004) Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase. Mol. Cell 15: 703-711
    • (2004) Mol. Cell , vol.15 , pp. 703-711
    • Miller, G.J.1    Hurley, J.H.2
  • 46
    • 22744443710 scopus 로고    scopus 로고
    • Inositide evolution - Towards turtle domination?
    • Irvine R. F. (2005) Inositide evolution - towards turtle domination? J. Physiol. 566: 295-300
    • (2005) J. Physiol. , vol.566 , pp. 295-300
    • Irvine, R.F.1
  • 48
    • 24344495294 scopus 로고    scopus 로고
    • Signal transduction during environmental stress: InsP(8) operates within highly restricted contexts
    • Choi K., Mollapour E. and Shears S. B. (2005) Signal transduction during environmental stress: InsP(8) operates within highly restricted contexts. Cell Signal. 17: 1533-1541
    • (2005) Cell Signal. , vol.17 , pp. 1533-1541
    • Choi, K.1    Mollapour, E.2    Shears, S.B.3
  • 49
    • 0032552889 scopus 로고    scopus 로고
    • Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate
    • Huang C. F., Voglmaier S. M., Bembenek M. E., Saiardi A. and Snyder S. H. (1998) Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate. Biochemistry 37: 14998-15004
    • (1998) Biochemistry , vol.37 , pp. 14998-15004
    • Huang, C.F.1    Voglmaier, S.M.2    Bembenek, M.E.3    Saiardi, A.4    Snyder, S.H.5
  • 50
    • 0032538976 scopus 로고    scopus 로고
    • A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase
    • Safrany S. T., Caffrey J. J., Yang X., Bembenek M. E., Moyer M. B., Burkhart W. A. et al. (1998) A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase. Embo J. 17: 6599-6607
    • (1998) Embo J. , vol.17 , pp. 6599-6607
    • Safrany, S.T.1    Caffrey, J.J.2    Yang, X.3    Bembenek, M.E.4    Moyer, M.B.5    Burkhart, W.A.6
  • 51
    • 0034725078 scopus 로고    scopus 로고
    • Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family
    • Caffrey J. J., Safrany S. T., Yang X. and Shears S. B. (2000) Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family. J. Biol. Chem. 275: 12730-12736
    • (2000) J. Biol. Chem. , vol.275 , pp. 12730-12736
    • Caffrey, J.J.1    Safrany, S.T.2    Yang, X.3    Shears, S.B.4
  • 52
    • 0033544954 scopus 로고    scopus 로고
    • Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates
    • Yang X., Safrany S. T. and Shears S. B. (1999) Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates. J. Biol. Chem. 274: 35434-35440
    • (1999) J. Biol. Chem. , vol.274 , pp. 35434-35440
    • Yang, X.1    Safrany, S.T.2    Shears, S.B.3
  • 53
    • 0346668345 scopus 로고    scopus 로고
    • Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate
    • Fisher D. I., Safrany S. T., Strike P., McLennan A. G. and Cartwright J. L. (2002) Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate. J. Biol. Chem. 277: 47313-47317
    • (2002) J. Biol. Chem. , vol.277 , pp. 47313-47317
    • Fisher, D.I.1    Safrany, S.T.2    Strike, P.3    McLennan, A.G.4    Cartwright, J.L.5
  • 54
    • 0242684477 scopus 로고    scopus 로고
    • Disruption and overexpression of the Schizosaccharomyces pombe apsl gene, and effects on growth rate, morphology and intracellular diadenosine 5′,5‴-P1,P5-pentaphosphate and diphosphoinositol polyphosphate concentrations
    • Ingram S. W., Safrany S. T. and Barnes L. D. (2003) Disruption and overexpression of the Schizosaccharomyces pombe apsl gene, and effects on growth rate, morphology and intracellular diadenosine 5′,5‴-P1,P5- pentaphosphate and diphosphoinositol polyphosphate concentrations. Biochem. J. 369: 519-528
    • (2003) Biochem. J. , vol.369 , pp. 519-528
    • Ingram, S.W.1    Safrany, S.T.2    Barnes, L.D.3
  • 55
    • 0033694225 scopus 로고    scopus 로고
    • Abscisic acid-induced changes in inositol metabolism in Spirodela polyrrhiza
    • Flores S. and Smart C. C. (2000) Abscisic acid-induced changes in inositol metabolism in Spirodela polyrrhiza. Planta 211: 823-832
    • (2000) Planta , vol.211 , pp. 823-832
    • Flores, S.1    Smart, C.C.2
  • 56
    • 0029814788 scopus 로고    scopus 로고
    • Inositol phosphates in barley (Hordeum vulgare L.) aleurone tissue are stereochemically similar to the products of breakdown of InsP6 in vitro by wheat-bran phytase
    • Brearley C. A. and Hanke D. E. (1996) Inositol phosphates in barley (Hordeum vulgare L.) aleurone tissue are stereochemically similar to the products of breakdown of InsP6 in vitro by wheat-bran phytase. Biochem. J. 318 (Pt 1): 279-286
    • (1996) Biochem. J. , vol.318 , Issue.1 PART , pp. 279-286
    • Brearley, C.A.1    Hanke, D.E.2
  • 57
  • 58
    • 0028858141 scopus 로고
    • Suppressors of a Saccharomyces cerevisiae pkcl mutation identify alleles of the phosphatase gene PTC1 and of a novel gene encoding a putative basic leucine zipper protein
    • Huang K. N. and Symington L. S. (1995) Suppressors of a Saccharomyces cerevisiae pkcl mutation identify alleles of the phosphatase gene PTC1 and of a novel gene encoding a putative basic leucine zipper protein. Genetics 141: 1275-1285
    • (1995) Genetics , vol.141 , pp. 1275-1285
    • Huang, K.N.1    Symington, L.S.2
  • 59
    • 0037176835 scopus 로고    scopus 로고
    • Inositol pyrophosphates are required for DNA hyperrecombination in protein kinase c1 mutant yeast
    • Luo H. R., Saiardi A., Yu H., Nagata E., Ye K. and Snyder S. H. (2002) Inositol pyrophosphates are required for DNA hyperrecombination in protein kinase c1 mutant yeast. Biochemistry 41: 2509-2515
    • (2002) Biochemistry , vol.41 , pp. 2509-2515
    • Luo, H.R.1    Saiardi, A.2    Yu, H.3    Nagata, E.4    Ye, K.5    Snyder, S.H.6
  • 61
    • 0037189551 scopus 로고    scopus 로고
    • In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis
    • Dubois E., Scherens B., Vierendeels F., Ho M. M., Messenguy F. and Shears S. B. (2002) In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis. J. Biol. Chem. 277: 23755-23763
    • (2002) J. Biol. Chem. , vol.277 , pp. 23755-23763
    • Dubois, E.1    Scherens, B.2    Vierendeels, F.3    Ho, M.M.4    Messenguy, F.5    Shears, S.B.6
  • 62
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P., Giot L., Cagney G., Mansfield T. A., Judson R. S., Knight J. R. et al. (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403: 623-627
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 63
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., Gruhler A., Heilbut A., Bader G. D., Moore L., Adams S. L. et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3    Bader, G.D.4    Moore, L.5    Adams, S.L.6
  • 65
    • 13844311012 scopus 로고    scopus 로고
    • Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases
    • USA
    • Saiardi A., Resnick A. C., Snowman A. M., Wendland B. and Snyder S. H. (2005) Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases. Proc. Natl. Acad. Sci. USA 102: 1911-1914
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 1911-1914
    • Saiardi, A.1    Resnick, A.C.2    Snowman, A.M.3    Wendland, B.4    Snyder, S.H.5
  • 66
    • 2442542568 scopus 로고    scopus 로고
    • Recent advances in telomere biology: Implications for human cancer
    • Meeker A. K. and De Marzo A. M. (2004) Recent advances in telomere biology: implications for human cancer. Curr. Opin. Oncol. 16: 32-38
    • (2004) Curr. Opin. Oncol. , vol.16 , pp. 32-38
    • Meeker, A.K.1    De Marzo, A.M.2
  • 68
    • 0035989348 scopus 로고    scopus 로고
    • Regulation of genome stability by TEL1 and MEC1, yeast homologs of the mammalian ATM and ATR genes
    • Craven R. J., Greenwell P. W., Dominska M. and Petes T. D. (2002) Regulation of genome stability by TEL1 and MEC1, yeast homologs of the mammalian ATM and ATR genes. Genetics 161: 493-507
    • (2002) Genetics , vol.161 , pp. 493-507
    • Craven, R.J.1    Greenwell, P.W.2    Dominska, M.3    Petes, T.D.4
  • 69
    • 0034610290 scopus 로고    scopus 로고
    • Protein kinase activity of Tel1p and Mec1p, two Saccharomyces cerevisiae proteins related to the human ATM protein kinase
    • USA
    • Mallory J. C. and Petes T. D. (2000) Protein kinase activity of Tel1p and Mec1p, two Saccharomyces cerevisiae proteins related to the human ATM protein kinase. Proc. Natl. Acad. Sci. USA 97: 13749-13754
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 13749-13754
    • Mallory, J.C.1    Petes, T.D.2
  • 70
    • 0029150855 scopus 로고
    • TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1
    • Morrow D. M., Tagle D. A., Shiloh Y., Collins F. S. and Hieter P. (1995) TEL1, an S. cerevisiae homolog of the human gene mutated in ataxia telangiectasia, is functionally related to the yeast checkpoint gene MEC1. Cell 82: 831-840
    • (1995) Cell , vol.82 , pp. 831-840
    • Morrow, D.M.1    Tagle, D.A.2    Shiloh, Y.3    Collins, F.S.4    Hieter, P.5
  • 71
    • 0037414868 scopus 로고    scopus 로고
    • Regulation of chromatin remodeling by inositol polyphosphates
    • Steger D. J., Haswell E. S., Miller A. L., Wente S. R. and O'Shea E. K. (2003) Regulation of chromatin remodeling by inositol polyphosphates. Science 299: 114-116
    • (2003) Science , vol.299 , pp. 114-116
    • Steger, D.J.1    Haswell, E.S.2    Miller, A.L.3    Wente, S.R.4    O'Shea, E.K.5
  • 72
    • 24644503488 scopus 로고    scopus 로고
    • Inositol polyphosphate multikinase is a nuclear PI3-kinase with transcriptional regulatory activity
    • USA
    • Resnick A. C., Snowman A. M., Kang B. N., Hurt K. J., Snyder S. H. and Saiardi A. (2005) Inositol polyphosphate multikinase is a nuclear PI3-kinase with transcriptional regulatory activity. Proc. Natl. Acad. Sci. USA 102: 12783-12788
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 12783-12788
    • Resnick, A.C.1    Snowman, A.M.2    Kang, B.N.3    Hurt, K.J.4    Snyder, S.H.5    Saiardi, A.6
  • 73
    • 0025859989 scopus 로고
    • Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP-2
    • Beck K. A. and Keen J. H. (1991) Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP-2. J. Biol. Chem. 266: 4442-4447
    • (1991) J. Biol. Chem. , vol.266 , pp. 4442-4447
    • Beck, K.A.1    Keen, J.H.2
  • 75
  • 76
    • 0029128910 scopus 로고
    • The interaction of coatomer with inositol polyphosphates is conserved in Saccharomyces cerevisiae
    • Ali N., Duden R., Bembenek M. E. and Shears S. B. (1995) The interaction of coatomer with inositol polyphosphates is conserved in Saccharomyces cerevisiae. Biochem. J. 310 (Pt 1): 279-284
    • (1995) Biochem. J. , vol.310 , Issue.1 PART , pp. 279-284
    • Ali, N.1    Duden, R.2    Bembenek, M.E.3    Shears, S.B.4
  • 77
    • 0028263636 scopus 로고
    • Golgi coatomer binds, and forms K(+)-selective channels gated by, inositol polyphosphates
    • Fleischer B., Xie J., Mayrleitner M., Shears S. B., Palmer D. J. and Fleischer S. (1994) Golgi coatomer binds, and forms K(+)-selective channels gated by, inositol polyphosphates. J. Biol. Chem. 269: 17826-17832
    • (1994) J. Biol. Chem. , vol.269 , pp. 17826-17832
    • Fleischer, B.1    Xie, J.2    Mayrleitner, M.3    Shears, S.B.4    Palmer, D.J.5    Fleischer, S.6
  • 78
    • 0028925007 scopus 로고
    • Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3
    • Ye W., Ali N., Bembenek M. E., Shears S. B. and Lafer E. M. (1995) Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3. J. Biol. Chem. 270: 1564-1568
    • (1995) J. Biol. Chem. , vol.270 , pp. 1564-1568
    • Ye, W.1    Ali, N.2    Bembenek, M.E.3    Shears, S.B.4    Lafer, E.M.5
  • 79
    • 0037131521 scopus 로고    scopus 로고
    • Endocytosis: Driving membranes around the bend
    • Hurley J. H. and Wendland B. (2002) Endocytosis: driving membranes around the bend. Cell 111: 143-146
    • (2002) Cell , vol.111 , pp. 143-146
    • Hurley, J.H.1    Wendland, B.2
  • 80
    • 17944372902 scopus 로고    scopus 로고
    • GRAB: A physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase
    • Luo H. R., Saiardi A., Nagata E., Ye K., Yu H., Jung T. S. et al. (2001) GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. Neuron 31: 439-451
    • (2001) Neuron , vol.31 , pp. 439-451
    • Luo, H.R.1    Saiardi, A.2    Nagata, E.3    Ye, K.4    Yu, H.5    Jung, T.S.6
  • 81
    • 0037205230 scopus 로고    scopus 로고
    • Tumor suppressor PTEN mediates sensing of chemoattractant gradients
    • Iijima M. and Devreotes P. (2002) Tumor suppressor PTEN mediates sensing of chemoattractant gradients. Cell 109: 599-610
    • (2002) Cell , vol.109 , pp. 599-610
    • Iijima, M.1    Devreotes, P.2
  • 82
    • 0032536857 scopus 로고    scopus 로고
    • Turnover of bis-diphosphoinositol tetrakisphosphate in a smooth muscle cell line is regulated by beta2-adrenergic receptors through a cAMP-mediated. A-kinase-independent mechanism
    • Safrany S. T. and Shears S. B. (1998) Turnover of bis-diphosphoinositol tetrakisphosphate in a smooth muscle cell line is regulated by beta2-adrenergic receptors through a cAMP-mediated. A-kinase-independent mechanism. EMBO J. 17: 1710-1716
    • (1998) EMBO J. , vol.17 , pp. 1710-1716
    • Safrany, S.T.1    Shears, S.B.2
  • 83
    • 6344257046 scopus 로고    scopus 로고
    • Signaling by higher inositol polyphosphates. Synthesis of bisdiphosphoinositol tetrakisphosphate ('InsP8') is selectively activated by hyperosinotic stress
    • Pesesse X., Choi K., Zhang T. and Shears S. B. (2004) Signaling by higher inositol polyphosphates. Synthesis of bisdiphosphoinositol tetrakisphosphate ('InsP8') is selectively activated by hyperosinotic stress. J. Biol. Chem. 279: 43378-43381
    • (2004) J. Biol. Chem. , vol.279 , pp. 43378-43381
    • Pesesse, X.1    Choi, K.2    Zhang, T.3    Shears, S.B.4
  • 84
    • 0035816638 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 2 mediates growth suppressive and apoptotic effects of interferon-beta in ovarian carcinoma cells
    • Morrison B. H., Bauer J. A., Kalvakolanu D. V. and Lindner D. J. (2001) Inositol hexakisphosphate kinase 2 mediates growth suppressive and apoptotic effects of interferon-beta in ovarian carcinoma cells. J. Biol. Chem. 276: 24965-24970
    • (2001) J. Biol. Chem. , vol.276 , pp. 24965-24970
    • Morrison, B.H.1    Bauer, J.A.2    Kalvakolanu, D.V.3    Lindner, D.J.4
  • 85
    • 85047699544 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 2 sensitizes ovarian carcinoma cells to multiple cancer therapeutics
    • Morrison B. H., Bauer J. A., Hu J., Grane R. W., Ozdemir A. M., Chawla-Sarkar M. et al. (2002) Inositol hexakisphosphate kinase 2 sensitizes ovarian carcinoma cells to multiple cancer therapeutics. Oncogene 21: 1882-1889
    • (2002) Oncogene , vol.21 , pp. 1882-1889
    • Morrison, B.H.1    Bauer, J.A.2    Hu, J.3    Grane, R.W.4    Ozdemir, A.M.5    Chawla-Sarkar, M.6
  • 86
    • 12844251293 scopus 로고    scopus 로고
    • Apo2L/TRAIL induction and nuclear translocation of inositol hexakisphosphate kinase 2 during IFN-beta-induced apoptosis in ovarian carcinoma
    • Morrison B. H., Tang Z., Jacobs B. S., Bauer J. A. and Lindner D. J. (2005) Apo2L/TRAIL induction and nuclear translocation of inositol hexakisphosphate kinase 2 during IFN-beta-induced apoptosis in ovarian carcinoma. Biochem. J. 385: 595-603
    • (2005) Biochem. J. , vol.385 , pp. 595-603
    • Morrison, B.H.1    Tang, Z.2    Jacobs, B.S.3    Bauer, J.A.4    Lindner, D.J.5
  • 87
    • 12544255427 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase-2, a physiologic mediator of cell death
    • Nagata E., Luo H. R., Saiardi A., Bae B. I., Suzuki N. and Snyder S. H. (2005) Inositol hexakisphosphate kinase-2, a physiologic mediator of cell death. J. Biol. Chem. 280: 1634-1640
    • (2005) J. Biol. Chem. , vol.280 , pp. 1634-1640
    • Nagata, E.1    Luo, H.R.2    Saiardi, A.3    Bae, B.I.4    Suzuki, N.5    Snyder, S.H.6
  • 88
    • 0037057284 scopus 로고    scopus 로고
    • Oncogenic transformation by beta-catenin: Deletion analysis and characterization of selected target genes
    • Aoki M., Sobek V., Maslyar D. J., Hecht A. and Vogt P. K. (2002) Oncogenic transformation by beta-catenin: deletion analysis and characterization of selected target genes. Oncogene 21: 6983-6991
    • (2002) Oncogene , vol.21 , pp. 6983-6991
    • Aoki, M.1    Sobek, V.2    Maslyar, D.J.3    Hecht, A.4    Vogt, P.K.5
  • 89
    • 0032729458 scopus 로고    scopus 로고
    • Signaling through beta-catenin and Lef/Tcf
    • Novak A. and Dedhar S. (1999) Signaling through beta-catenin and Lef/Tcf. Cell. Mol. Life Sci. 56: 523-537
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 523-537
    • Novak, A.1    Dedhar, S.2
  • 90
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis P. (2000) Wnt signaling and cancer. Genes Dev. 14: 1837-1851
    • (2000) Genes Dev. , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 92
    • 13844256151 scopus 로고    scopus 로고
    • Solution behaviour of myo-inositol hexakisphosphate in the presence of multivalent cations. Prediction of a neutral pentamagnesium species under cytosolic/nuclear conditions
    • Torres J., Dominguez S., Cerda M. F., Obal G., Mederos A., Irvine R. F. et al. (2005) Solution behaviour of myo-inositol hexakisphosphate in the presence of multivalent cations. Prediction of a neutral pentamagnesium species under cytosolic/nuclear conditions. J. Inorg. Biochem. 99: 828-840
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 828-840
    • Torres, J.1    Dominguez, S.2    Cerda, M.F.3    Obal, G.4    Mederos, A.5    Irvine, R.F.6
  • 93
    • 8144228588 scopus 로고    scopus 로고
    • Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates
    • Komander D., Fairservice A., Deak M., Kular G. S., Prescott A. R., Peter Downes C. et al. (2004) Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates. EMBO J. 23: 3918-3928
    • (2004) EMBO J. , vol.23 , pp. 3918-3928
    • Komander, D.1    Fairservice, A.2    Deak, M.3    Kular, G.S.4    Prescott, A.R.5    Peter Downes, C.6
  • 94
    • 0000076196 scopus 로고
    • A complete intracellular unit for incorporation of amino-acid into storage protein utilizing adenosine triphosphate generated from phytate
    • Morton R. K. and Raison J. K. (1963) A complete intracellular unit for incorporation of amino-acid into storage protein utilizing adenosine triphosphate generated from phytate. Nature 200: 429-433
    • (1963) Nature , vol.200 , pp. 429-433
    • Morton, R.K.1    Raison, J.K.2
  • 96
    • 10844254761 scopus 로고    scopus 로고
    • Signal transduction. Unexpected mediators of protein phosphorylation
    • York J. D. and Hunter T. (2004) Signal transduction. Unexpected mediators of protein phosphorylation. Science 306: 2053-2055
    • (2004) Science , vol.306 , pp. 2053-2055
    • York, J.D.1    Hunter, T.2
  • 98
    • 0030897146 scopus 로고    scopus 로고
    • Identification of a cDNA/protein leading to an increased Pi-uptake in Xenopus laevis oocytes
    • Norbis F., Boll M., Stange G., Markovich D., Verrey F., Biber J. et al. (1997) Identification of a cDNA/protein leading to an increased Pi-uptake in Xenopus laevis oocytes. J. Membr. Biol. 156: 19-24
    • (1997) J. Membr. Biol. , vol.156 , pp. 19-24
    • Norbis, F.1    Boll, M.2    Stange, G.3    Markovich, D.4    Verrey, F.5    Biber, J.6
  • 99
    • 0038162581 scopus 로고    scopus 로고
    • Arg82p is a bifunctional protein whose inositol polyphosphate kinase activity is essential for nitrogen and PHO gene expression but not for Mcm1p chaperoning in yeast
    • El Alami M., Messenguy F., Scherens B. and Dubois E. (2003) Arg82p is a bifunctional protein whose inositol polyphosphate kinase activity is essential for nitrogen and PHO gene expression but not for Mcm1p chaperoning in yeast. Mol. Microbiol. 49: 457-468
    • (2003) Mol. Microbiol. , vol.49 , pp. 457-468
    • El Alami, M.1    Messenguy, F.2    Scherens, B.3    Dubois, E.4
  • 100
    • 18844442599 scopus 로고    scopus 로고
    • A systematic high-throughput screen of a yeast deletion collection for mutants defective in PHO5 regulation
    • Huang S. and O'Shea E. K. (2005) A systematic high-throughput screen of a yeast deletion collection for mutants defective in PHO5 regulation. Genetics 169: 1859-1871
    • (2005) Genetics , vol.169 , pp. 1859-1871
    • Huang, S.1    O'Shea, E.K.2
  • 101
    • 21644489427 scopus 로고    scopus 로고
    • Plc1p, Arg82p and Kcs1p, enzymes involved in inositol pyrophosphate synthesis, are essential for phosphate regulation and polyphosphate accumulation in Saccharomyces cerevisiae
    • Auesukaree C., Tochio H., Shirakawa M., Kaneko Y. and Harashima S. (2005) Plc1p, Arg82p and Kcs1p, enzymes involved in inositol pyrophosphate synthesis, are essential for phosphate regulation and polyphosphate accumulation in Saccharomyces cerevisiae. J. Biol. Chem. 280: 25127-25133
    • (2005) J. Biol. Chem. , vol.280 , pp. 25127-25133
    • Auesukaree, C.1    Tochio, H.2    Shirakawa, M.3    Kaneko, Y.4    Harashima, S.5
  • 102
    • 0035664839 scopus 로고    scopus 로고
    • The TOR signal transduction cascade controls cellular differentiation in response to nutrients
    • Cutler N. S., Pan X., Heitman J. and Cardenas M. E. (2001) The TOR signal transduction cascade controls cellular differentiation in response to nutrients. Mol. Biol. Cell 12: 4103-4113
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4103-4113
    • Cutler, N.S.1    Pan, X.2    Heitman, J.3    Cardenas, M.E.4
  • 103
    • 0032915417 scopus 로고    scopus 로고
    • Regulation of ribosome biogenesis by the rapamyein-sensitive TOR-signaling pathway in Saccharomyces cerevisiae
    • Powers T. and Walter P. (1999) Regulation of ribosome biogenesis by the rapamyein-sensitive TOR-signaling pathway in Saccharomyces cerevisiae. Mol. Biol. Cell 10: 987-1000
    • (1999) Mol. Biol. Cell , vol.10 , pp. 987-1000
    • Powers, T.1    Walter, P.2
  • 104
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J. D., Higgins D. G. and Gibson T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 105
    • 0034695549 scopus 로고    scopus 로고
    • The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site
    • Bertsch U., Deschermeier C., Fanick W., Girkontaite I., Hillemeier K., Johnen H. et al. (2000) The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site. J. Biol. Chem. 275: 1557-1564
    • (2000) J. Biol. Chem. , vol.275 , pp. 1557-1564
    • Bertsch, U.1    Deschermeier, C.2    Fanick, W.3    Girkontaite, I.4    Hillemeier, K.5    Johnen, H.6
  • 106
    • 0030930307 scopus 로고    scopus 로고
    • Structural identification of the myo-inositol 1,4,5-trisphosphate-binding domain in rat brain inositol 1,4,5-trisphosphate 3-kinase
    • Togashi S., Takazawa K., Endo T., Erneux C. and Onaya T. (1997) Structural identification of the myo-inositol 1,4,5-trisphosphate-binding domain in rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 326 (Pt 1): 221-225
    • (1997) Biochem. J. , vol.326 , Issue.1 PART , pp. 221-225
    • Togashi, S.1    Takazawa, K.2    Endo, T.3    Erneux, C.4    Onaya, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.