메뉴 건너뛰기




Volumn 393, Issue 9, 2012, Pages 979-998

Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis

Author keywords

High energy phosphate; Pi uptake regulation; PP InsP5; PP2 InsP4

Indexed keywords

CYCLIN DEPENDENT KINASE; DIPHOSPHOINOSITOL PHOSPHATE DERIVATIVE; INOSITOL PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84869441865     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0133     Document Type: Conference Paper
Times cited : (73)

References (134)
  • 1
    • 84865618402 scopus 로고    scopus 로고
    • Freeware Version 11.01, Advanced Chemistry Development, Inc., Toronto, ON, Canada
    • ACD/ChemSketch. (2012). Freeware Version 11.01, Advanced Chemistry Development, Inc., Toronto, ON, Canada (www. acdlabs.com) .
    • (2012) ACD/ChemSketch
  • 2
    • 0010991556 scopus 로고
    • Cyclitol confusion
    • Agranoff, B.W. (1978). Cyclitol confusion. Trends Biochem. Sci. 3, N283 - N285.
    • (1978) Trends Biochem. , vol.3
    • Agranoff, B.W.1
  • 3
    • 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., Brocker, M., Shears, S.B., and Mayr, G.W. (1997). Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327, 553-560.
    • (1997) Biochem. J. , vol.327 , pp. 553-560
    • Albert, C.1    Safrany, S.T.2    Bembenek, M.E.3    Reddy, K.M.4    Reddy, K.5    Falck, J.6    Brocker, M.7    Shears, S.B.8    Mayr, G.W.9
  • 4
    • 33745736445 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export
    • Alcazar-Roman, A.R., Tran, E.J., Guo, S., and Wente, S.R. (2006). Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat. Cell Biol. 8, 711-716.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 711-716
    • Alcazar-Roman, A.R.1    Tran, E.J.2    Guo, S.3    Wente, S.R.4
  • 5
    • 0027460280 scopus 로고
    • Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside endoplasmic reticulum
    • Ali, N., Craxton, A., and Shears, S.B. (1993). Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside endoplasmic reticulum. J. Biol. Chem. 268, 6161-6167.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6161-6167
    • Ali, N.1    Craxton, A.2    Shears, S.B.3
  • 6
    • 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
  • 7
    • 75849158417 scopus 로고    scopus 로고
    • Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates HIV-1 Gag release
    • Azevedo, C., Burton, A., Ruiz-Mateos, E., Marsh, M., and Saiardi, A. (2009). Inositol pyrophosphate mediated pyrophosphorylation of AP3B1 regulates HIV-1 Gag release. Proc. Natl. Acad. Sci. USA 106, 21161-21166.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21161-21166
    • Azevedo, C.1    Burton, A.2    Ruiz-Mateos, E.3    Marsh, M.4    Saiardi, A.5
  • 10
    • 40649083560 scopus 로고    scopus 로고
    • Gene deletion of inositol hexakisphosphate kinase 1 reveals inositol pyrophosphate regulation of insulin secretion, growth, and spermiogenesis
    • Bhandari, R., Juluri, K.R., Resnick, A.C., and Snyder, S.H. (2008). Gene deletion of inositol hexakisphosphate kinase 1 reveals inositol pyrophosphate regulation of insulin secretion, growth, and spermiogenesis. Proc. Natl. Acad. Sci. USA 105, 2349-2353.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2349-2353
    • Bhandari, R.1    Juluri, K.R.2    Resnick, A.C.3    Snyder, S.H.4
  • 11
    • 75649152860 scopus 로고    scopus 로고
    • Growth-limiting intracellular metabolites in yeast growing under diverse nutrient limitations
    • Boer, V.M., Crutchfi eld, C.A., Bradley, P.H., Botstein, D., and Rabinowitz, J.D. (2010). Growth-limiting intracellular metabolites in yeast growing under diverse nutrient limitations. Mol. Biol. Cell 21, 198-211.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 198-211
    • Boer, V.M.1    Crutchfi Eld, C.A.2    Bradley, P.H.3    Botstein, D.4    Rabinowitz, J.D.5
  • 14
    • 0034725078 scopus 로고    scopus 로고
    • Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases
    • 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) An Expanding Nudt Family. J. Biol. Chem. , vol.275 , pp. 12730-12736
    • Caffrey, J.J.1    Safrany, S.T.2    Yang, X.3    Shears, S.B.4
  • 16
    • 0036469785 scopus 로고    scopus 로고
    • Pho85 and signaling environmental conditions
    • Carroll, A.S. and O' Shea, E.K. (2002). Pho85 and signaling environmental conditions. Trends Biochem. Sci. 27, 87-93.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 87-93
    • Carroll, A.S.1    O'Shea, E.K.2
  • 19
    • 0347722634 scopus 로고    scopus 로고
    • The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase
    • Chang, S.C., Miller, A.L., Feng, Y., Wente, S.R., and Majerus, P.W. (2002). The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem. 277, 43836-43843.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43836-43843
    • Chang, S.C.1    Miller, A.L.2    Feng, Y.3    Wente, S.R.4    Majerus, P.W.5
  • 20
    • 24344495294 scopus 로고    scopus 로고
    • Signal transduction during environmental stress: InsP8 operates within highly restricted contexts
    • Choi, K., Mollapour, E., and Shears, S.B. (2005). Signal transduction during environmental stress: InsP8 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
  • 21
    • 35648948848 scopus 로고    scopus 로고
    • Purifi cation, sequencing, and molecular identifi cation of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress
    • Choi, J.H., Williams, J., Cho, J., Falck, J.R., and Shears, S.B. (2007). Purifi cation, sequencing, and molecular identifi cation of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress. J. Biol. Chem. 282, 30763-30775.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30763-30775
    • Choi, J.H.1    Williams, J.2    Cho, J.3    Falck, J.R.4    Shears, S.B.5
  • 22
    • 47949131441 scopus 로고    scopus 로고
    • Cellular energetic status supervises the synthesis of bis-diphosphoinositol tetrakisphosphate independently of AMP-activated protein kinase
    • Choi, K., Mollapour, E., Choi, J.H., and Shears, S.B. (2008). Cellular energetic status supervises the synthesis of bis-diphosphoinositol tetrakisphosphate independently of AMP-activated protein kinase. Mol. Pharmacol. 74, 527-536.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 527-536
    • Choi, K.1    Mollapour, E.2    Choi, J.H.3    Shears, S.B.4
  • 24
    • 0030684148 scopus 로고    scopus 로고
    • Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase
    • Craxton, A., Caffrey, J.J., Burkhart, W., Safrany, S.T., and Shears, S.B. (1997). Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328, 75-81.
    • (1997) Biochem. J. , vol.328 , pp. 75-81
    • Craxton, A.1    Caffrey, J.J.2    Burkhart, W.3    Safrany, S.T.4    Shears, S.B.5
  • 25
    • 0033084143 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1
    • Currie, R.A., Walker, K.S., Gray, A., Deak, M., Casamayor, A., Downes, C.P., Cohen, P., Alessi, D.R., and Lucocq, J. (1999). Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1. Biochem. J. 337, 575-583.
    • (1999) Biochem. J. , vol.337 , pp. 575-583
    • Currie, R.A.1    Walker, K.S.2    Gray, A.3    Deak, M.4    Casamayor, A.5    Downes, C.P.6    Cohen, P.7    Alessi, D.R.8    Lucocq, J.9
  • 27
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs, T.A., Tainer, J.A., and Lees-Miller, S.P. (2010). A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair (Amst.) 9, 1307-1314.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 28
    • 11144252845 scopus 로고    scopus 로고
    • PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway
    • Dokladda, K., Green, K.A., Pan, D.A., and Hardie, D.G. (2005). PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway. FEBS Lett. 579, 236-240.
    • (2005) Febs Lett. , vol.579 , pp. 236-240
    • Dokladda, K.1    Green, K.A.2    Pan, D.A.3    Hardie, D.G.4
  • 30
    • 67149111580 scopus 로고    scopus 로고
    • Adenylate kinase and AMP signaling networks: Metabolic monitoring, signal communication and body energy sensing
    • Dzeja, P. and Terzic, A. (2009). Adenylate kinase and AMP signaling networks: metabolic monitoring, signal communication and body energy sensing. Int. J. Mol. Sci. 10, 1729-1772.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1729-1772
    • Dzeja, P.1    Terzic, A.2
  • 31
    • 0037112834 scopus 로고    scopus 로고
    • Functional interaction between DNA-PKcs and telomerase in telomere length maintenance
    • Espejel, S., Franco, S., Sgura, A., Gae, D., Bailey, S.M., Taccioli, G.E., and Blasco, M.A. (2002). Functional interaction between DNA-PKcs and telomerase in telomere length maintenance. EMBO J. 21, 6275-6287.
    • (2002) Embo J. , vol.21 , pp. 6275-6287
    • Espejel, S.1    Franco, S.2    Sgura, A.3    Gae, D.4    Bailey, S.M.5    Taccioli, G.E.6    Blasco, M.A.7
  • 32
    • 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
  • 33
    • 35649018626 scopus 로고    scopus 로고
    • Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases
    • Fridy, P.C., Otto, J.C., Dollins, D.E., and York, J.D. (2007). Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases. J. Biol. Chem. 282, 30754-30762.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30754-30762
    • Fridy, P.C.1    Otto, J.C.2    Dollins, D.E.3    York, J.D.4
  • 34
    • 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, 583-590.
    • (1993) Biochem. J. , vol.293 , pp. 583-590
    • Glennon, M.C.1    Shears, S.B.2
  • 35
    • 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
  • 36
    • 0019013983 scopus 로고
    • Noninvasive 31 P NMR probes of free Mg 2 +, MgATP, and MgADP in intact Ehrlich ascites tumor cells
    • Gupta, R.K. and Yushok, W.D. (1980). Noninvasive 31 P NMR probes of free Mg 2 +, MgATP, and MgADP in intact Ehrlich ascites tumor cells. Proc. Natl. Acad. Sci. USA 77, 2487-2491.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2487-2491
    • Gupta, R.K.1    Yushok, W.D.2
  • 37
    • 80054698886 scopus 로고    scopus 로고
    • Effect of the inositol polyphosphate InsP(6) on DNA-PK-dependent phosphorylation
    • Hanakahi, L. (2011). Effect of the inositol polyphosphate InsP(6) on DNA-PK-dependent phosphorylation. Mol. Cancer Res. 9, 1366-1376.
    • (2011) Mol. Cancer Res. , vol.9 , pp. 1366-1376
    • Hanakahi, L.1
  • 38
    • 33845667820 scopus 로고    scopus 로고
    • Phosphate transfer from inositol pyrophosphates InsP5PP and InsP4(PP)2: A semi-empirical investigation
    • Hand, C.E. and Honek, J.F. (2007). Phosphate transfer from inositol pyrophosphates InsP5PP and InsP4(PP)2: a semi-empirical investigation. Bioorg. Med. Chem. Lett. 17, 183-188.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 183-188
    • Hand, C.E.1    Honek, J.F.2
  • 39
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • Hardie, D.G. (2011). AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev. 25, 1895-1908.
    • (2011) Genes Dev. , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 40
    • 0037031921 scopus 로고    scopus 로고
    • An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase
    • Hidaka, K., Caffrey, J.J., Hua, L., Zhang, T., Falck, J.R., Nickel, G.C., Carrel, L., Barnes, L.D., and Shears, S.B. (2002). An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase. J. Biol. Chem. 277, 32730-32738.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32730-32738
    • Hidaka, K.1    Caffrey, J.J.2    Hua, L.3    Zhang, T.4    Falck, J.R.5    Nickel, G.C.6    Carrel, L.7    Barnes, L.D.8    Shears, S.B.9
  • 41
    • 20544441070 scopus 로고    scopus 로고
    • DNA repair: How to PIKK a partner
    • Hiom, K. (2005). DNA repair: how to PIKK a partner. Curr. Biol. 15, R473 - R475.
    • (2005) Curr. Biol , vol.15
    • Hiom, K.1
  • 42
    • 34748832943 scopus 로고    scopus 로고
    • Pho85, a multifunctional cyclin-dependent protein kinase in budding yeast
    • Huang, D., Friesen, H., and Andrews, B. (2007). Pho85, a multifunctional cyclin-dependent protein kinase in budding yeast. Mol. Microbiol. 66, 303-314.
    • (2007) Mol. Microbiol. , vol.66 , pp. 303-314
    • Huang, D.1    Friesen, H.2    Andrews, B.3
  • 45
    • 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
  • 46
    • 0024511763 scopus 로고
    • Numbering of atoms in myo-inositol
    • IUPAC-IUB. Biochem
    • IUPAC-IUB. (1989). Numbering of atoms in myo-inositol. Recommendations 1988. Biochem. J. 258, 1-2.
    • (1989) Recommendations 1988 , vol.258 , pp. 1-2
  • 47
    • 38349049373 scopus 로고    scopus 로고
    • Structural analysis of the carboxy terminal PH domain of pleckstrin bound to d-myo-inositol 1,2,3,5,6-pentakisphosphate
    • Jackson, S.G., Zhang, Y., Haslam, R.J., and Junop, M.S. (2007). Structural analysis of the carboxy terminal PH domain of pleckstrin bound to d -myo-inositol 1,2,3,5,6-pentakisphosphate. BMC Struct. Biol. 7, 80.
    • (2007) BMC Struct. Biol , vol.7 , pp. 80
    • Jackson, S.G.1    Zhang, Y.2    Haslam, R.J.3    Junop, M.S.4
  • 48
    • 79751535258 scopus 로고    scopus 로고
    • Inositol pentakisphosphate isomers bind PH domains with varying specifi city and inhibit phosphoinositide interactions
    • Jackson, S.G., Al-Saigh, S., Schultz, C., and Junop, M.S. (2011). Inositol pentakisphosphate isomers bind PH domains with varying specifi city and inhibit phosphoinositide interactions. BMC Struct. Biol. 11, 11.
    • (2011) BMC Struct , vol.11 , pp. 11
    • Jackson, S.G.1    Al-Saigh, S.2    Schultz, C.3    Junop, M.S.4
  • 49
    • 0028207513 scopus 로고
    • Phosphorylation of the transcription factor PHO4 by a cyclin- CDK complex, PHO80-PHO85
    • Kaffman, A., Herskowitz, I., Tjian, R., and O' Shea, E.K. (1994). Phosphorylation of the transcription factor PHO4 by a cyclin- CDK complex, PHO80-PHO85. Science 263, 1153-1156.
    • (1994) Science , vol.263 , pp. 1153-1156
    • Kaffman, A.1    Herskowitz, I.2    Tjian, R.3    O'Shea, E.K.4
  • 50
    • 33846005154 scopus 로고    scopus 로고
    • Protein kinase CK2 is inhibited by human nucleolar phosphoprotein p140 in an inositol hexakisphosphate-dependent manner
    • Kim, Y.K., Lee, K.J., Jeon, H., and Yu, Y.G. (2006). Protein kinase CK2 is inhibited by human nucleolar phosphoprotein p140 in an inositol hexakisphosphate-dependent manner. J. Biol. Chem. 281, 36752-36757.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36752-36757
    • Kim, Y.K.1    Lee, K.J.2    Jeon, H.3    Yu, Y.G.4
  • 52
    • 33646502116 scopus 로고    scopus 로고
    • If the prophet does not come to the mountain: Dynamics of signaling complexes in NF-κB activation
    • Kovalenko, A. and Wallach, D. (2006). If the prophet does not come to the mountain: dynamics of signaling complexes in NF-κB activation. Mol. Cell 22, 433-436.
    • (2006) Mol. Cell , vol.22 , pp. 433-436
    • Kovalenko, A.1    Wallach, D.2
  • 53
    • 0026732710 scopus 로고
    • Mammalian skeletal-muscle fi bers distinguished by contents of phosphocreatine, ATP, and P i
    • Kushmerick, M.J., Moerland, T.S., and Wiseman, R.W. (1992). Mammalian skeletal-muscle fi bers distinguished by contents of phosphocreatine, ATP, and P i . Proc. Natl. Acad. Sci. USA 89, 7521-7525.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7521-7525
    • Kushmerick, M.J.1    Moerland, T.S.2    Wiseman, R.W.3
  • 54
    • 0032052761 scopus 로고    scopus 로고
    • Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast
    • Kwast, K.E., Burke, P.V., and Poyton, R.O. (1998). Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast. J. Exp. Biol. 201, 1177-1195.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1177-1195
    • Kwast, K.E.1    Burke, P.V.2    Poyton, R.O.3
  • 55
    • 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, 715-720.
    • (1996) Biochem. J. , vol.315 , pp. 715-720
    • Laussmann, T.1    Eujen, R.2    Weisshuhn, C.M.3    Thiel, U.4    Vogel, G.5
  • 56
    • 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
  • 57
    • 34147092063 scopus 로고    scopus 로고
    • Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates
    • Lee, Y.S., Mulugu, S., York, J.D., and O' Shea, E.K. (2007). Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates. Science 316, 109-112.
    • (2007) Science , vol.316 , pp. 109-112
    • Lee, Y.S.1    Mulugu, S.2    York, J.D.3    O'Shea, E.K.4
  • 58
    • 52949090393 scopus 로고    scopus 로고
    • Characterization of the InsP6- dependent interaction between CK2 Nopp140
    • Lee, W.K., Lee, S.Y., Kim, W.I., Rho, Y.H., Bae, Y.S., Lee, C., Kim, I.Y., and Yu, Y.G. (2008a). Characterization of the InsP6- dependent interaction between CK2 and Nopp140. Biochem. Biophys. Res. Commun. 376, 439-444.
    • (2008) Biochem. Biophys , vol.376 , pp. 439-444
    • Lee, W.K.1    Lee, S.Y.2    Kim, W.I.3    Rho, Y.H.4    Bae, Y.S.5    Lee, C.6    Kim, I.Y.7    Yu, Y.G.8
  • 60
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M.A. and Ferguson, K.M. (2000). Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18.
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 61
    • 34248401144 scopus 로고    scopus 로고
    • Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate- metabolising Nudix hydrolases
    • Leslie, N.R., McLennan, A.G., and Safrany, S.T. (2002). Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate- metabolising Nudix hydrolases. BMC Biochem. 3, 20.
    • (2002) BMC Biochem , vol.3 , pp. 20
    • Leslie, N.R.1    McLennan, A.G.2    Safrany, S.T.3
  • 62
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • Letunic, I., Doerks, T., and Bork, P. (2012). SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40, D302 - D305.
    • (2012) Nucleic Acids Res , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 63
    • 59449101103 scopus 로고    scopus 로고
    • Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases
    • Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D., and Mayr, G.W. (2009). Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284, 1863-1872.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1863-1872
    • Lin, H.1    Fridy, P.C.2    Ribeiro, A.A.3    Choi, J.H.4    Barma, D.K.5    Vogel, G.6    Falck, J.R.7    Shears, S.B.8    York, J.D.9    Mayr, G.W.10
  • 64
    • 82255179513 scopus 로고    scopus 로고
    • Emerging roles of the SUMO pathway in development
    • Lomeli, H. and Vazquez, M. (2011). Emerging roles of the SUMO pathway in development. Cell. Mol. Life Sci. 68, 4045-4064.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 4045-4064
    • Lomeli, H.1    Vazquez, M.2
  • 65
    • 80052707792 scopus 로고    scopus 로고
    • Identifi cation of an evolutionarily conserved family of inorganic polyphosphate endopolyphosphatases
    • Lonetti, A., Szijgyarto, Z., Bosch, D., Loss, O., Azevedo, C., and Saiardi, A. (2011). Identifi cation of an evolutionarily conserved family of inorganic polyphosphate endopolyphosphatases. J. Biol. Chem. 286, 31966-31974.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31966-31974
    • Lonetti, A.1    Szijgyarto, Z.2    Bosch, D.3    Loss, O.4    Azevedo, C.5    Saiardi, A.6
  • 66
    • 38349073475 scopus 로고    scopus 로고
    • DNA damage response at functional and dysfunctional telomeres
    • Longhese, M.P. (2008). DNA damage response at functional and dysfunctional telomeres. Genes Dev. 22, 125-140.
    • (2008) Genes Dev. , vol.22 , pp. 125-140
    • Longhese, M.P.1
  • 67
    • 0141540848 scopus 로고    scopus 로고
    • Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns(3,4,5)P3 interactions
    • Luo, H.R., Huang, Y.E., Chen, J.C., Saiardi, A., Iijima, M., Ye, K., Huang, Y., Nagata, E., Devreotes, P., and Snyder, S.H. (2003). Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns(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    Huang, Y.7    Nagata, E.8    Devreotes, P.9    Snyder, S.H.10
  • 68
    • 0037192767 scopus 로고    scopus 로고
    • Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs
    • Ma, Y. and Lieber, M.R. (2002). Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs. J. Biol. Chem. 277, 10756-10759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10756-10759
    • Ma, Y.1    Lieber, M.R.2
  • 69
    • 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
  • 70
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning, B.D. and Cantley, L.C. (2007). AKT/PKB signaling: navigating downstream. Cell 129, 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 71
    • 0036806311 scopus 로고    scopus 로고
    • Evolution of protein kinase signaling from yeast to man
    • Manning, G., Plowman, G.D., Hunter, T., and Sudarsanam, S. (2002a). Evolution of protein kinase signaling from yeast to man. Trends Biochem. Sci. 27, 514-520.
    • (2002) Trends Biochem. , vol.27 , pp. 514-520
    • Manning, G.1    Plowman, G.D.2    Hunter, T.3    Sudarsanam, S.4
  • 73
    • 0024075976 scopus 로고
    • A novel metal-dye detection system permits picomolar-range h.p.l.c. analysis of inositol polyphosphates from non-radioactively labelled cell or tissue specimens
    • Mayr, G.W. (1988). A novel metal-dye detection system permits picomolar-range h.p.l.c. analysis of inositol polyphosphates from non-radioactively labelled cell or tissue specimens. Biochem. J. 254, 585-591.
    • (1988) Biochem. J. , vol.254 , pp. 585-591
    • Mayr, G.W.1
  • 74
    • 0027116062 scopus 로고
    • Phosphoinositol diphosphates - Nonenzymatic formation in vitro and occurrence in vivo in the cellular slime-mold Dictyostelium
    • Mayr, G.W., Radenberg, T., Thiel, U., Vogel, G., and Stephens, L.R. (1992). Phosphoinositol diphosphates - nonenzymatic formation in vitro and occurrence in vivo in the cellular slime-mold Dictyostelium . Carbohydr. Res. 234, 247-262.
    • (1992) Carbohydr. Res. , vol.234 , pp. 247-262
    • Mayr, G.W.1    Radenberg, T.2    Thiel, U.3    Vogel, G.4    Stephens, L.R.5
  • 75
    • 17144366551 scopus 로고    scopus 로고
    • Antiproliferative plant and synthetic polyphenolics are specifi c 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 specifi c 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
  • 76
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan, A.G. (2006). The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63, 123-143.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 78
    • 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
  • 79
    • 78649335829 scopus 로고    scopus 로고
    • Cellular regulators of protein kinase CK2
    • Montenarh, M. (2010). Cellular regulators of protein kinase CK2. Cell Tissue Res. 342, 139-146.
    • (2010) Cell Tissue Res , vol.342 , pp. 139-146
    • Montenarh, M.1
  • 80
    • 79954598438 scopus 로고    scopus 로고
    • A conserved mechanism of DEADbox ATPase activation by nucleoporins and InsP6 in mRNA export
    • Montpetit, B., Thomsen, N.D., Helmke, K.J., Seeliger, M.A., Berger, J.M., and Weis, K. (2011). A conserved mechanism of DEADbox ATPase activation by nucleoporins and InsP6 in mRNA export. Nature 472, 238-242.
    • (2011) Nature , vol.472 , pp. 238-242
    • Montpetit, B.1    Thomsen, N.D.2    Helmke, K.J.3    Seeliger, M.A.4    Berger, J.M.5    Weis, K.6
  • 81
    • 34447538402 scopus 로고    scopus 로고
    • Effect of inositol hexakisphosphate kinase 2 on transforming growth factor β-activated kinase 1 and NF-κB activation
    • Morrison, B.H., Bauer, J.A., Lupica, J.A., Tang, Z., Schmidt, H., DiDonato, J.A., and Lindner, D.J. (2007). Effect of inositol hexakisphosphate kinase 2 on transforming growth factor β-activated kinase 1 and NF-κB activation. J. Biol. Chem. 282, 15349-15356.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15349-15356
    • Morrison, B.H.1    Bauer, J.A.2    Lupica, J.A.3    Tang, Z.4    Schmidt, H.5    Didonato, J.A.6    Lindner, D.J.7
  • 82
    • 85047676330 scopus 로고
    • Acadesine: The prototype adenosine regulating agent for reducing myocardial ischaemic injury
    • Mullane, K. (1993). Acadesine: the prototype adenosine regulating agent for reducing myocardial ischaemic injury. Cardiovasc. Res. 27, 43-47.
    • (1993) Cardiovasc. Res. , vol.27 , pp. 43-47
    • Mullane, K.1
  • 85
    • 85045801771 scopus 로고
    • Numbering of atoms in myo-inositol. Recommendations 1988. Nomenclature Committee of the International Union of Biochemistry (NC-IUB)
    • NC-IUB. (1989). Numbering of atoms in myo-inositol. Recommendations 1988. Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Biochem. J. 258, 1-2.
    • (1989) Biochem. J. , vol.258 , pp. 1-2
  • 86
    • 0030897146 scopus 로고    scopus 로고
    • Identifi cation of a cDNA/protein leading to an increased P i -uptake in Xenopus laevis oocytes
    • Norbis, F., Boll, M., Stange, G., Markovich, D., Verrey, F., Biber, J., and Murer, H. (1997). Identifi cation of a cDNA/protein leading to an increased P i -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    Murer, H.7
  • 87
    • 0028842364 scopus 로고
    • Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/ AP180) and inhibits clathrin cage assembly in vitro
    • Norris, F.A., Ungewickell, E., and Majerus, P.W. (1995). Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/ 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
  • 88
    • 0033637520 scopus 로고    scopus 로고
    • New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis
    • Ogawa, N., DeRisi, J., and Brown, P.O. (2000). New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis. Mol. Biol. Cell 11, 4309-4321.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4309-4321
    • Ogawa, N.1    Derisi, J.2    Brown, P.O.3
  • 89
    • 67449093365 scopus 로고    scopus 로고
    • Characterization of a selective inhibitor of inositol hexakisphosphate kinases: Use in defi ning biological roles and metabolic relationships of inositol pyrophosphates
    • Padmanabhan, U., Dollins, D.E., Fridy, P.C., York, J.D., and Downes, C.P. (2009). Characterization of a selective inhibitor of inositol hexakisphosphate kinases: use in defi ning biological roles and metabolic relationships of inositol pyrophosphates. J. Biol. Chem. 284, 10571-10582.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10571-10582
    • Padmanabhan, U.1    Dollins, D.E.2    Fridy, P.C.3    York, J.D.4    Downes, C.P.5
  • 90
    • 33644757915 scopus 로고    scopus 로고
    • The post-translational synthesis of a polyaminederived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)
    • Park, M.H. (2006). The post-translational synthesis of a polyaminederived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A). J. Biochem. 139, 161-169.
    • (2006) J. Biochem. , vol.139 , pp. 161-169
    • Park, M.H.1
  • 91
    • 6344257046 scopus 로고    scopus 로고
    • Signaling by higher inositol polyphosphates. Synthesis of bisdiphosphoinositol tetrakisphosphate (' InsP8') is selectively activated by hyperosmotic 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 hyperosmotic 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
  • 93
    • 80052026626 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling
    • Prasad, A., Jia, Y., Chakraborty, A., Li, Y., Jain, S.K., Zhong, J., Roy, S.G., Loison, F., Mondal, S., Sakai, J., et al. (2011). Inositol hexakisphosphate kinase 1 regulates neutrophil function in innate immunity by inhibiting phosphatidylinositol-(3,4,5)-trisphosphate signaling. Nat. Immunol. 12, 752-760.
    • (2011) Nat. Immunol. , vol.12 , pp. 752-760
    • Prasad, A.1    Jia, Y.2    Chakraborty, A.3    Li, Y.4    Jain, S.K.5    Zhong, J.6    Roy, S.G.7    Loison, F.8    Mondal, S.9    Sakai, J.10
  • 94
    • 0023525741 scopus 로고
    • Ca 2 +, cAMP, and phospholipid- derived messengers in coupling mechanisms of insulin secretion
    • Prentki, M. and Matschinsky, F.M. (1987). Ca 2 +, cAMP, and phospholipid- derived messengers in coupling mechanisms of insulin secretion. Physiol. Rev. 67, 1185-1248.
    • (1987) Physiol. Rev. , vol.67 , pp. 1185-1248
    • Prentki, M.1    Matschinsky, F.M.2
  • 95
    • 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
  • 96
    • 0032536857 scopus 로고    scopus 로고
    • Turnover of bis-diphosphoinositol tetrakisphosphate in a smooth muscle cell line is regulated by β2-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 β2-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
  • 97
    • 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., and Shears, S.B. (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    Shears, S.B.7
  • 99
    • 0033581832 scopus 로고    scopus 로고
    • Synthesis of diphosphoinositol pentakisphosphate by a newly identifi ed 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 identifi ed 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
  • 101
    • 0035914367 scopus 로고    scopus 로고
    • Identifi cation and characterization of a novel inositol hexakisphosphate kinase
    • Saiardi, A., Nagata, E., Luo, H.R., Snowman, A.M., and Snyder, S.H. (2001). Identifi cation 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
  • 103
    • 13844311012 scopus 로고    scopus 로고
    • Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases
    • 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. USA , vol.102 , pp. 1911-1914
    • Saiardi, A.1    Resnick, A.C.2    Snowman, A.M.3    Wendland, B.4    Snyder, S.H.5
  • 104
    • 33645130011 scopus 로고    scopus 로고
    • Glucose signaling in Saccharomyces cerevisiae
    • Santangelo, G.M. (2006). Glucose signaling in Saccharomyces cerevisiae . Microbiol. Mol. Biol. Rev. 70, 253-282.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 253-282
    • Santangelo, G.M.1
  • 106
    • 0005614201 scopus 로고
    • Über eine neue, aus dem muskelfl eische gewonnene zuckerart
    • Scherer, J. (1850).Über eine neue, aus dem Muskelfl eische gewonnene Zuckerart. Justus Liebigs Ann. Chem. 73, 322-328.
    • (1850) Justus Liebigs Ann. Chem. , vol.73 , pp. 322-328
    • Scherer, J.1
  • 107
    • 0028052088 scopus 로고
    • Phosphateregulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81
    • Schneider, K.R., Smith, R.L., and O' Shea, E.K. (1994). Phosphateregulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81. Science 266, 122-126.
    • (1994) Science , vol.266 , pp. 122-126
    • Schneider, K.R.1    Smith, R.L.2    O'Shea, E.K.3
  • 108
    • 0032497840 scopus 로고    scopus 로고
    • The versatility of inositol phosphates as cellular signals
    • Shears, S.B. (1998). The versatility of inositol phosphates as cellular signals. Biochim. Biophys. Acta 1436, 49-67.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 49-67
    • Shears, S.B.1
  • 109
    • 76649120255 scopus 로고    scopus 로고
    • The long-awaited demonstration of protein pyrophosphorylation by IP7 in vivo
    • Acad. Sci. USA 107, E17; author reply
    • Shears, S. (2010). The long-awaited demonstration of protein pyrophosphorylation by IP7 in vivo? Proc. Natl. Acad. Sci. USA 107, E17; author reply E18.
    • Proc. Natl.
    • Shears, S.1
  • 110
    • 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
  • 111
    • 79954464059 scopus 로고    scopus 로고
    • Diphosphoinositol polyphosphates: What are the mechanisms?
    • Shears, S.B., Gokhale, N.A., Wang, H., and Zaremba, A. (2011). Diphosphoinositol polyphosphates: what are the mechanisms? Adv. Enzyme Regul. 51, 13-25.
    • (2011) Adv Enzyme Regul. , vol.51 , pp. 13-25
    • Shears, S.B.1    Gokhale, N.A.2    Wang, H.3    Zaremba, A.4
  • 112
    • 69249229528 scopus 로고    scopus 로고
    • Telomere length regulation: Coupling DNA end processing to feedback regulation of telomerase
    • Shore, D. and Bianchi, A. (2009). Telomere length regulation: coupling DNA end processing to feedback regulation of telomerase. EMBO J. 28, 2309-2322.
    • (2009) Embo J. , vol.28 , pp. 2309-2322
    • Shore, D.1    Bianchi, A.2
  • 114
    • 4243190170 scopus 로고    scopus 로고
    • Partially phosphorylated Pho4 activates transcription of a subset of phosphate-responsive genes
    • Springer, M., Wykoff, D.D., Miller, N., and O' Shea, E.K. (2003). Partially phosphorylated Pho4 activates transcription of a subset of phosphate-responsive genes. PLoS Biol. 1, E28.
    • (2003) PLoS Biol. , vol.1
    • Springer, M.1    Wykoff, D.D.2    Miller, N.3    O'Shea, E.K.4
  • 115
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • Steinberg, G.R. and Kemp, B.E. (2009). AMPK in health and disease. Physiol. Rev. 89, 1025-1078.
    • (2009) Physiol. Rev. , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 116
    • 0027536427 scopus 로고
    • The detection, purifi cation, 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., Jackson, T.R., Hawkins, P.T., and Mayr, G.W. (1993). The detection, purifi cation, 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    Jackson, T.R.7    Hawkins, P.T.8    Mayr, G.W.9
  • 117
    • 0020827065 scopus 로고
    • Regulation of cytosolic free Ca 2 + concentration in acinar cells of rat pancreas
    • Streb, H. and Schulz, I. (1983). Regulation of cytosolic free Ca 2 + concentration in acinar cells of rat pancreas. Am. J. Physiol. 245, G347 - G357.
    • (1983) Am. J. Physiol , vol.245
    • Streb, H.1    Schulz, I.2
  • 118
    • 0020643801 scopus 로고
    • Release of Ca 2 + from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • Streb, H., Irvine, R.F., Berridge, M.J., and Schulz, I. (1983). Release of Ca 2 + from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306, 67-69.
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 119
    • 0028127291 scopus 로고
    • The intracellular distribution of inositol polyphosphates in HL60 promyeloid cells
    • Stuart, J.A., Anderson, K.L., French, P.J., Kirk, C.J., and Michell, R.H. (1994). The intracellular distribution of inositol polyphosphates in HL60 promyeloid cells. Biochem. J. 303, 517-525.
    • (1994) Biochem. J. , vol.303 , pp. 517-525
    • Stuart, J.A.1    Anderson, K.L.2    French, P.J.3    Kirk, C.J.4    Michell, R.H.5
  • 120
    • 0028073143 scopus 로고
    • Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase
    • Sullivan, J.E., Brocklehurst, K.J., Marley, A.E., Carey, F., Carling, D., and Beri, R.K. (1994). Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase. FEBS Lett. 353, 33-36.
    • (1994) Febs Lett. , vol.353 , pp. 33-36
    • Sullivan, J.E.1    Brocklehurst, K.J.2    Marley, A.E.3    Carey, F.4    Carling, D.5    Beri, R.K.6
  • 121
    • 81055137383 scopus 로고    scopus 로고
    • Infl uence of inositol pyrophosphates on cellular energy dynamics
    • Szijgyarto, Z., Garedew, A., Azevedo, C., and Saiardi, A. (2011). Infl uence of inositol pyrophosphates on cellular energy dynamics. Science 334, 802-805.
    • (2011) Science , vol.334 , pp. 802-805
    • Szijgyarto, Z.1    Garedew, A.2    Azevedo, C.3    Saiardi, A.4
  • 122
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specifi city in protein phosphorylation
    • Ubersax, J.A. and Ferrell, J.E., Jr. (2007). Mechanisms of specifi city in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8, 530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 123
    • 33745601407 scopus 로고    scopus 로고
    • The behaviour of myo-inositol hexakisphosphate in the presence of magnesium(II) and calcium(II): Protein-free soluble InsP(6) is limited to 49 μm under cytosolic/ nuclear conditions
    • Veiga, N., Torres, J., Dominguez, S., Mederos, A., Irvine, R.F., Diaz, A., and Kremer, C. (2006). The behaviour of myo-inositol hexakisphosphate in the presence of magnesium(II) and calcium(II): protein-free soluble InsP(6) is limited to 49 μM under cytosolic/ nuclear conditions. J. Inorg. Biochem. 100, 1800-1810.
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 1800-1810
    • Veiga, N.1    Torres, J.2    Dominguez, S.3    Mederos, A.4    Irvine, R.F.5    Diaz, A.6    Kremer, C.7
  • 124
    • 23844551508 scopus 로고    scopus 로고
    • Increased levels of inositol hexakisphosphate (InsP6) protect HEK293 cells from tumor necrosis factor (α)- and Fas-induced apoptosis
    • Verbsky, J. and Majerus, P.W. (2005). Increased levels of inositol hexakisphosphate (InsP6) protect HEK293 cells from tumor necrosis factor (α)- and Fas-induced apoptosis. J. Biol. Chem. 280, 29263-29268.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29263-29268
    • Verbsky, J.1    Majerus, P.W.2
  • 125
    • 0037199965 scopus 로고    scopus 로고
    • The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
    • Verbsky, J.W., Wilson, M.P., Kisseleva, M.V., Majerus, P.W., and Wente, S.R. (2002). The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase. J. Biol. Chem. 277, 31857-31862.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31857-31862
    • Verbsky, J.W.1    Wilson, M.P.2    Kisseleva, M.V.3    Majerus, P.W.4    Wente, S.R.5
  • 127
  • 128
    • 83655198346 scopus 로고    scopus 로고
    • Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding
    • Wang, H., Falck, J.R., Hall, T.M., and Shears, S.B. (2011). Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8, 111-116.
    • (2011) Nat. Chem. Biol. , vol.8 , pp. 111-116
    • Wang, H.1    Falck, J.R.2    Hall, T.M.3    Shears, S.B.4
  • 129
    • 33748986212 scopus 로고    scopus 로고
    • ATP synthase: Subunit-subunit interactions in the stator stalk
    • Weber, J. (2006). ATP synthase: subunit-subunit interactions in the stator stalk. Biochim. Biophys. Acta 1757, 1162-1170.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1162-1170
    • Weber, J.1
  • 130
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich, C.S., Erzberger, J.P., Flick, J.S., Berger, J.M., Thorner, J., and Weis, K. (2006). Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat. Cell Biol. 8, 668-676.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 668-676
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, J.5    Weis, K.6
  • 131
    • 0028925007 scopus 로고
    • Inhibition of clathrin assembly by high-affi nity binding of specifi c inositol polyphosphates to the synapse-specifi c clathrin assembly protein Ap-3
    • Ye, W.L., Ali, N., Bembenek, M.E., Shears, S.B., and Lafer, E.M. (1995). Inhibition of clathrin assembly by high-affi nity binding of specifi c inositol polyphosphates to the synapse-specifi c clathrin assembly protein Ap-3. J. Biol. Chem. 270, 1564-1568.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1564-1568
    • Ye, W.L.1    Ali, N.2    Bembenek, M.E.3    Shears, S.B.4    Lafer, E.M.5
  • 134
    • 2942577753 scopus 로고    scopus 로고
    • Aggravation of necrotic death of glucose-deprived cells by the MEK1 inhibitors U0126 and PD184161 through depletion of ATP
    • Yung, H.W., Wyttenbach, A., and Tolkovsky, A.M. (2004). Aggravation of necrotic death of glucose-deprived cells by the MEK1 inhibitors U0126 and PD184161 through depletion of ATP. Biochem. Pharmacol. 68, 351-360.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 351-360
    • Yung, H.W.1    Wyttenbach, A.2    Tolkovsky, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.