메뉴 건너뛰기




Volumn 39, Issue , 2006, Pages 263-290

Inositol phosphates and phosphoinositides in health and disease

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84934876809     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (170)
  • 1
    • 4444374646 scopus 로고    scopus 로고
    • OCRL mutation analysis in Italian patients with Lowe syndrome
    • Addis, M., Loi, M., Lepiani, C., Cau, M., and Melis, M. A., 2004, OCRL mutation analysis in Italian patients with Lowe syndrome. Hum. Mutat. 23: 524-525.
    • (2004) Hum. Mutat , vol.23 , pp. 524-525
    • Addis, M.1    Loi, M.2    Lepiani, C.3    Cau, M.4    Melis, M.A.5
  • 2
    • 0031031312 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease: Mechanisms and therapeutic strategies
    • Aisen, P. S., 1997, Inflammation and Alzheimer's disease: Mechanisms and therapeutic strategies. Gerontology 43: 143-149.
    • (1997) Gerontology , vol.43 , pp. 143-149
    • Aisen, P.S.1
  • 3
    • 0008836304 scopus 로고    scopus 로고
    • Lithium, phosphatidylinositol signaling, and bipolar disorder
    • American Psychiatric Press, Manji, H.K., Bowden, C.L., and Belmaker, R.H. (eds.), Inc., Washington, DC
    • Atack, J. R., 2000, Lithium, phosphatidylinositol signaling, and bipolar disorder. In: Manji, H. K., Bowden, C. L., and Belmaker, R. H. (eds.), Bipolar Medications: Mechanism of Action. American Psychiatric Press, Inc., Washington, DC.
    • (2000) Bipolar Medications: Mechanism of Action
    • Atack, J.R.1
  • 4
    • 0026742127 scopus 로고
    • The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
    • Attree, O., Olivos, I. M., Okabe, I., Bailey, L. C., Nelson, D. L., Lewis, R. A., McInnes, R. R., and Nussbaum, R. L., 1992, The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature 358: 239-242.
    • (1992) Nature , vol.358 , pp. 239-242
    • Attree, O.1    Olivos, I.M.2    Okabe, I.3    Bailey, L.C.4    Nelson, D.L.5    Lewis, R.A.6    McInnes, R.R.7    Nussbaum, R.L.8
  • 6
    • 0033588069 scopus 로고    scopus 로고
    • Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme
    • Bachhawat, N., and Mande, S. C., 1999, Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme. J. Mol. Biol. 291: 531-536.
    • (1999) J. Mol. Biol , vol.291 , pp. 531-536
    • Bachhawat, N.1    Mande, S.C.2
  • 8
    • 3342900250 scopus 로고    scopus 로고
    • Bipolar disorder
    • Belmaker, R. H., 2004, Bipolar disorder. N. Engl. J. Med. 351: 476-486.
    • (2004) N. Engl. J. Med , vol.351 , pp. 476-486
    • Belmaker, R.H.1
  • 9
    • 0037096759 scopus 로고    scopus 로고
    • Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1
    • Berger, P., Bonneick, S., Willi, S., Wymann, M., and Suter, U., 2002, Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum. Mol. Genet. 11: 1569-1579.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1569-1579
    • Berger, P.1    Bonneick, S.2    Willi, S.3    Wymann, M.4    Suter, U.5
  • 10
    • 0023062987 scopus 로고
    • Inositol trisphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M. J., 1987, Inositol trisphosphate and diacylglycerol: Two interacting second messengers. Annu. Rev. Biochem. 56: 159-193.
    • (1987) Annu. Rev. Biochem , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 11
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J., 1993, Inositol trisphosphate and calcium signalling. Nature 361: 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 12
    • 0020465411 scopus 로고
    • Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands
    • Berridge, M. J., Downes, C. P., and Hanley, M. R., 1982, Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands. Biochem. J. 206: 587-595.
    • (1982) Biochem. J , vol.206 , pp. 587-595
    • Berridge, M.J.1    Downes, C.P.2    Hanley, M.R.3
  • 13
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge, M. J., and Irvine, R. F., 1989, Inositol phosphates and cell signalling. Nature 341: 197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 14
    • 0034805868 scopus 로고    scopus 로고
    • The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3, 4, 5-trisphosphate levels in CHO-IR cells stimulated by insulin
    • Blero, D., De Smedt, F., Pesesse, X., Paternotte, N., Moreau, C., Payrastre, B., and Erneux, C., 2001, The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3, 4, 5-trisphosphate levels in CHO-IR cells stimulated by insulin. Biochem. Biophys. Res. Commun. 282: 839-843.
    • (2001) Biochem. Biophys. Res. Commun , vol.282 , pp. 839-843
    • Blero, D.1    De Smedt, F.2    Pesesse, X.3    Paternotte, N.4    Moreau, C.5    Payrastre, B.6    Erneux, C.7
  • 15
    • 0034703432 scopus 로고    scopus 로고
    • Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway
    • Blondeau, F., Laporte, J., Bodin, S., Superti-Furga, G., Payrastre, B., and Mandel, J. L., 2000, Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. Hum. Mol. Genet. 9: 2223-2229.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2223-2229
    • Blondeau, F.1    Laporte, J.2    Bodin, S.3    Superti-Furga, G.4    Payrastre, B.5    Mandel, J.L.6
  • 16
    • 0037596986 scopus 로고    scopus 로고
    • Neurotransmission and the central nervous system
    • Hradman, J.G., Limbird, L.E., and Gilman, A.G. (eds.), 10th ed., Section III, Chapter 12. The McGraw-Hill companies
    • Bloom, F. E., 2001, Neurotransmission and the central nervous system. In: Hradman, J. G., Limbird, L. E., and Gilman, A. G. (eds.), Goodman and Gilman's The Pharmacological Basis of Therapeutics, 10th ed., Section III, Chapter 12. The McGraw-Hill companies.
    • (2001) Goodman and Gilman's The Pharmacological Basis of Therapeutics
    • Bloom, F.E.1
  • 18
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer, R., Gray, S., and Kawas, C., 1998, Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am. J. Public Health 88: 1337-1342.
    • (1998) Am. J. Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 20
    • 0032571257 scopus 로고    scopus 로고
    • Insulin increases the association of Akt-2 with Glut4-containing vesicles
    • Calera, M. R., Martinez, C., Liu, H., Jack, A. K., Birnbaum, M. J., and Pilch, P. F., 1998, Insulin increases the association of Akt-2 with Glut4-containing vesicles. J. Biol. Chem. 273: 7201-7204.
    • (1998) J. Biol. Chem , vol.273 , pp. 7201-7204
    • Calera, M.R.1    Martinez, C.2    Liu, H.3    Jack, A.K.4    Birnbaum, M.J.5    Pilch, P.F.6
  • 21
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C., 2002, The phosphoinositide 3-kinase pathway. Science 296: 1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 22
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley, L. C., and Neel, B. G., 1999, New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. U. S. A. 96: 4240-4245.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 23
    • 0032730257 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes
    • Carman, G. M., and Henry, S. A., 1999, Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes. Prog. Lipid Res. 38: 361-399.
    • (1999) Prog. Lipid Res , vol.38 , pp. 361-399
    • Carman, G.M.1    Henry, S.A.2
  • 24
    • 0033014180 scopus 로고    scopus 로고
    • The mood-stabilizing agent valproate inhibits the activity of glycogen synthase kinase-3
    • Chen, G., Huang, L. D., Jiang, Y. M., and Manji, H. K., 1999a, The mood-stabilizing agent valproate inhibits the activity of glycogen synthase kinase-3. J. Neurochem. 72: 1327-1330.
    • (1999) J. Neurochem , vol.72 , pp. 1327-1330
    • Chen, G.1    Huang, L.D.2    Jiang, Y.M.3    Manji, H.K.4
  • 25
    • 0032956630 scopus 로고    scopus 로고
    • The mood-stabilizing agents lithium and valproate robustly increase the levels of the neuroprotective protein bcl-2 in the CNS
    • Chen, G., Zeng, W. Z., Yuan, P. X., Huang, L. D., Jiang, Y. M., Zhao, Z. H., and Manji, H. K., 1999b, The mood-stabilizing agents lithium and valproate robustly increase the levels of the neuroprotective protein bcl-2 in the CNS. J. Neurochem. 72: 879-882.
    • (1999) J. Neurochem , vol.72 , pp. 879-882
    • Chen, G.1    Zeng, W.Z.2    Yuan, P.X.3    Huang, L.D.4    Jiang, Y.M.5    Zhao, Z.H.6    Manji, H.K.7
  • 26
    • 0034634004 scopus 로고    scopus 로고
    • Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase
    • Chen, L., Zhou, C., Yang, H., and Roberts, M. F., 2000, Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase. Biochemistry 39: 12415-12423.
    • (2000) Biochemistry , vol.39 , pp. 12415-12423
    • Chen, L.1    Zhou, C.2    Yang, H.3    Roberts, M.F.4
  • 28
    • 0023654039 scopus 로고
    • The metabolism of tris-and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes
    • Connolly, T. M., Bansal, V. S., Bross, T. E., Irvine, R. F., and Majerus, P. W., 1987, The metabolism of tris-and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes. J. Biol. Chem. 262: 2146-2149.
    • (1987) J. Biol. Chem , vol.262 , pp. 2146-2149
    • Connolly, T.M.1    Bansal, V.S.2    Bross, T.E.3    Irvine, R.F.4    Majerus, P.W.5
  • 29
    • 0030833392 scopus 로고    scopus 로고
    • Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy
    • de Gouyon, B. M., Zhao, W., Laporte, J., Mandel, J. L., Metzenberg, A., and Herman, G. E., 1997, Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy. Hum. Mol. Genet. 6: 1499-1504.
    • (1997) Hum. Mol. Genet , vol.6 , pp. 1499-1504
    • de Gouyon, B.M.1    Zhao, W.2    Laporte, J.3    Mandel, J.L.4    Metzenberg, A.5    Herman, G.E.6
  • 31
    • 0034134216 scopus 로고    scopus 로고
    • Ocrl1, a PtdIns(4, 5)P(2) 5-phosphatase, is localized to the trans-Golgi network of fibroblasts and epithelial cells
    • Dressman, M. A., Olivos-Glander, I. M., Nussbaum, R. L., and Suchy, S. F., 2000, Ocrl1, a PtdIns(4, 5)P(2) 5-phosphatase, is localized to the trans-Golgi network of fibroblasts and epithelial cells. J. Histochem. Cytochem. 48: 179-190.
    • (2000) J. Histochem. Cytochem , vol.48 , pp. 179-190
    • Dressman, M.A.1    Olivos-Glander, I.M.2    Nussbaum, R.L.3    Suchy, S.F.4
  • 32
    • 0038250543 scopus 로고    scopus 로고
    • IP-6 & inosito: Adjuvant chemotherapy of colon cancer. A pilot clinical trial
    • Druzijanic, N., Juricic, J., Perko, Z., and Kraljevic, D., 2002, IP-6 & inosito: Adjuvant chemotherapy of colon cancer. A pilot clinical trial. Rev. Oncologia 4: 171.
    • (2002) Rev. Oncologia , vol.4
    • Druzijanic, N.1    Juricic, J.2    Perko, Z.3    Kraljevic, D.4
  • 33
    • 0030611201 scopus 로고    scopus 로고
    • Inositol hexakisphosphate stimulates non-Ca2+-mediated and primes Ca2+-mediated exocytosis of insulin by activation of protein kinase C
    • Efanov, A. M., Zaitsev, S. V., and Berggren, P. O., 1997, Inositol hexakisphosphate stimulates non-Ca2+-mediated and primes Ca2+-mediated exocytosis of insulin by activation of protein kinase C. Proc. Natl. Acad. Sci. U. S. A. 94: 4435-4439.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 4435-4439
    • Efanov, A.M.1    Zaitsev, S.V.2    Berggren, P.O.3
  • 34
    • 0038732463 scopus 로고    scopus 로고
    • Phytic acid (IP6), novel broad spectrum anti-neoplastic agent: A systematic review
    • Fox, C. H., and Eberl, M., 2002, Phytic acid (IP6), novel broad spectrum anti-neoplastic agent: A systematic review. Complement. Ther. Med. 10: 229-234.
    • (2002) Complement. Ther. Med , vol.10 , pp. 229-234
    • Fox, C.H.1    Eberl, M.2
  • 35
    • 0037111475 scopus 로고    scopus 로고
    • Evidence that SHIP-1 contributes to phosphatidylinositol 3, 4, 5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors
    • Freeburn, R. W., Wright, K. L., Burgess, S. J., Astoul, E., Cantrell, D. A., and Ward, S. G., 2002, Evidence that SHIP-1 contributes to phosphatidylinositol 3, 4, 5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors. J. Immunol. 169: 5441-5450.
    • (2002) J. Immunol , vol.169 , pp. 5441-5450
    • Freeburn, R.W.1    Wright, K.L.2    Burgess, S.J.3    Astoul, E.4    Cantrell, D.A.5    Ward, S.G.6
  • 36
    • 0033785307 scopus 로고    scopus 로고
    • Synaptic plasticity in hippocampal CA1 neurons of mice lacking type 1 inositol-1, 4, 5-trisphosphate receptors
    • Fujii, S., Matsumoto, M., Igarashi, K., Kato, H., and Mikoshiba, K., 2000, Synaptic plasticity in hippocampal CA1 neurons of mice lacking type 1 inositol-1, 4, 5-trisphosphate receptors. Learn. Mem. 7: 312-320.
    • (2000) Learn. Mem , vol.7 , pp. 312-320
    • Fujii, S.1    Matsumoto, M.2    Igarashi, K.3    Kato, H.4    Mikoshiba, K.5
  • 37
    • 0028978364 scopus 로고
    • Diminished [3H]inositol(1, 4, 5)P3 but not [3H]inositol(1, 3, 4, 5)P4 binding in Alzheimer's disease brain
    • Garlind, A., Cowburn, R. F., Forsell, C., Ravid, R., Winblad, B., and Fowler, C. J., 1995, Diminished [3H]inositol(1, 4, 5)P3 but not [3H]inositol(1, 3, 4, 5)P4 binding in Alzheimer's disease brain. Brain Res. 681: 160-166.
    • (1995) Brain Res , vol.681 , pp. 160-166
    • Garlind, A.1    Cowburn, R.F.2    Forsell, C.3    Ravid, R.4    Winblad, B.5    Fowler, C.J.6
  • 38
    • 0030937114 scopus 로고    scopus 로고
    • The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood
    • Geier, S. J., Algate, P. A., Carlberg, K., Flowers, D., Friedman, C., Trask, B., and Rohrschneider, L. R., 1997, The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood 89: 1876-1885.
    • (1997) Blood , vol.89 , pp. 1876-1885
    • Geier, S.J.1    Algate, P.A.2    Carlberg, K.3    Flowers, D.4    Friedman, C.5    Trask, B.6    Rohrschneider, L.R.7
  • 39
    • 10644255687 scopus 로고    scopus 로고
    • AR-A014418, a selective GSK-3 inhibitor, produces antidepressant-like effects in the forced swim test
    • Gould, T. D., Einat, H., Bhat, R., and Manji, H. K., 2004c, AR-A014418, a selective GSK-3 inhibitor, produces antidepressant-like effects in the forced swim test. Int. J. Neuropsychopharmacol. 1-4.
    • (2004) Int. J. Neuropsychopharmacol , pp. 1-4
    • Gould, T.D.1    Einat, H.2    Bhat, R.3    Manji, H.K.4
  • 40
    • 4243196940 scopus 로고    scopus 로고
    • Emerging experimental therapeutics for bipolar disorder: Insights from the molecular and cellular actions of current mood stabilizers
    • Gould, T. D., Quiroz, J. A., Singh, J., Zarate, C. A., and Manji, H. K., 2004a, Emerging experimental therapeutics for bipolar disorder: Insights from the molecular and cellular actions of current mood stabilizers. Mol. Psychiatry 9: 734-755.
    • (2004) Mol. Psychiatry , vol.9 , pp. 734-755
    • Gould, T.D.1    Quiroz, J.A.2    Singh, J.3    Zarate, C.A.4    Manji, H.K.5
  • 41
    • 1442284539 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3: A target for novel bipolar disorder treatments
    • Gould, T. D., Zarate, C. A., and Manji, H. K., 2004b, Glycogen synthase kinase-3: A target for novel bipolar disorder treatments. J. Clin. Psychiatry. 65: 10-21.
    • (2004) J. Clin. Psychiatry , vol.65 , pp. 10-21
    • Gould, T.D.1    Zarate, C.A.2    Manji, H.K.3
  • 42
    • 16544365907 scopus 로고    scopus 로고
    • Dietary myo-inositol hexaphosphate prevents dystrophic calcifications in soft tissues: A pilot study in Wistar rats
    • Grases, F., Perello, J., Prieto, R. M., Simonet, B. M., and Torres, J. J., 2004, Dietary myo-inositol hexaphosphate prevents dystrophic calcifications in soft tissues: A pilot study in Wistar rats. Life Sci. 75: 11-19.
    • (2004) Life Sci , vol.75 , pp. 11-19
    • Grases, F.1    Perello, J.2    Prieto, R.M.3    Simonet, B.M.4    Torres, J.J.5
  • 43
    • 0019127799 scopus 로고
    • The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
    • Hallcher, L. M., and Sherman, W. R., 1980, The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem. 255: 10896-10901.
    • (1980) J. Biol. Chem , vol.255 , pp. 10896-10901
    • Hallcher, L.M.1    Sherman, W.R.2
  • 44
    • 0009713456 scopus 로고    scopus 로고
    • Decreased inositol (1, 4, 5)-trisphosphate receptor levels in Alzheimer's disease cerebral cortex: Selectivity of changes and possible correlation to pathological severity
    • Haug, L. S., Ostvold, A. C., Cowburn, R. F., Garlind, A., Winblad, B., Bogdanovich, N., and Walaas, S. I., 1996, Decreased inositol (1, 4, 5)-trisphosphate receptor levels in Alzheimer's disease cerebral cortex: Selectivity of changes and possible correlation to pathological severity. Neurodegeneration 5: 169-176.
    • (1996) Neurodegeneration , vol.5 , pp. 169-176
    • Haug, L.S.1    Ostvold, A.C.2    Cowburn, R.F.3    Garlind, A.4    Winblad, B.5    Bogdanovich, N.6    Walaas, S.I.7
  • 45
    • 0027484499 scopus 로고
    • Inhibition of iron-catalysed hydroxyl radical formation by inositol polyphosphates: A possible physiological function for myo-inositol hexakisphosphate
    • Hawkins, P. T., Poyner, D. R., Jackson, T. R., Letcher, A. J., Lander, D. A., and Irvine, R. F., 1993, Inhibition of iron-catalysed hydroxyl radical formation by inositol polyphosphates: A possible physiological function for myo-inositol hexakisphosphate. Biochem. J. 294(Pt 3): 929-934.
    • (1993) Biochem. J , vol.294 , pp. 929-934
    • Hawkins, P.T.1    Poyner, D.R.2    Jackson, T.R.3    Letcher, A.J.4    Lander, D.A.5    Irvine, R.F.6
  • 47
    • 0036159210 scopus 로고    scopus 로고
    • Characterization of mutations in fifty North American patients with X-linked myotubular myopathy
    • Herman, G. E., Kopacz, K., Zhao, W., Mills, P. L., Metzenberg, A., and Das, S., 2002, Characterization of mutations in fifty North American patients with X-linked myotubular myopathy. Hum. Mutat. 19: 114-121.
    • (2002) Hum. Mutat , vol.19 , pp. 114-121
    • Herman, G.E.1    Kopacz, K.2    Zhao, W.3    Mills, P.L.4    Metzenberg, A.5    Das, S.6
  • 48
    • 0022272288 scopus 로고
    • Inositol tetrakis-and pentakisphosphates in GH4 cells
    • Heslop, J. P., Irvine, R. F., Tashjian, A. H., Jr., and Berridge, M. J., 1985, Inositol tetrakis-and pentakisphosphates in GH4 cells. J. Exp. Biol. 119: 395-401.
    • (1985) J. Exp. Biol , vol.119 , pp. 395-401
    • Heslop, J.P.1    Irvine, R.F.2    Tashjian, A.H.3    Berridge, M.J.4
  • 49
    • 0023705726 scopus 로고
    • Properties of inositol polyphosphate 1-phosphatase
    • Inhorn, R. C., and Majerus, P. W., 1988, Properties of inositol polyphosphate 1-phosphatase. J. Biol. Chem. 263: 14559-14565.
    • (1988) J. Biol. Chem , vol.263 , pp. 14559-14565
    • Inhorn, R.C.1    Majerus, P.W.2
  • 50
    • 0021678647 scopus 로고
    • Inositol trisphosphates in carbachol-stimulated rat parotid glands
    • Irvine, R. F., Letcher, A. J., Lander, D. J., and Downes, C. P., 1984, Inositol trisphosphates in carbachol-stimulated rat parotid glands. Biochem. J. 223: 237-243.
    • (1984) Biochem. J , vol.223 , pp. 237-243
    • Irvine, R.F.1    Letcher, A.J.2    Lander, D.J.3    Downes, C.P.4
  • 51
    • 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
  • 52
    • 0029830687 scopus 로고    scopus 로고
    • A biologic function for an "orphan" messenger: D-myo-inositol 3, 4, 5, 6-tetrakisphosphate selectively blocks epithelial calcium-activated chloride channels
    • Ismailov, II, Fuller, C. M., Berdiev, B. K., Shlyonsky, V. G., Benos, D. J., and Barrett, K. E., 1996, A biologic function for an "orphan" messenger: D-myo-inositol 3, 4, 5, 6-tetrakisphosphate selectively blocks epithelial calcium-activated chloride channels. Proc. Natl. Acad. Sci. U. S. A. 93: 10505-10509.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 10505-10509
    • Ismailov, I.I.1    Fuller, C.M.2    Berdiev, B.K.3    Shlyonsky, V.G.4    Benos, D.J.5    Barrett, K.E.6
  • 53
    • 0030060695 scopus 로고    scopus 로고
    • Arrhythmogenic action of thrombin during myocardial reperfusion via release of inositol 1, 4, 5-triphosphate
    • Jacobsen, A. N., Du, X. J., Lambert, K. A., Dart, A. M., and Woodcock, E. A., 1996, Arrhythmogenic action of thrombin during myocardial reperfusion via release of inositol 1, 4, 5-triphosphate. Circulation 93: 23-26.
    • (1996) Circulation , vol.93 , pp. 23-26
    • Jacobsen, A.N.1    Du, X.J.2    Lambert, K.A.3    Dart, A.M.4    Woodcock, E.A.5
  • 54
    • 0038361129 scopus 로고    scopus 로고
    • Functional overlap between murine Inpp5b and Ocrl1 may explain why deficiency of the murine ortholog for OCRL1 does not cause Lowe syndrome in mice
    • Janne, P. A., Suchy, S. F., Bernard, D., MacDonald, M., Crawley, J., Grinberg, A., Wynshaw-Boris, A., Westphal, H., and Nussbaum, R. L., 1998, Functional overlap between murine Inpp5b and Ocrl1 may explain why deficiency of the murine ortholog for OCRL1 does not cause Lowe syndrome in mice. J. Clin. Invest. 101: 2042-2053.
    • (1998) J. Clin. Invest , vol.101 , pp. 2042-2053
    • Janne, P.A.1    Suchy, S.F.2    Bernard, D.3    McDonald, M.4    Crawley, J.5    Grinberg, A.6    Wynshaw-Boris, A.7    Westphal, H.8    Nussbaum, R.L.9
  • 55
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes
    • Jope, R. S., 2003, Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol. Sci. 24: 441-443.
    • (2003) Trends Pharmacol. Sci , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 56
    • 84934882213 scopus 로고    scopus 로고
    • 1D-myo-inositol 3-phosphate synthase: Conversion, regulation, and putative target of mood stabilizers
    • Ju, S., Greenberg, M. L., in press, 1D-myo-inositol 3-phosphate synthase: Conversion, regulation, and putative target of mood stabilizers. Clin. Neurosci. Res.
    • Clin. Neurosci. Res
    • Ju, S.1    Greenberg, M.L.2
  • 57
    • 2542422679 scopus 로고    scopus 로고
    • Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast
    • Ju, S., Shaltiel, G., Shamir, A., Agam, G., and Greenberg, M. L., 2004, Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast. J. Biol. Chem. 279: 21759-21765.
    • (2004) J. Biol. Chem , vol.279 , pp. 21759-21765
    • Ju, S.1    Shaltiel, G.2    Shamir, A.3    Agam, G.4    Greenberg, M.L.5
  • 58
    • 1842420631 scopus 로고    scopus 로고
    • Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on beta-catenin in mouse hippocampus
    • Kaidanovich-Beilin, O., Milman, A., Weizman, A., Pick, C. G., and Eldar-Finkelman, H., 2004, Rapid antidepressive-like activity of specific glycogen synthase kinase-3 inhibitor and its effect on beta-catenin in mouse hippocampus. Biol. Psychiatry 55: 781-784.
    • (2004) Biol. Psychiatry , vol.55 , pp. 781-784
    • Kaidanovich-Beilin, O.1    Milman, A.2    Weizman, A.3    Pick, C.G.4    Eldar-Finkelman, H.5
  • 60
    • 0038376537 scopus 로고    scopus 로고
    • Insulin signaling: GLUT4 vesicles exit via the exocyst
    • Kanzaki, M., and Pessin, J. E., 2003, Insulin signaling: GLUT4 vesicles exit via the exocyst. Curr. Biol. 13: R574-R576.
    • (2003) Curr. Biol , vol.13 , pp. 574-576
    • Kanzaki, M.1    Pessin, J.E.2
  • 61
    • 0030054398 scopus 로고    scopus 로고
    • Overexpression of catalytic subunit p110alpha of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes
    • Katagiri, H., Asano, T., Ishihara, H., Inukai, K., Shibasaki, Y., Kikuchi, M., Yazaki, Y., and Oka, Y., 1996, Overexpression of catalytic subunit p110alpha of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes. J. Biol. Chem. 271: 16987-16990.
    • (1996) J. Biol. Chem , vol.271 , pp. 16987-16990
    • Katagiri, H.1    Asano, T.2    Ishihara, H.3    Inukai, K.4    Shibasaki, Y.5    Kikuchi, M.6    Yazaki, Y.7    Oka, Y.8
  • 62
    • 0027461948 scopus 로고
    • Different intracellular localization of inositol 1, 4, 5-trisphosphate and ryanodine receptors in cardiomyocytes
    • Kijima, Y., Saito, A., Jetton, T. L., Magnuson, M. A., and Fleischer, S., 1993, Different intracellular localization of inositol 1, 4, 5-trisphosphate and ryanodine receptors in cardiomyocytes. J. Biol. Chem. 268: 3499-3506.
    • (1993) J. Biol. Chem , vol.268 , pp. 3499-3506
    • Kijima, Y.1    Saito, A.2    Jetton, T.L.3    Magnuson, M.A.4    Fleischer, S.5
  • 63
    • 0024804990 scopus 로고
    • Inositol 1, 4, 5-trisphosphate binding sites in the brain: Regional distribution, characterization, and alterations in brains of patients with Parkinson's disease
    • Kitamura, N., Hashimoto, T., Nishino, N., and Tanaka, C., 1989, Inositol 1, 4, 5-trisphosphate binding sites in the brain: Regional distribution, characterization, and alterations in brains of patients with Parkinson's disease. J. Mol. Neurosci. 1: 181-187.
    • (1989) J. Mol. Neurosci , vol.1 , pp. 181-187
    • Kitamura, N.1    Hashimoto, T.2    Nishino, N.3    Tanaka, C.4
  • 64
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla, F. M., 2002, Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 3: 862-872.
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 66
    • 0031665007 scopus 로고    scopus 로고
    • Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human
    • Laporte, J., Blondeau, F., Buj-Bello, A., Tentler, D., Kretz, C., Dahl, N., and Mandel, J. L., 1998, Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human. Hum. Mol. Genet. 7: 1703-1712.
    • (1998) Hum. Mol. Genet , vol.7 , pp. 1703-1712
    • Laporte, J.1    Blondeau, F.2    Buj-Bello, A.3    Tentler, D.4    Kretz, C.5    Dahl, N.6    Mandel, J.L.7
  • 67
    • 9044222886 scopus 로고    scopus 로고
    • A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast
    • Laporte, J., Hu, L. J., Kretz, C., Mandel, J. L., Kioschis, P., Coy, J. F., Klauck, S. M., Poustka, A., and Dahl, N., 1996, A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. Nat. Genet. 13: 175-182.
    • (1996) Nat. Genet , vol.13 , pp. 175-182
    • Laporte, J.1    Hu, L.J.2    Kretz, C.3    Mandel, J.L.4    Kioschis, P.5    Coy, J.F.6    Klauck, S.M.7    Poustka, A.8    Dahl, N.9
  • 69
    • 0028925784 scopus 로고
    • cAMP-but not Ca(2+)-regulated Cl-conductance in the oviduct is defective in mouse model of cystic fibrosis
    • Leung, A. Y., Wong, P. Y., Gabriel, S. E., Yankaskas, J. R., and Boucher, R. C., 1995, cAMP-but not Ca(2+)-regulated Cl-conductance in the oviduct is defective in mouse model of cystic fibrosis. Am. J. Physiol. 268: C708-C712.
    • (1995) Am. J. Physiol , vol.268 , pp. 708-712
    • Leung, A.Y.1    Wong, P.Y.2    Gabriel, S.E.3    Yankaskas, J.R.4    Boucher, R.C.5
  • 71
    • 0035850791 scopus 로고    scopus 로고
    • The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity
    • Liang, Y., Hua, Z., Liang, X., Xu, Q., and Lu, G., 2001, The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity. J. Mol. Biol. 313: 123-137.
    • (2001) J. Mol. Biol , vol.313 , pp. 123-137
    • Liang, Y.1    Hua, Z.2    Liang, X.3    Xu, Q.4    Lu, G.5
  • 74
    • 0032523199 scopus 로고    scopus 로고
    • The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis
    • Liu, Q., Shalaby, F., Jones, J., Bouchard, D., and Dumont, D. J., 1998, The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis. Blood 91: 2753-2759.
    • (1998) Blood , vol.91 , pp. 2753-2759
    • Liu, Q.1    Shalaby, F.2    Jones, J.3    Bouchard, D.4    Dumont, D.J.5
  • 75
    • 0019333277 scopus 로고
    • Stereochemistry of the myo-inositol-1-phosphate synthase reaction
    • Loewus, M. W., Loewus, F. A., Brillinger, G. U., Otsuka, H., and Floss, H. G., 1980, Stereochemistry of the myo-inositol-1-phosphate synthase reaction. J. Biol. Chem. 255: 11710-11712.
    • (1980) J. Biol. Chem , vol.255 , pp. 11710-11712
    • Loewus, M.W.1    Loewus, F.A.2    Brillinger, G.U.3    Otsuka, H.4    Floss, H.G.5
  • 76
    • 0033933227 scopus 로고    scopus 로고
    • Calcium channelopathies
    • Lorenzon, N. M., and Beam, K. G., 2000, Calcium channelopathies. Kidney Int. 57: 794-802.
    • (2000) Kidney Int , vol.57 , pp. 794-802
    • Lorenzon, N.M.1    Beam, K.G.2
  • 77
    • 0029888482 scopus 로고    scopus 로고
    • Antagonistic effect of inositol pentakisphosphate on inositol triphosphate receptors
    • Lu, P. J., Shieh, W. R., and Chen, C. S., 1996, Antagonistic effect of inositol pentakisphosphate on inositol triphosphate receptors. Biochem. Biophys. Res. Commun. 220: 637-642.
    • (1996) Biochem. Biophys. Res. Commun , vol.220 , pp. 637-642
    • Lu, P.J.1    Shieh, W.R.2    Chen, C.S.3
  • 78
    • 0026601692 scopus 로고
    • Inositol 1, 3, 4, 5-tetrakisphosphate activates an endothelial Ca(2+)-permeable channel
    • Luckhoff, A., and Clapham, D. E., 1992, Inositol 1, 3, 4, 5-tetrakisphosphate activates an endothelial Ca(2+)-permeable channel. Nature 355: 356-358.
    • (1992) Nature , vol.355 , pp. 356-358
    • Luckhoff, A.1    Clapham, D.E.2
  • 79
    • 0142227019 scopus 로고    scopus 로고
    • Targeting the PI3K-Akt pathway in human cancer: Rationale and promise
    • Luo, J., Manning, B. D., and Cantley, L. C., 2003, Targeting the PI3K-Akt pathway in human cancer: Rationale and promise. Cancer Cell 4: 257-262.
    • (2003) Cancer Cell , vol.4 , pp. 257-262
    • Luo, J.1    Manning, B.D.2    Cantley, L.C.3
  • 81
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3, 4, 5-trisphosphate
    • Maehama, T., and Dixon, J. E., 1998, The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3, 4, 5-trisphosphate. J. Biol. Chem. 273: 13375-13378.
    • (1998) J. Biol. Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 82
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: Novel phosphoinositide phosphatases
    • Maehama, T., Taylor, G. S., and Dixon, J. E., 2001, PTEN and myotubularin: Novel phosphoinositide phosphatases. Annu. Rev. Biochem. 70: 247-279.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 247-279
    • Maehama, T.1    Taylor, G.S.2    Dixon, J.E.3
  • 83
    • 0141682777 scopus 로고    scopus 로고
    • Diversification and evolution of L-myo-inositol 1-phosphate synthase
    • Majumder, A. L., Chatterjee, A., Ghosh Dastidar, K., and Majee, M., 2003, Diversification and evolution of L-myo-inositol 1-phosphate synthase. FEBS Lett. 553: 3-10.
    • (2003) FEBS Lett , vol.553 , pp. 3-10
    • Majumder, A.L.1    Chatterjee, A.2    Ghosh Dastidar, K.3    Majee, M.4
  • 84
    • 0032827466 scopus 로고    scopus 로고
    • Lithium at 50: Have the neuroprotective effects of this unique cation been overlooked?
    • Manji, H. K., Moore, G. J., and Chen, G., 1999, Lithium at 50: Have the neuroprotective effects of this unique cation been overlooked? Biol. Psychiatry 46: 929-940.
    • (1999) Biol. Psychiatry , vol.46 , pp. 929-940
    • Manji, H.K.1    Moore, G.J.2    Chen, G.3
  • 87
    • 0346056793 scopus 로고    scopus 로고
    • Nuclear inositides: Facts and perspectives
    • Martelli, A. M., Manzoli, L., and Cocco, L., 2004, Nuclear inositides: Facts and perspectives. Pharmacol. Ther. 101: 47-64.
    • (2004) Pharmacol. Ther , vol.101 , pp. 47-64
    • Martelli, A.M.1    Manzoli, L.2    Cocco, L.3
  • 88
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • Martin, T. F., 1998, Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14: 231-264.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 231-264
    • Martin, T.F.1
  • 90
    • 0034194089 scopus 로고    scopus 로고
    • Calcium signaling in the ER: Its role in neuronal plasticity and neurodegenerative disorders
    • Mattson, M. P., LaFerla, F. M., Chan, S. L., Leissring, M. A., Shepel, P. N., and Geiger, J. D., 2000a, Calcium signaling in the ER: Its role in neuronal plasticity and neurodegenerative disorders. Trends Neurosci. 23: 222-229.
    • (2000) Trends Neurosci , vol.23 , pp. 222-229
    • Mattson, M.P.1    LaFerla, F.M.2    Chan, S.L.3    Leissring, M.A.4    Shepel, P.N.5    Geiger, J.D.6
  • 91
    • 0034652369 scopus 로고    scopus 로고
    • Presenilin-1 mutation increases neuronal vulnerability to focal ischemia in vivo and to hypoxia and glucose deprivation in cell culture: Involvement of perturbed calcium homeostasis
    • Mattson, M. P., Zhu, H., Yu, J., and Kindy, M. S., 2000b, Presenilin-1 mutation increases neuronal vulnerability to focal ischemia in vivo and to hypoxia and glucose deprivation in cell culture: Involvement of perturbed calcium homeostasis. J. Neurosci. 20: 1358-1364.
    • (2000) J. Neurosci , vol.20 , pp. 1358-1364
    • Mattson, M.P.1    Zhu, H.2    Yu, J.3    Kindy, M.S.4
  • 92
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases
    • McGeer, P. L., and McGeer, E. G., 1995, The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Res. Brain Res. Rev. 21: 195-218.
    • (1995) Brain Res. Brain Res. Rev , vol.21 , pp. 195-218
    • McGeer, P.L.1    McGeer, E.G.2
  • 93
    • 0035369841 scopus 로고    scopus 로고
    • Mechanisms of Ca(2+)-dependent transcription
    • Mellstrom, B., and Naranjo, J. R., 2001, Mechanisms of Ca(2+)-dependent transcription. Curr. Opin. Neurobiol. 11: 312-319.
    • (2001) Curr. Opin. Neurobiol , vol.11 , pp. 312-319
    • Mellstrom, B.1    Naranjo, J.R.2
  • 94
    • 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, J.W.3    Shears, S.B.4
  • 97
    • 0033860781 scopus 로고    scopus 로고
    • OCRL1 mutation analysis in French Lowe syndrome patients: Implications for molecular diagnosis strategy and genetic counseling
    • Monnier, N., Satre, V., Lerouge, E., Berthoin, F., and Lunardi, J., 2000, OCRL1 mutation analysis in French Lowe syndrome patients: Implications for molecular diagnosis strategy and genetic counseling. Hum. Mutat. 16: 157-165.
    • (2000) Hum. Mutat , vol.16 , pp. 157-165
    • Monnier, N.1    Satre, V.2    Lerouge, E.3    Berthoin, F.4    Lunardi, J.5
  • 98
    • 0032744013 scopus 로고    scopus 로고
    • Temporal dissociation between lithium-induced changes in frontal lobe myo-inositol and clinical response in manic-depressive illness
    • Moore, G. J., Bebchuk, J. M., Parrish, J. K., Faulk, M. W., Arfken, C. L., Strahl-Bevacqua, J., and Manji, H. K., 1999, Temporal dissociation between lithium-induced changes in frontal lobe myo-inositol and clinical response in manic-depressive illness. Am. J. Psychiatry 156: 1902-1908.
    • (1999) Am. J. Psychiatry , vol.156 , pp. 1902-1908
    • Moore, G.J.1    Bebchuk, J.M.2    Parrish, J.K.3    Faulk, M.W.4    Arfken, C.L.5    Strahl-Bevacqua, J.6    Manji, H.K.7
  • 99
    • 0023488494 scopus 로고
    • Synergism of inositol trisphosphate and tetrakisphosphate in activating Ca2+-dependent K+ channels
    • Morris, A. P., Gallacher, D. V., Irvine, R. F., and Petersen, O. H., 1987, Synergism of inositol trisphosphate and tetrakisphosphate in activating Ca2+-dependent K+ channels. Nature 330: 653-655.
    • (1987) Nature , vol.330 , pp. 653-655
    • Morris, A.P.1    Gallacher, D.V.2    Irvine, R.F.3    Petersen, O.H.4
  • 100
    • 0025785054 scopus 로고
    • Increased myocardial inositol trisphosphate levels during alpha 1-adrenergic stimulation and reperfusion of ischaemic rat heart
    • Mouton, R., Huisamen, B., and Lochner, A., 1991, Increased myocardial inositol trisphosphate levels during alpha 1-adrenergic stimulation and reperfusion of ischaemic rat heart. J. Mol. Cell. Cardiol. 23: 841-850.
    • (1991) J. Mol. Cell. Cardiol , vol.23 , pp. 841-850
    • Mouton, R.1    Huisamen, B.2    Lochner, A.3
  • 102
    • 0016231591 scopus 로고
    • Biosynthesis of myo-inositol in rat mammary gland. Isolation and properties of the enzymes
    • Naccarato, W. F., Ray, R. E., and Wells, W. W., 1974, Biosynthesis of myo-inositol in rat mammary gland. Isolation and properties of the enzymes. Arch. Biochem. Biophys. 164: 194-201.
    • (1974) Arch. Biochem. Biophys , vol.164 , pp. 194-201
    • Naccarato, W.F.1    Ray, R.E.2    Wells, W.W.3
  • 103
    • 0034724747 scopus 로고    scopus 로고
    • The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes
    • Nakashima, N., Sharma, P. M., Imamura, T., Bookstein, R., and Olefsky, J. M., 2000, The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes. J. Biol. Chem. 275: 12889-12895.
    • (2000) J. Biol. Chem , vol.275 , pp. 12889-12895
    • Nakashima, N.1    Sharma, P.M.2    Imamura, T.3    Bookstein, R.4    Olefsky, J.M.5
  • 104
    • 0036167307 scopus 로고    scopus 로고
    • Revised prevalence estimates of mental disorders in the United States: Using a clinical significance criterion to reconcile 2 surveys' estimates
    • Narrow, W. E., Rae, D. S., Robins, L. N., and Regier, D. A., 2002, Revised prevalence estimates of mental disorders in the United States: Using a clinical significance criterion to reconcile 2 surveys' estimates. Arch. Gen. Psychiatry 59: 115-123.
    • (2002) Arch. Gen. Psychiatry , vol.59 , pp. 115-123
    • Narrow, W.E.1    Rae, D.S.2    Robins, L.N.3    Regier, D.A.4
  • 106
  • 107
    • 0028146616 scopus 로고
    • Blockage of chemotactic peptideinduced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidylinositol 3-kinase
    • Okada, T., Sakuma, L., Fukui, Y., Hazeki, O., and Ui, M., 1994, Blockage of chemotactic peptideinduced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidylinositol 3-kinase. J. Biol. Chem. 269: 3563-3567.
    • (1994) J. Biol. Chem , vol.269 , pp. 3563-3567
    • Okada, T.1    Sakuma, L.2    Fukui, Y.3    Hazeki, O.4    Ui, M.5
  • 108
    • 0029120280 scopus 로고
    • The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex
    • Olivos-Glander, I. M., Janne, P. A., and Nussbaum, R. L., 1995, The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex. Am. J. Hum. Genet. 57: 817-823.
    • (1995) Am. J. Hum. Genet , vol.57 , pp. 817-823
    • Olivos-Glander, I.M.1    Janne, P.A.2    Nussbaum, R.L.3
  • 109
    • 17844371042 scopus 로고    scopus 로고
    • Regulation of phosphoinositide metabolism, Akt phosphorylation, and glucose transport by PTEN (phosphatase and tensin homolog deleted on chromosome 10) in 3T3-L1 adipocytes
    • Ono, H., Katagiri, H., Funaki, M., Anai, M., Inukai, K., Fukushima, Y., Sakoda, H., Ogihara, T., Onishi, Y., Fujishiro, M., Kikuchi, M., Oka, Y., and Asano, T., 2001, Regulation of phosphoinositide metabolism, Akt phosphorylation, and glucose transport by PTEN (phosphatase and tensin homolog deleted on chromosome 10) in 3T3-L1 adipocytes. Mol. Endocrinol. 15: 1411-1422.
    • (2001) Mol. Endocrinol , vol.15 , pp. 1411-1422
    • Ono, H.1    Katagiri, H.2    Funaki, M.3    Anai, M.4    Inukai, K.5    Fukushima, Y.6    Sakoda, H.7    Ogihara, T.8    Onishi, Y.9    Fujishiro, M.10    Kikuchi, M.11    Oka, Y.12    Asano, T.13
  • 110
    • 3943105516 scopus 로고    scopus 로고
    • Inositol 1, 4, 5-trisphosphate receptors as signal integrators
    • Patterson, R. L., Boehning, D., and Snyder, S. H., 2004, Inositol 1, 4, 5-trisphosphate receptors as signal integrators. Annu. Rev. Biochem. 73: 437-465.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 437-465
    • Patterson, R.L.1    Boehning, D.2    Snyder, S.H.3
  • 111
    • 0038538512 scopus 로고    scopus 로고
    • Phosphoinositide signaling disorders in human diseases
    • Pendaries, C., Tronchere, H., Plantavid, M., and Payrastre, B., 2003, Phosphoinositide signaling disorders in human diseases. FEBS Lett. 546: 25-31.
    • (2003) FEBS Lett , vol.546 , pp. 25-31
    • Pendaries, C.1    Tronchere, H.2    Plantavid, M.3    Payrastre, B.4
  • 113
    • 0037717381 scopus 로고
    • Sur la synthese de l' ether hexaphosphorique de l' inosite avec le principe phosphoorganique de reserve des plantes vertes
    • Posternak, S., 1919, Sur la synthese de l' ether hexaphosphorique de l' inosite avec le principe phosphoorganique de reserve des plantes vertes. C. R. Acad. Sci. 169: 138-140.
    • (1919) C.R. Acad. Sci , vol.169 , pp. 138-140
    • Posternak, S.1
  • 115
    • 0025730289 scopus 로고
    • Role of erythrocyte organic phosphates in blood oxygen transport in anemic quail
    • Riera, M., Fuster, J. F., and Palacios, L., 1991, Role of erythrocyte organic phosphates in blood oxygen transport in anemic quail. Am. J. Physiol. 260: R798-R803.
    • (1991) Am. J. Physiol , vol.260 , pp. 798-803
    • Riera, M.1    Fuster, J.F.2    Palacios, L.3
  • 116
    • 0038016550 scopus 로고    scopus 로고
    • Antagonists of myo-inositol 3, 4, 5, 6-tetrakisphosphate allow repeated epithelial chloride secretion
    • Rudolf, M. T., Dinkel, C., Traynor-Kaplan, A. E., and Schultz, C., 2003, Antagonists of myo-inositol 3, 4, 5, 6-tetrakisphosphate allow repeated epithelial chloride secretion. Bioorg. Med. Chem. 11: 3315-3329.
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 3315-3329
    • Rudolf, M.T.1    Dinkel, C.2    Traynor-Kaplan, A.E.3    Schultz, C.4
  • 117
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel, A. R., and Kahn, C. R., 2001, Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414: 799-806.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 118
    • 0025279786 scopus 로고
    • Myotubular myopathy: Arrest of morphogenesis of myofibres associated with persistence of fetal vimentin and desmin. Four cases compared with fetal and neonatal muscle
    • Sarnat, H. B., 1990, Myotubular myopathy: Arrest of morphogenesis of myofibres associated with persistence of fetal vimentin and desmin. Four cases compared with fetal and neonatal muscle. Can. J. Neurol. Sci. 17: 109-123.
    • (1990) Can. J. Neurol. Sci , vol.17 , pp. 109-123
    • Sarnat, H.B.1
  • 119
    • 0032745240 scopus 로고    scopus 로고
    • BCR/ABL directly inhibits expression of SHIP, an SH2-containing polyinositol-5-phosphatase involved in the regulation of hematopoiesis
    • Sattler, M., Verma, S., Byrne, C. H., Shrikhande, G., Winkler, T., Algate, P. A., Rohrschneider, L. R., and Griffin, J. D., 1999, BCR/ABL directly inhibits expression of SHIP, an SH2-containing polyinositol-5-phosphatase involved in the regulation of hematopoiesis. Mol. Cell. Biol. 19: 7473-7480.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7473-7480
    • Sattler, M.1    Verma, S.2    Byrne, C.H.3    Shrikhande, G.4    Winkler, T.5    Algate, P.A.6    Rohrschneider, L.R.7    Griffin, J.D.8
  • 120
    • 8644279885 scopus 로고    scopus 로고
    • Role for a novel signaling intermediate, phosphatidylinositol 5-phosphate, in insulin-regulated F-actin stress fiber breakdown and GLUT4 translocation
    • Sbrissa, D., Ikonomov, O. C., Strakova, J., and Shisheva, A., 2004, Role for a novel signaling intermediate, phosphatidylinositol 5-phosphate, in insulin-regulated F-actin stress fiber breakdown and GLUT4 translocation. Endocrinology 145: 4853-4865.
    • (2004) Endocrinology , vol.145 , pp. 4853-4865
    • Sbrissa, D.1    Ikonomov, O.C.2    Strakova, J.3    Shisheva, A.4
  • 121
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J., 1991, The molecular pathology of Alzheimer's disease. Neuron 6: 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 122
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J., 2001, Alzheimer's disease: Genes, proteins, and therapy. Physiol. Rev. 81: 741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 125
    • 0032540944 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase activity by adenovirus-mediated gene transfer and its effect on insulin action
    • Sharma, P. M., Egawa, K., Huang, Y., Martin, J. L., Huvar, I., Boss, G. R., and Olefsky, J. M., 1998, Inhibition of phosphatidylinositol 3-kinase activity by adenovirus-mediated gene transfer and its effect on insulin action. J. Biol. Chem. 273: 18528-18537.
    • (1998) J. Biol. Chem , vol.273 , pp. 18528-18537
    • Sharma, P.M.1    Egawa, K.2    Huang, Y.3    Martin, J.L.4    Huvar, I.5    Boss, G.R.6    Olefsky, J.M.7
  • 126
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • Shepherd, P. R., Withers, D. J., and Siddle, K., 1998, Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling. Biochem. J. 333(Pt 3): 471-490.
    • (1998) Biochem. J , vol.333 , pp. 471-490
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 127
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman, G. I., 2000, Cellular mechanisms of insulin resistance. J. Clin. Invest. 106: 171-176.
    • (2000) J. Clin. Invest , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 128
    • 0036796784 scopus 로고    scopus 로고
    • Chronic treatment with both lithium and sodium valproate may normalize phosphoinositol cycle activity in bipolar patients
    • Silverstone, P. H., Wu, R. H., O'Donnell, T., Ulrich, M., Asghar, S. J., and Hanstock, C. C., 2002, Chronic treatment with both lithium and sodium valproate may normalize phosphoinositol cycle activity in bipolar patients. Hum. Psychopharmacol. 17: 321-327.
    • (2002) Hum. Psychopharmacol , vol.17 , pp. 321-327
    • Silverstone, P.H.1    Wu, R.H.2    O'Donnell, T.3    Ulrich, M.4    Asghar, S.J.5    Hanstock, C.C.6
  • 129
    • 0034176401 scopus 로고    scopus 로고
    • The effect of inositol 1, 3, 4, 5-tetrakisphosphate on inositol trisphosphate-induced Ca2+ mobilization in freshly isolated and cultured mouse lacrimal acinar cells
    • Smith, P. M., Harmer, A. R., Letcher, A. J., and Irvine, R. F., 2000, The effect of inositol 1, 3, 4, 5-tetrakisphosphate on inositol trisphosphate-induced Ca2+ mobilization in freshly isolated and cultured mouse lacrimal acinar cells. Biochem. J. 347(Pt 1): 77-82.
    • (2000) Biochem. J , vol.347 , pp. 77-82
    • Smith, P.M.1    Harmer, A.R.2    Letcher, A.J.3    Irvine, R.F.4
  • 131
    • 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., Jackson, T. R., Hawkins, P. T., and Mayr, G. W., 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    Jackson, T.R.7    Hawkins, P.T.8    Mayr, G.W.9
  • 132
    • 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., Hanley, M. R., Kay, R. R., and Irvine, R. F., 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 , 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    Hanley, M.R.7    Kay, R.R.8    Irvine, R.F.9
  • 133
    • 0020643801 scopus 로고
    • Release of Ca2+ 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 Ca2+ 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
  • 135
    • 1342288871 scopus 로고    scopus 로고
    • Dysregulated IP3 signaling in cortical neurons of knock-in mice expressing an Alzheimer's-linked mutation in presenilin1 results in exaggerated Ca2+ signals and altered membrane excitability
    • Stutzmann, G. E., Caccamo, A., LaFerla, F. M., and Parker, I., 2004, Dysregulated IP3 signaling in cortical neurons of knock-in mice expressing an Alzheimer's-linked mutation in presenilin1 results in exaggerated Ca2+ signals and altered membrane excitability. J. Neurosci. 24: 508-513.
    • (2004) J. Neurosci , vol.24 , pp. 508-513
    • Stutzmann, G.E.1    Caccamo, A.2    LaFerla, F.M.3    Parker, I.4
  • 136
    • 0036882117 scopus 로고    scopus 로고
    • The deficiency of PIP2 5-phosphatase in Lowe syndrome affects actin polymerization
    • Suchy, S. F., and Nussbaum, R. L., 2002, The deficiency of PIP2 5-phosphatase in Lowe syndrome affects actin polymerization. Am. J. Hum. Genet. 71: 1420-1427.
    • (2002) Am. J. Hum. Genet , vol.71 , pp. 1420-1427
    • Suchy, S.F.1    Nussbaum, R.L.2
  • 137
    • 0028880052 scopus 로고
    • Lowe syndrome, a deficiency of phosphatidylinositol 4, 5-bisphosphate 5-phosphatase in the Golgi apparatus
    • Suchy, S. F., Olivos-Glander, I. M., and Nussabaum, R. L., 1995, Lowe syndrome, a deficiency of phosphatidylinositol 4, 5-bisphosphate 5-phosphatase in the Golgi apparatus. Hum. Mol. Genet. 4: 2245-2250.
    • (1995) Hum. Mol. Genet , vol.4 , pp. 2245-2250
    • Suchy, S.F.1    Olivos-Glander, I.M.2    Nussabaum, R.L.3
  • 138
    • 0023693795 scopus 로고
    • Activation of a low specific activity form of DNA polymerase alpha by inositol-1, 4-bisphosphate
    • Sylvia, V., Curtin, G., Norman, J., Stec, J., and Busbee, D., 1988, Activation of a low specific activity form of DNA polymerase alpha by inositol-1, 4-bisphosphate. Cell 54: 651-658.
    • (1988) Cell , vol.54 , pp. 651-658
    • Sylvia, V.1    Curtin, G.2    Norman, J.3    Stec, J.4    Busbee, D.5
  • 139
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1
    • Tang, T. S., Tu, H., Chan, E. Y., Maximov, A., Wang, Z., Wellington, C. L., Hayden, M. R., and Bezprozvanny, I., 2003, Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1. Neuron 39: 227-239.
    • (2003) Neuron , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6    Hayden, M.R.7    Bezprozvanny, I.8
  • 140
    • 0033033506 scopus 로고    scopus 로고
    • Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients
    • Tanner, S. M., Schneider, V., Thomas, N. S., Clarke, A., Lazarou, L., and Liechti-Gallati, S., 1999, Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients. Neuromuscul. Disord. 9: 41-49.
    • (1999) Neuromuscul. Disord , vol.9 , pp. 41-49
    • Tanner, S.M.1    Schneider, V.2    Thomas, N.S.3    Clarke, A.4    Lazarou, L.5    Liechti-Gallati, S.6
  • 141
    • 0038575866 scopus 로고    scopus 로고
    • Inositol hexaphosphate (IP6) enhances the anti-proliferative effects of adriamycin and tamoxifen in breast cancer
    • Tantivejkul, K., Vucenik, I., Eiseman, J., and Shamsuddin, A. M., 2003, Inositol hexaphosphate (IP6) enhances the anti-proliferative effects of adriamycin and tamoxifen in breast cancer. Breast Cancer Res. Treat. 79: 301-312.
    • (2003) Breast Cancer Res. Treat , vol.79 , pp. 301-312
    • Tantivejkul, K.1    Vucenik, I.2    Eiseman, J.3    Shamsuddin, A.M.4
  • 142
    • 0034244437 scopus 로고    scopus 로고
    • Inaugural article: Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate
    • Taylor, G. S., Maehama, T., and Dixon, J. E., 2000, Inaugural article: Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. Proc. Natl. Acad. Sci. U. S. A. 97: 8910-8915.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 8910-8915
    • Taylor, G.S.1    Maehama, T.2    Dixon, J.E.3
  • 145
    • 0029857713 scopus 로고    scopus 로고
    • Intracellular inositol 1, 3, 4, 5-tetrakisphosphate enhances the calcium current in hippocampal CA1 neurones of the gerbil after ischaemia
    • Tsubokawa, H., Oguro, K., Robinson, H. P., Masuzawa, T., and Kawai, N., 1996, Intracellular inositol 1, 3, 4, 5-tetrakisphosphate enhances the calcium current in hippocampal CA1 neurones of the gerbil after ischaemia. J. Physiol. 497(Pt 1): 67-78.
    • (1996) J. Physiol , vol.497 , pp. 67-78
    • Tsubokawa, H.1    Oguro, K.2    Robinson, H.P.3    Masuzawa, T.4    Kawai, N.5
  • 146
    • 1842690628 scopus 로고    scopus 로고
    • Myotubularin regulates the function of the late endosome through the gram domainphosphatidylinositol 3, 5-bisphosphate interaction
    • Tsujita, K., Itoh, T., Ijuin, T., Yamamoto, A., Shisheva, A., Laporte, J., and Takenawa, T., 2004, Myotubularin regulates the function of the late endosome through the gram domainphosphatidylinositol 3, 5-bisphosphate interaction. J. Biol. Chem. 279: 13817-13824.
    • (2004) J. Biol. Chem , vol.279 , pp. 13817-13824
    • Tsujita, K.1    Itoh, T.2    Ijuin, T.3    Yamamoto, A.4    Shisheva, A.5    Laporte, J.6    Takenawa, T.7
  • 148
    • 0033539501 scopus 로고    scopus 로고
    • Increased levels of plasma lysosomal enzymes in patients with Lowe syndrome
    • Ungewickell, A. J., and Majerus, P. W., 1999, Increased levels of plasma lysosomal enzymes in patients with Lowe syndrome. Proc. Natl. Acad. Sci. U. S. A. 96: 13342-13344.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 13342-13344
    • Ungewickell, A.J.1    Majerus, P.W.2
  • 149
    • 4544273742 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatase Ocrl associates with endosomes that are partially coated with clathrin
    • Ungewickell, A., Ward, M. E., Ungewickell, E., and Majerus, P. W., 2004, The inositol polyphosphate 5-phosphatase Ocrl associates with endosomes that are partially coated with clathrin. Proc. Natl. Acad. Sci. U. S. A. 101: 13501-13506.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 13501-13506
    • Ungewickell, A.1    Ward, M.E.2    Ungewickell, E.3    Majerus, P.W.4
  • 150
    • 0035805569 scopus 로고    scopus 로고
    • Lithium and valproate decrease inositol mass and increase expression of the yeast INO1 and INO2 genes for inositol biosynthesis
    • Vaden, D. L., Ding, D., Peterson, B., and Greenberg, M. L., 2001, Lithium and valproate decrease inositol mass and increase expression of the yeast INO1 and INO2 genes for inositol biosynthesis. J. Biol. Chem. 276: 15466-15471.
    • (2001) J. Biol. Chem , vol.276 , pp. 15466-15471
    • Vaden, D.L.1    Ding, D.2    Peterson, B.3    Greenberg, M.L.4
  • 152
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco, I., and Sawyers, C. L., 2002, The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat. Rev. Cancer 2: 489-501.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 153
  • 154
    • 0242526048 scopus 로고    scopus 로고
    • Cancer inhibition by inositol hexaphosphate (IP6) and inositol: From laboratory to clinic
    • Vucenik, I., and Shamsuddin, A. M., 2003, Cancer inhibition by inositol hexaphosphate (IP6) and inositol: From laboratory to clinic. J. Nutr. 133: 3778S-3784S.
    • (2003) J. Nutr , vol.133 , pp. 3778-3784
    • Vucenik, I.1    Shamsuddin, A.M.2
  • 155
    • 0031011142 scopus 로고    scopus 로고
    • Inositol 1, 4, 5-trisphosphate in blood and skeletal muscle in human malignant hyperthermia
    • Wappler, F., Scholz, J., Kochling, A., Steinfath, M., Krause, T., and Schulte am Esch, J., 1997, Inositol 1, 4, 5-trisphosphate in blood and skeletal muscle in human malignant hyperthermia. Br. J. Anaesth. 78: 541-547.
    • (1997) Br. J. Anaesth , vol.78 , pp. 541-547
    • Wappler, F.1    Scholz, J.2    Kochling, A.3    Steinfath, M.4    Krause, T.5    Schulte am Esch, J.6
  • 156
    • 0025924459 scopus 로고
    • Reduced striatal [3H]inositol 1, 4, 5-trisphosphate binding in Huntington's disease
    • Warsh, J. J., Politsky, J. M., Li, P. P., Kish, S. J., and Hornykiewicz, O., 1991, Reduced striatal [3H]inositol 1, 4, 5-trisphosphate binding in Huntington's disease. J. Neurochem. 56: 1417-1422.
    • (1991) J. Neurochem , vol.56 , pp. 1417-1422
    • Warsh, J.J.1    Politsky, J.M.2    Li, P.P.3    Kish, S.J.4    Hornykiewicz, O.5
  • 157
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman, M., Kaplan, D. R., Schaffhausen, B., Cantley, L., and Roberts, T. M., 1985, Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315: 239-242.
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 158
    • 0037118050 scopus 로고    scopus 로고
    • A common mechanism of action for three mood-stabilizing drugs
    • Williams, R. S., Cheng, L., Mudge, A. W., and Harwood, A. J., 2002, A common mechanism of action for three mood-stabilizing drugs. Nature 417: 292-295.
    • (2002) Nature , vol.417 , pp. 292-295
    • Williams, R.S.1    Cheng, L.2    Mudge, A.W.3    Harwood, A.J.4
  • 159
    • 0035313805 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphoinositide phosphatases: Bringing bioinformatics to the lab bench
    • Wishart, M. J., Taylor, G. S., Slama, J. T., and Dixon, J. E., 2001, PTEN and myotubularin phosphoinositide phosphatases: Bringing bioinformatics to the lab bench. Curr. Opin. Cell Biol. 13: 172-181.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 172-181
    • Wishart, M.J.1    Taylor, G.S.2    Slama, J.T.3    Dixon, J.E.4
  • 160
    • 0030971956 scopus 로고    scopus 로고
    • Inositol phosphates and inositol phospholipids: How big is the iceberg?
    • Woodcock, E. A., 1997, Inositol phosphates and inositol phospholipids: How big is the iceberg? Mol. Cell. Endocrinol. 127: 1-10.
    • (1997) Mol. Cell. Endocrinol , vol.127 , pp. 1-10
    • Woodcock, E.A.1
  • 161
    • 0030272372 scopus 로고    scopus 로고
    • Ins(1, 4, 5)P3 during myocardial ischemia and its relationship to the development of arrhythmias
    • Woodcock, E. A., Lambert, K. A., and Du, X. J., 1996, Ins(1, 4, 5)P3 during myocardial ischemia and its relationship to the development of arrhythmias. J. Mol. Cell. Cardiol. 28: 2129-2138.
    • (1996) J. Mol. Cell. Cardiol , vol.28 , pp. 2129-2138
    • Woodcock, E.A.1    Lambert, K.A.2    Du, X.J.3
  • 163
    • 0037154957 scopus 로고    scopus 로고
    • A distinct form of calcium release down-regulates membrane excitability in neocortical pyramidal cells
    • Yamamoto, K., Hashimoto, K., Nakano, M., Shimohama, S., and Kato, N., 2002, A distinct form of calcium release down-regulates membrane excitability in neocortical pyramidal cells. Neuroscience 109: 665-676.
    • (2002) Neuroscience , vol.109 , pp. 665-676
    • Yamamoto, K.1    Hashimoto, K.2    Nakano, M.3    Shimohama, S.4    Kato, N.5
  • 164
    • 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
  • 166
    • 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
  • 167
    • 0028083206 scopus 로고
    • Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis
    • York, J. D., Saffitz, J. E., and Majerus, P. W., 1994, Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis. J. Biol. Chem. 269: 19992-19999.
    • (1994) J. Biol. Chem , vol.269 , pp. 19992-19999
    • York, J.D.1    Saffitz, J.E.2    Majerus, P.W.3
  • 168
    • 0032803927 scopus 로고    scopus 로고
    • Calcium signaling molecules in human cerebellum at midgestation and in ataxia
    • Zecevic, N., Milosevic, A., and Ehrlich, B. E., 1999, Calcium signaling molecules in human cerebellum at midgestation and in ataxia. Early Hum. Dev. 54: 103-116.
    • (1999) Early Hum. Dev , vol.54 , pp. 103-116
    • Zecevic, N.1    Milosevic, A.2    Ehrlich, B.E.3
  • 169
    • 0031914642 scopus 로고    scopus 로고
    • Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4, 5-bisphosphate
    • Zhang, X., Hartz, P. A., Philip, E., Racusen, L. C., and Majerus, P. W., 1998, Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4, 5-bisphosphate. J. Biol. Chem. 273: 1574-1582.
    • (1998) J. Biol. Chem , vol.273 , pp. 1574-1582
    • Zhang, X.1    Hartz, P.A.2    Philip, E.3    Racusen, L.C.4    Majerus, P.W.5
  • 170
    • 0029060795 scopus 로고
    • The protein deficient in Lowe syndrome is a phosphatidylinositol-4, 5-bisphosphate 5-phosphatase
    • Zhang, X., Jefferson, A. B., Auethavekiat, V., and Majerus, P. W., 1995, The protein deficient in Lowe syndrome is a phosphatidylinositol-4, 5-bisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. U. S. A. 92: 4853-4856.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 4853-4856
    • Zhang, X.1    Jefferson, A.B.2    Auethavekiat, V.3    Majerus, P.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.