메뉴 건너뛰기




Volumn 15, Issue 5, 2004, Pages 689-701

Structure of a human inositol 1,4,5-trisphosphate 3-kinase: Substrate binding reveals why it is not a phosphoinositide 3-kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; INOSITOL TRISPHOSPHATE 3 KINASE; PHOSPHATE; PHOSPHATIDYLINOSITOL 3 KINASE;

EID: 4444223742     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.08.004     Document Type: Article
Times cited : (83)

References (56)
  • 2
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M.J. Inositol trisphosphate and calcium signalling. Nature. 361:1993;315-325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 3
    • 0034695549 scopus 로고    scopus 로고
    • The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site
    • Bertsch U., Deschermeier C., Fanick W., Girkontaite I., Hillemeier K., Johnen H., Weglohner W., Emmrich F., Mayr G.W. The second messenger binding site of inositol 1,4,5-trisphosphate 3-kinase is centered in the catalytic domain and related to the inositol trisphosphate receptor site. J. Biol. Chem. 275:2000;1557-1564
    • (2000) J. Biol. Chem. , vol.275 , pp. 1557-1564
    • Bertsch, U.1    Deschermeier, C.2    Fanick, W.3    Girkontaite, I.4    Hillemeier, K.5    Johnen, H.6    Weglohner, W.7    Emmrich, F.8    Mayr, G.W.9
  • 4
    • 0026612494 scopus 로고
    • Sustained Ca2+ signaling in mouse lacrimal acinar cells due to photolysis of "caged" glycerophosphoryl-myo-inositol 4,5-bisphosphate
    • Bird G.S., Obie J.F., Putney J.W. Jr. Sustained Ca2+ signaling in mouse lacrimal acinar cells due to photolysis of "caged" glycerophosphoryl-myo-inositol 4,5-bisphosphate. J. Biol. Chem. 267:1992;17722-17725
    • (1992) J. Biol. Chem. , vol.267 , pp. 17722-17725
    • Bird, G.S.1    Obie, J.F.2    Putney Jr., J.W.3
  • 6
    • 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., Majerus P.W. The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem. 277:2002;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
  • 7
    • 0036305943 scopus 로고    scopus 로고
    • Sequence and structure classification of kinases
    • Cheek S., Zhang H., Grishin N.V. Sequence and structure classification of kinases. J. Mol. Biol. 320:2002;855-881
    • (2002) J. Mol. Biol. , vol.320 , pp. 855-881
    • Cheek, S.1    Zhang, H.2    Grishin, N.V.3
  • 8
    • 0025303820 scopus 로고
    • Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase
    • Choi K.Y., Kim H.K., Lee S.Y., Moon K.H., Sim S.S., Kim J.W., Chung H.K., Rhee S.G. Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase. Science. 248:1990;64-66
    • (1990) Science , vol.248 , pp. 64-66
    • Choi, K.Y.1    Kim, H.K.2    Lee, S.Y.3    Moon, K.H.4    Sim, S.S.5    Kim, J.W.6    Chung, H.K.7    Rhee, S.G.8
  • 9
    • 0032548839 scopus 로고    scopus 로고
    • Inositol trisphosphate mediates a RAS-independent response to LET-23 receptor tyrosine kinase activation in C. elegans
    • Clandinin T.R., DeModena J.A., Sternberg P.W. Inositol trisphosphate mediates a RAS-independent response to LET-23 receptor tyrosine kinase activation in C. elegans. Cell. 92:1998;523-533
    • (1998) Cell , vol.92 , pp. 523-533
    • Clandinin, T.R.1    Demodena, J.A.2    Sternberg, P.W.3
  • 10
    • 0027232398 scopus 로고
    • 2+ by rat brain inositol 1,4,5-trisphosphate 3-kinase
    • 2+ by rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 291:1993;811-816
    • (1993) Biochem. J. , vol.291 , pp. 811-816
    • Communi, D.1    Takazawa, K.2    Erneux, C.3
  • 11
    • 0029165902 scopus 로고
    • Molecular study and regulation of D-myo-inositol 1,4,5-trisphosphate 3-kinase
    • Communi D., Vanweyenberg V., Erneux C. Molecular study and regulation of D-myo-inositol 1,4,5-trisphosphate 3-kinase. Cell. Signal. 7:1995;643-650
    • (1995) Cell. Signal. , vol.7 , pp. 643-650
    • Communi, D.1    Vanweyenberg, V.2    Erneux, C.3
  • 12
    • 0030891857 scopus 로고    scopus 로고
    • D-myo-inositol 1,4,5-trisphosphate 3-kinase a is activated by receptor activation through a calcium:calmodulin-dependent protein kinase II phosphorylation mechanism
    • Communi D., Vanweyenberg V., Erneux C. D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calcium:calmodulin- dependent protein kinase II phosphorylation mechanism. EMBO J. 16:1997;1943-1952
    • (1997) EMBO J. , vol.16 , pp. 1943-1952
    • Communi, D.1    Vanweyenberg, V.2    Erneux, C.3
  • 14
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 15
    • 0034531694 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C
    • Dewaste V., Pouillon V., Moreau C., Shears S., Takazawa K., Erneux C. Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C. Biochem. J. 352:2000;343-351
    • (2000) Biochem. J. , vol.352 , pp. 343-351
    • Dewaste, V.1    Pouillon, V.2    Moreau, C.3    Shears, S.4    Takazawa, K.5    Erneux, C.6
  • 17
    • 0034672620 scopus 로고    scopus 로고
    • Inositol polyphosphate kinase activity of Arg82/ArgRIII is not required for the regulation of the arginine metabolism in yeast
    • Dubois E., Dewaste V., Erneux C., Messenguy F. Inositol polyphosphate kinase activity of Arg82/ArgRIII is not required for the regulation of the arginine metabolism in yeast. FEBS Lett. 486:2000;300-304
    • (2000) FEBS Lett. , vol.486 , pp. 300-304
    • Dubois, E.1    Dewaste, V.2    Erneux, C.3    Messenguy, F.4
  • 18
    • 0037189551 scopus 로고    scopus 로고
    • In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis
    • Dubois E., Scherens B., Vierendeels F., Ho M.M., Messenguy F., Shears S.B. In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis. J. Biol. Chem. 277:2002;23755-23763
    • (2002) J. Biol. Chem. , vol.277 , pp. 23755-23763
    • Dubois, E.1    Scherens, B.2    Vierendeels, F.3    Ho, M.M.4    Messenguy, F.5    Shears, S.B.6
  • 19
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • Goldberg J., Nairn A.C., Kuriyan J. Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell. 84:1996;875-887
    • (1996) Cell , vol.84 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 20
    • 0032804537 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinase: A link between protein kinase and glutathione synthase folds
    • Grishin N.V. Phosphatidylinositol phosphate kinase. a link between protein kinase and glutathione synthase folds J. Mol. Biol. 291:1999;239-247
    • (1999) J. Mol. Biol. , vol.291 , pp. 239-247
    • Grishin, N.V.1
  • 22
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., Kuriyan J. The conformational plasticity of protein kinases. Cell. 109:2002;275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 23
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine R.F., Schell M.J. Back in the water. the return of the inositol phosphates Nat. Rev. Mol. Cell Biol. 2:2001;327-338
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 24
    • 0022491949 scopus 로고
    • The inositol tris/tetrakisphosphate pathway-demonstration of Ins(1,4,5)P3 3-kinase activity in animal tissues
    • Irvine R.F., Letcher A.J., Heslop J.P., Berridge M.J. The inositol tris/tetrakisphosphate pathway-demonstration of Ins(1,4,5)P3 3-kinase activity in animal tissues. Nature. 320:1986;631-634
    • (1986) Nature , vol.320 , pp. 631-634
    • Irvine, R.F.1    Letcher, A.J.2    Heslop, J.P.3    Berridge, M.J.4
  • 25
    • 0034711248 scopus 로고    scopus 로고
    • Biochemical and functional characterization of inositol 1,3,4,5, 6-pentakisphosphate 2-kinases
    • Ives E.B., Nichols J., Wente S.R., York J.D. Biochemical and functional characterization of inositol 1,3,4,5, 6-pentakisphosphate 2-kinases. J. Biol. Chem. 275:2000;36575-36583
    • (2000) J. Biol. Chem. , vol.275 , pp. 36575-36583
    • Ives, E.B.1    Nichols, J.2    Wente, S.R.3    York, J.D.4
  • 26
    • 0032456588 scopus 로고    scopus 로고
    • Enhanced hippocampal CA1 LTP but normal spatial learning in inositol 1,4,5-trisphosphate 3-kinase(A)-deficient mice
    • Jun K., Choi G., Yang S.G., Choi K.Y., Kim H., Chan G.C., Storm D.R., Albert C., Mayr G.W., Lee C.J., et al. Enhanced hippocampal CA1 LTP but normal spatial learning in inositol 1,4,5-trisphosphate 3-kinase(A)-deficient mice. Learn. Mem. 5:1998;317-330
    • (1998) Learn. Mem. , vol.5 , pp. 317-330
    • Jun, K.1    Choi, G.2    Yang, S.G.3    Choi, K.Y.4    Kim, H.5    Chan, G.C.6    Storm, D.R.7    Albert, C.8    Mayr, G.W.9    Lee, C.J.10
  • 28
    • 0034872365 scopus 로고    scopus 로고
    • Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides
    • Lemmon M.A., Ferguson K.M. Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides. Biochem. Soc. Trans. 29:2001;377-384
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 377-384
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 31
    • 0036215864 scopus 로고    scopus 로고
    • Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase
    • Madhusudan, Akamine P., Xuong N.H., Taylor S.S. Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase. Nat. Struct. Biol. 9:2002;273-277
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 273-277
    • Madhusudan1    Akamine, P.2    Xuong, N.H.3    Taylor, S.S.4
  • 32
    • 0025968702 scopus 로고
    • Inositol 1,4,5-trisphosphate 3-kinase distribution in the rat brain. High levels in the hippocampal CA1 pyramidal and cerebellar Purkinje cells suggest its involvement in some memory processes
    • Mailleux P., Takazawa K., Erneux C., Vanderhaeghen J.J. Inositol 1,4,5-trisphosphate 3-kinase distribution in the rat brain. High levels in the hippocampal CA1 pyramidal and cerebellar Purkinje cells suggest its involvement in some memory processes. Brain Res. 539:1991;203-210
    • (1991) Brain Res. , vol.539 , pp. 203-210
    • Mailleux, P.1    Takazawa, K.2    Erneux, C.3    Vanderhaeghen, J.J.4
  • 33
    • 0023991581 scopus 로고
    • Partial purification and some properties of rat brain inositol 1,4,5-trisphosphate 3-kinase
    • Morris A.J., Murray K.J., England P.J., Downes C.P., Michell R.H. Partial purification and some properties of rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 251:1988;157-163
    • (1988) Biochem. J. , vol.251 , pp. 157-163
    • Morris, A.J.1    Murray, K.J.2    England, P.J.3    Downes, C.P.4    Michell, R.H.5
  • 34
    • 0038165444 scopus 로고    scopus 로고
    • Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm
    • Nalaskowski M.M., Bertsch U., Fanick W., Stockebrand M.C., Schmale H., Mayr G.W. Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm. J. Biol. Chem. 278:2003;19765-19776
    • (2003) J. Biol. Chem. , vol.278 , pp. 19765-19776
    • Nalaskowski, M.M.1    Bertsch, U.2    Fanick, W.3    Stockebrand, M.C.4    Schmale, H.5    Mayr, G.W.6
  • 35
    • 0034677903 scopus 로고    scopus 로고
    • A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control
    • Odom A.R., Stahlberg A., Wente S.R., York J.D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science. 287:2000;2026-2029
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 36
    • 1842839883 scopus 로고    scopus 로고
    • Ins(1,4,5)P(3) metabolism and the family of IP(3)-3Kinases
    • Pattni K., Banting G. Ins(1,4,5)P(3) metabolism and the family of IP(3)-3Kinases. Cell. Signal. 16:2004;643-654
    • (2004) Cell. Signal. , vol.16 , pp. 643-654
    • Pattni, K.1    Banting, G.2
  • 39
    • 0032544230 scopus 로고    scopus 로고
    • Structure of type IIβ phosphatidylinositol phosphate kinase: A protein kinase fold flattened for interfacial phosphorylation
    • Rao V.D., Misra S., Boronenkov I.V., Anderson R.A., Hurley J.H. Structure of type IIβ phosphatidylinositol phosphate kinase. a protein kinase fold flattened for interfacial phosphorylation Cell. 94:1998;829-839
    • (1998) Cell , vol.94 , pp. 829-839
    • Rao, V.D.1    Misra, S.2    Boronenkov, I.V.3    Anderson, R.A.4    Hurley, J.H.5
  • 40
    • 0033581832 scopus 로고    scopus 로고
    • Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
    • Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9:1999;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
  • 41
    • 0035956860 scopus 로고    scopus 로고
    • Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate
    • Saiardi A., Nagata E., Luo H.R., Sawa A., Luo X., Snowman A.M., Snyder S.H. Mammalian inositol polyphosphate multikinase synthesizes inositol 1,4,5-trisphosphate and an inositol pyrophosphate. Proc. Natl. Acad. Sci. USA. 98:2001;2306-2311
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2306-2311
    • Saiardi, A.1    Nagata, E.2    Luo, H.R.3    Sawa, A.4    Luo, X.5    Snowman, A.M.6    Snyder, S.H.7
  • 43
    • 0035813147 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate 3-kinase a associates with F-actin and dendritic spines via its N terminus
    • Schell M.J., Erneux C., Irvine R.F. Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus. J. Biol. Chem. 276:2001;37537-37546
    • (2001) J. Biol. Chem. , vol.276 , pp. 37537-37546
    • Schell, M.J.1    Erneux, C.2    Irvine, R.F.3
  • 44
    • 0942290439 scopus 로고    scopus 로고
    • How versatile are inositol phosphate kinases?
    • Shears S.B. How versatile are inositol phosphate kinases? Biochem. J. 377:2004;265-280
    • (2004) Biochem. J. , vol.377 , pp. 265-280
    • Shears, S.B.1
  • 45
    • 0026002899 scopus 로고
    • Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase
    • Takazawa K., Erneux C. Identification of residues essential for catalysis and binding of calmodulin in rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 280:1991;125-129
    • (1991) Biochem. J. , vol.280 , pp. 125-129
    • Takazawa, K.1    Erneux, C.2
  • 46
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor S.S., Radzio-Andzelm E. Three protein kinase structures define a common motif. Structure. 2:1994;345-355
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 47
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger T.C., Berendzen J. Automated structure solution for MIR and MAD. Acta Crystallogr. D. 55:1999;849-861
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 48
    • 0030930307 scopus 로고    scopus 로고
    • Structural identification of the myo-inositol 1,4,5-trisphosphate-binding domain in rat brain inositol 1,4,5-trisphosphate 3-kinase
    • Togashi S., Takazawa K., Endo T., Erneux C., Onaya T. Structural identification of the myo-inositol 1,4,5-trisphosphate-binding domain in rat brain inositol 1,4,5-trisphosphate 3-kinase. Biochem. J. 326:1997;221-225
    • (1997) Biochem. J. , vol.326 , pp. 221-225
    • Togashi, S.1    Takazawa, K.2    Endo, T.3    Erneux, C.4    Onaya, T.5
  • 49
    • 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., Wente S.R. The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase. J. Biol. Chem. 277:2002;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
  • 50
    • 0033581886 scopus 로고    scopus 로고
    • Structural insights into phosphoinositide 3-kinase catalysis and signalling
    • Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L. Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature. 402:1999;313-320
    • (1999) Nature , vol.402 , pp. 313-320
    • Walker, E.H.1    Perisic, O.2    Ried, C.3    Stephens, L.4    Williams, R.L.5
  • 52
    • 17544366147 scopus 로고    scopus 로고
    • Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme
    • Wilson M.P., Majerus P.W. Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme. J. Biol. Chem. 271:1996;11904-11910
    • (1996) J. Biol. Chem. , vol.271 , pp. 11904-11910
    • Wilson, M.P.1    Majerus, P.W.2
  • 53
    • 0026508136 scopus 로고
    • Ultrastructural localization of inositol 1,4,5-trisphosphate 3-kinase in rat cerebellar cortex
    • Yamada M., Kakita A., Mizuguchi M., Rhee S.G., Kim S.U., Ikuta F. Ultrastructural localization of inositol 1,4,5-trisphosphate 3-kinase in rat cerebellar cortex. Brain Res. 578:1992;41-48
    • (1992) Brain Res. , vol.578 , pp. 41-48
    • Yamada, M.1    Kakita, A.2    Mizuguchi, M.3    Rhee, S.G.4    Kim, S.U.5    Ikuta, F.6
  • 54
    • 0035947077 scopus 로고    scopus 로고
    • Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity
    • Yamaguchi H., Matsushita M., Nairn A.C., Kuriyan J. Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity. Mol. Cell. 7:2001;1047-1057
    • (2001) Mol. Cell , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1    Matsushita, M.2    Nairn, A.C.3    Kuriyan, J.4
  • 55
    • 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., Wente S.R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science. 285:1999;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
  • 56
    • 0032923648 scopus 로고    scopus 로고
    • Use of phosphorofluoridate analogues of D-myo-inositol 1,4,5-trisphosphate to assess the involvement of ionic interactions in its recognition by the receptor and metabolising enzymes
    • Yoshimura K., Watanabe Y., Erneux C., Hirata M. Use of phosphorofluoridate analogues of D-myo-inositol 1,4,5-trisphosphate to assess the involvement of ionic interactions in its recognition by the receptor and metabolising enzymes. Cell. Signal. 11:1999;117-125
    • (1999) Cell. Signal. , vol.11 , pp. 117-125
    • Yoshimura, K.1    Watanabe, Y.2    Erneux, C.3    Hirata, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.