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Volumn 13, Issue 2, 2003, Pages 101-106

Fluorescence imaging of signaling networks

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 0037307441     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)00040-5     Document Type: Review
Times cited : (61)

References (64)
  • 1
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi J.L., et al. Exploring the metabolic and genetic control of gene expression on a genomic scale. Science. 278:1997;680-686.
    • (1997) Science , vol.278 , pp. 680-686
    • DeRisi, J.L.1
  • 2
    • 0035712849 scopus 로고    scopus 로고
    • Advances in proteome analysis by mass spectrometry
    • Griffin T.J., et al. Advances in proteome analysis by mass spectrometry. Curr. Opin. Biotechnol. 12:2001;607-612.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 607-612
    • Griffin, T.J.1
  • 3
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T., et al. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol. 11:2001;504-511.
    • (2001) Trends Cell Biol. , vol.11 , pp. 504-511
    • Pawson, T.1
  • 4
    • 0037199968 scopus 로고    scopus 로고
    • Hierarchical organization of modularity in metabolic networks
    • Ravasz E., et al. Hierarchical organization of modularity in metabolic networks. Science. 297:2002;1551-1555.
    • (2002) Science , vol.297 , pp. 1551-1555
    • Ravasz, E.1
  • 5
    • 0037165942 scopus 로고    scopus 로고
    • Combinatorial synthesis of genetic networks
    • Guet C.C., et al. Combinatorial synthesis of genetic networks. Science. 296:2002;1466-1470.
    • (2002) Science , vol.296 , pp. 1466-1470
    • Guet, C.C.1
  • 6
    • 0036578795 scopus 로고    scopus 로고
    • Network motifs in the transcriptional regulation network of Escherichia coli
    • Shen-Orr S.S., et al. Network motifs in the transcriptional regulation network of Escherichia coli. Nat. Genet. 31:2002;64-68.
    • (2002) Nat. Genet. , vol.31 , pp. 64-68
    • Shen-Orr, S.S.1
  • 7
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson G., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocrinol. Rev. 22:2001;153-183.
    • (2001) Endocrinol. Rev. , vol.22 , pp. 153-183
    • Pearson, G.1
  • 9
    • 0036196195 scopus 로고    scopus 로고
    • Intracellular transport mechanisms of signal transducers
    • Dorn G.W. 2nd, Mochly-Rosen D. Intracellular transport mechanisms of signal transducers. Annu. Rev. Physiol. 64:2002;407-429.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 407-429
    • Dorn G.W. II1    Mochly-Rosen, D.2
  • 10
    • 0035224759 scopus 로고    scopus 로고
    • The versatility and complexity of calcium signalling
    • Berridge M.J. The versatility and complexity of calcium signalling. Novartis Found. Symp. 239:2001;52-64.
    • (2001) Novartis Found. Symp. , vol.239 , pp. 52-64
    • Berridge, M.J.1
  • 11
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • Teruel M.N., Meyer T. Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell. 103:2000;181-184.
    • (2000) Cell , vol.103 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 12
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering C., et al. Comparative assessment of large-scale data sets of protein-protein interactions. Nature. 417:2002;399-403.
    • (2002) Nature , vol.417 , pp. 399-403
    • Von Mering, C.1
  • 13
    • 0035222942 scopus 로고    scopus 로고
    • Protein interaction maps for model organisms
    • Walhout A.J., Vidal M. Protein interaction maps for model organisms. Nat. Rev. Mol. Cell Biol. 2:2001;55-62.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 55-62
    • Walhout, A.J.1    Vidal, M.2
  • 14
    • 0035860551 scopus 로고    scopus 로고
    • A gene expression map for Caenorhabditis elegans
    • Kim S.K., et al. A gene expression map for Caenorhabditis elegans. Science. 293:2001;2087-2092.
    • (2001) Science , vol.293 , pp. 2087-2092
    • Kim, S.K.1
  • 15
    • 0034671792 scopus 로고    scopus 로고
    • Global analysis of the genetic network controlling a bacterial cell cycle
    • Laub M.T., et al. Global analysis of the genetic network controlling a bacterial cell cycle. Science. 290:2000;2144-2148.
    • (2000) Science , vol.290 , pp. 2144-2148
    • Laub, M.T.1
  • 16
    • 0035805255 scopus 로고    scopus 로고
    • Integrated genomic and proteomic analyses of a systematically perturbed metabolic network
    • Ideker T., et al. Integrated genomic and proteomic analyses of a systematically perturbed metabolic network. Science. 292:2001;929-934.
    • (2001) Science , vol.292 , pp. 929-934
    • Ideker, T.1
  • 17
    • 0036699526 scopus 로고    scopus 로고
    • Revealing modular organization in the yeast transcriptional network
    • Ihmels J., et al. Revealing modular organization in the yeast transcriptional network. Nat. Genet. 31:2002;370-377.
    • (2002) Nat. Genet. , vol.31 , pp. 370-377
    • Ihmels, J.1
  • 18
    • 0037087575 scopus 로고    scopus 로고
    • Subcellular localization of the yeast proteome
    • Kumar A., et al. Subcellular localization of the yeast proteome. Genes Dev. 16:2002;707-719.
    • (2002) Genes Dev. , vol.16 , pp. 707-719
    • Kumar, A.1
  • 19
    • 0034089165 scopus 로고    scopus 로고
    • Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library
    • Ding D.Q., et al. Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library. Genes Cells. 5:2000;169-190.
    • (2000) Genes Cells , vol.5 , pp. 169-190
    • Ding, D.Q.1
  • 20
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • Simpson J.C., et al. Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep. 1:2000;287-292.
    • (2000) EMBO Rep. , vol.1 , pp. 287-292
    • Simpson, J.C.1
  • 21
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67:1998;509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 22
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized receptor-mediated tyrosine phosphorylation in living cells
    • Stauffer T.P., Meyer T. Compartmentalized receptor-mediated tyrosine phosphorylation in living cells. J. Cell Biol. 139:1997;1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 23
    • 0036520682 scopus 로고    scopus 로고
    • Fluorescence photobleaching analysis for the study of cellular dynamics
    • Klonis N., et al. Fluorescence photobleaching analysis for the study of cellular dynamics. Eur. Biophys. J. 31:2002;36-51.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 36-51
    • Klonis, N.1
  • 24
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits E.A., Neefjes J.J. From fixed to FRAP: measuring protein mobility and activity in living cells. Nat. Cell Biol. 3:2001;E145-E147.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 145-E147
    • Reits, E.A.1    Neefjes, J.J.2
  • 25
    • 0019829560 scopus 로고
    • A non-disruptive technique for loading calcium buffers and indicators into cells
    • Tsien R.Y. A non-disruptive technique for loading calcium buffers and indicators into cells. Nature. 290:1981;527-528.
    • (1981) Nature , vol.290 , pp. 527-528
    • Tsien, R.Y.1
  • 26
    • 0028604576 scopus 로고
    • Source of nuclear calcium signals
    • Allbritton N.L., et al. Source of nuclear calcium signals. Proc. Natl Acad. Sci. U.S.A. 91:1994;12458-12462.
    • (1994) Proc. Natl Acad. Sci. U.S.A. , vol.91 , pp. 12458-12462
    • Allbritton, N.L.1
  • 27
    • 0026659512 scopus 로고
    • 2+ revealed by specifically targeted recombinant aequorin
    • 2+ revealed by specifically targeted recombinant aequorin. Nature. 358:1992;325-327.
    • (1992) Nature , vol.358 , pp. 325-327
    • Rizzuto, R.1
  • 28
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane phosphatidylinositol-4,5 biphosphate concentration monitored in living cells
    • Stauffer T.P., et al. Receptor-induced transient reduction in plasma membrane phosphatidylinositol-4,5 biphosphate concentration monitored in living cells. Curr. Biol. 8:1998;343-346.
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1
  • 29
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • Venkateswarlu K., et al. Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8:1998;463-466.
    • (1998) Curr. Biol. , vol.8 , pp. 463-466
    • Venkateswarlu, K.1
  • 30
    • 0031834338 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase and Akt by Tie1: A potential role for Tie2 in endothelial cell survival
    • Kontos C.D., et al. Activation of phosphatidylinositol 3-kinase and Akt by Tie1: a potential role for Tie2 in endothelial cell survival. Mol. Cell. Biol. 18:1998;4131-4140.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4131-4140
    • Kontos, C.D.1
  • 31
    • 0034234718 scopus 로고    scopus 로고
    • How accurately can we image inositol lipids in living cells?
    • Balla T., et al. How accurately can we image inositol lipids in living cells? Trends Pharmacol. Sci. 21:2000;238-241.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 238-241
    • Balla, T.1
  • 32
    • 0035313710 scopus 로고    scopus 로고
    • Subcellular targeting by membrane lipids
    • Hurley J.H., Meyer T. Subcellular targeting by membrane lipids. Curr. Opin. Cell Biol. 13:2001;146-152.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 146-152
    • Hurley, J.H.1    Meyer, T.2
  • 33
    • 0019494948 scopus 로고
    • Cell-substrate contacts illuminated by total internal reflection fluorescence
    • Axelrod D. Cell-substrate contacts illuminated by total internal reflection fluorescence. J. Cell Biol. 89:1981;141-145.
    • (1981) J. Cell Biol. , vol.89 , pp. 141-145
    • Axelrod, D.1
  • 34
    • 0035315984 scopus 로고    scopus 로고
    • A real-time view of life within 100 nm of the plasma membrane
    • Steyer J.A., Almers W. A real-time view of life within 100 nm of the plasma membrane. Nat. Rev. Mol. Cell Biol. 2:2001;268-275.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 268-275
    • Steyer, J.A.1    Almers, W.2
  • 35
    • 0035943029 scopus 로고    scopus 로고
    • 2+ oscillations and waves by oscillating translocation and activation of protein kinase C
    • 2+ oscillations and waves by oscillating translocation and activation of protein kinase C. Curr. Biol. 11:2001;1089-1097.
    • (2001) Curr. Biol. , vol.11 , pp. 1089-1097
    • Codazzi, F.1
  • 36
    • 0034638836 scopus 로고    scopus 로고
    • Spatial sensing in fibroblasts mediated by 3′ phosphoinositides
    • Haugh J.M., et al. Spatial sensing in fibroblasts mediated by 3′ phosphoinositides. J. Cell Biol. 151:2000;1269-1280.
    • (2000) J. Cell Biol. , vol.151 , pp. 1269-1280
    • Haugh, J.M.1
  • 37
    • 0037040545 scopus 로고    scopus 로고
    • Parallel single cell monitoring of receptor-triggered membrane translocation of a calcium sensing protein module
    • Teruel M.N., Meyer T. Parallel single cell monitoring of receptor-triggered membrane translocation of a calcium sensing protein module. Science. 295:2002;1910-1912.
    • (2002) Science , vol.295 , pp. 1910-1912
    • Teruel, M.N.1    Meyer, T.2
  • 38
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47:1978;819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 39
    • 0034304491 scopus 로고    scopus 로고
    • Watching proteins in the wild: Fluorescence methods to study protein dynamics in living cells
    • Chamberlain C., Hahn K.M. Watching proteins in the wild: fluorescence methods to study protein dynamics in living cells. Traffic. 1:2000;755-762.
    • (2000) Traffic , vol.1 , pp. 755-762
    • Chamberlain, C.1    Hahn, K.M.2
  • 40
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok B.A., Heim R. Using GFP in FRET-based applications. Trends Cell Biol. 9:1999;57-60.
    • (1999) Trends Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 41
    • 0031011418 scopus 로고    scopus 로고
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators. J. Biol. Chem. 272:1997;13270-13274.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13270-13274
    • Romoser, V.A.1
  • 42
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin. Nature. 388:1997;882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 43
    • 0035341596 scopus 로고    scopus 로고
    • Imaging biochemistry inside cells
    • Wouters F.S., et al. Imaging biochemistry inside cells. Trends Cell Biol. 11:2001;203-211.
    • (2001) Trends Cell Biol. , vol.11 , pp. 203-211
    • Wouters, F.S.1
  • 44
    • 0035805510 scopus 로고    scopus 로고
    • Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer
    • van der Wal J., et al. Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer. J. Biol. Chem. 276:2001;15337-15344.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15337-15344
    • Van der Wal, J.1
  • 45
    • 0035407522 scopus 로고    scopus 로고
    • KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: Measurements in living cells using FRET
    • Majoul I., et al. KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev. Cell. 1:2001;139-153.
    • (2001) Dev. Cell , vol.1 , pp. 139-153
    • Majoul, I.1
  • 46
    • 0034644603 scopus 로고    scopus 로고
    • Localized Rac activation dynamics visualized in living cells
    • Kraynov V.S., et al. Localized Rac activation dynamics visualized in living cells. Science. 290:2000;333-337.
    • (2000) Science , vol.290 , pp. 333-337
    • Kraynov, V.S.1
  • 47
    • 0035963331 scopus 로고    scopus 로고
    • Spatio-temporal images of growth-factor-induced activation of Ras and Rap1
    • Mochizuki N., et al. Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature. 411:2001;1065-1068.
    • (2001) Nature , vol.411 , pp. 1065-1068
    • Mochizuki, N.1
  • 48
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo
    • Kurokawa K., et al. A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem. 276:2001;31305-31310.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31305-31310
    • Kurokawa, K.1
  • 49
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting A.Y., et al. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl Acad. Sci. U.S.A. 98:2001;15003-15008.
    • (2001) Proc. Natl Acad. Sci. U.S.A. , vol.98 , pp. 15003-15008
    • Ting, A.Y.1
  • 50
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang J., et al. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl Acad. Sci. U.S.A. 98:2001;14997-15002.
    • (2001) Proc. Natl Acad. Sci. U.S.A. , vol.98 , pp. 14997-15002
    • Zhang, J.1
  • 51
    • 0037062424 scopus 로고    scopus 로고
    • A monomeric red fluorescent protein
    • Campbell R.E., et al. A monomeric red fluorescent protein. Proc. Natl Acad. Sci. U.S.A. 99:2002;7877-7882.
    • (2002) Proc. Natl Acad. Sci. U.S.A. , vol.99 , pp. 7877-7882
    • Campbell, R.E.1
  • 52
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch R.E., et al. Calcium oscillations increase the efficiency and specificity of gene expression. Nature. 392:1998;933-936.
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1
  • 53
    • 0032580157 scopus 로고
    • 2+ spike frequency can optimize gene expression
    • 2+ spike frequency can optimize gene expression. Nature. 392:1988;936-941.
    • (1988) Nature , vol.392 , pp. 936-941
    • Li, W.1
  • 54
    • 0022575044 scopus 로고
    • Repetitive transient rises in cytoplasmic free calcium in hormone-stimulated hepatocytes
    • Woods N.M., et al. Repetitive transient rises in cytoplasmic free calcium in hormone-stimulated hepatocytes. Nature. 319:1986;600-602.
    • (1986) Nature , vol.319 , pp. 600-602
    • Woods, N.M.1
  • 55
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell J.E. Jr, Machleder E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science. 280:1998;895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell J.E., Jr.1    Machleder, E.M.2
  • 56
    • 0032472195 scopus 로고    scopus 로고
    • Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter
    • Zlokarnik G., et al. Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter. Science. 279:1998;84-88.
    • (1998) Science , vol.279 , pp. 84-88
    • Zlokarnik, G.1
  • 57
    • 0035477390 scopus 로고    scopus 로고
    • Genetically encoded optical sensors of neuronal activity and cellular function
    • Guerrero G., Isacoff E.Y. Genetically encoded optical sensors of neuronal activity and cellular function. Curr. Opin. Neurobiol. 11:2001;601-607.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 601-607
    • Guerrero, G.1    Isacoff, E.Y.2
  • 58
    • 0030659755 scopus 로고    scopus 로고
    • GLUT4 vesicle dynamics in living 3T3 L1 adipocytes visualized with green-fluorescent protein
    • Oatey P.B., et al. GLUT4 vesicle dynamics in living 3T3 L1 adipocytes visualized with green-fluorescent protein. Biochem. J. 327:1997;637-642.
    • (1997) Biochem. J. , vol.327 , pp. 637-642
    • Oatey, P.B.1
  • 59
    • 0035233367 scopus 로고    scopus 로고
    • Recent advances in chemical approaches to the study of biological systems
    • Shogren-Knaak M.A., et al. Recent advances in chemical approaches to the study of biological systems. Annu. Rev. Cell Dev. Biol. 17:2001;405-433.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 405-433
    • Shogren-Knaak, M.A.1
  • 60
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer D.M., et al. Controlling signal transduction with synthetic ligands. Science. 262:1993;1019-1024.
    • (1993) Science , vol.262 , pp. 1019-1024
    • Spencer, D.M.1
  • 61
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer T.U., et al. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science. 286:1999;971-974.
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1
  • 62
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A., et al. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature. 391:1998;806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1
  • 63
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir S.M., et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature. 411:2001;494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1
  • 64
    • 0002810051 scopus 로고    scopus 로고
    • GFP-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea E., et al. GFP-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140:1998;1-14.
    • (1998) J. Cell Biol. , vol.140 , pp. 1-14
    • Oancea, E.1


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