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Volumn 16, Issue 5, 2004, Pages 674-683

Using live FRET imaging to reveal early protein-protein interactions during T cell activation;Erratum: Using live FRET imaging to reveal early protein-protein interactions during T cell activation (Current Opinion in Immunology (2004) 16 (418) DOI: 10.1016/j.coi.2004.05.019)

Author keywords

YFP; bioluminescence resonance energy transfer; T cell receptor; green fluorescent protein; IL; cyan fluorescent protein; FRET; CFP; GFP; fluorescence resonance energy transfer; FLIM; BRET; TCR; fluorescence lifetime imaging microscopy; interleukin

Indexed keywords

ERRATUM; RETRACTED ARTICLE; ANIMAL; CELL COMMUNICATION; FLUORESCENCE MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; IMMUNOLOGY; LYMPHOCYTE ACTIVATION; PROTEIN BINDING; REVIEW; T LYMPHOCYTE;

EID: 15944400980     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2004.05.019     Document Type: Review
Times cited : (23)

References (65)
  • 4
    • 0346244099 scopus 로고    scopus 로고
    • T-cell-antigen recognition and the immunological synapse
    • J.B. Huppa M.M. Davis T-cell-antigen recognition and the immunological synapse Nat Rev Immunol 3 2003 973 983
    • (2003) Nat Rev Immunol , vol.3 , pp. 973-983
    • Huppa, J.B.1    Davis, M.M.2
  • 5
    • 0037306064 scopus 로고    scopus 로고
    • An architectural perspective on signaling by the pre-, alphabeta and gammadelta T cell receptors
    • S.M. Hayes E.W. Shores P.E. Love An architectural perspective on signaling by the pre-, alphabeta and gammadelta T cell receptors Immunol Rev 191 2003 28 37
    • (2003) Immunol Rev , vol.191 , pp. 28-37
    • Hayes, S.M.1    Shores, E.W.2    Love, P.E.3
  • 7
    • 0036801024 scopus 로고    scopus 로고
    • Probing T cell membrane organization using dimeric MHC-Ig complexes
    • T. Fahmy J. Bieler J. Schneck Probing T cell membrane organization using dimeric MHC-Ig complexes J Immunol Methods 268 2002 93 106
    • (2002) J Immunol Methods , vol.268 , pp. 93-106
    • Fahmy, T.1    Bieler, J.2    Schneck, J.3
  • 8
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications
    • S.R. Adams R.E. Campbell L.A. Gross B.R. Martin G.K. Walkup Y. Yao J. Llopis R.Y. Tsien New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo : synthesis and biological applications J Am Chem Soc 124 2002 6063 6076
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 10
    • 0037032454 scopus 로고    scopus 로고
    • Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair
    • T. Zimmermann J. Rietdorf A. Girod V. Georget R. Pepperkok Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair FEBS Lett 531 2002 245 249
    • (2002) FEBS Lett , vol.531 , pp. 245-249
    • Zimmermann, T.1    Rietdorf, J.2    Girod, A.3    Georget, V.4    Pepperkok, R.5
  • 11
    • 85120202845 scopus 로고    scopus 로고
    • Zal T, Gascoigne NRJ: Photobleaching-Corrected FRET Efficiency Imaging of Live Cells . Biophys J 2004, 86 in press.
  • 12
    • 0036224370 scopus 로고    scopus 로고
    • Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse
    • T. Zal M.A. Zal N.R. Gascoigne Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse Immunity 16 2002 521 534
    • (2002) Immunity , vol.16 , pp. 521-534
    • Zal, T.1    Zal, M.A.2    Gascoigne, N.R.3
  • 13
    • 0036924067 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based stoichiometry in living cells
    • A. Hoppe K. Christensen J.A. Swanson Fluorescence resonance energy transfer-based stoichiometry in living cells Biophys J 83 2002 3652 3664
    • (2002) Biophys J , vol.83 , pp. 3652-3664
    • Hoppe, A.1    Christensen, K.2    Swanson, J.A.3
  • 14
    • 0742321790 scopus 로고    scopus 로고
    • phiFLIM: a new method to avoid aliasing in frequency-domain fluorescence lifetime imaging microscopy
    • E.B. Van Munster T.W. Gadella Jr. phiFLIM: a new method to avoid aliasing in frequency-domain fluorescence lifetime imaging microscopy J Microsc 213 2004 29 38
    • (2004) J Microsc , vol.213 , pp. 29-38
    • Van Munster, E.B.1    Gadella, T.W.2
  • 15
    • 0036164650 scopus 로고    scopus 로고
    • Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell
    • M. Elangovan R.N. Day A. Periasamy Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell J Microsc 205 2002 3 14
    • (2002) J Microsc , vol.205 , pp. 3-14
    • Elangovan, M.1    Day, R.N.2    Periasamy, A.3
  • 17
    • 0347756761 scopus 로고    scopus 로고
    • Protein localization in living cells and tissues using FRET and FLIM
    • Y. Chen J.D. Mills A. Periasamy Protein localization in living cells and tissues using FRET and FLIM Differentiation 71 2003 528 541
    • (2003) Differentiation , vol.71 , pp. 528-541
    • Chen, Y.1    Mills, J.D.2    Periasamy, A.3
  • 19
    • 0037763890 scopus 로고    scopus 로고
    • Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment
    • J.V. Rocheleau M. Edidin D.W. Piston Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment Biophys J 84 2003 4078 4086
    • (2003) Biophys J , vol.84 , pp. 4078-4086
    • Rocheleau, J.V.1    Edidin, M.2    Piston, D.W.3
  • 21
    • 0036708469 scopus 로고    scopus 로고
    • Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM)
    • A.H. Clayton Q.S. Hanley D.J. Arndt-Jovin V. Subramaniam T.M. Jovin Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM) Biophys J 83 2002 1631 1649
    • (2002) Biophys J , vol.83 , pp. 1631-1649
    • Clayton, A.H.1    Hanley, Q.S.2    Arndt-Jovin, D.J.3    Subramaniam, V.4    Jovin, T.M.5
  • 22
    • 85120227140 scopus 로고    scopus 로고
    • Rizzo MA, Springer GH, Granada B, Piston DW: An improved cyan fluorescent protein variant useful for FRET . Nat Biotechnol 2004.
  • 24
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • O. Zapata-Hommer O. Griesbeck Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP BMC Biotechnol 3 2003 5
    • (2003) BMC Biotechnol , vol.3 , pp. 5
    • Zapata-Hommer, O.1    Griesbeck, O.2
  • 25
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • M. Krogsgaard N. Prado E.J. Adams X.L. He D.C. Chow D.B. Wilson K.C. Garcia M.M. Davis Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation Mol Cell 12 2003 1367 1378
    • (2003) Mol Cell , vol.12 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Adams, E.J.3    He, X.L.4    Chow, D.C.5    Wilson, D.B.6    Garcia, K.C.7    Davis, M.M.8
  • 26
    • 0037188899 scopus 로고    scopus 로고
    • Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation
    • D. Gil W.W. Schamel M. Montoya F. Sanchez-Madrid B. Alarcon Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation Cell 109 2002 901 912
    • (2002) Cell , vol.109 , pp. 901-912
    • Gil, D.1    Schamel, W.W.2    Montoya, M.3    Sanchez-Madrid, F.4    Alarcon, B.5
  • 27
    • 1242307780 scopus 로고    scopus 로고
    • Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif
    • A. Sigalov D. Aivazian L. Stern Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif Biochemistry 43 2004 2049 2061
    • (2004) Biochemistry , vol.43 , pp. 2049-2061
    • Sigalov, A.1    Aivazian, D.2    Stern, L.3
  • 29
    • 0035879126 scopus 로고    scopus 로고
    • Monomeric class I molecules mediate TCR/CD3 epsilon/CD8 interaction on the surface of T cells
    • M.S. Block A.J. Johnson Y. Mendez-Fernandez L.R. Pease Monomeric class I molecules mediate TCR/CD3 epsilon/CD8 interaction on the surface of T cells J Immunol 167 2001 821 826
    • (2001) J Immunol , vol.167 , pp. 821-826
    • Block, M.S.1    Johnson, A.J.2    Mendez-Fernandez, Y.3    Pease, L.R.4
  • 30
    • 0037218840 scopus 로고    scopus 로고
    • High affinity xenoreactive TCR:MHC interaction recruits CD8 in absence of binding to MHC
    • J. Buslepp S.E. Kerry D. Loftus J.A. Frelinger E. Appella E.J. Collins High affinity xenoreactive TCR:MHC interaction recruits CD8 in absence of binding to MHC J Immunol 170 2003 373 383
    • (2003) J Immunol , vol.170 , pp. 373-383
    • Buslepp, J.1    Kerry, S.E.2    Loftus, D.3    Frelinger, J.A.4    Appella, E.5    Collins, E.J.6
  • 31
  • 32
    • 0344458247 scopus 로고
    • T-cell receptor-CD4 physical association in a murine T-cell hybridoma: induction by antigen receptor ligation
    • R.S. Mittler S.J. Goldman G.L. Spitalny S.J. Burakoff T-cell receptor-CD4 physical association in a murine T-cell hybridoma: induction by antigen receptor ligation Proc Natl Acad Sci USA 86 1989 8531 8535
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8531-8535
    • Mittler, R.S.1    Goldman, S.J.2    Spitalny, G.L.3    Burakoff, S.J.4
  • 33
    • 0026577623 scopus 로고
    • Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system
    • G. Szaba Jr. P.S. Pine J.L. Weaver M. Kasari A. Aszalos Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system Biophys J 61 1992 661 670
    • (1992) Biophys J , vol.61 , pp. 661-670
    • Szaba, G.1    Pine, P.S.2    Weaver, J.L.3    Kasari, M.4    Aszalos, A.5
  • 34
    • 0026612329 scopus 로고
    • p56lck association with CD4 is required for the interaction between CD4 and the TCR/CD3 complex and for optimal antigen stimulation
    • T.L. Collins S. Uniyal J. Shin J.L. Strominger R.S. Mittler S.J. Burakoff p56lck association with CD4 is required for the interaction between CD4 and the TCR/CD3 complex and for optimal antigen stimulation J Immunol 148 1992 2159 2162
    • (1992) J Immunol , vol.148 , pp. 2159-2162
    • Collins, T.L.1    Uniyal, S.2    Shin, J.3    Strominger, J.L.4    Mittler, R.S.5    Burakoff, S.J.6
  • 35
    • 0031048822 scopus 로고    scopus 로고
    • The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands
    • J. Madrenas L.A. Chau J. Smith J.A. Bluestone R.N. Germain The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands J Exp Med 185 1997 219 229
    • (1997) J Exp Med , vol.185 , pp. 219-229
    • Madrenas, J.1    Chau, L.A.2    Smith, J.3    Bluestone, J.A.4    Germain, R.N.5
  • 36
    • 1042290495 scopus 로고    scopus 로고
    • Molecular interactions at the T cell-antigen-presenting cell interface
    • N.R.J. Gascoigne T. Zal Molecular interactions at the T cell-antigen-presenting cell interface Curr Opin Immunol 16 2004 114 119
    • (2004) Curr Opin Immunol , vol.16 , pp. 114-119
    • Gascoigne, N.R.J.1    Zal, T.2
  • 37
    • 0034714184 scopus 로고    scopus 로고
    • Differential clustering of CD4 and CD3ζ during T cell recognition
    • M.F. Krummel M.D. Sjaastad C. Wülfing M.M. Davis Differential clustering of CD4 and CD3ζ during T cell recognition Science 289 2000 1349 1352
    • (2000) Science , vol.289 , pp. 1349-1352
    • Krummel, M.F.1    Sjaastad, M.D.2    Wülfing, C.3    Davis, M.M.4
  • 38
    • 0036906497 scopus 로고    scopus 로고
    • Dynamics of p56lck translocation to the T cell immunological synapse following agonist and antagonist stimulation
    • L.I. Ehrlich P.J. Ebert M.F. Krummel A. Weiss M.M. Davis Dynamics of p56lck translocation to the T cell immunological synapse following agonist and antagonist stimulation Immunity 17 2002 809 822
    • (2002) Immunity , vol.17 , pp. 809-822
    • Ehrlich, L.I.1    Ebert, P.J.2    Krummel, M.F.3    Weiss, A.4    Davis, M.M.5
  • 39
    • 0025746628 scopus 로고
    • Physical associations between CD45 and CD4 or CD8 occur as late activation events in antigen receptor-stimulated human T cells
    • R.S. Mittler B.M. Rankin P.A. Kiener Physical associations between CD45 and CD4 or CD8 occur as late activation events in antigen receptor-stimulated human T cells J Immunol 147 1991 3434 3440
    • (1991) J Immunol , vol.147 , pp. 3434-3440
    • Mittler, R.S.1    Rankin, B.M.2    Kiener, P.A.3
  • 40
    • 18544371851 scopus 로고    scopus 로고
    • Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction
    • S. Dornan Z. Sebestyen J. Gamble P. Nagy A. Bodnar L. Alldridge S. Doe N. Holmes L.K. Goff P. Beverley Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction J Biol Chem 277 2002 1912 1918
    • (2002) J Biol Chem , vol.277 , pp. 1912-1918
    • Dornan, S.1    Sebestyen, Z.2    Gamble, J.3    Nagy, P.4    Bodnar, A.5    Alldridge, L.6    Doe, S.7    Holmes, N.8    Goff, L.K.9    Beverley, P.10
  • 42
    • 0036303142 scopus 로고    scopus 로고
    • A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility
    • J.W. Legg C.A. Lewis M. Parsons T. Ng C.M. Isacke A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility Nat Cell Biol 4 2002 399 407
    • (2002) Nat Cell Biol , vol.4 , pp. 399-407
    • Legg, J.W.1    Lewis, C.A.2    Parsons, M.3    Ng, T.4    Isacke, C.M.5
  • 44
    • 0347988150 scopus 로고    scopus 로고
    • Lateral membrane protein associations of CD4 in lymphoid cells detected by cross-linking and mass spectrometry
    • O.K. Bernhard M.M. Sheil A.L. Cunningham Lateral membrane protein associations of CD4 in lymphoid cells detected by cross-linking and mass spectrometry Biochemistry 43 2004 256 264
    • (2004) Biochemistry , vol.43 , pp. 256-264
    • Bernhard, O.K.1    Sheil, M.M.2    Cunningham, A.L.3
  • 45
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer
    • A.K. Kenworthy M. Edidin Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer J Cell Biol 142 1998 69 84
    • (1998) J Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 46
    • 85120231306 scopus 로고    scopus 로고
    • Glebov OO, Nichols BJ: Lipid raft proteins have a random distribution during localized activation of the T-cell receptor . Nat Cell Biol 2004.
  • 49
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • M. Sato T. Ozawa K. Inukai T. Asano Y. Umezawa Fluorescent indicators for imaging protein phosphorylation in single living cells Nat Biotechnol 20 2002 287 294
    • (2002) Nat Biotechnol , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 50
    • 1242330282 scopus 로고    scopus 로고
    • A Ratiometric Expressible FRET Sensor for Phosphoinositides Displays a Signal Change in Highly Dynamic Membrane Structures in Fibroblasts
    • G. Cicchetti M. Biernacki J. Farquharson P.G. Allen A Ratiometric Expressible FRET Sensor for Phosphoinositides Displays a Signal Change in Highly Dynamic Membrane Structures in Fibroblasts Biochemistry 43 2004 1939 1949
    • (2004) Biochemistry , vol.43 , pp. 1939-1949
    • Cicchetti, G.1    Biernacki, M.2    Farquharson, J.3    Allen, P.G.4
  • 51
    • 0036853106 scopus 로고    scopus 로고
    • Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse
    • P.S. Costello M. Gallagher D.A. Cantrell Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse Nat Immunol 3 2002 1082 1089
    • (2002) Nat Immunol , vol.3 , pp. 1082-1089
    • Costello, P.S.1    Gallagher, M.2    Cantrell, D.A.3
  • 52
    • 0036852243 scopus 로고    scopus 로고
    • Imaging antigen-induced PI3K activation in T cells
    • J. Harriague G. Bismuth Imaging antigen-induced PI3K activation in T cells Nat Immunol 3 2002 1090 1096
    • (2002) Nat Immunol , vol.3 , pp. 1090-1096
    • Harriague, J.1    Bismuth, G.2
  • 53
    • 0037446762 scopus 로고    scopus 로고
    • Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling
    • A. Seth T. Otomo H.L. Yin M.K. Rosen Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling Biochemistry 42 2003 3997 4008
    • (2003) Biochemistry , vol.42 , pp. 3997-4008
    • Seth, A.1    Otomo, T.2    Yin, H.L.3    Rosen, M.K.4
  • 54
    • 3042793082 scopus 로고    scopus 로고
    • Study of g-protein-coupled receptor-protein interactions by bioluminescence resonance energy transfer
    • K.M. Kroeger K.A. Eidne Study of g-protein-coupled receptor-protein interactions by bioluminescence resonance energy transfer Methods Mol Biol 259 2004 323 334
    • (2004) Methods Mol Biol , vol.259 , pp. 323-334
    • Kroeger, K.M.1    Eidne, K.A.2
  • 55
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins
    • Y. Xu D.W. Piston C.H. Johnson A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins Proc Natl Acad Sci USA 96 1999 151 156
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 56
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • C.D. Hu Y. Chinenov T.K. Kerppola Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation Mol Cell 9 2002 789 798
    • (2002) Mol Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 57
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • C.D. Hu T.K. Kerppola Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis Nat Biotechnol 21 2003 539 545
    • (2003) Nat Biotechnol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 58
    • 0035984722 scopus 로고    scopus 로고
    • Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions
    • A. Galarneau M. Primeau L.E. Trudeau S.W. Michnick Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions Nat Biotechnol 20 2002 619 622
    • (2002) Nat Biotechnol , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 59
    • 0037180571 scopus 로고    scopus 로고
    • Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies
    • R. Paulmurugan Y. Umezawa S.S. Gambhir Noninvasive imaging of protein-protein interactions in living subjects by using reporter protein complementation and reconstitution strategies Proc Natl Acad Sci USA 99 2002 15608 15613
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15608-15613
    • Paulmurugan, R.1    Umezawa, Y.2    Gambhir, S.S.3
  • 60
    • 0037125999 scopus 로고    scopus 로고
    • A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins
    • T. Kohl K.G. Heinze R. Kuhlemann A. Koltermann P. Schwille A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins Proc Natl Acad Sci USA 99 2002 12161 12166
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12161-12166
    • Kohl, T.1    Heinze, K.G.2    Kuhlemann, R.3    Koltermann, A.4    Schwille, P.5
  • 61
  • 63
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • O. Griesbeck G.S. Baird R.E. Campbell D.A. Zacharias R.Y. Tsien Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications J Biol Chem 276 2001 29188 29194
    • (2001) J Biol Chem , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 64
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • T. Nagai K. Ibata E.S. Park M. Kubota K. Mikoshiba A. Miyawaki A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications Nat Biotechnol 20 2002 87 90
    • (2002) Nat Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 65
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • J.D. Violin J. Zhang R.Y. Tsien A.C. Newton A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J Cell Biol 161 2003 899 909
    • (2003) J Cell Biol , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4


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