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Volumn 5, Issue 2, 2010, Pages

A flow cytometry-based FRET assay to identify and analyse protein-protein interactions in living cells

Author keywords

[No Author keywords available]

Indexed keywords

NEF PROTEIN; TETHERIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VPU PROTEIN; BST2 PROTEIN, HUMAN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; HYBRID PROTEIN; LEUKOCYTE ANTIGEN; MEMBRANE PROTEIN; PHOTOPROTEIN; VPU PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77949591605     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009344     Document Type: Article
Times cited : (129)

References (40)
  • 1
    • 34047202181 scopus 로고    scopus 로고
    • Deciphering protein-protein interactions. Part I. Experimental techniques and databases
    • Shoemaker BA, Panchenko AR (2007) Deciphering protein-protein interactions. Part I. Experimental techniques and databases. PLoS Comput Biol 3: e42.
    • (2007) PLoS Comput Biol , vol.3
    • Shoemaker, B.A.1    Panchenko, A.R.2
  • 2
    • 13844277017 scopus 로고    scopus 로고
    • New methodologies for measuring protein interactions in vivo and in vitro
    • Piehler J (2005) New methodologies for measuring protein interactions in vivo and in vitro. Curr Opin Struct Biol 15: 4-14.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 4-14
    • Piehler, J.1
  • 3
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin PR (2000) The renaissance of fluorescence resonance energy transfer. Nat Struct Biol 7: 730-734.
    • (2000) Nat Struct Biol , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 4
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • Piston DW, Kremers GJ (2007) Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem Sci 32: 407-414.
    • (2007) Trends Biochem Sci , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 5
    • 0142138241 scopus 로고    scopus 로고
    • Analysis of protein interactions using fluorescence technologies
    • Yan Y, Marriott G (2003) Analysis of protein interactions using fluorescence technologies. Curr Opin Chem Biol 7: 635-640.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 635-640
    • Yan, Y.1    Marriott, G.2
  • 6
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney C, Danuser G (2003) FRET or no FRET: a quantitative comparison. Biophys J 84: 3992-4010.
    • (2003) Biophys J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 7
    • 33845359060 scopus 로고    scopus 로고
    • FRET and colocalization analyzer-a method to validate measurements of sensitized emission FRET acquired by confocal microscopy and available as an ImageJ Plug-in
    • Hachet-Haas M, Converset N, Marchal O, Matthes H, Gioria S, et al. (2006) FRET and colocalization analyzer-a method to validate measurements of sensitized emission FRET acquired by confocal microscopy and available as an ImageJ Plug-in. Microsc Res Tech 69: 941-956.
    • (2006) Microsc Res Tech , vol.69 , pp. 941-956
    • Hachet-Haas, M.1    Converset, N.2    Marchal, O.3    Matthes, H.4    Gioria, S.5
  • 8
    • 0033605542 scopus 로고    scopus 로고
    • Imaging protein kinase Calpha activation in cells
    • Ng T, Squire A, Hansra G, Bornancin F, Prevostel C, et al. (1999) Imaging protein kinase Calpha activation in cells. Science 283: 2085-2089.
    • (1999) Science , vol.283 , pp. 2085-2089
    • Ng, T.1    Squire, A.2    Hansra, G.3    Bornancin, F.4    Prevostel, C.5
  • 9
    • 0035430344 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    • Chan FK, Siegel RM, Zacharias D, Swofford R, Holmes KL, et al. (2001) Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein. Cytometry 44: 361-368.
    • (2001) Cytometry , vol.44 , pp. 361-368
    • Chan, F.K.1    Siegel, R.M.2    Zacharias, D.3    Swofford, R.4    Holmes, K.L.5
  • 10
    • 0346874407 scopus 로고    scopus 로고
    • A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP - >YFP fluorescence resonance energy transfer (FRET)
    • He L, Olson DP, Wu X, Karpova TS, McNally JG, et al. (2003) A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP - >YFP fluorescence resonance energy transfer (FRET). Cytometry A 55: 71-85.
    • (2003) Cytometry A , vol.55 , pp. 71-85
    • He, L.1    Olson, D.P.2    Wu, X.3    Karpova, T.S.4    McNally, J.G.5
  • 11
    • 11244334124 scopus 로고    scopus 로고
    • TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation
    • He L, Grammer AC, Wu X, Lipsky PE (2004) TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation. J Biol Chem 279: 55855-55865.
    • (2004) J Biol Chem , vol.279 , pp. 55855-55865
    • He, L.1    Grammer, A.C.2    Wu, X.3    Lipsky, P.E.4
  • 14
    • 0034720711 scopus 로고    scopus 로고
    • Measurement of molecular interactions in living cells by fluorescence resonance energy transfer between variants of the green fluorescent protein
    • Siegel RM, Chan FK, Zacharias DA, Swofford R, Holmes KL, et al. (2000) Measurement of molecular interactions in living cells by fluorescence resonance energy transfer between variants of the green fluorescent protein. Sci STKE 2000: PL1.
    • (2000) Sci STKE 2000
    • Siegel, R.M.1    Chan, F.K.2    Zacharias, D.A.3    Swofford, R.4    Holmes, K.L.5
  • 15
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins-ensuring viral survival in a hostile environment
    • Malim MH, Emerman M (2008) HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host Microbe 3: 388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 16
    • 0031924395 scopus 로고    scopus 로고
    • Functional analysis of the human immunodeficiency virus type 1 Rev protein oligomerization interface
    • Thomas SL, Oft M, Jaksche H, Casari G, Heger P, et al. (1998) Functional analysis of the human immunodeficiency virus type 1 Rev protein oligomerization interface. J Virol 72: 2935-2944.
    • (1998) J Virol , vol.72 , pp. 2935-2944
    • Thomas, S.L.1    Oft, M.2    Jaksche, H.3    Casari, G.4    Heger, P.5
  • 17
    • 38549095979 scopus 로고    scopus 로고
    • Neil SJ, Zang T, Bieniasz PD (2008) Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451: 425-430.
    • Neil SJ, Zang T, Bieniasz PD (2008) Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451: 425-430.
  • 18
    • 0141521574 scopus 로고    scopus 로고
    • Down-modulation of mature major histocompatibility complex class II and upregulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles
    • Schindler M, Wurfl S, Benaroch P, Greenough TC, Daniels R, et al. (2003) Down-modulation of mature major histocompatibility complex class II and upregulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles. J Virol 77: 10548-10556.
    • (2003) J Virol , vol.77 , pp. 10548-10556
    • Schindler, M.1    Wurfl, S.2    Benaroch, P.3    Greenough, T.C.4    Daniels, R.5
  • 19
    • 3342929537 scopus 로고    scopus 로고
    • Retroviral mRNA nuclear export elements regulate protein function and virion assembly
    • Swanson CM, Puffer BA, Ahmad KM, Doms RW, Malim MH (2004) Retroviral mRNA nuclear export elements regulate protein function and virion assembly. EMBO J 23: 2632-2640.
    • (2004) EMBO J , vol.23 , pp. 2632-2640
    • Swanson, C.M.1    Puffer, B.A.2    Ahmad, K.M.3    Doms, R.W.4    Malim, M.H.5
  • 20
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • Schubert U, Anton LC, Bacik I, Cox JH, Bour S, et al. (1998) CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J Virol 72: 2280-2288.
    • (1998) J Virol , vol.72 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5
  • 23
    • 53449083627 scopus 로고    scopus 로고
    • Role of HIV-1 Vpu protein for virus spread and pathogenesis
    • Nomaguchi M, Fujita M, Adachi A (2008) Role of HIV-1 Vpu protein for virus spread and pathogenesis. Microbes Infect 10: 960-967.
    • (2008) Microbes Infect , vol.10 , pp. 960-967
    • Nomaguchi, M.1    Fujita, M.2    Adachi, A.3
  • 24
    • 33745122662 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef: Adapting to intracellular trafficking pathways
    • Roeth JF, Collins KL (2006) Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways. Microbiol Mol Biol Rev 70: 548-563.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 548-563
    • Roeth, J.F.1    Collins, K.L.2
  • 25
    • 0036187980 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis
    • Greenway AL, McPhee DA, Allen K, Johnstone R, Holloway G, et al. (2002) Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis. J Virol 76: 2692-2702.
    • (2002) J Virol , vol.76 , pp. 2692-2702
    • Greenway, A.L.1    McPhee, D.A.2    Allen, K.3    Johnstone, R.4    Holloway, G.5
  • 26
    • 33745070227 scopus 로고    scopus 로고
    • Nefmediated suppression of T cell activation was lost in a lentiviral lineage that gave rise to HIV-1
    • Schindler M, Munch J, Kutsch O, Li H, Santiago ML, et al. (2006) Nefmediated suppression of T cell activation was lost in a lentiviral lineage that gave rise to HIV-1. Cell 125: 1055-1067.
    • (2006) Cell , vol.125 , pp. 1055-1067
    • Schindler, M.1    Munch, J.2    Kutsch, O.3    Li, H.4    Santiago, M.L.5
  • 27
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains
    • Schubert U, Bour S, Ferrer-Montiel AV, Montal M, Maldarell F, et al. (1996) The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J Virol 70: 809-819.
    • (1996) J Virol , vol.70 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3    Montal, M.4    Maldarell, F.5
  • 28
    • 0030048198 scopus 로고    scopus 로고
    • Labeling neural cells using adenoviral gene transfer of membrane-targeted GFP
    • Moriyoshi K, Richards LJ, Akazawa C, O'Leary DD, Nakanishi S (1996) Labeling neural cells using adenoviral gene transfer of membrane-targeted GFP. Neuron 16: 255-260.
    • (1996) Neuron , vol.16 , pp. 255-260
    • Moriyoshi, K.1    Richards, L.J.2    Akazawa, C.3    O'Leary, D.D.4    Nakanishi, S.5
  • 29
    • 0346340064 scopus 로고    scopus 로고
    • The gene product Murr1 restricts HIV-1 replication in resting CD4+ lymphocytes
    • Ganesh L, Burstein E, Guha-Niyogi A, Louder MK, Mascola JR, et al. (2003) The gene product Murr1 restricts HIV-1 replication in resting CD4+ lymphocytes. Nature 426: 853-857.
    • (2003) Nature , vol.426 , pp. 853-857
    • Ganesh, L.1    Burstein, E.2    Guha-Niyogi, A.3    Louder, M.K.4    Mascola, J.R.5
  • 30
    • 0033519235 scopus 로고    scopus 로고
    • Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain
    • Xu XN, Laffert B, Screaton GR, Kraft M, Wolf D, et al. (1999) Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain. J Exp Med 189: 1489-1496.
    • (1999) J Exp Med , vol.189 , pp. 1489-1496
    • Xu, X.N.1    Laffert, B.2    Screaton, G.R.3    Kraft, M.4    Wolf, D.5
  • 31
    • 0036435652 scopus 로고    scopus 로고
    • The conserved process of TCR/CD3 complex down-modulation by SIV Nef is mediated by the central core, not endocytic motifs
    • Schaefer TM, Bell I, Pfeifer ME, Ghosh M, Trible RP, et al. (2002) The conserved process of TCR/CD3 complex down-modulation by SIV Nef is mediated by the central core, not endocytic motifs. Virology 302: 106-122.
    • (2002) Virology , vol.302 , pp. 106-122
    • Schaefer, T.M.1    Bell, I.2    Pfeifer, M.E.3    Ghosh, M.4    Trible, R.P.5
  • 32
    • 0028816432 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: Implications for the mechanism of degradation
    • Bour S, Schubert U, Strebel K (1995) The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation. J Virol 69: 1510-1520.
    • (1995) J Virol , vol.69 , pp. 1510-1520
    • Bour, S.1    Schubert, U.2    Strebel, K.3
  • 33
    • 67249157032 scopus 로고    scopus 로고
    • Mitchell RS, Katsura C, Skasko MA, Fitzpatrick K, Lau D, et al. (2009) Vpu antagonizes BST-2-mediated restriction of HIV-1 release via beta-TrCP and endo-lysosomal trafficking. PLoS Pathog 5: e1000450.
    • Mitchell RS, Katsura C, Skasko MA, Fitzpatrick K, Lau D, et al. (2009) Vpu antagonizes BST-2-mediated restriction of HIV-1 release via beta-TrCP and endo-lysosomal trafficking. PLoS Pathog 5: e1000450.
  • 35
    • 0028348370 scopus 로고
    • The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alphahelix-turn-alpha-helix-motif
    • Schubert U, Henklein P, Boldyreff B, Wingender E, Strebel K, et al. (1994) The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alphahelix-turn-alpha-helix-motif. J Mol Biol 236: 16-25.
    • (1994) J Mol Biol , vol.236 , pp. 16-25
    • Schubert, U.1    Henklein, P.2    Boldyreff, B.3    Wingender, E.4    Strebel, K.5
  • 37
    • 7444258608 scopus 로고    scopus 로고
    • Recent advances in the understanding of HIV-1 Vpu accessory protein functions
    • Binette J, Cohen EA (2004) Recent advances in the understanding of HIV-1 Vpu accessory protein functions. Curr Drug Targets Immune Endocr Metabol Disord 4: 297-307.
    • (2004) Curr Drug Targets Immune Endocr Metabol Disord , vol.4 , pp. 297-307
    • Binette, J.1    Cohen, E.A.2
  • 38
    • 0036580169 scopus 로고    scopus 로고
    • Protein interactions: Two methods for assessment of the reliability of high throughput observations
    • Deane CM, Salwinski L, Xenarios I, Eisenberg D (2002) Protein interactions: two methods for assessment of the reliability of high throughput observations. Mol Cell Proteomics 1: 349-356.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 349-356
    • Deane, C.M.1    Salwinski, L.2    Xenarios, I.3    Eisenberg, D.4
  • 40
    • 36949000237 scopus 로고    scopus 로고
    • Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps
    • Huang H, Jedynak BM, Bader JS (2007) Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps. PLoS Comput Biol 3: e214.
    • (2007) PLoS Comput Biol , vol.3
    • Huang, H.1    Jedynak, B.M.2    Bader, J.S.3


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