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Volumn 127, Issue 8, 2014, Pages 1621-1629

Chromophore-assisted laser inactivation - towards a spatiotemporal-functional analysis of proteins, and the ablation of chromatin, organelle and cell function

Author keywords

Chromophore; Imaging; Photosensitizer; Reactive oxygen species; Spatiotemporal inactivation

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; KILLERRED PROTEIN; MINISOG PROTEIN; PROTEIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; CHROMATIN; CYTOSKELETON PROTEIN; GREEN FLUORESCENT PROTEIN; KILLER RED PROTEIN, ANTHOMEDUSAE; MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 84898866185     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.144527     Document Type: Article
Times cited : (39)

References (106)
  • 2
    • 84891722219 scopus 로고    scopus 로고
    • Highly efficient CRISPR/Cas9-mediated knock-in in zebrafish by homologyindependent DNA repair
    • Auer, T. O., Duroure, K., De Cian, A., Concordet, J. P. and Del Bene, F. (2014). Highly efficient CRISPR/Cas9-mediated knock-in in zebrafish by homologyindependent DNA repair. Genome Res. 24, 142-153.
    • (2014) Genome Res. , vol.24 , pp. 142-153
    • Auer, T.O.1    Duroure, K.2    De Cian, A.3    Concordet, J.P.4    Del Bene, F.5
  • 3
    • 33746860809 scopus 로고    scopus 로고
    • Singlet oxygen generation by UVA light exposure of endogenous photosensitizers
    • Baier, J., Maisch, T., Maier, M., Engel, E., Landthaler, M. and Bäumler, W. (2006). Singlet oxygen generation by UVA light exposure of endogenous photosensitizers. Biophys. J. 91, 1452-1459.
    • (2006) Biophys. J. , vol.91 , pp. 1452-1459
    • Baier, J.1    Maisch, T.2    Maier, M.3    Engel, E.4    Landthaler, M.5    Bäumler, W.6
  • 4
    • 84855495293 scopus 로고    scopus 로고
    • Light inactivation of water transport and protein-protein interactions of aquaporin-Killer Red chimeras
    • Baumgart, F., Rossi, A. and Verkman, A. S. (2012). Light inactivation of water transport and protein-protein interactions of aquaporin-Killer Red chimeras. J. Gen. Physiol. 139, 83-91.
    • (2012) J. Gen. Physiol. , vol.139 , pp. 83-91
    • Baumgart, F.1    Rossi, A.2    Verkman, A.S.3
  • 5
    • 0036203661 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation: a high-throughput tool for direct target validation of proteins
    • Beck, S., Sakurai, T., Eustace, B. K., Beste, G., Schier, R., Rudert, F. and Jay, D. G. (2002). Fluorophore-assisted light inactivation: a high-throughput tool for direct target validation of proteins. Proteomics 2, 247-255.
    • (2002) Proteomics , vol.2 , pp. 247-255
    • Beck, S.1    Sakurai, T.2    Eustace, B.K.3    Beste, G.4    Schier, R.5    Rudert, F.6    Jay, D.G.7
  • 7
    • 84873311048 scopus 로고    scopus 로고
    • Mapping the subcellular distribution of α-synuclein in neurons using genetically encoded probes for correlated light and electron microscopy: implications for Parkinson's disease pathogenesis
    • Boassa, D., Berlanga, M. L., Yang, M. A., Terada, M., Hu, J., Bushong, E. A., Hwang, M., Masliah, E., George, J. M. and Ellisman, M. H. (2013). Mapping the subcellular distribution of α-synuclein in neurons using genetically encoded probes for correlated light and electron microscopy: implications for Parkinson's disease pathogenesis. J. Neurosci. 33, 2605-2615.
    • (2013) J. Neurosci. , vol.33 , pp. 2605-2615
    • Boassa, D.1    Berlanga, M.L.2    Yang, M.A.3    Terada, M.4    Hu, J.5    Bushong, E.A.6    Hwang, M.7    Masliah, E.8    George, J.M.9    Ellisman, M.H.10
  • 8
    • 2642557066 scopus 로고    scopus 로고
    • Progress towards understanding the nature of chromatid breakage
    • Bryant, P. E., Gray, L. J. and Peresse, N. (2004). Progress towards understanding the nature of chromatid breakage. Cytogenet. Genome Res. 104, 65-71.
    • (2004) Cytogenet. Genome Res. , vol.104 , pp. 65-71
    • Bryant, P.E.1    Gray, L.J.2    Peresse, N.3
  • 9
    • 0034650664 scopus 로고    scopus 로고
    • Micro-scale chromophore-assisted laser inactivation of nerve growth cone proteins
    • Buchstaller, A. and Jay, D. G. (2000). Micro-scale chromophore-assisted laser inactivation of nerve growth cone proteins. Microsc. Res. Tech. 48, 97-106.
    • (2000) Microsc. Res. Tech. , vol.48 , pp. 97-106
    • Buchstaller, A.1    Jay, D.G.2
  • 11
    • 34548788526 scopus 로고    scopus 로고
    • Chromophore-assisted light inactivation (CALI) using the phototoxic fluorescent protein KillerRed
    • Bulina, M. E., Lukyanov, K. A., Britanova, O. V., Onichtchouk, D., Lukyanov, S. and Chudakov, D. M. (2006b). Chromophore-assisted light inactivation (CALI) using the phototoxic fluorescent protein KillerRed. Nat. Protoc. 1, 947-953.
    • (2006) Nat. Protoc. , vol.1 , pp. 947-953
    • Bulina, M.E.1    Lukyanov, K.A.2    Britanova, O.V.3    Onichtchouk, D.4    Lukyanov, S.5    Chudakov, D.M.6
  • 12
    • 84871591497 scopus 로고    scopus 로고
    • A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase Aregulatory subunit I (PKA-RI) to the plasma membrane
    • Burgers, P. P., Ma, Y., Margarucci, L., Mackey, M., van der Heyden, M. A., Ellisman, M., Scholten, A., Taylor, S. S. and Heck, A. J. (2012). A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase Aregulatory subunit I (PKA-RI) to the plasma membrane. J. Biol. Chem. 287, 43789-43797.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43789-43797
    • Burgers, P.P.1    Ma, Y.2    Margarucci, L.3    Mackey, M.4    van der Heyden, M.A.5    Ellisman, M.6    Scholten, A.7    Taylor, S.S.8    Heck, A.J.9
  • 13
    • 84884692956 scopus 로고    scopus 로고
    • AAV-mediated, optogenetic ablation of Müller Glia leads to structural and functional changes in the mouse retina
    • Byrne, L. C., Khalid, F., Lee, T., Zin, E. A., Greenberg, K. P., Visel, M., Schaffer, D. V. and Flannery, J. G. (2013). AAV-mediated, optogenetic ablation of Müller Glia leads to structural and functional changes in the mouse retina. PLoS ONE 8, e76075.
    • (2013) PLoS ONE , vol.8
    • Byrne, L.C.1    Khalid, F.2    Lee, T.3    Zin, E.A.4    Greenberg, K.P.5    Visel, M.6    Schaffer, D.V.7    Flannery, J.G.8
  • 14
    • 69349092404 scopus 로고    scopus 로고
    • Structural basis for the phototoxicity of the fluorescent protein KillerRed
    • Carpentier, P., Violot, S., Blanchoin, L. and Bourgeois, D. (2009). Structural basis for the phototoxicity of the fluorescent protein KillerRed. FEBS Lett. 583, 2839-2842.
    • (2009) FEBS Lett. , vol.583 , pp. 2839-2842
    • Carpentier, P.1    Violot, S.2    Blanchoin, L.3    Bourgeois, D.4
  • 16
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody, C. W., Prasher, D. C., Westler, W. M., Prendergast, F. G. and Ward, W. W. (1993). Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 32, 1212-1218.
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 17
    • 84868133042 scopus 로고    scopus 로고
    • GFP-like phototransformation mechanisms in the cytotoxic fluorescent protein KillerRed unraveled by structural and spectroscopic investigations
    • de Rosny, E. and Carpentier, P. (2012). GFP-like phototransformation mechanisms in the cytotoxic fluorescent protein KillerRed unraveled by structural and spectroscopic investigations. J. Am. Chem. Soc. 134, 18015-18021.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18015-18021
    • de Rosny, E.1    Carpentier, P.2
  • 18
    • 78650902662 scopus 로고    scopus 로고
    • Optogenetics
    • Deisseroth, K. (2011). Optogenetics. Nat. Methods 8, 26-29.
    • (2011) Nat. Methods , vol.8 , pp. 26-29
    • Deisseroth, K.1
  • 21
    • 84892574066 scopus 로고    scopus 로고
    • Essential function of dynamin in the invasive properties and actin architecture of v-Src induced podosomes/invadosomes
    • Destaing, O., Ferguson, S. M., Grichine, A., Oddou, C., De Camilli, P., Albiges-Rizo, C. and Baron, R. (2013). Essential function of dynamin in the invasive properties and actin architecture of v-Src induced podosomes/invadosomes. PLoS ONE 8, e77956.
    • (2013) PLoS ONE , vol.8
    • Destaing, O.1    Ferguson, S.M.2    Grichine, A.3    Oddou, C.4    De Camilli, P.5    Albiges-Rizo, C.6    Baron, R.7
  • 22
    • 0027379381 scopus 로고
    • Fasciclin I and II have distinct roles in the development of grasshopper pioneer neurons
    • Diamond, P., Mallavarapu, A., Schnipper, J., Booth, J., Park, L., O'Connor, T. P. and Jay, D. G. (1993). Fasciclin I and II have distinct roles in the development of grasshopper pioneer neurons. Neuron 11, 409-421.
    • (1993) Neuron , vol.11 , pp. 409-421
    • Diamond, P.1    Mallavarapu, A.2    Schnipper, J.3    Booth, J.4    Park, L.5    O'Connor, T.P.6    Jay, D.G.7
  • 23
    • 84879264708 scopus 로고    scopus 로고
    • ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering
    • Gaj, T., Gersbach, C. A. and Barbas, C. F., III (2013). ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering. Trends Biotechnol. 31, 397-405.
    • (2013) Trends Biotechnol. , vol.31 , pp. 397-405
    • Gaj, T.1    Gersbach, C.A.2    Barbas, C.F.3
  • 24
    • 0035933577 scopus 로고    scopus 로고
    • Green fluorescent protein-based halide indicators with improved chloride and iodide affinities
    • Galietta, L. J., Haggie, P. M. and Verkman, A. S. (2001). Green fluorescent protein-based halide indicators with improved chloride and iodide affinities. FEBS Lett. 499, 220-224.
    • (2001) FEBS Lett. , vol.499 , pp. 220-224
    • Galietta, L.J.1    Haggie, P.M.2    Verkman, A.S.3
  • 25
    • 34247546735 scopus 로고    scopus 로고
    • Development of a multistage classifier for a monitoring system of cell activity based on imaging of chromosomal dynamics
    • Gambe, A. E., Ono, R. M., Matsunaga, S., Kutsuna, N., Higaki, T., Higashi, T., Hasezawa, S., Uchiyama, S. and Fukui, K. (2007). Development of a multistage classifier for a monitoring system of cell activity based on imaging of chromosomal dynamics. Cytometry 71A, 286-296.
    • (2007) Cytometry , vol.71 A , pp. 286-296
    • Gambe, A.E.1    Ono, R.M.2    Matsunaga, S.3    Kutsuna, N.4    Higaki, T.5    Higashi, T.6    Hasezawa, S.7    Uchiyama, S.8    Fukui, K.9
  • 26
    • 84876838711 scopus 로고    scopus 로고
    • The hierarchy of the 3D genome
    • Gibcus, J. H. and Dekker, J. (2013). The hierarchy of the 3D genome. Mol. Cell 49, 773-782.
    • (2013) Mol. Cell , vol.49 , pp. 773-782
    • Gibcus, J.H.1    Dekker, J.2
  • 27
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R. and Tsien, R. Y. (1998). Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 28
    • 35948932520 scopus 로고    scopus 로고
    • The biarsenical dye Lumio exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells
    • Hearps, A. C., Pryor, M. J., Kuusisto, H. V., Rawlinson, S. M., Piller, S. C. and Jans, D. A. (2007). The biarsenical dye Lumio exhibits a reduced ability to specifically detect tetracysteine-containing proteins within live cells. J. Fluoresc. 17, 593-597.
    • (2007) J. Fluoresc. , vol.17 , pp. 593-597
    • Hearps, A.C.1    Pryor, M.J.2    Kuusisto, H.V.3    Rawlinson, S.M.4    Piller, S.C.5    Jans, D.A.6
  • 29
    • 84871932211 scopus 로고    scopus 로고
    • Application of visualization techniques for cell and tissue engineering
    • Higashi, T., Watanabe, W. and Matsunaga, S. (2013). Application of visualization techniques for cell and tissue engineering. J. Biosci. Bioeng. 115, 122-126.
    • (2013) J. Biosci. Bioeng. , vol.115 , pp. 122-126
    • Higashi, T.1    Watanabe, W.2    Matsunaga, S.3
  • 32
    • 17444404900 scopus 로고    scopus 로고
    • Toward understanding the mechanism of chromophore-assisted laser inactivation--evidence for the primary photochemical steps
    • Horstkotte, E., Schröder, T., Niewöhner, J., Thiel, E. and Henning, S. W. (2005). Toward understanding the mechanism of chromophore-assisted laser inactivation--evidence for the primary photochemical steps. Photochem Photobiol 81, 358-366.
    • (2005) Photochem Photobiol , vol.81 , pp. 358-366
    • Horstkotte, E.1    Schröder, T.2    Niewöhner, J.3    Thiel, E.4    Henning, S.W.5
  • 33
    • 67349152310 scopus 로고    scopus 로고
    • Regulation of neurite outgrowth mediated by neuronal calcium sensor-1 and inositol 1,4,5-trisphosphate receptor in nerve growth cones
    • Iketani, M., Imaizumi, C., Nakamura, F., Jeromin, A., Mikoshiba, K., Goshima, Y. and Takei, K. (2009). Regulation of neurite outgrowth mediated by neuronal calcium sensor-1 and inositol 1,4,5-trisphosphate receptor in nerve growth cones. Neuroscience 161, 743-752.
    • (2009) Neuroscience , vol.161 , pp. 743-752
    • Iketani, M.1    Imaizumi, C.2    Nakamura, F.3    Jeromin, A.4    Mikoshiba, K.5    Goshima, Y.6    Takei, K.7
  • 35
    • 79955506970 scopus 로고    scopus 로고
    • Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk
    • Ivashchenko, O., Van Veldhoven, P. P., Brees, C., Ho, Y. S., Terlecky, S. R. and Fransen, M. (2011). Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk. Mol. Biol. Cell 22, 1440-1451.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1440-1451
    • Ivashchenko, O.1    Van Veldhoven, P.P.2    Brees, C.3    Ho, Y.S.4    Terlecky, S.R.5    Fransen, M.6
  • 36
    • 49849101836 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation in cell biology
    • Jacobson, K., Rajfur, Z., Vitriol, E. and Hahn, K. (2008). Chromophore-assisted laser inactivation in cell biology. Trends Cell Biol. 18, 443-450.
    • (2008) Trends Cell Biol. , vol.18 , pp. 443-450
    • Jacobson, K.1    Rajfur, Z.2    Vitriol, E.3    Hahn, K.4
  • 37
    • 84861213214 scopus 로고    scopus 로고
    • Irradiation-induced protein inactivation reveals Golgi enzyme cycling to cell periphery
    • Jarvela, T. and Linstedt, A. D. (2012). Irradiation-induced protein inactivation reveals Golgi enzyme cycling to cell periphery. J. Cell Sci. 125, 973-980.
    • (2012) J. Cell Sci. , vol.125 , pp. 973-980
    • Jarvela, T.1    Linstedt, A.D.2
  • 38
    • 84891812680 scopus 로고    scopus 로고
    • Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization
    • Jarvela, T. and Linstedt, A. D. (2014). Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization. Mol. Biol. Cell 25, 133-144.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 133-144
    • Jarvela, T.1    Linstedt, A.D.2
  • 39
    • 0000601644 scopus 로고
    • Selective destruction of protein function by chromophoreassisted laser inactivation
    • Jay, D. G. (1988). Selective destruction of protein function by chromophoreassisted laser inactivation. Proc. Natl. Acad. Sci. USA 85, 5454-5458.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5454-5458
    • Jay, D.G.1
  • 40
    • 0025244280 scopus 로고
    • Laser inactivation of fasciclin I disrupts axon adhesion of grasshopper pioneer neurons
    • Jay, D. G. and Keshishian, H. (1990). Laser inactivation of fasciclin I disrupts axon adhesion of grasshopper pioneer neurons. Nature 348, 548-550.
    • (1990) Nature , vol.348 , pp. 548-550
    • Jay, D.G.1    Keshishian, H.2
  • 41
    • 80053013758 scopus 로고    scopus 로고
    • Chemical tags for labeling proteins inside living cells
    • Jing, C. and Cornish, V. W. (2011). Chemical tags for labeling proteins inside living cells. Acc. Chem. Res. 44, 784-792.
    • (2011) Acc. Chem. Res. , vol.44 , pp. 784-792
    • Jing, C.1    Cornish, V.W.2
  • 42
    • 65349089375 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation of alpha- and gamma-tubulin SNAP-tag fusion proteins inside living cells
    • Keppler, A. and Ellenberg, J. (2009). Chromophore-assisted laser inactivation of alpha- and gamma-tubulin SNAP-tag fusion proteins inside living cells. ACS Chem. Biol. 4, 127-138.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 127-138
    • Keppler, A.1    Ellenberg, J.2
  • 43
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H., Vogel, H. and Johnsson, K. (2002). A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21, 86-89.
    • (2002) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 44
    • 84880135868 scopus 로고    scopus 로고
    • A method for selective ablation of neurons in C. elegans using the phototoxic fluorescent protein, KillerRed
    • Kobayashi, J., Shidara, H., Morisawa, Y., Kawakami, M., Tanahashi, Y., Hotta, K. and Oka, K. (2013). A method for selective ablation of neurons in C. elegans using the phototoxic fluorescent protein, KillerRed. Neurosci. Lett. 548, 261-264.
    • (2013) Neurosci. Lett. , vol.548 , pp. 261-264
    • Kobayashi, J.1    Shidara, H.2    Morisawa, Y.3    Kawakami, M.4    Tanahashi, Y.5    Hotta, K.6    Oka, K.7
  • 46
    • 84895811308 scopus 로고    scopus 로고
    • Novel method for sitespecific induction of oxidative DNA damage reveals differences in recruitment of repair proteins to heterochromatin and euchromatin
    • [Epub ahead of print] doi:10.1093/nar/gkt1233
    • Lan, L., Nakajima, S., Wei, L., Sun, L., Hsieh, C. L., Sobol, R. W., Bruchez, M., Van Houten, B., Yasui, A. and Levine, A. S. (2013). Novel method for sitespecific induction of oxidative DNA damage reveals differences in recruitment of repair proteins to heterochromatin and euchromatin. Nucl. Acids Res. [Epub ahead of print] doi:10.1093/nar/gkt1233.
    • (2013) Nucl. Acids Res
    • Lan, L.1    Nakajima, S.2    Wei, L.3    Sun, L.4    Hsieh, C.L.5    Sobol, R.W.6    Bruchez, M.7    Van Houten, B.8    Yasui, A.9    Levine, A.S.10
  • 48
    • 0028333737 scopus 로고
    • Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals
    • Liao, J. C., Roider, J. and Jay, D. G. (1994). Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals. Proc. Natl. Acad. Sci. USA. 91, 2659-2663.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 2659-2663
    • Liao, J.C.1    Roider, J.2    Jay, D.G.3
  • 49
    • 84887016390 scopus 로고    scopus 로고
    • A genetically-encoded KillerRed protein as an intrinsically generated photosensitizer for photodynamic therapy
    • Liao, Z. X., Li, Y. C., Lu, H. M. and Sung, H. W. (2014). A genetically-encoded KillerRed protein as an intrinsically generated photosensitizer for photodynamic therapy. Biomaterials 35, 500-508.
    • (2014) Biomaterials , vol.35 , pp. 500-508
    • Liao, Z.X.1    Li, Y.C.2    Lu, H.M.3    Sung, H.W.4
  • 50
    • 84864982866 scopus 로고    scopus 로고
    • Advances in high-resolution imaging - techniques for three-dimensional imaging of cellular structures
    • Lidke, D. S. and Lidke, K. A. (2012). Advances in high-resolution imaging - techniques for three-dimensional imaging of cellular structures. J. Cell Sci. 125, 2571-2580.
    • (2012) J. Cell Sci. , vol.125 , pp. 2571-2580
    • Lidke, D.S.1    Lidke, K.A.2
  • 51
    • 84880688619 scopus 로고    scopus 로고
    • Optogenetic inhibition of synaptic release with chromophore-assisted light inactivation (CALI)
    • Lin, J. Y., Sann, S. B., Zhou, K., Nabavi, S., Proulx, C. D., Malinow, R., Jin, Y. and Tsien, R. Y. (2013). Optogenetic inhibition of synaptic release with chromophore-assisted light inactivation (CALI). Neuron 79, 241-253.
    • (2013) Neuron , vol.79 , pp. 241-253
    • Lin, J.Y.1    Sann, S.B.2    Zhou, K.3    Nabavi, S.4    Proulx, C.D.5    Malinow, R.6    Jin, Y.7    Tsien, R.Y.8
  • 52
    • 77955574421 scopus 로고    scopus 로고
    • T vector bearing KillerRed protein marker for red/white cloning screening
    • Liu, X., Liu, X., Zhou, Y., Zou, D., Shi, R., Li, Z. and Zheng, D. (2010). T vector bearing KillerRed protein marker for red/white cloning screening. Anal. Biochem. 405, 272-274.
    • (2010) Anal. Biochem. , vol.405 , pp. 272-274
    • Liu, X.1    Liu, X.2    Zhou, Y.3    Zou, D.4    Shi, R.5    Li, Z.6    Zheng, D.7
  • 55
    • 0037028010 scopus 로고    scopus 로고
    • Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I
    • Marek, K. W. and Davis, G. W. (2002). Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I. Neuron 36, 805-813.
    • (2002) Neuron , vol.36 , pp. 805-813
    • Marek, K.W.1    Davis, G.W.2
  • 56
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin, B. R., Giepmans, B. N., Adams, S. R. and Tsien, R. Y. (2005). Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23, 1308-1314.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.2    Adams, S.R.3    Tsien, R.Y.4
  • 57
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey, V. (2000). The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28, 283-296.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 60
    • 64749107238 scopus 로고    scopus 로고
    • Mechanism of chromophore assisted laser inactivation employing fluorescent proteins
    • McLean, M. A., Rajfur, Z., Chen, Z., Humphrey, D., Yang, B., Sligar, S. G. and Jacobson, K. (2009). Mechanism of chromophore assisted laser inactivation employing fluorescent proteins. Anal. Chem. 81, 1755-1761.
    • (2009) Anal. Chem. , vol.81 , pp. 1755-1761
    • McLean, M.A.1    Rajfur, Z.2    Chen, Z.3    Humphrey, D.4    Yang, B.5    Sligar, S.G.6    Jacobson, K.7
  • 61
    • 84888797993 scopus 로고    scopus 로고
    • Genetically encoded immunophotosensitizer 4D5scFv-miniSOG is a highly selective agent for targeted photokilling of tumor cells in vitro
    • Mironova, K. E., Proshkina, G. M., Ryabova, A. V., Stremovskiy, O. A., Lukyanov, S. A., Petrov, R. V. and Deyev, S. M. (2013). Genetically encoded immunophotosensitizer 4D5scFv-miniSOG is a highly selective agent for targeted photokilling of tumor cells in vitro. Theranostics 3, 831-840.
    • (2013) Theranostics , vol.3 , pp. 831-840
    • Mironova, K.E.1    Proshkina, G.M.2    Ryabova, A.V.3    Stremovskiy, O.A.4    Lukyanov, S.A.5    Petrov, R.V.6    Deyev, S.M.7
  • 62
    • 84862990847 scopus 로고    scopus 로고
    • An actomyosin-based barrier inhibits cell mixing at compartmental boundaries in Drosophila embryos
    • 1-9
    • Monier, B., Pélissier-Monier, A., Brand, A. H. and Sanson, B. (2010). An actomyosin-based barrier inhibits cell mixing at compartmental boundaries in Drosophila embryos. Nat. Cell Biol. 12, 60-65, 1-9.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 60-65
    • Monier, B.1    Pélissier-Monier, A.2    Brand, A.H.3    Sanson, B.4
  • 63
    • 0030294867 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation of a repulsive axonal guidance molecule
    • Müller, B. K., Jay, D. G. and Bonhoeffer, F. (1996). Chromophore-assisted laser inactivation of a repulsive axonal guidance molecule. Curr. Biol. 6, 1497-1502.
    • (1996) Curr. Biol. , vol.6 , pp. 1497-1502
    • Müller, B.K.1    Jay, D.G.2    Bonhoeffer, F.3
  • 64
  • 65
    • 68349127373 scopus 로고    scopus 로고
    • HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification
    • Ohana, R. F., Encell, L. P., Zhao, K., Simpson, D., Slater, M. R., Urh, M. and Wood, K. V. (2009). HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification. Protein Expr. Purif. 68, 110-120.
    • (2009) Protein Expr. Purif. , vol.68 , pp. 110-120
    • Ohana, R.F.1    Encell, L.P.2    Zhao, K.3    Simpson, D.4    Slater, M.R.5    Urh, M.6    Wood, K.V.7
  • 66
    • 84884134220 scopus 로고    scopus 로고
    • Oxygen-dependent photochemistry and photophysics of "miniSOG," a protein-encased flavin
    • Pimenta, F. M., Jensen, R. L., Breitenbach, T., Etzerodt, M. and Ogilby, P. R. (2013). Oxygen-dependent photochemistry and photophysics of "miniSOG," a protein-encased flavin. Photochem. Photobiol. 89, 1116-1126.
    • (2013) Photochem. Photobiol. , vol.89 , pp. 1116-1126
    • Pimenta, F.M.1    Jensen, R.L.2    Breitenbach, T.3    Etzerodt, M.4    Ogilby, P.R.5
  • 68
    • 84860812078 scopus 로고    scopus 로고
    • Photo-inducible cell ablation in Caenorhabditis elegans using the genetically encoded singlet oxygen generating protein miniSOG
    • Qi, Y. B., Garren, E. J., Shu, X., Tsien, R. Y. and Jin, Y. (2012). Photo-inducible cell ablation in Caenorhabditis elegans using the genetically encoded singlet oxygen generating protein miniSOG. Proc. Natl. Acad. Sci. USA 109, 7499-7504.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 7499-7504
    • Qi, Y.B.1    Garren, E.J.2    Shu, X.3    Tsien, R.Y.4    Jin, Y.5
  • 69
    • 0036228954 scopus 로고    scopus 로고
    • Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins
    • Rajfur, Z., Roy, P., Otey, C., Romer, L. and Jacobson, K. (2002). Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nat. Cell Biol. 4, 286-293.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 286-293
    • Rajfur, Z.1    Roy, P.2    Otey, C.3    Romer, L.4    Jacobson, K.5
  • 70
    • 65649152639 scopus 로고    scopus 로고
    • Culturing thick brain slices: an interstitial 3D microperfusion system for enhanced viability
    • Rambani, K., Vukasinovic, J., Glezer, A. and Potter, S. M. (2009). Culturing thick brain slices: an interstitial 3D microperfusion system for enhanced viability. J. Neurosci. Methods 180, 243-254.
    • (2009) J. Neurosci. Methods , vol.180 , pp. 243-254
    • Rambani, K.1    Vukasinovic, J.2    Glezer, A.3    Potter, S.M.4
  • 71
    • 78651455171 scopus 로고    scopus 로고
    • Diffusion pathways of oxygen species in the phototoxic fluorescent protein KillerRed
    • Roy, A., Carpentier, P., Bourgeois, D. and Field, M. (2010). Diffusion pathways of oxygen species in the phototoxic fluorescent protein KillerRed. Photochem. Photobiol. Sci. 9, 1342-1350.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1342-1350
    • Roy, A.1    Carpentier, P.2    Bourgeois, D.3    Field, M.4
  • 74
    • 0036679141 scopus 로고    scopus 로고
    • Ephrin-A5 restricts topographically specific arborization in the chick retinotectal projection in vivo
    • Sakurai, T., Wong, E., Drescher, U., Tanaka, H. and Jay, D. G. (2002). Ephrin-A5 restricts topographically specific arborization in the chick retinotectal projection in vivo. Proc. Natl. Acad. Sci. USA 99, 10795-10800.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10795-10800
    • Sakurai, T.1    Wong, E.2    Drescher, U.3    Tanaka, H.4    Jay, D.G.5
  • 75
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J. M., Knieb, E., Lempert, U. and Briggs, W. R. (2000). Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 77
    • 84883442783 scopus 로고    scopus 로고
    • Localization microscopy coming of age: from concepts to biological impact
    • Sauer, M. (2013). Localization microscopy coming of age: from concepts to biological impact. J. Cell Sci. 126, 3505-3513.
    • (2013) J. Cell Sci. , vol.126 , pp. 3505-3513
    • Sauer, M.1
  • 78
    • 33747275824 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation of even skipped in Drosophila precisely phenocopies genetic loss of function
    • Schröder, R., Tautz, D. and Jay, D. G. (1996). Chromophore-assisted laser inactivation of even skipped in Drosophila precisely phenocopies genetic loss of function. Dev. Genes Evol. 206, 86-88.
    • (1996) Dev. Genes Evol. , vol.206 , pp. 86-88
    • Schröder, R.1    Tautz, D.2    Jay, D.G.3
  • 79
    • 0345320436 scopus 로고    scopus 로고
    • Elimination of EVE protein by CALI in the short germ band insect Tribolium suggests a conserved pair-rule function for even skipped
    • Schröder, R., Jay, D. G. and Tautz, D. (1999). Elimination of EVE protein by CALI in the short germ band insect Tribolium suggests a conserved pair-rule function for even skipped. Mech. Dev. 80, 191-195.
    • (1999) Mech. Dev. , vol.80 , pp. 191-195
    • Schröder, R.1    Jay, D.G.2    Tautz, D.3
  • 82
    • 84866479441 scopus 로고    scopus 로고
    • Deleterious effects of mitochondrial ROS generated by KillerRed photodynamic action in human cell lines and C. elegans
    • Shibuya, T. and Tsujimoto, Y. (2012). Deleterious effects of mitochondrial ROS generated by KillerRed photodynamic action in human cell lines and C. elegans. J. Photochem. Photobiol. B 117, 1-12.
    • (2012) J. Photochem. Photobiol. B , vol.117 , pp. 1-12
    • Shibuya, T.1    Tsujimoto, Y.2
  • 83
    • 28044447182 scopus 로고    scopus 로고
    • Intracellular disruption of mitochondria in a living HeLa cell with a 76-MHz femtosecond laser oscillator
    • Shimada, T., Watanabe, W., Matsunaga, S., Higashi, T., Ishii, H., Fukui, K., Isobe, K. and Itoh, K. (2005). Intracellular disruption of mitochondria in a living HeLa cell with a 76-MHz femtosecond laser oscillator. Opt Express 13, 9869-9880.
    • (2005) Opt Express , vol.13 , pp. 9869-9880
    • Shimada, T.1    Watanabe, W.2    Matsunaga, S.3    Higashi, T.4    Ishii, H.5    Fukui, K.6    Isobe, K.7    Itoh, K.8
  • 86
    • 0034802605 scopus 로고    scopus 로고
    • The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also nonspecifically to endogenous cysteine-rich proteins
    • Stroffekova, K., Proenza, C. and Beam, K. G. (2001). The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also nonspecifically to endogenous cysteine-rich proteins. Pflugers Arch. 442, 859-866.
    • (2001) Pflugers Arch. , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 90
    • 23644433309 scopus 로고    scopus 로고
    • Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein
    • Tanabe, T., Oyamada, M., Fujita, K., Dai, P., Tanaka, H. and Takamatsu, T. (2005). Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein. Nat. Methods 2, 503-505.
    • (2005) Nat. Methods , vol.2 , pp. 503-505
    • Tanabe, T.1    Oyamada, M.2    Fujita, K.3    Dai, P.4    Tanaka, H.5    Takamatsu, T.6
  • 91
    • 84896731736 scopus 로고    scopus 로고
    • CRISPR-based technologies: prokaryotic defense weapons repurposed
    • Terns, R. M. and Terns, M. P. (2014). CRISPR-based technologies: prokaryotic defense weapons repurposed. Trends Genet. 30, 111-118.
    • (2014) Trends Genet. , vol.30 , pp. 111-118
    • Terns, R.M.1    Terns, M.P.2
  • 93
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998). The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 94
    • 84894295644 scopus 로고    scopus 로고
    • Peptide tag/probe pairs based on the coordination chemistry for protein labeling
    • Uchinomiya, S., Ojida, A. and Hamachi, I. (2014). Peptide tag/probe pairs based on the coordination chemistry for protein labeling. Inorg. Chem. 53, 1816-1823.
    • (2014) Inorg. Chem. , vol.53 , pp. 1816-1823
    • Uchinomiya, S.1    Ojida, A.2    Hamachi, I.3
  • 96
    • 34249847071 scopus 로고    scopus 로고
    • Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins
    • Vitriol, E. A., Uetrecht, A. C., Shen, F., Jacobson, K. and Bear, J. E. (2007). Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins. Proc. Natl. Acad. Sci. USA 104, 6702-6707.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6702-6707
    • Vitriol, E.A.1    Uetrecht, A.C.2    Shen, F.3    Jacobson, K.4    Bear, J.E.5
  • 97
    • 84880411148 scopus 로고    scopus 로고
    • Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia
    • Vitriol, E. A., Wise, A. L., Berginski, M. E., Bamburg, J. R. and Zheng, J. Q. (2013). Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia. Mol. Biol. Cell 24, 2238-2247.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2238-2247
    • Vitriol, E.A.1    Wise, A.L.2    Berginski, M.E.3    Bamburg, J.R.4    Zheng, J.Q.5
  • 98
    • 79951787815 scopus 로고    scopus 로고
    • Positioning effects of KillerRed inside of cells correlate with DNA strand breaks after activation with visible light
    • Waldeck, W., Mueller, G., Wiessler, M., Tóth, K. and Braun, K. (2011). Positioning effects of KillerRed inside of cells correlate with DNA strand breaks after activation with visible light. Int. J. Med. Sci. 8, 97-105.
    • (2011) Int. J. Med. Sci. , vol.8 , pp. 97-105
    • Waldeck, W.1    Mueller, G.2    Wiessler, M.3    Tóth, K.4    Braun, K.5
  • 99
    • 84867273800 scopus 로고    scopus 로고
    • ROSinduced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy
    • Wang, Y., Nartiss, Y., Steipe, B., McQuibban, G. A. and Kim, P. K. (2012). ROSinduced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy. Autophagy 8, 1462-1476.
    • (2012) Autophagy , vol.8 , pp. 1462-1476
    • Wang, Y.1    Nartiss, Y.2    Steipe, B.3    McQuibban, G.A.4    Kim, P.K.5
  • 103
    • 51649086103 scopus 로고    scopus 로고
    • In vivo manipulation of fluorescently labeled organelles in living cells by multiphoton excitation
    • Watanabe, W., Matsunaga, S., Higashi, T., Fukui, K. and Itoh, K. (2008). In vivo manipulation of fluorescently labeled organelles in living cells by multiphoton excitation. J. Biomed. Opt. 13, 031213.
    • (2008) J. Biomed. Opt. , vol.13 , pp. 031213
    • Watanabe, W.1    Matsunaga, S.2    Higashi, T.3    Fukui, K.4    Itoh, K.5
  • 104
    • 84887016927 scopus 로고    scopus 로고
    • Rapid and permanent neuronal inactivation in vivo via subcellular generation of reactive oxygen with the use of KillerRed
    • Williams, D. C., Bejjani, R. E., Ramirez, P. M., Coakley, S., Kim, S. A., Lee, H., Wen, Q., Samuel, A., Lu, H., Hilliard, M. A. et al. (2013). Rapid and permanent neuronal inactivation in vivo via subcellular generation of reactive oxygen with the use of KillerRed. Cell Rep. 5, 553-563.
    • (2013) Cell Rep. , vol.5 , pp. 553-563
    • Williams, D.C.1    Bejjani, R.E.2    Ramirez, P.M.3    Coakley, S.4    Kim, S.A.5    Lee, H.6    Wen, Q.7    Samuel, A.8    Lu, H.9    Hilliard, M.A.10
  • 105
    • 80053430054 scopus 로고    scopus 로고
    • Spatiotemporally controlled initiation of Parkinmediated mitophagy within single cells
    • Yang, J. Y. and Yang, W. Y. (2011). Spatiotemporally controlled initiation of Parkinmediated mitophagy within single cells. Autophagy 7, 1230-1238.
    • (2011) Autophagy , vol.7 , pp. 1230-1238
    • Yang, J.Y.1    Yang, W.Y.2
  • 106
    • 84887700488 scopus 로고    scopus 로고
    • Position of UNC-13 in the active zone regulates synaptic vesicle release probability and release kinetics
    • Zhou, K., Stawicki, T. M., Goncharov, A. and Jin, Y. (2013). Position of UNC-13 in the active zone regulates synaptic vesicle release probability and release kinetics. eLife. 2, e01180.
    • (2013) eLife , vol.2
    • Zhou, K.1    Stawicki, T.M.2    Goncharov, A.3    Jin, Y.4


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