메뉴 건너뛰기




Volumn 18, Issue 9, 2008, Pages 443-450

Chromophore-assisted laser inactivation in cell biology

Author keywords

[No Author keywords available]

Indexed keywords

DYE; REACTIVE OXYGEN METABOLITE;

EID: 49849101836     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2008.07.001     Document Type: Review
Times cited : (113)

References (44)
  • 1
    • 0000601644 scopus 로고
    • Selective destruction of protein function by chromophore-assisted laser inactivation
    • Jay D.G. Selective destruction of protein function by chromophore-assisted laser inactivation. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 5454-5458
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5454-5458
    • Jay, D.G.1
  • 2
    • 0030297176 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation (CALI): probing protein function in situ with a high degree of spatial and temporal resolution
    • Wang F.S., and Jay D.G. Chromophore-assisted laser inactivation (CALI): probing protein function in situ with a high degree of spatial and temporal resolution. Trends Cell Biol. 6 (1996) 442-445
    • (1996) Trends Cell Biol. , vol.6 , pp. 442-445
    • Wang, F.S.1    Jay, D.G.2
  • 3
    • 0026589934 scopus 로고
    • Spatial specificity of chromophore assisted laser inactivation of protein function
    • Linden K.G., et al. Spatial specificity of chromophore assisted laser inactivation of protein function. Biophys. J. 61 (1992) 956-962
    • (1992) Biophys. J. , vol.61 , pp. 956-962
    • Linden, K.G.1
  • 4
    • 0028333737 scopus 로고
    • Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals
    • Liao J.C., et al. Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 2659-2663
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 2659-2663
    • Liao, J.C.1
  • 5
    • 0018098182 scopus 로고
    • Photoradiation therapy for the treatment of malignant tumors
    • Dougherty T.J., et al. Photoradiation therapy for the treatment of malignant tumors. Cancer Res. 38 (1978) 2628-2635
    • (1978) Cancer Res. , vol.38 , pp. 2628-2635
    • Dougherty, T.J.1
  • 6
    • 0016157921 scopus 로고
    • Light and electron microscopy of laser microirradiated chromosomes
    • Rattner J.B., and Berns M.W. Light and electron microscopy of laser microirradiated chromosomes. J. Cell Biol. 62 (1974) 526-533
    • (1974) J. Cell Biol. , vol.62 , pp. 526-533
    • Rattner, J.B.1    Berns, M.W.2
  • 7
    • 0019409694 scopus 로고
    • Fluorescence photobleaching recovery in solutions of labeled actin
    • Lanni F., et al. Fluorescence photobleaching recovery in solutions of labeled actin. Biophys. J. 35 (1981) 351-364
    • (1981) Biophys. J. , vol.35 , pp. 351-364
    • Lanni, F.1
  • 8
    • 0024076815 scopus 로고
    • Fluorescent microtubules break up under illumination
    • Vigers G.P., et al. Fluorescent microtubules break up under illumination. J. Cell Biol. 107 (1988) 1011-1024
    • (1988) J. Cell Biol. , vol.107 , pp. 1011-1024
    • Vigers, G.P.1
  • 9
    • 0036203661 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation: a high-throughput tool for direct target validation of proteins
    • Beck S., et al. Fluorophore-assisted light inactivation: a high-throughput tool for direct target validation of proteins. Proteomics 2 (2002) 247-255
    • (2002) Proteomics , vol.2 , pp. 247-255
    • Beck, S.1
  • 10
    • 34249025106 scopus 로고    scopus 로고
    • Chromophore-assisted light inactivation of pKi-67 leads to inhibition of ribosomal RNA synthesis
    • Rahmanzadeh R., et al. Chromophore-assisted light inactivation of pKi-67 leads to inhibition of ribosomal RNA synthesis. Cell Prolif. 40 (2007) 422-430
    • (2007) Cell Prolif. , vol.40 , pp. 422-430
    • Rahmanzadeh, R.1
  • 11
    • 0347568469 scopus 로고    scopus 로고
    • Genetically targeted chromophore-assisted light inactivation
    • Tour O., et al. Genetically targeted chromophore-assisted light inactivation. Nat. Biotechnol. 21 (2003) 1505-1508
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1505-1508
    • Tour, O.1
  • 12
    • 0037028010 scopus 로고    scopus 로고
    • Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I
    • Marek K.W., and Davis G.W. Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I. Neuron 36 (2002) 805-813
    • (2002) Neuron , vol.36 , pp. 805-813
    • Marek, K.W.1    Davis, G.W.2
  • 13
    • 3042793777 scopus 로고    scopus 로고
    • A general approach for chemical labeling and rapid, spatially controlled protein inactivation
    • Marks K.M., et al. A general approach for chemical labeling and rapid, spatially controlled protein inactivation. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9982-9987
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9982-9987
    • Marks, K.M.1
  • 14
    • 38349193692 scopus 로고    scopus 로고
    • Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer
    • Yogo T., et al. Selective photoinactivation of protein function through environment-sensitive switching of singlet oxygen generation by photosensitizer. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 28-32
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 28-32
    • Yogo, T.1
  • 15
    • 0036228954 scopus 로고    scopus 로고
    • Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins
    • Rajfur Z., et al. Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nat. Cell Biol. 4 (2002) 286-293
    • (2002) Nat. Cell Biol. , vol.4 , pp. 286-293
    • Rajfur, Z.1
  • 16
    • 23644433309 scopus 로고    scopus 로고
    • Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein
    • Tanabe T., et al. Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein. Nat. Methods 2 (2005) 503-505
    • (2005) Nat. Methods , vol.2 , pp. 503-505
    • Tanabe, T.1
  • 17
    • 34249847071 scopus 로고    scopus 로고
    • Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins
    • Vitriol E.A., et al. Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 6702-6707
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6702-6707
    • Vitriol, E.A.1
  • 18
    • 0034705317 scopus 로고    scopus 로고
    • Negative regulation of fibroblast motility by Ena/VASP proteins
    • Bear J.E., et al. Negative regulation of fibroblast motility by Ena/VASP proteins. Cell 101 (2000) 717-728
    • (2000) Cell , vol.101 , pp. 717-728
    • Bear, J.E.1
  • 19
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • Bear J.E., et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell 109 (2002) 509-521
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1
  • 20
    • 30544443562 scopus 로고    scopus 로고
    • A genetically encoded photosensitizer
    • Bulina M.E., et al. A genetically encoded photosensitizer. Nat. Biotechnol. 24 (2006) 95-99
    • (2006) Nat. Biotechnol. , vol.24 , pp. 95-99
    • Bulina, M.E.1
  • 21
    • 14744281201 scopus 로고    scopus 로고
    • Balancing the generation and elimination of reactive oxygen species
    • Rodriguez R., and Redman R. Balancing the generation and elimination of reactive oxygen species. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 3175-3176
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3175-3176
    • Rodriguez, R.1    Redman, R.2
  • 22
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: metabolism, oxidative stress, and signal transduction
    • Apel K., and Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu. Rev. Plant Biol. 55 (2004) 373-399
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 23
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • Davies M.J. Singlet oxygen-mediated damage to proteins and its consequences. Biochem. Biophys. Res. Commun. 305 (2003) 761-770
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 761-770
    • Davies, M.J.1
  • 24
    • 17444404900 scopus 로고    scopus 로고
    • Toward understanding the mechanism of chromophore-assisted laser inactivation-evidence for the primary photochemical steps
    • Horstkotte E., et al. Toward understanding the mechanism of chromophore-assisted laser inactivation-evidence for the primary photochemical steps. Photochem. Photobiol. 81 (2005) 358-366
    • (2005) Photochem. Photobiol. , vol.81 , pp. 358-366
    • Horstkotte, E.1
  • 25
    • 28544439052 scopus 로고    scopus 로고
    • Correlative microscopy and electron tomography of GFP through photooxidation
    • Grabenbauer M., et al. Correlative microscopy and electron tomography of GFP through photooxidation. Nat. Methods 2 (2005) 857-862
    • (2005) Nat. Methods , vol.2 , pp. 857-862
    • Grabenbauer, M.1
  • 26
    • 0026777346 scopus 로고
    • Current perspectives of singlet oxygen detection in biological environments
    • Gorman A.A., and Rodgers M.A. Current perspectives of singlet oxygen detection in biological environments. J. Photochem. Photobiol. B 14 (1992) 159-176
    • (1992) J. Photochem. Photobiol. B , vol.14 , pp. 159-176
    • Gorman, A.A.1    Rodgers, M.A.2
  • 27
    • 0034513772 scopus 로고    scopus 로고
    • Green fluorescent protein photobleaching: a model for protein damage by endogenous and exogenous singlet oxygen
    • Greenbaum L., et al. Green fluorescent protein photobleaching: a model for protein damage by endogenous and exogenous singlet oxygen. Biol. Chem. 381 (2000) 1251-1258
    • (2000) Biol. Chem. , vol.381 , pp. 1251-1258
    • Greenbaum, L.1
  • 28
    • 33645921635 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation
    • Yan P., et al. Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation. Biochemistry 45 (2006) 4736-4748
    • (2006) Biochemistry , vol.45 , pp. 4736-4748
    • Yan, P.1
  • 29
    • 0032516015 scopus 로고    scopus 로고
    • Chromophore-assisted light inactivation and self-organization of microtubules and motors
    • Surrey T., et al. Chromophore-assisted light inactivation and self-organization of microtubules and motors. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4293-4298
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4293-4298
    • Surrey, T.1
  • 30
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans B.N., et al. The fluorescent toolbox for assessing protein location and function. Science 312 (2006) 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1
  • 31
    • 34547448862 scopus 로고    scopus 로고
    • Fluorescent proteins: maturation, photochemistry and photophysics
    • Remington S.J. Fluorescent proteins: maturation, photochemistry and photophysics. Curr. Opin. Struct. Biol. 16 (2006) 714-721
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 714-721
    • Remington, S.J.1
  • 32
    • 37749053853 scopus 로고    scopus 로고
    • Singlet oxygen photosensitization by EGFP and its chromophore HBDI
    • Jimenez-Banzo A., et al. Singlet oxygen photosensitization by EGFP and its chromophore HBDI. Biophys. J. 94 (2008) 168-172
    • (2008) Biophys. J. , vol.94 , pp. 168-172
    • Jimenez-Banzo, A.1
  • 33
    • 0033261708 scopus 로고    scopus 로고
    • Photodynamic properties of green fluorescent proteins investigated by fluorescence correlation spectroscopy
    • Widengren J., et al. Photodynamic properties of green fluorescent proteins investigated by fluorescence correlation spectroscopy. Chem. Phys. 250 (1999) 171-186
    • (1999) Chem. Phys. , vol.250 , pp. 171-186
    • Widengren, J.1
  • 34
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • Haupts U., et al. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13573-13578
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 13573-13578
    • Haupts, U.1
  • 35
    • 0043141513 scopus 로고    scopus 로고
    • The role of dark states in the photodynamics of the green fluorescent protein examined with two-color fluorescence excitation spectroscopy
    • Jung G., et al. The role of dark states in the photodynamics of the green fluorescent protein examined with two-color fluorescence excitation spectroscopy. J. Phys. Chem. A. 104 (2000) 873-877
    • (2000) J. Phys. Chem. A. , vol.104 , pp. 873-877
    • Jung, G.1
  • 36
    • 33845934415 scopus 로고    scopus 로고
    • Major signal increase in fluorescence microscopy through dark-state relaxation
    • Donnert G., et al. Major signal increase in fluorescence microscopy through dark-state relaxation. Nat. Methods 4 (2007) 81-86
    • (2007) Nat. Methods , vol.4 , pp. 81-86
    • Donnert, G.1
  • 37
    • 0018181437 scopus 로고
    • Photoinduced crosslinking of membrane proteins by fluorescein isothiocyanate
    • Lepock J.R., et al. Photoinduced crosslinking of membrane proteins by fluorescein isothiocyanate. Biochem. Biophys. Res. Commun. 85 (1978) 344-350
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 344-350
    • Lepock, J.R.1
  • 38
    • 33749345272 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation produces both targeted and collateral effects on N-type calcium channel modulation in rat sympathetic neurons
    • Guo J., et al. Fluorophore-assisted light inactivation produces both targeted and collateral effects on N-type calcium channel modulation in rat sympathetic neurons. J. Physiol. 576 (2006) 477-492
    • (2006) J. Physiol. , vol.576 , pp. 477-492
    • Guo, J.1
  • 39
    • 0029411059 scopus 로고
    • Chromophore-assisted laser inactivation of subunits of the T-cell receptor in living cells is spatially restricted
    • Liao J.C., et al. Chromophore-assisted laser inactivation of subunits of the T-cell receptor in living cells is spatially restricted. Photochem. Photobiol. 62 (1995) 923-929
    • (1995) Photochem. Photobiol. , vol.62 , pp. 923-929
    • Liao, J.C.1
  • 40
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: new insights into mechanism and regulation
    • Wear M.A., and Cooper J.A. Capping protein: new insights into mechanism and regulation. Trends Biochem. Sci. 29 (2004) 418-428
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 41
    • 0026848362 scopus 로고
    • Quenching of singlet oxygen by biomolecules from L1210 leukemia cells
    • Baker A., and Kanofsky J.R. Quenching of singlet oxygen by biomolecules from L1210 leukemia cells. Photochem. Photobiol. 55 (1992) 523-528
    • (1992) Photochem. Photobiol. , vol.55 , pp. 523-528
    • Baker, A.1    Kanofsky, J.R.2
  • 42
    • 34948875233 scopus 로고    scopus 로고
    • Measuring the lifetime of singlet oxygen in a single cell: addressing the issue of cell viability
    • Hatz S., et al. Measuring the lifetime of singlet oxygen in a single cell: addressing the issue of cell viability. Photochem. Photobiol. Sci. 6 (2007) 1106-1116
    • (2007) Photochem. Photobiol. Sci. , vol.6 , pp. 1106-1116
    • Hatz, S.1
  • 43
    • 37149032225 scopus 로고    scopus 로고
    • A general system for evaluating the efficiency of chromophore-assisted light inactivation (CALI) of proteins reveals Ru(II) tris-bipyridyl as an unusually efficient "warhead"
    • Lee J., et al. A general system for evaluating the efficiency of chromophore-assisted light inactivation (CALI) of proteins reveals Ru(II) tris-bipyridyl as an unusually efficient "warhead". Mol. Biosyst. 4 (2008) 59-65
    • (2008) Mol. Biosyst. , vol.4 , pp. 59-65
    • Lee, J.1
  • 44
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing
    • Miyoshi T., et al. Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing. J. Cell Biol. 175 (2006) 947-955
    • (2006) J. Cell Biol. , vol.175 , pp. 947-955
    • Miyoshi, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.