메뉴 건너뛰기




Volumn 3, Issue 4, 2009, Pages 255-264

Photochemical tools to study dynamic biological processes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79951881305     PISSN: 19552068     EISSN: 1955205X     Source Type: Journal    
DOI: 10.2976/1.3132954     Document Type: Article
Times cited : (69)

References (125)
  • 1
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J, Smirnova, I, Kasho, V, Verner, G, Kaback, HR, and Iwata, S (2003). "Structure and mechanism of the lactose permease of Escherichia coli." Science 301(5633), 610-615.
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 3
    • 0027480532 scopus 로고
    • Controlling cell chemistry with caged compounds
    • Adams, SR, and Tsien, RY (1993). "Controlling cell chemistry with caged compounds." Annu. Rev. Physiol. 55, 755-784.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 755-784
    • Adams, S.R.1    Tsien, R.Y.2
  • 4
    • 0032508693 scopus 로고    scopus 로고
    • Design of organic molecules with large twophoton absorption cross sections
    • Albota, M, et al. (1998). "Design of organic molecules with large twophoton absorption cross sections." Science 281(5383), 1653-1656.
    • (1998) Science , vol.281 , Issue.5383 , pp. 1653-1656
    • Albota, M.1
  • 5
    • 2942533032 scopus 로고    scopus 로고
    • Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein
    • Anderson, S, Srajer, V, Pahl, R, Rajagopal, S, Schotte, F, Anfinrud, P, Wulff, M, and Moffat, K (2004). "Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein." Structure (London) 12(6), 1039-1045.
    • (2004) Structure (London) , vol.12 , Issue.6 , pp. 1039-1045
    • Anderson, S.1    Srajer, V.2    Pahl, R.3    Rajagopal, S.4    Schotte, F.5    Anfinrud, P.6    Wulff, M.7    Moffat, K.8
  • 6
    • 37549037064 scopus 로고    scopus 로고
    • A proposed time-resolved x-ray scattering approach to track local and global conformational changes in membrane transport proteins
    • Andersson, M, Vincent, J, van der Spoel, D, Davidsson, J, and Neutze, R (2008). "A proposed time-resolved x-ray scattering approach to track local and global conformational changes in membrane transport proteins." Structure (London) 16(1), 21-28.
    • (2008) Structure (London) , vol.16 , Issue.1 , pp. 21-28
    • Andersson, M.1    Vincent, J.2    van der Spoel, D.3    Davidsson, J.4    Neutze, R.5
  • 7
    • 0034928842 scopus 로고    scopus 로고
    • Photo-mediated gene activation using caged RNA/DNA in zebrafish embryos
    • Ando, H, Furuta, T, Tsien, RY, and Okamoto, H (2001). "Photo-mediated gene activation using caged RNA/DNA in zebrafish embryos." Nat. Genet. 28(4), 317-325.
    • (2001) Nat. Genet. , vol.28 , Issue.4 , pp. 317-325
    • Ando, H.1    Furuta, T.2    Tsien, R.Y.3    Okamoto, H.4
  • 9
    • 0033516286 scopus 로고    scopus 로고
    • α-haloacetophenone derivatives as photoreversible covalent inhibitors of protein tyrosine phosphatases
    • Arabaci, G, Guo, X-C, Beebe, KD, Coggeshall, KM, and Pei, D (1999). "α-haloacetophenone derivatives as photoreversible covalent inhibitors of protein tyrosine phosphatases." J. Am. Chem. Soc. 121(21), 5085-5086.
    • (1999) J. Am. Chem. Soc. , vol.121 , Issue.21 , pp. 5085-5086
    • Arabaci, G.1    Guo, X.-C.2    Beebe, K.D.3    Coggeshall, K.M.4    Pei, D.5
  • 10
    • 33748546615 scopus 로고    scopus 로고
    • O-nitrobenzyl photolabile protecting groups with red-shifted absorption: Syntheses and uncaging cross-sections for one- and two-photon excitation
    • Aujard, I, Benbrahim, C, Gouget, M, Ruel, O, Baudin, JB, Neveu, P, and Jullien, L (2006). "o-nitrobenzyl photolabile protecting groups with red-shifted absorption: syntheses and uncaging cross-sections for one- and two-photon excitation." Chem. Eur. J. 12(26), 6865-6879.
    • (2006) Chem. Eur. J , vol.12 , Issue.26 , pp. 6865-6879
    • Aujard, I.1    Benbrahim, C.2    Gouget, M.3    Ruel, O.4    Baudin, J.B.5    Neveu, P.6    Jullien, L.7
  • 12
    • 33846187169 scopus 로고    scopus 로고
    • Time-resolved IR spectroscopy with caged compounds: An introduction
    • Goeldner, M, and Givens, R (eds.), Wiley-VCH,Weinheim
    • Barth, A (2005). "Time-resolved IR spectroscopy with caged compounds: an introduction." Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules, Goeldner, M, and Givens, R (eds.), pp. 369-410,Wiley-VCH,Weinheim.
    • (2005) Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules , pp. 369-410
    • Barth, A.1
  • 13
    • 1942469425 scopus 로고    scopus 로고
    • Time-resolved crystallographic studies of lightinduced structural changes in the photosynthetic reaction center
    • Baxter, RH, Ponomarenko, N, Srajer, V, Pahl, R, Moffat, K, and Norris, JR (2004). "Time-resolved crystallographic studies of lightinduced structural changes in the photosynthetic reaction center." Proc. Natl. Acad. Sci. U.S.A. 101(16), 5982-5987.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.16 , pp. 5982-5987
    • Baxter, R.H.1    Ponomarenko, N.2    Srajer, V.3    Pahl, R.4    Moffat, K.5    Norris, J.R.6
  • 14
    • 0031777123 scopus 로고    scopus 로고
    • Caged peptides and proteins by targeted chemical modification
    • Bayley, H, Chang, CY, Miller, WT, Niblack, B, and Pan, P (1998). "Caged peptides and proteins by targeted chemical modification." Methods Enzymol. 291, 117-135.
    • (1998) Methods Enzymol , vol.291 , pp. 117-135
    • Bayley, H.1    Chang, C.Y.2    Miller, W.T.3    Niblack, B.4    Pan, P.5
  • 15
    • 0038383546 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis in mapping ion channel function
    • Beene, DL, Dougherty, DA, and Lester, HA (2003). "Unnatural amino acid mutagenesis in mapping ion channel function." Curr. Opin. Neurobiol. 13(3), 264-270.
    • (2003) Curr. Opin. Neurobiol , vol.13 , Issue.3 , pp. 264-270
    • Beene, D.L.1    Dougherty, D.A.2    Lester, H.A.3
  • 16
    • 0035871239 scopus 로고    scopus 로고
    • Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence
    • Billinton, N, and Knight, AW (2001). "Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence." Anal. Biochem. 291(2), 175-197.
    • (2001) Anal. Biochem. , vol.291 , Issue.2 , pp. 175-197
    • Billinton, N.1    Knight, A.W.2
  • 17
    • 0036007052 scopus 로고    scopus 로고
    • Photolabile protecting groups and linkers
    • Bochet, CG (2002). "Photolabile protecting groups and linkers." J. Chem. Soc., Perkin Trans. 1 (2), 125-152.
    • (2002) J. Chem. Soc., Perkin Trans. , vol.1 , Issue.2 , pp. 125-152
    • Bochet, C.G.1
  • 18
    • 0030504664 scopus 로고    scopus 로고
    • Feasibility and realization of singlepulse Laue diffraction on macromolecular crystals at ESRF
    • Bourgeois, D, et al. (1996). "Feasibility and realization of singlepulse Laue diffraction on macromolecular crystals at ESRF." J. Synchrotron Radiat. 3(2), 65-74.
    • (1996) J. Synchrotron Radiat. , vol.3 , Issue.2 , pp. 65-74
    • Bourgeois, D.1
  • 19
    • 25844521524 scopus 로고    scopus 로고
    • Advances in kinetic protein crystallography
    • Bourgeois, D, and Royant, A (2005). "Advances in kinetic protein crystallography." Curr. Opin. Struct. Biol. 15(5), 538-547.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , Issue.5 , pp. 538-547
    • Bourgeois, D.1    Royant, A.2
  • 21
    • 25844516394 scopus 로고    scopus 로고
    • New perspectives in kinetic protein crystallography using caged compounds
    • Goeldner, M, and Givens, R (eds.), Wiley-VCH,Weinheim
    • Bourgeois, D, and Weik, M (2005). "New perspectives in kinetic protein crystallography using caged compounds." Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules, Goeldner, M, and Givens, R (eds.), pp. 410-434,Wiley-VCH,Weinheim.
    • (2005) Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules , pp. 410-434
    • Bourgeois, D.1    Weik, M.2
  • 22
    • 0036801279 scopus 로고    scopus 로고
    • Stimulating neurons with light
    • Callaway, EM, and Yuste, R (2002). "Stimulating neurons with light." Curr. Opin. Neurobiol. 12(5), 587-592.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , Issue.5 , pp. 587-592
    • Callaway, E.M.1    Yuste, R.2
  • 24
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M, Tu, Y, Euskirchen, G, Ward, WW, and Prasher, DC (1994). "Green fluorescent protein as a marker for gene expression." Science 263(5148), 802-805.
    • (1994) Science , vol.263 , Issue.5148 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 25
    • 27944475132 scopus 로고    scopus 로고
    • Fluorescent proteins as a toolkit for in vivo imaging
    • Chudakov, DM, Lukyanov, S, and Lukyanov, KA (2005). "Fluorescent proteins as a toolkit for in vivo imaging." Trends Biotechnol. 23(12), 605-613.
    • (2005) Trends Biotechnol , vol.23 , Issue.12 , pp. 605-613
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 26
    • 36248987741 scopus 로고    scopus 로고
    • Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography
    • Colletier, JP, et al. (2007). "Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography." Acta Crystallogr., Sect. D: Biol. Crystallogr. 63(11), 1115-1128.
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , Issue.11 , pp. 1115-1128
    • Colletier, J.P.1
  • 27
    • 0000107109 scopus 로고
    • Caged nucleotides and neurotransmitters
    • Morrison, H (ed.), Wiley, NewYork
    • Corrie, JET, and Trentham, DR (1993). "Caged nucleotides and neurotransmitters." Bioorganic Photochemistry, Morrison, H (ed.), Vol. 2, pp. 243-305,Wiley, NewYork.
    • (1993) Bioorganic Photochemistry , vol.2 , pp. 243-305
    • Corrie, J.E.T.1    Trentham, D.R.2
  • 28
    • 36148937535 scopus 로고    scopus 로고
    • 3D nanoscopy: Bringing biological nanostructures into sharp focus
    • Dedecker, P, Flors, C, Hotta, J, Uji-i, H, and Hofkens, J (2007). "3D nanoscopy: bringing biological nanostructures into sharp focus." Angew. Chem., Int. Ed. 46(44), 8330-8332.
    • (2007) Angew. Chem., Int. Ed. , vol.46 , Issue.44 , pp. 8330-8332
    • Dedecker, P.1    Flors, C.2    Hotta, J.3    Uji-I, H.4    Hofkens, J.5
  • 29
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk, W, Strickler, JH, and Webb, WW (1990). "Two-photon laser scanning fluorescence microscopy." Science 248(4951), 73-76.
    • (1990) Science , vol.248 , Issue.4951 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 30
    • 0037415438 scopus 로고    scopus 로고
    • Synthesis of caged myo-inositol 1,3,4,5-tetrakisphosphate
    • Dinkel, C, and Schultz, C (2003). "Synthesis of caged myo-inositol 1,3,4,5-tetrakisphosphate." Tetrahedron Lett. 44, 1157-1159.
    • (2003) Tetrahedron Lett , vol.44 , pp. 1157-1159
    • Dinkel, C.1    Schultz, C.2
  • 31
    • 33746456503 scopus 로고    scopus 로고
    • Helping cells to tell a colorful tale
    • Eisenstein, M (2006). "Helping cells to tell a colorful tale." Nat. Methods 3(8), 647-654.
    • (2006) Nat. Methods , vol.3 , Issue.8 , pp. 647-654
    • Eisenstein, M.1
  • 32
    • 34547638628 scopus 로고    scopus 로고
    • Caged compounds: Photorelease technology for control of cellular chemistry and physiology
    • Ellis-Davies, GC (2007). "Caged compounds: photorelease technology for control of cellular chemistry and physiology." Nat. Methods 4(8), 619-628.
    • (2007) Nat. Methods , vol.4 , Issue.8 , pp. 619-628
    • Ellis-Davies, G.C.1
  • 34
    • 34250807672 scopus 로고    scopus 로고
    • 4-carboxymethoxy-5,7-dinitroindolinyl-glu: An improved caged glutamate for expeditious ultraviolet and two-photon photolysis in brain slices
    • Ellis-Davies, GC, Matsuzaki, M, Paukert, M, Kasai, H, and Bergles, DE (2007). "4-carboxymethoxy-5,7-dinitroindolinyl-glu: an improved caged glutamate for expeditious ultraviolet and two-photon photolysis in brain slices." J. Neurosci. 27(25), 6601-6604.
    • (2007) J. Neurosci. , vol.27 , Issue.25 , pp. 6601-6604
    • Ellis-Davies, G.C.1    Matsuzaki, M.2    Paukert, M.3    Kasai, H.4    Bergles, D.E.5
  • 35
    • 0017684571 scopus 로고
    • Synthesis, structure, and reactivity of adenosine cyclic 3',5'-phosphate benzyl triesters
    • Engels, J, and Schlaeger, EJ (1977). "Synthesis, structure, and reactivity of adenosine cyclic 3',5'-phosphate benzyl triesters." J. Med. Chem. 20(7), 907-911.
    • (1977) J. Med. Chem. , vol.20 , Issue.7 , pp. 907-911
    • Engels, J.1    Schlaeger, E.J.2
  • 37
    • 38949147781 scopus 로고    scopus 로고
    • Fluorescence nanoscopy with optical sectioning by two-photon induced molecular switching using continuous-wave lasers
    • Folling, J, Belov, V, Riedel, D, Schonle, A, Egner, A, Eggeling, C, Bossi, M, and Hell, SW (2008). "Fluorescence nanoscopy with optical sectioning by two-photon induced molecular switching using continuous-wave lasers." ChemPhysChem 9(2), 321-326.
    • (2008) ChemPhysChem , vol.9 , Issue.2 , pp. 321-326
    • Folling, J.1    Belov, V.2    Riedel, D.3    Schonle, A.4    Egner, A.5    Eggeling, C.6    Bossi, M.7    Hell, S.W.8
  • 40
    • 34547870514 scopus 로고    scopus 로고
    • Two-photon uncaging with fluorescence reporting: Evaluation of the o-hydroxycinnamic platform
    • Gagey, N, Neveu, P, Benbrahim, C, Goetz, B, Aujard, I, Baudin, JB, and Jullien, L (2007). "Two-photon uncaging with fluorescence reporting: evaluation of the o-hydroxycinnamic platform." J. Am. Chem. Soc. 129(32), 9986-9998.
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.32 , pp. 9986-9998
    • Gagey, N.1    Neveu, P.2    Benbrahim, C.3    Goetz, B.4    Aujard, I.5    Baudin, J.B.6    Jullien, L.7
  • 42
    • 33846190069 scopus 로고    scopus 로고
    • Caged neurotransmitters for probing neuronal circuits, neuronal integration and synaptic plasticity
    • Goeldner, M, and Givens, R (eds.), Wiley-VCH,Weinheim
    • Gillespie, DC, Kim, G, and Kandler, K. (2005). "Caged neurotransmitters for probing neuronal circuits, neuronal integration and synaptic plasticity." Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules, Goeldner, M, and Givens, R (eds.), pp. 232-251,Wiley-VCH,Weinheim.
    • (2005) Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules , pp. 232-251
    • Gillespie, D.C.1    Kim, G.2    Kandler, K.3
  • 44
    • 33750974905 scopus 로고    scopus 로고
    • Photoremovable protecting groups used for the caging of biomolecules. Caging of ATP and glutamate: Comparative analyses
    • Goeldner, M, and Givens, R (eds.), Wiley-VCH,Weinheim
    • Goeldner, M (2005). "Photoremovable protecting groups used for the caging of biomolecules. Caging of ATP and glutamate: comparative analyses." Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules, Goeldner, M, and Givens, R (eds.), pp. 76-94,Wiley-VCH,Weinheim.
    • (2005) Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules , pp. 76-94
    • Goeldner, M.1
  • 46
    • 84967678516 scopus 로고
    • Über Elementarakte mit zwei Quantensprüngen
    • Göppert-Mayer, M (1931). "Über Elementarakte mit zwei Quantensprüngen." Ann. Phys. 9, 273-294.
    • (1931) Ann. Phys. , vol.9 , pp. 273-294
    • Göppert-Mayer, M.1
  • 47
    • 54249091226 scopus 로고    scopus 로고
    • Optical switches for remote and noninvasive control of cell signaling
    • Gorostiza, P, and Isacoff, EY (2008). "Optical switches for remote and noninvasive control of cell signaling." Science 322(5900), 395-399.
    • (2008) Science , vol.322 , Issue.5900 , pp. 395-399
    • Gorostiza, P.1    Isacoff, E.Y.2
  • 48
    • 60549086255 scopus 로고    scopus 로고
    • Imaging biological structures with fluorescence photoactivation localization microscopy
    • Gould, TJ, Verkhusha, VV, and Hess, ST (2009). "Imaging biological structures with fluorescence photoactivation localization microscopy." Nat. Protocols 4(3), 291-308.
    • (2009) Nat. Protocols , vol.4 , Issue.3 , pp. 291-308
    • Gould, T.J.1    Verkhusha, V.V.2    Hess, S.T.3
  • 49
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, BA, Adams, SR, and Tsien, RY (1998). "Specific covalent labeling of recombinant protein molecules inside live cells." Science 281(5374), 269-272.
    • (1998) Science , vol.281 , Issue.5374 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 50
    • 23444448243 scopus 로고    scopus 로고
    • Adding value to fusion proteins through covalent labelling
    • Gronemeyer, T, Godin, G, and Johnsson, K (2005). "Adding value to fusion proteins through covalent labelling." Curr. Opin. Biotechnol. 16(4), 453-458.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , Issue.4 , pp. 453-458
    • Gronemeyer, T.1    Godin, G.2    Johnsson, K.3
  • 51
    • 49249137761 scopus 로고    scopus 로고
    • Photolabile glutamate protecting group with high one- and two-photon uncaging efficiencies
    • Gug, S, et al. (2008a). "Photolabile glutamate protecting group with high one- and two-photon uncaging efficiencies." ChemBioChem 9(8), 1303-1307.
    • (2008) ChemBioChem , vol.9 , Issue.8 , pp. 1303-1307
    • Gug, S.1
  • 52
    • 56749143937 scopus 로고    scopus 로고
    • Molecular engineering of photoremovable protecting groups for two-photon uncaging
    • Gug, S, Bolze, F, Specht, A, Bourgogne, C, Goeldner, M, and Nicoud, JF (2008b). "Molecular engineering of photoremovable protecting groups for two-photon uncaging." Angew. Chem., Int. Ed. 47(49), 9525-9529.
    • (2008) Angew. Chem., Int. Ed. , vol.47 , Issue.49 , pp. 9525-9529
    • Gug, S.1    Bolze, F.2    Specht, A.3    Bourgogne, C.4    Goeldner, M.5    Nicoud, J.F.6
  • 54
    • 53849105450 scopus 로고    scopus 로고
    • {7-[bis(carboxymethyl)amino]coumarin-4-yl}methoxycarbonyl derivatives for photorelease of carboxylic acids, alcohols/phenols, thioalcohols/thiophenols, and amines
    • Hagen, V, Dekowski, B, Kotzur, N, Lechler, R, Wiesner, B, Briand, B, and Beyermann, M (2008). "{7-[bis(carboxymethyl)amino]coumarin-4-yl}methoxycarbonyl derivatives for photorelease of carboxylic acids, alcohols/phenols, thioalcohols/thiophenols, and amines." Chem. Eur. J. 14(5), 1621-1627.
    • (2008) Chem. Eur. J , vol.14 , Issue.5 , pp. 1621-1627
    • Hagen, V.1    Dekowski, B.2    Kotzur, N.3    Lechler, R.4    Wiesner, B.5    Briand, B.6    Beyermann, M.7
  • 56
    • 33645534518 scopus 로고    scopus 로고
    • Synthesis and characterization of water-soluble two-photon excited blue fluorescent chromophores for bioimaging
    • Hayek, A, Bolze, F, Nicoud, J, Baldeck, PL, and Mely, Y (2006). "Synthesis and characterization of water-soluble two-photon excited blue fluorescent chromophores for bioimaging." Photochem. Photobiol. Sci. 5(1), 102-106.
    • (2006) Photochem. Photobiol. Sci. , vol.5 , Issue.1 , pp. 102-106
    • Hayek, A.1    Bolze, F.2    Nicoud, J.3    Baldeck, P.L.4    Mely, Y.5
  • 57
    • 43149084618 scopus 로고    scopus 로고
    • Multiphoton absorbing materials: Molecular designs, characterizations, and applications
    • He, GS, Tan, LS, Zheng, Q, and Prasad, PN (2008). "Multiphoton absorbing materials: molecular designs, characterizations, and applications." Chem. Rev. 108(4), 1245-1330.
    • (2008) Chem. Rev. , vol.108 , Issue.4 , pp. 1245-1330
    • He, G.S.1    Tan, L.S.2    Zheng, Q.3    Prasad, P.N.4
  • 58
    • 0021771662 scopus 로고
    • T4 RNA ligase mediated preparation of novel 'chemically misacylated' tRNAPheS
    • Heckler, TG, Chang, LH, Zama, Y, Naka, T, Chorghade, MS, and Hecht, SM (1984). "T4 RNA ligase mediated preparation of novel 'chemically misacylated' tRNAPheS." Biochemistry 23(7), 1468-1473.
    • (1984) Biochemistry , vol.23 , Issue.7 , pp. 1468-1473
    • Heckler, T.G.1    Chang, L.H.2    Zama, Y.3    Naka, T.4    Chorghade, M.S.5    Hecht, S.M.6
  • 59
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • Hell, SW (2007). "Far-field optical nanoscopy." Science 316(5828), 1153-1158.
    • (2007) Science , vol.316 , Issue.5828 , pp. 1153-1158
    • Hell, S.W.1
  • 60
    • 30944450665 scopus 로고    scopus 로고
    • Deep tissue two-photon microscopy
    • Helmchen, F, and Denk, W (2005). "Deep tissue two-photon microscopy." Nat. Methods 2(12), 932-940.
    • (2005) Nat. Methods , vol.2 , Issue.12 , pp. 932-940
    • Helmchen, F.1    Denk, W.2
  • 61
    • 77649236115 scopus 로고    scopus 로고
    • Photochemical release of neurotransmitters-transient kinetic investigation of membrane-bound receptors on the surface of cells in the microsecond-to-millisecond time region
    • Goeldner, M, and Givens, R (eds.), Wiley-VCH,Weinheim
    • Hess, GP (2005). "Photochemical release of neurotransmitters-transient kinetic investigation of membrane-bound receptors on the surface of cells in the microsecond-to-millisecond time region." Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules, Goeldner, M, and Givens, R (eds.), pp. 205-231, Wiley-VCH,Weinheim.
    • (2005) Dynamic Studies in Biology, Phototriggers, Photoswitches and Caged Biomolecules , pp. 205-231
    • Hess, G.P.1
  • 62
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess, ST, Girirajan, TP, and Mason, MD (2006). "Ultra-high resolution imaging by fluorescence photoactivation localization microscopy." Biophys. J. 91(11), 4258-4272.
    • (2006) Biophys. J , vol.91 , Issue.11 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.2    Mason, M.D.3
  • 64
    • 7444230904 scopus 로고    scopus 로고
    • Unveiling functional protein motions with picosecond x-ray crystallography and molecular dynamics simulations
    • Hummer, G, Schotte, F, and Anfinrud, PA (2004). "Unveiling functional protein motions with picosecond x-ray crystallography and molecular dynamics simulations." Proc. Natl. Acad. Sci. U.S.A. 101(43), 15330-15334.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.43 , pp. 15330-15334
    • Hummer, G.1    Schotte, F.2    Anfinrud, P.A.3
  • 65
    • 23844525079 scopus 로고    scopus 로고
    • Ultrafast x-ray diffraction of transient molecular structures in solution
    • Ihee, H, Lorenc, M, Kim, TK, Kong, QY, Cammarata, M, Lee, JH, Bratos, S, and Wulff, M (2005b). "Ultrafast x-ray diffraction of transient molecular structures in solution." Science 309(5738), 1223-1227.
    • (2005) Science , vol.309 , Issue.5738 , pp. 1223-1227
    • Ihee, H.1    Lorenc, M.2    Kim, T.K.3    Kong, Q.Y.4    Cammarata, M.5    Lee, J.H.6    Bratos, S.7    Wulff, M.8
  • 67
    • 49849101836 scopus 로고    scopus 로고
    • Chromophoreassisted laser inactivation in cell biology
    • Jacobson, K, Rajfur, Z, Vitriol, E, and Hahn, K (2008). "Chromophoreassisted laser inactivation in cell biology." Trends Cell Biol. 18(9), 443-450.
    • (2008) Trends Cell Biol , vol.18 , Issue.9 , pp. 443-450
    • Jacobson, K.1    Rajfur, Z.2    Vitriol, E.3    Hahn, K.4
  • 68
    • 12344332762 scopus 로고    scopus 로고
    • Protein chemistry on the surface of living cells
    • Johnsson, N, George, N, and Johnsson, K (2005). "Protein chemistry on the surface of living cells." ChemBioChem 6(1), 47-52.
    • (2005) ChemBioChem , vol.6 , Issue.1 , pp. 47-52
    • Johnsson, N.1    George, N.2    Johnsson, K.3
  • 69
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5'-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan, JH, Forbush, B, III, and Hoffman, JF (1978). "Rapid photolytic release of adenosine 5'-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts." Biochemistry 17(10), 1929-1935.
    • (1978) Biochemistry , vol.17 , Issue.10 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush III, B.2    Hoffman, J.F.3
  • 70
    • 39549113171 scopus 로고    scopus 로고
    • Imaging in vivo: Watching the brain in action
    • Kerr, JN, and Denk, W (2008). "Imaging in vivo: watching the brain in action." Nat. Rev. Neurosci. 9(3), 195-205.
    • (2008) Nat. Rev. Neurosci. , vol.9 , Issue.3 , pp. 195-205
    • Kerr, J.N.1    Denk, W.2
  • 71
    • 33745467167 scopus 로고    scopus 로고
    • Spatiotemporal reaction kinetics of an ultrafast photoreaction pathway visualized by time-resolved liquid x-ray diffraction
    • Kim, TK, et al. (2006). "Spatiotemporal reaction kinetics of an ultrafast photoreaction pathway visualized by time-resolved liquid x-ray diffraction." Proc. Natl. Acad. Sci. U.S.A. 103(25), 9410-9415.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , Issue.25 , pp. 9410-9415
    • Kim, T.K.1
  • 72
    • 0036183506 scopus 로고    scopus 로고
    • The efficiency of two-photon photolysis of a 'caged' fluorophore, o-1-(2-nitrophenyl)ethylpyranine, in relation to photodamage of synaptic terminals
    • Kiskin, NI, Chillingworth, R, McCray, JA, Piston, D, and Ogden, D (2002). "The efficiency of two-photon photolysis of a 'caged' fluorophore, o-1-(2-nitrophenyl)ethylpyranine, in relation to photodamage of synaptic terminals." Eur. Biophys. J. 30(8), 588-604.
    • (2002) Eur. Biophys. J , vol.30 , Issue.8 , pp. 588-604
    • Kiskin, N.I.1    Chillingworth, R.2    McCray, J.A.3    Piston, D.4    Ogden, D.5
  • 73
    • 34249781985 scopus 로고    scopus 로고
    • Highly activateable and rapidly releaseable caged fluorescein derivatives
    • Kobayashi, T, Urano, Y, Kamiya, M, Ueno, T, Kojima, H, and Nagano, T (2007). "Highly activateable and rapidly releaseable caged fluorescein derivatives." J. Am. Chem. Soc. 129(21), 6696-6697.
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.21 , pp. 6696-6697
    • Kobayashi, T.1    Urano, Y.2    Kamiya, M.3    Ueno, T.4    Kojima, H.5    Nagano, T.6
  • 74
    • 33644812369 scopus 로고    scopus 로고
    • Photochemical tools for remote control of ion channels in excitable cells
    • Kramer, RH, Chambers, JJ, and Trauner, D (2005). "Photochemical tools for remote control of ion channels in excitable cells." Nat. Chem. Biol. 1(7), 360-365.
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.7 , pp. 360-365
    • Kramer, R.H.1    Chambers, J.J.2    Trauner, D.3
  • 75
    • 27744567862 scopus 로고    scopus 로고
    • The preparation and in vivo applications of caged peptides and proteins
    • Lawrence, DS (2005). "The preparation and in vivo applications of caged peptides and proteins." Curr. Opin. Chem. Biol. 9(6), 570-575.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.6 , pp. 570-575
    • Lawrence, D.S.1
  • 76
    • 67649243556 scopus 로고    scopus 로고
    • Illumination the chemistry of life: Design, synthesis, and applications of caged and related photoresponsive compounds
    • Lee, H, Larson, D, and Lawrence, D (2009). "Illumination the chemistry of life: design, synthesis, and applications of caged and related photoresponsive compounds." ACS Chem. Biol.
    • (2009) ACS Chem. Biol.
    • Lee, H.1    Larson, D.2    Lawrence, D.3
  • 77
    • 27744566468 scopus 로고    scopus 로고
    • Dependence of the two-photon absorption cross section on the conjugation of the phenylacetylene linker in dipolar donorbridge-acceptor chromophores
    • Lee, S, Thomas, K, Thayumanavan, S, and Bardeen, C (2005). "Dependence of the two-photon absorption cross section on the conjugation of the phenylacetylene linker in dipolar donorbridge-acceptor chromophores." J. Phys. Chem. A 109(43), 9767-9774.
    • (2005) J. Phys. Chem. A , vol.109 , Issue.43 , pp. 9767-9774
    • Lee, S.1    Thomas, K.2    Thayumanavan, S.3    Bardeen, C.4
  • 79
    • 37249093065 scopus 로고    scopus 로고
    • Fluorescent proteins for photoactivation experiments
    • Lippincott-Schwartz, J, and Patterson, GH (2008). "Fluorescent proteins for photoactivation experiments." Methods Cell Biol. 85, 45-61.
    • (2008) Methods Cell Biol , vol.85 , pp. 45-61
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 81
    • 0042970456 scopus 로고    scopus 로고
    • Photoreversible inhibition of cholinesterases: Catalytic serine-labeled caged butyrylcholinesterase
    • Loudwig, S, Nicolet, Y, Masson, P, Fontecilla-Camps, JC, Bon, S, Nachon, F, and Goeldner, M (2003). "Photoreversible inhibition of cholinesterases: catalytic serine-labeled caged butyrylcholinesterase." ChemBioChem 4(8), 762-767.
    • (2003) ChemBioChem , vol.4 , Issue.8 , pp. 762-767
    • Loudwig, S.1    Nicolet, Y.2    Masson, P.3    Fontecilla-Camps, J.C.4    Bon, S.5    Nachon, F.6    Goeldner, M.7
  • 85
    • 0029964532 scopus 로고    scopus 로고
    • Light-directed generation of the actin-activated ATPase activity of caged heavy meromyosin
    • Marriott, G, and Heidecker, M (1996). "Light-directed generation of the actin-activated ATPase activity of caged heavy meromyosin." Biochemistry 35(10), 3170-3174.
    • (1996) Biochemistry , vol.35 , Issue.10 , pp. 3170-3174
    • Marriott, G.1    Heidecker, M.2
  • 86
    • 33746734322 scopus 로고    scopus 로고
    • Biologically active molecules with a 'light switch'
    • Mayer, G, and Heckel, A (2006). "Biologically active molecules with a 'light switch'." Angew. Chem., Int. Ed. 45(30), 4900-4921.
    • (2006) Angew. Chem., Int. Ed. , vol.45 , Issue.30 , pp. 4900-4921
    • Mayer, G.1    Heckel, A.2
  • 87
    • 36248965157 scopus 로고    scopus 로고
    • Light-dependent RNA interference with nucleobase-caged siRNAs
    • Mikat, V, and Heckel, A (2007). "Light-dependent RNA interference with nucleobase-caged siRNAs." RNA 13(12), 2341-2347.
    • (2007) RNA , vol.13 , Issue.12 , pp. 2341-2347
    • Mikat, V.1    Heckel, A.2
  • 89
    • 0031904189 scopus 로고    scopus 로고
    • Ultrafast time-resolved crystallography
    • Moffat, K (1998). "Ultrafast time-resolved crystallography." Nat. Struct.Biol. 5, 641-643.
    • (1998) Nat. Struct.Biol. , vol.5 , pp. 641-643
    • Moffat, K.1
  • 90
    • 4344649800 scopus 로고    scopus 로고
    • Potential impact of an x-ray free electron laser on structural biology
    • Neutze, R, Huldt, G, Hajdu, J, and van der Spoel, D (2004). "Potential impact of an x-ray free electron laser on structural biology." Radiat. Phys. Chem. 71, 905-916.
    • (2004) Radiat. Phys. Chem. , vol.71 , pp. 905-916
    • Neutze, R.1    Huldt, G.2    Hajdu, J.3    van der Spoel, D.4
  • 92
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond x-ray pulses
    • Neutze, R, Wouts, R, van der Spoel, D, Weckert, E, and Hajdu, J (2000). "Potential for biomolecular imaging with femtosecond x-ray pulses." Nature (London) 406(6797), 752-757.
    • (2000) Nature (London) , vol.406 , Issue.6797 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    van der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 94
    • 35748932679 scopus 로고    scopus 로고
    • Two-photon photostimulation and imaging of neural circuits
    • Nikolenko, V, Poskanzer, KE, and Yuste, R (2007). "Two-photon photostimulation and imaging of neural circuits." Nat. Methods 4(11), 943-950.
    • (2007) Nat. Methods , vol.4 , Issue.11 , pp. 943-950
    • Nikolenko, V.1    Poskanzer, K.E.2    Yuste, R.3
  • 95
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, CJ, Anthony-Cahill, SJ, Griffith, MC, and Schultz, PG (1989). "A general method for site-specific incorporation of unnatural amino acids into proteins." Science 244(4901), 182-188.
    • (1989) Science , vol.244 , Issue.4901 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 96
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of halobacterium halobium
    • Oesterhelt, D, and Stoeckenius, W (1971). "Rhodopsin-like protein from the purple membrane of halobacterium halobium." Nature (London), New Biol. 233(39), 149-152.
    • (1971) Nature (London), New Biol. , vol.233 , Issue.39 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 97
    • 63349093335 scopus 로고    scopus 로고
    • Synthesis and photochemical properties of photo-cleavable crosslinkers
    • Omran, Z, and Specht, A (2009). "Synthesis and photochemical properties of photo-cleavable crosslinkers." Tetrahedron Lett. 50(20), 2434-2436.
    • (2009) Tetrahedron Lett. , vol.50 , Issue.20 , pp. 2434-2436
    • Omran, Z.1    Specht, A.2
  • 98
    • 40149090001 scopus 로고    scopus 로고
    • Synthesis and photochemical properties of a light-activated fluorophore to label His-tagged proteins
    • Orange, C, Specht, A, Puliti, D, Sakr, E, Furuta, T, Winsor, B, and Goeldner, M(2008). "Synthesis and photochemical properties of a light-activated fluorophore to label His-tagged proteins." Chem. Commun. (Cambridge) (10), 1217-1219.
    • (2008) Chem. Commun. (Cambridge) , vol.10 , pp. 1217-1219
    • Orange, C.1    Specht, A.2    Puliti, D.3    Sakr, E.4    Furuta, T.5    Winsor, B.6    Goeldner, M.7
  • 99
    • 0032032613 scopus 로고    scopus 로고
    • Preparation and photoactivation of caged fluorophores and caged proteins using a new class of heterobifunctional, photocleavable cross-linking reagents
    • Ottl, J, Gabriel, D, and Marriott, G (1998). "Preparation and photoactivation of caged fluorophores and caged proteins using a new class of heterobifunctional, photocleavable cross-linking reagents." Bioconjugate Chem. 9(2), 143-151.
    • (1998) Bioconjugate Chem. , vol.9 , Issue.2 , pp. 143-151
    • Ottl, J.1    Gabriel, D.2    Marriott, G.3
  • 100
    • 28044450132 scopus 로고    scopus 로고
    • Synthetic and photochemical studies of substituted 1-acyl-7-nitroindolines
    • Papageorgiou, G, Ogden, D, Kelly, G, and Corrie, JE (2005). "Synthetic and photochemical studies of substituted 1-acyl-7-nitroindolines." Photochem. Photobiol. Sci. 4(11), 887-896.
    • (2005) Photochem. Photobiol. Sci. , vol.4 , Issue.11 , pp. 887-896
    • Papageorgiou, G.1    Ogden, D.2    Kelly, G.3    Corrie, J.E.4
  • 101
    • 58149117807 scopus 로고    scopus 로고
    • Patterned two-photon illumination by spatiotemporal shaping of ultrashort pulses
    • Papagiakoumou, E, de Sars, V, Oron, D, and Emiliani, V (2008). "Patterned two-photon illumination by spatiotemporal shaping of ultrashort pulses." Opt. Express 16(26), 22039-22047.
    • (2008) Opt. Express , vol.16 , Issue.26 , pp. 22039-22047
    • Papagiakoumou, E.1    de Sars, V.2    Oron, D.3    Emiliani, V.4
  • 103
    • 0000576453 scopus 로고    scopus 로고
    • Photoremovable protecting groups: Reaction mechanisms and applications
    • Pelliccioli, AP, and Wirz, J (2002). "Photoremovable protecting groups: reaction mechanisms and applications." Photochem. Photobiol. Sci. 1(7), 441-458.
    • (2002) Photochem. Photobiol. Sci. , vol.1 , Issue.7 , pp. 441-458
    • Pelliccioli, A.P.1    Wirz, J.2
  • 104
    • 0033961309 scopus 로고    scopus 로고
    • Observation of unstable species in enzyme-catalyzed transformations using protein crystallography
    • Petsko, GA, and Ringe, D (2000). "Observation of unstable species in enzyme-catalyzed transformations using protein crystallography." Curr. Opin. Chem. Biol. 4(1), 89-94.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , Issue.1 , pp. 89-94
    • Petsko, G.A.1    Ringe, D.2
  • 105
    • 11844294715 scopus 로고    scopus 로고
    • A structural pathway for signaling in the E46Q mutant of photoactive yellow protein
    • Rajagopal, S, Anderson, S, Srajer, V, Schmidt, M, Pahl, R, and Moffat, K (2005). "A structural pathway for signaling in the E46Q mutant of photoactive yellow protein." Structure (London) 13(1), 55-63.
    • (2005) Structure (London) , vol.13 , Issue.1 , pp. 55-63
    • Rajagopal, S.1    Anderson, S.2    Srajer, V.3    Schmidt, M.4    Pahl, R.5    Moffat, K.6
  • 107
    • 16344373731 scopus 로고    scopus 로고
    • Optical switching of dipolar interactions on proteins
    • Sakata, T, Yan, Y, and Marriott, G (2005). "Optical switching of dipolar interactions on proteins." Proc. Natl. Acad. Sci. U.S.A. 102(13), 4759-4764.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , Issue.13 , pp. 4759-4764
    • Sakata, T.1    Yan, Y.2    Marriott, G.3
  • 108
    • 0033857394 scopus 로고    scopus 로고
    • Crystallographic structure determination of unstable species
    • Schlichting, I (2000). "Crystallographic structure determination of unstable species." Acc. Chem. Res. 33(8), 532-538.
    • (2000) Acc. Chem. Res. , vol.33 , Issue.8 , pp. 532-538
    • Schlichting, I.1
  • 109
    • 0030852353 scopus 로고    scopus 로고
    • Triggering methods in crystallographic enzyme kinetics
    • Schlichting, I, and Goody, RS (1997). "Triggering methods in crystallographic enzyme kinetics." Methods Enzymol. 277, 467-490.
    • (1997) Methods Enzymol , vol.277 , pp. 467-490
    • Schlichting, I.1    Goody, R.S.2
  • 111
    • 34248196084 scopus 로고    scopus 로고
    • Coumarin-caged glycine that can be photolyzed within 3 microseconds by visible light
    • Shembekar, VR, Chen, Y, Carpenter, BK, and Hess, GP (2007). "Coumarin-caged glycine that can be photolyzed within 3 microseconds by visible light." Biochemistry 46(18), 5479-5484.
    • (2007) Biochemistry , vol.46 , Issue.18 , pp. 5479-5484
    • Shembekar, V.R.1    Chen, Y.2    Carpenter, B.K.3    Hess, G.P.4
  • 112
    • 33750981525 scopus 로고    scopus 로고
    • New photoremovable protecting groups for carboxylic acids with high photolytic efficiencies at near-UV irradiation. Application to the photocontrolled release of L-glutamate
    • Specht, A, Thomann, JS, Alarcon, K, Wittayanan, W, Ogden, D, Furuta, T, Kurakawa, Y, and Goeldner, M (2006). "New photoremovable protecting groups for carboxylic acids with high photolytic efficiencies at near-UV irradiation. Application to the photocontrolled release of L-glutamate." ChemBioChem 7(11), 1690-1695.
    • (2006) ChemBioChem , vol.7 , Issue.11 , pp. 1690-1695
    • Specht, A.1    Thomann, J.S.2    Alarcon, K.3    Wittayanan, W.4    Ogden, D.5    Furuta, T.6    Kurakawa, Y.7    Goeldner, M.8
  • 113
    • 0035814133 scopus 로고    scopus 로고
    • Cryophotolysis of ortho-nitrobenzyl derivatives of enzyme ligands for the potential kinetic crystallography of macromolecules
    • Specht, A, Ursby, T, Weik, M, Peng, L, Kroon, J, Bourgeois, D, and Goeldner, M (2001). "Cryophotolysis of ortho-nitrobenzyl derivatives of enzyme ligands for the potential kinetic crystallography of macromolecules." ChemBioChem 2(11), 845-848.
    • (2001) ChemBioChem , vol.2 , Issue.11 , pp. 845-848
    • Specht, A.1    Ursby, T.2    Weik, M.3    Peng, L.4    Kroon, J.5    Bourgeois, D.6    Goeldner, M.7
  • 114
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction
    • Srajer, V, Ren, Z, Teng, TY, Schmidt, M, Ursby, T, Bourgeois, D, Pradervand, C, Schildkamp, W, Wulff, M, and Moffat, K (2001). "Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction." Biochemistry 40(46), 13802-13815.
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 115
    • 0034851478 scopus 로고    scopus 로고
    • Trapping reaction intermediates in macromolecular crystals for structural analyses
    • Stoddard, BL (2001). "Trapping reaction intermediates in macromolecular crystals for structural analyses." Methods 24(2), 125-138.
    • (2001) Methods , vol.24 , Issue.2 , pp. 125-138
    • Stoddard, B.L.1
  • 116
    • 4544231739 scopus 로고    scopus 로고
    • Site-specific incorporation of unnatural amino acids into proteins
    • Stromgaard, A, Jensen, AA, and Stromgaard, K (2004). "Site-specific incorporation of unnatural amino acids into proteins." ChemBioChem 5(7), 909-916.
    • (2004) ChemBioChem , vol.5 , Issue.7 , pp. 909-916
    • Stromgaard, A.1    Jensen, A.A.2    Stromgaard, K.3
  • 117
    • 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(7), 503-505.
    • (2005) Nat. Methods , vol.2 , Issue.7 , pp. 503-505
    • Tanabe, T.1    Oyamada, M.2    Fujita, K.3    Dai, P.4    Tanaka, H.5    Takamatsu, T.6
  • 118
    • 58049136203 scopus 로고    scopus 로고
    • Enhanced two-photon absorption of organic chromophores: Theoretical and experimental assessments
    • Terenziani, F, Katan, C, Badaeva, E, Tretiak, S, and Blanchard-Desce, M (2008). "Enhanced two-photon absorption of organic chromophores: theoretical and experimental assessments." Adv. Mater. (Weinheim, Ger.) 20(24), 4641-4678.
    • (2008) Adv. Mater. (Weinheim, Ger.) , vol.20 , Issue.24 , pp. 4641-4678
    • Terenziani, F.1    Katan, C.2    Badaeva, E.3    Tretiak, S.4    Blanchard-Desce, M.5
  • 119
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot, JA, and Mitchison, TJ (1991). "Actin microfilament dynamics in locomoting cells." Nature (London) 352(6331), 126-131.
    • (1991) Nature (London) , vol.352 , Issue.6331 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 120
  • 123
    • 0023661727 scopus 로고
    • Kinetics of smooth and skeletal muscle activation by laser pulse photolysis of caged inositol 1,4,5-trisphosphate
    • Walker, JW, Somlyo, AV, Goldman, YE, Somlyo, AP, and Trentham, DR (1987). "Kinetics of smooth and skeletal muscle activation by laser pulse photolysis of caged inositol 1,4,5-trisphosphate." Nature (London) 327(6119), 249-252.
    • (1987) Nature (London) , vol.327 , Issue.6119 , pp. 249-252
    • Walker, J.W.1    Somlyo, A.V.2    Goldman, Y.E.3    Somlyo, A.P.4    Trentham, D.R.5
  • 124
    • 1842637652 scopus 로고    scopus 로고
    • New caged coumarin fluorophores with extraordinary uncaging cross sections suitable for biological imaging applications
    • Zhao, Y, Zheng, Q, Dakin, K, Xu, K, Martinez, ML, and Li, WH (2004). "New caged coumarin fluorophores with extraordinary uncaging cross sections suitable for biological imaging applications." J. Am. Chem. Soc. 126(14), 4653-4663.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.14 , pp. 4653-4663
    • Zhao, Y.1    Zheng, Q.2    Dakin, K.3    Xu, K.4    Martinez, M.L.5    Li, W.H.6
  • 125
    • 0242353872 scopus 로고    scopus 로고
    • Nonlinear magic: Multiphoton microscopy in the biosciences
    • Zipfel, WR, Williams, RM, and Webb, WW (2003). "Nonlinear magic: multiphoton microscopy in the biosciences." Nat. Biotechnol. 21(11), 1369-1377.
    • (2003) Nat. Biotechnol. , vol.21 , Issue.11 , pp. 1369-1377
    • Zipfel, W.R.1    Williams, R.M.2    Webb, W.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.