메뉴 건너뛰기




Volumn 20, Issue 1, 2014, Pages 60-68

Chromophore chemistry of fluorescent proteins controlled by light

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN; GREEN PHOTOACTIVATABLE FLUORESCENT PROTEIN; PEPTIDES AND PROTEINS; PROTEIN; RED FLUORESCENT PROTEIN; RED PHOTOACTIVATABLE FLUORESCENT PROTEIN; UNCLASSIFIED DRUG;

EID: 84899963630     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.04.010     Document Type: Review
Times cited : (61)

References (57)
  • 1
    • 84867534610 scopus 로고    scopus 로고
    • Red fluorescent proteins: advanced imaging applications and future design
    • Shcherbakova D.M., Subach O.M., Verkhusha V.V. Red fluorescent proteins: advanced imaging applications and future design. Angew Chem Int Ed Engl 2012, 51:10724-10738.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 10724-10738
    • Shcherbakova, D.M.1    Subach, O.M.2    Verkhusha, V.V.3
  • 2
    • 33747179417 scopus 로고    scopus 로고
    • Imaging intracellular fluorescent proteins at nanometer resolution
    • Betzig E., Patterson G.H., Sougrat R., et al. Imaging intracellular fluorescent proteins at nanometer resolution. Science 2006, 313:1642-1645.
    • (2006) Science , vol.313 , pp. 1642-1645
    • Betzig, E.1    Patterson, G.H.2    Sougrat, R.3
  • 3
    • 80054021016 scopus 로고    scopus 로고
    • Diffraction-unlimited all-optical imaging and writing with a photochromic GFP
    • Grotjohann T., Testa I., Leutenegger M., et al. Diffraction-unlimited all-optical imaging and writing with a photochromic GFP. Nature 2011, 478:204-208.
    • (2011) Nature , vol.478 , pp. 204-208
    • Grotjohann, T.1    Testa, I.2    Leutenegger, M.3
  • 4
    • 77955452640 scopus 로고    scopus 로고
    • Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET
    • Subach F.V., Zhang L., Gadella T.W., et al. Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET. Chem Biol 2010, 17:745-755.
    • (2010) Chem Biol , vol.17 , pp. 745-755
    • Subach, F.V.1    Zhang, L.2    Gadella, T.W.3
  • 5
    • 80052281149 scopus 로고    scopus 로고
    • A photoswitchable orange-to-far-red fluorescent protein, PSmOrange
    • Subach O.M., Patterson G.H., Ting L.M., et al. A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nat Methods 2011, 8:771-777.
    • (2011) Nat Methods , vol.8 , pp. 771-777
    • Subach, O.M.1    Patterson, G.H.2    Ting, L.M.3
  • 6
    • 84868556564 scopus 로고    scopus 로고
    • Optical control of protein activity by fluorescent protein domains
    • Zhou X.X., Chung H.K., Lam A.J., Lin M.Z. Optical control of protein activity by fluorescent protein domains. Science 2012, 338:810-814.
    • (2012) Science , vol.338 , pp. 810-814
    • Zhou, X.X.1    Chung, H.K.2    Lam, A.J.3    Lin, M.Z.4
  • 7
    • 82355188370 scopus 로고    scopus 로고
    • Directed molecular evolution to design advanced red fluorescent proteins
    • Subach F.V., Piatkevich K.D., Verkhusha V.V. Directed molecular evolution to design advanced red fluorescent proteins. Nat Methods 2011, 8:1019-1026.
    • (2011) Nat Methods , vol.8 , pp. 1019-1026
    • Subach, F.V.1    Piatkevich, K.D.2    Verkhusha, V.V.3
  • 8
    • 84865094423 scopus 로고    scopus 로고
    • Chromophore transformations in red fluorescent proteins
    • Subach F.V., Verkhusha V.V. Chromophore transformations in red fluorescent proteins. Chem Rev 2012, 112:4308-4327.
    • (2012) Chem Rev , vol.112 , pp. 4308-4327
    • Subach, F.V.1    Verkhusha, V.V.2
  • 9
    • 70349388235 scopus 로고    scopus 로고
    • Excited state proton transfer in the red fluorescent protein mKeima
    • Henderson J.N., Osborn M.F., Koon N., et al. Excited state proton transfer in the red fluorescent protein mKeima. J Am Chem Soc 2009, 131:13212-13213.
    • (2009) J Am Chem Soc , vol.131 , pp. 13212-13213
    • Henderson, J.N.1    Osborn, M.F.2    Koon, N.3
  • 10
    • 35648978040 scopus 로고    scopus 로고
    • Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies
    • Shu X., Kallio K., Shi X., et al. Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies. Biochemistry 2007, 46:12005-12013.
    • (2007) Biochemistry , vol.46 , pp. 12005-12013
    • Shu, X.1    Kallio, K.2    Shi, X.3
  • 11
    • 34247508566 scopus 로고    scopus 로고
    • Ultrafast excited-state dynamics of the photoswitchable protein Dronpa
    • Fron E., Flors C., Schweitzer G., et al. Ultrafast excited-state dynamics of the photoswitchable protein Dronpa. J Am Chem Soc 2007, 129:4870-4871.
    • (2007) J Am Chem Soc , vol.129 , pp. 4870-4871
    • Fron, E.1    Flors, C.2    Schweitzer, G.3
  • 12
    • 0033609034 scopus 로고    scopus 로고
    • Structural and spectral response of green fluorescent protein variants to changes in pH
    • Elsliger M.A., Wachter R.M., Hanson G.T., et al. Structural and spectral response of green fluorescent protein variants to changes in pH. Biochemistry 1999, 38:5296-5301.
    • (1999) Biochemistry , vol.38 , pp. 5296-5301
    • Elsliger, M.A.1    Wachter, R.M.2    Hanson, G.T.3
  • 13
    • 77955452640 scopus 로고    scopus 로고
    • Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET
    • Subach F.V., Zhang L., Gadella T.W., et al. Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET. Chem Biol 2010, 17:745-755.
    • (2010) Chem Biol , vol.17 , pp. 745-755
    • Subach, F.V.1    Zhang, L.2    Gadella, T.W.3
  • 14
    • 48249088102 scopus 로고    scopus 로고
    • Light-dependent regulation of structural flexibility in a photochromic fluorescent protein
    • Mizuno H., Mal T.K., Walchli M., et al. Light-dependent regulation of structural flexibility in a photochromic fluorescent protein. Proc Natl Acad Sci U S A 2008, 105:9227-9232.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9227-9232
    • Mizuno, H.1    Mal, T.K.2    Walchli, M.3
  • 15
    • 0034710921 scopus 로고    scopus 로고
    • The structure of the chromophore within DsRed, a red fluorescent protein from coral
    • Gross L.A., Baird G.S., Hoffman R.C., et al. The structure of the chromophore within DsRed, a red fluorescent protein from coral. Proc Natl Acad Sci U S A 2000, 97:11990-11995.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11990-11995
    • Gross, L.A.1    Baird, G.S.2    Hoffman, R.C.3
  • 16
    • 0242361312 scopus 로고    scopus 로고
    • Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein
    • Mizuno H., Mal T.K., Tong K.I., et al. Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein. Mol Cell 2003, 12:1051-1058.
    • (2003) Mol Cell , vol.12 , pp. 1051-1058
    • Mizuno, H.1    Mal, T.K.2    Tong, K.I.3
  • 17
    • 77950951096 scopus 로고    scopus 로고
    • Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins
    • Subach O.M., Malashkevich V.N., Zencheck W.D., et al. Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins. Chem Biol 2010, 17:333-341.
    • (2010) Chem Biol , vol.17 , pp. 333-341
    • Subach, O.M.1    Malashkevich, V.N.2    Zencheck, W.D.3
  • 18
    • 53649100738 scopus 로고    scopus 로고
    • Conversion of red fluorescent protein into a bright blue probe
    • Subach O.M., Gundorov I.S., Yoshimura M., et al. Conversion of red fluorescent protein into a bright blue probe. Chem Biol 2008, 15:1116-1124.
    • (2008) Chem Biol , vol.15 , pp. 1116-1124
    • Subach, O.M.1    Gundorov, I.S.2    Yoshimura, M.3
  • 20
    • 80054769169 scopus 로고    scopus 로고
    • A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching
    • Brakemann T., Stiel A.C., Weber G., et al. A reversibly photoswitchable GFP-like protein with fluorescence excitation decoupled from switching. Nat Biotechnol 2011, 29:942-947.
    • (2011) Nat Biotechnol , vol.29 , pp. 942-947
    • Brakemann, T.1    Stiel, A.C.2    Weber, G.3
  • 21
    • 75849129809 scopus 로고    scopus 로고
    • Photoactivation mechanism of PAmCherry based on crystal structures of the protein in the dark and fluorescent states
    • Subach F.V., Malashkevich V.N., Zencheck W.D., et al. Photoactivation mechanism of PAmCherry based on crystal structures of the protein in the dark and fluorescent states. Proc Natl Acad Sci U S A 2009, 106:21097-21102.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21097-21102
    • Subach, F.V.1    Malashkevich, V.N.2    Zencheck, W.D.3
  • 22
    • 67849111935 scopus 로고    scopus 로고
    • Structure and mechanism of the photoactivatable green fluorescent protein
    • Henderson J.N., Gepshtein R., Heenan J.R., et al. Structure and mechanism of the photoactivatable green fluorescent protein. J Am Chem Soc 2009, 131:4176-4177.
    • (2009) J Am Chem Soc , vol.131 , pp. 4176-4177
    • Henderson, J.N.1    Gepshtein, R.2    Heenan, J.R.3
  • 23
    • 0036140797 scopus 로고    scopus 로고
    • Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222
    • van Thor J.J., Gensch T., Hellingwerf K.J., Johnson L.N. Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat Struct Biol 2002, 9:37-41.
    • (2002) Nat Struct Biol , vol.9 , pp. 37-41
    • van Thor, J.J.1    Gensch, T.2    Hellingwerf, K.J.3    Johnson, L.N.4
  • 24
    • 0037939724 scopus 로고    scopus 로고
    • Light-driven decarboxylation of wild-type green fluorescent protein
    • Bell A.F., Stoner-Ma D., Wachter R.M., Tonge P.J. Light-driven decarboxylation of wild-type green fluorescent protein. J Am Chem Soc 2003, 125:6919-6926.
    • (2003) J Am Chem Soc , vol.125 , pp. 6919-6926
    • Bell, A.F.1    Stoner-Ma, D.2    Wachter, R.M.3    Tonge, P.J.4
  • 25
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson G.H., Lippincott-Schwartz J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 2002, 297:1873-1877.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 26
    • 77952059303 scopus 로고    scopus 로고
    • Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells
    • Subach F.V., Patterson G.H., Renz M., et al. Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J Am Chem Soc 2010, 132:6481-6491.
    • (2010) J Am Chem Soc , vol.132 , pp. 6481-6491
    • Subach, F.V.1    Patterson, G.H.2    Renz, M.3
  • 27
    • 80053102518 scopus 로고    scopus 로고
    • Superresolution imaging of multiple fluorescent proteins with highly overlapping emission spectra in living cells
    • Gunewardene M.S., Subach F.V., Gould T.J., et al. Superresolution imaging of multiple fluorescent proteins with highly overlapping emission spectra in living cells. Biophys J 2011, 101:1522-1528.
    • (2011) Biophys J , vol.101 , pp. 1522-1528
    • Gunewardene, M.S.1    Subach, F.V.2    Gould, T.J.3
  • 28
    • 21544445247 scopus 로고    scopus 로고
    • Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP
    • Nienhaus K., Nienhaus G.U., Wiedenmann J., Nar H. Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP. Proc Natl Acad Sci U S A 2005, 102:9156-9159.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9156-9159
    • Nienhaus, K.1    Nienhaus, G.U.2    Wiedenmann, J.3    Nar, H.4
  • 29
    • 66649126345 scopus 로고    scopus 로고
    • Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2
    • Adam V., Nienhaus K., Bourgeois D., Nienhaus G.U. Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2. Biochemistry 2009, 48:4905-4915.
    • (2009) Biochemistry , vol.48 , pp. 4905-4915
    • Adam, V.1    Nienhaus, K.2    Bourgeois, D.3    Nienhaus, G.U.4
  • 30
    • 72049104771 scopus 로고    scopus 로고
    • The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins
    • Tsutsui H., Shimizu H., Mizuno H., et al. The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins. Chem Biol 2009, 16:1140-1147.
    • (2009) Chem Biol , vol.16 , pp. 1140-1147
    • Tsutsui, H.1    Shimizu, H.2    Mizuno, H.3
  • 31
    • 57449111689 scopus 로고    scopus 로고
    • Structural characterization of IrisFP, an optical highlighter undergoing multiple photo-induced transformations
    • Adam V., Lelimousin M., Boehme S., et al. Structural characterization of IrisFP, an optical highlighter undergoing multiple photo-induced transformations. Proc Natl Acad Sci U S A 2008, 105:18343-18348.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18343-18348
    • Adam, V.1    Lelimousin, M.2    Boehme, S.3
  • 32
    • 80055083857 scopus 로고    scopus 로고
    • Rational design of photoconvertible and biphotochromic fluorescent proteins for advanced microscopy applications
    • Adam V., Moeyaert B., David C.C., et al. Rational design of photoconvertible and biphotochromic fluorescent proteins for advanced microscopy applications. Chem Biol 2011, 18:1241-1251.
    • (2011) Chem Biol , vol.18 , pp. 1241-1251
    • Adam, V.1    Moeyaert, B.2    David, C.C.3
  • 33
    • 34249844859 scopus 로고    scopus 로고
    • Structural basis for reversible photobleaching of a green fluorescent protein homologue
    • Henderson J.N., Ai H.W., Campbell R.E., Remington S.J. Structural basis for reversible photobleaching of a green fluorescent protein homologue. Proc Natl Acad Sci U S A 2007, 104:6672-6677.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6672-6677
    • Henderson, J.N.1    Ai, H.W.2    Campbell, R.E.3    Remington, S.J.4
  • 34
    • 33846850271 scopus 로고    scopus 로고
    • 1.8A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants
    • Stiel A.C., Trowitzsch S., Weber G., et al. 1.8A bright-state structure of the reversibly switchable fluorescent protein Dronpa guides the generation of fast switching variants. Biochem J 2007, 402:35-42.
    • (2007) Biochem J , vol.402 , pp. 35-42
    • Stiel, A.C.1    Trowitzsch, S.2    Weber, G.3
  • 35
    • 51349137408 scopus 로고    scopus 로고
    • Photoswitchable fluorescent proteins enable monochromatic multilabel imaging and dual color fluorescence nanoscopy
    • Andresen M., Stiel A.C., Folling J., et al. Photoswitchable fluorescent proteins enable monochromatic multilabel imaging and dual color fluorescence nanoscopy. Nat Biotechnol 2008, 26:1035-1040.
    • (2008) Nat Biotechnol , vol.26 , pp. 1035-1040
    • Andresen, M.1    Stiel, A.C.2    Folling, J.3
  • 36
    • 84861316505 scopus 로고    scopus 로고
    • Reversible photoswitching in fluorescent proteins: a mechanistic view
    • Bourgeois D., Adam V. Reversible photoswitching in fluorescent proteins: a mechanistic view. IUBMB Life 2012, 64:482-491.
    • (2012) IUBMB Life , vol.64 , pp. 482-491
    • Bourgeois, D.1    Adam, V.2
  • 37
    • 53249129686 scopus 로고    scopus 로고
    • Generation of monomeric reversibly switchable red fluorescent proteins for far-field fluorescence nanoscopy
    • Stiel A.C., Andresen M., Bock H., et al. Generation of monomeric reversibly switchable red fluorescent proteins for far-field fluorescence nanoscopy. Biophys J 2008, 95:2989-2997.
    • (2008) Biophys J , vol.95 , pp. 2989-2997
    • Stiel, A.C.1    Andresen, M.2    Bock, H.3
  • 38
    • 80054723847 scopus 로고    scopus 로고
    • Low-temperature chromophore isomerization reveals the photoswitching mechanism of the fluorescent protein Padron
    • Faro A.R., Carpentier P., Jonasson G., et al. Low-temperature chromophore isomerization reveals the photoswitching mechanism of the fluorescent protein Padron. J Am Chem Soc 2011, 133:16362-16365.
    • (2011) J Am Chem Soc , vol.133 , pp. 16362-16365
    • Faro, A.R.1    Carpentier, P.2    Jonasson, G.3
  • 39
    • 77951980192 scopus 로고    scopus 로고
    • Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron
    • Brakemann T., Weber G., Andresen M., et al. Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron. J Biol Chem 2010, 285:14603-14609.
    • (2010) J Biol Chem , vol.285 , pp. 14603-14609
    • Brakemann, T.1    Weber, G.2    Andresen, M.3
  • 40
    • 84857645570 scopus 로고    scopus 로고
    • A structural basis for reversible photoswitching of absorbance spectra in red fluorescent protein rsTagRFP
    • Pletnev S., Subach F.V., Dauter Z., et al. A structural basis for reversible photoswitching of absorbance spectra in red fluorescent protein rsTagRFP. J Mol Biol 2012, 417:144-151.
    • (2012) J Mol Biol , vol.417 , pp. 144-151
    • Pletnev, S.1    Subach, F.V.2    Dauter, Z.3
  • 41
    • 77955211891 scopus 로고    scopus 로고
    • Far-red fluorescent protein excitable with red lasers for flow cytometry and superresolution STED nanoscopy
    • Morozova K.S., Piatkevich K.D., Gould T.J., et al. Far-red fluorescent protein excitable with red lasers for flow cytometry and superresolution STED nanoscopy. Biophys J 2010, 99:L13-L15.
    • (2010) Biophys J , vol.99
    • Morozova, K.S.1    Piatkevich, K.D.2    Gould, T.J.3
  • 42
    • 84863584294 scopus 로고    scopus 로고
    • Widely accessible method for superresolution fluorescence imaging of living systems
    • Dedecker P., Mo G.C., Dertinger T., Zhang J. Widely accessible method for superresolution fluorescence imaging of living systems. Proc Natl Acad Sci U S A 2012, 109:10909-10914.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10909-10914
    • Dedecker, P.1    Mo, G.C.2    Dertinger, T.3    Zhang, J.4
  • 43
    • 77955170901 scopus 로고    scopus 로고
    • A photoactivatable marker protein for pulse-chase imaging with superresolution
    • Fuchs J., Bohme S., Oswald F., et al. A photoactivatable marker protein for pulse-chase imaging with superresolution. Nat Methods 2010, 7:627-630.
    • (2010) Nat Methods , vol.7 , pp. 627-630
    • Fuchs, J.1    Bohme, S.2    Oswald, F.3
  • 44
    • 84866419802 scopus 로고    scopus 로고
    • A FRET-facilitated photoswitching using an orange fluorescent protein with the fast photoconversion kinetics
    • Subach O.M., Entenberg D., Condeelis J.S., Verkhusha V.V. A FRET-facilitated photoswitching using an orange fluorescent protein with the fast photoconversion kinetics. J Am Chem Soc 2012, 134:14789-14799.
    • (2012) J Am Chem Soc , vol.134 , pp. 14789-14799
    • Subach, O.M.1    Entenberg, D.2    Condeelis, J.S.3    Verkhusha, V.V.4
  • 45
    • 59349110743 scopus 로고    scopus 로고
    • Photoactivatable mCherry for high-resolution two-color fluorescence microscopy
    • Subach F.V., Patterson G.H., Manley S., et al. Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nat Methods 2009, 6:153-159.
    • (2009) Nat Methods , vol.6 , pp. 153-159
    • Subach, F.V.1    Patterson, G.H.2    Manley, S.3
  • 46
    • 8344285764 scopus 로고    scopus 로고
    • Photoswitchable cyan fluorescent protein for protein tracking
    • Chudakov D.M., Verkhusha V.V., Staroverov D.B., et al. Photoswitchable cyan fluorescent protein for protein tracking. Nat Biotechnol 2004, 22:1435-1439.
    • (2004) Nat Biotechnol , vol.22 , pp. 1435-1439
    • Chudakov, D.M.1    Verkhusha, V.V.2    Staroverov, D.B.3
  • 47
    • 34548181882 scopus 로고    scopus 로고
    • Tracking intracellular protein movements using photoswitchable fluorescent proteins PS-CFP2 and Dendra2
    • Chudakov D.M., Lukyanov S., Lukyanov K.A. Tracking intracellular protein movements using photoswitchable fluorescent proteins PS-CFP2 and Dendra2. Nat Protoc 2007, 2:2024-2032.
    • (2007) Nat Protoc , vol.2 , pp. 2024-2032
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 48
    • 8644246666 scopus 로고    scopus 로고
    • EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion
    • Wiedenmann J., Ivanchenko S., Oswald F., et al. EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion. Proc Natl Acad Sci U S A 2004, 101:15905-15910.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15905-15910
    • Wiedenmann, J.1    Ivanchenko, S.2    Oswald, F.3
  • 49
    • 59349114686 scopus 로고    scopus 로고
    • A bright and photostable photoconvertible fluorescent protein
    • Mckinney S.A., Murphy C.S., Hazelwood K.L., et al. A bright and photostable photoconvertible fluorescent protein. Nat Methods 2009, 6:131-133.
    • (2009) Nat Methods , vol.6 , pp. 131-133
    • Mckinney, S.A.1    Murphy, C.S.2    Hazelwood, K.L.3
  • 50
    • 84863208605 scopus 로고    scopus 로고
    • Rational design of true monomeric and bright photoactivatable fluorescent proteins
    • Zhang M., Chang H., Zhang Y., et al. Rational design of true monomeric and bright photoactivatable fluorescent proteins. Nat Methods 2012, 9:727-729.
    • (2012) Nat Methods , vol.9 , pp. 727-729
    • Zhang, M.1    Chang, H.2    Zhang, Y.3
  • 51
    • 58049208311 scopus 로고    scopus 로고
    • MKikGR, a monomeric photoswitchable fluorescent protein
    • Habuchi S., Tsutsui H., Kochaniak A.B., et al. mKikGR, a monomeric photoswitchable fluorescent protein. PLoS ONE 2008, 3:e3944.
    • (2008) PLoS ONE , vol.3
    • Habuchi, S.1    Tsutsui, H.2    Kochaniak, A.B.3
  • 52
    • 77955555703 scopus 로고    scopus 로고
    • A monomeric photoconvertible fluorescent protein for imaging of dynamic protein localization
    • Hoi H., Shaner N.C., Davidson M.W., et al. A monomeric photoconvertible fluorescent protein for imaging of dynamic protein localization. J Mol Biol 2010, 401:776-791.
    • (2010) J Mol Biol , vol.401 , pp. 776-791
    • Hoi, H.1    Shaner, N.C.2    Davidson, M.W.3
  • 53
    • 84871104092 scopus 로고    scopus 로고
    • MMaple: a photoconvertible fluorescent protein for use in multiple imaging modalities
    • Mcevoy A.L., Hoi H., Bates M., et al. mMaple: a photoconvertible fluorescent protein for use in multiple imaging modalities. PLoS ONE 2012, 7:e51314.
    • (2012) PLoS ONE , vol.7
    • Mcevoy, A.L.1    Hoi, H.2    Bates, M.3
  • 54
    • 8844260411 scopus 로고    scopus 로고
    • Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting
    • Ando R., Mizuno H., Miyawaki A. Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting. Science 2004, 306:1370-1373.
    • (2004) Science , vol.306 , pp. 1370-1373
    • Ando, R.1    Mizuno, H.2    Miyawaki, A.3
  • 55
    • 36148939818 scopus 로고    scopus 로고
    • A stroboscopic approach for fast photoactivation-localization microscopy with Dronpa mutants
    • Flors C., Hotta J., Uji-i H., et al. A stroboscopic approach for fast photoactivation-localization microscopy with Dronpa mutants. J Am Chem Soc 2007, 129:13970-13977.
    • (2007) J Am Chem Soc , vol.129 , pp. 13970-13977
    • Flors, C.1    Hotta, J.2    Uji-i, H.3
  • 56
    • 84863347338 scopus 로고    scopus 로고
    • A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications
    • Chang H., Zhang M., Ji W., et al. A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications. Proc Natl Acad Sci U S A 2012, 109:4455-4460.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4455-4460
    • Chang, H.1    Zhang, M.2    Ji, W.3
  • 57
    • 84878979145 scopus 로고    scopus 로고
    • RsEGFP2 enables fast RESOLFT nanoscopy of living cells
    • Grotjohann T., Testa I., Reuss M., et al. rsEGFP2 enables fast RESOLFT nanoscopy of living cells. eLife 2012, 1:e00248.
    • (2012) eLife , vol.1
    • Grotjohann, T.1    Testa, I.2    Reuss, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.