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Volumn 9, Issue 4, 2014, Pages 910-928

Engineering and characterizing monomeric fluorescent proteins for live-cell imaging applications

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; MONOMERIC FLUORESCENT PROTEIN; OLIGONUCLEOTIDE; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG; GREEN FLUORESCENT PROTEIN; PEPTIDE LIBRARY;

EID: 84897136274     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2014.054     Document Type: Article
Times cited : (49)

References (57)
  • 1
  • 2
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W. & Prasher, D.C. Green fluorescent protein as a marker for gene expression. Science 263, 802-805 (1994).
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 4
    • 0032867477 scopus 로고    scopus 로고
    • Fluorescent proteins from nonbioluminescent Anthozoa species
    • Matz, M.V. et al. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat. Biotechnol. 17, 969-973 (1999).
    • (1999) Nat. Biotechnol. , vol.17 , pp. 969-973
    • Matz, M.V.1
  • 5
    • 0037062424 scopus 로고    scopus 로고
    • A monomeric red fluorescent protein
    • Campbell, R.E. et al. A monomeric red fluorescent protein. Proc. Natl. Acad. Sci. USA 99, 7877-7882 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7877-7882
    • Campbell, R.E.1
  • 6
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp
    • Shaner, N.C. et al. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22, 1567-1572 (2004).
    • (2004) Red Fluorescent Protein. Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1
  • 7
    • 33845751079 scopus 로고    scopus 로고
    • Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: Structural characterization and applications in fluorescence imaging
    • Ai, H., Henderson, J.N., Remington, S.J. & Campbell, R.E. Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging. Biochem. J. 400, 531-540 (2006).
    • (2006) Biochem. J. , vol.400 , pp. 531-540
    • Ai, H.1    Henderson, J.N.2    Remington, S.J.3    Campbell, R.E.4
  • 8
    • 84886799054 scopus 로고    scopus 로고
    • An engineered monomeric Zoanthus sp
    • Hoi, H. et al. An engineered monomeric Zoanthus sp. Yellow fluorescent protein. Chem. Biol. 20, 1296-1304 (2013).
    • (2013) Yellow Fluorescent Protein. Chem. Biol. , vol.20 , pp. 1296-1304
    • Hoi, H.1
  • 9
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • Baird, G.S., Zacharias, D.A. & Tsien, R.Y. Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97, 11984-11989 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 10
    • 0035370120 scopus 로고    scopus 로고
    • Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomeric DsRed-tagged proteins
    • Lauf, U., Lopez, P. & Falk, M.M. Expression of fluorescently tagged connexins: a novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett. 498, 11-15 (2001).
    • (2001) FEBS Lett. , vol.498 , pp. 11-15
    • Lauf, U.1    Lopez, P.2    Falk, M.M.3
  • 11
    • 0036434301 scopus 로고    scopus 로고
    • An approach for reducing unwanted oligomerisation of DsRed fusion proteins
    • Gavin, P., Devenish, R.J. & Prescott, M. An approach for reducing unwanted oligomerisation of DsRed fusion proteins. Biochem. Biophys. Res. Commun. 298, 707-713 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 707-713
    • Gavin, P.1    Devenish, R.J.2    Prescott, M.3
  • 12
    • 0037063328 scopus 로고    scopus 로고
    • Intracellular localization of herpes simplex virus type 1 thymidine kinase fused to different fluorescent proteins depends on choice of fluorescent tag
    • Soling, A., Simm, A. & Rainov, N. Intracellular localization of herpes simplex virus type 1 thymidine kinase fused to different fluorescent proteins depends on choice of fluorescent tag. FEBS Lett. 527, 153-158 (2002).
    • (2002) FEBS Lett. , vol.527 , pp. 153-158
    • Soling, A.1    Simm, A.2    Rainov, N.3
  • 13
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • Shaner, N.C. et al. Improving the photostability of bright monomeric orange and red fluorescent proteins. Nat. Methods 5, 545-551 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 545-551
    • Shaner, N.C.1
  • 14
    • 0141483388 scopus 로고    scopus 로고
    • A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling
    • Karasawa, S., Araki, T., Yamamoto-Hino, M. & Miyawaki, A. A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling. J. Biol. Chem. 278, 34167-34171 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34167-34171
    • Karasawa, S.1    Araki, T.2    Yamamoto-Hino, M.3    Miyawaki, A.4
  • 15
    • 84877578867 scopus 로고    scopus 로고
    • A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum
    • Shaner, N.C. et al. A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum. Nat. Methods 10, 407-409 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 407-409
    • Shaner, N.C.1
  • 16
    • 3142736368 scopus 로고    scopus 로고
    • Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer
    • Karasawa, S., Araki, T., Nagai, T., Mizuno, H. & Miyawaki, A. Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem. J. 381, 307-312 (2004).
    • (2004) Biochem. J. , vol.381 , pp. 307-312
    • Karasawa, S.1    Araki, T.2    Nagai, T.3    Mizuno, H.4    Miyawaki, A.5
  • 17
    • 8644246666 scopus 로고    scopus 로고
    • EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion
    • Wiedenmann, J. et al. EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion. Proc. Natl. Acad. Sci. USA 101, 15905-15910 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15905-15910
    • Wiedenmann, J.1
  • 18
    • 33645747837 scopus 로고    scopus 로고
    • Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light
    • Gurskaya, N.G. et al. Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light. Nat. Biotechnol. 24, 461-465 (2006).
    • (2006) Nat. Biotechnol. , vol.24 , pp. 461-465
    • Gurskaya, N.G.1
  • 19
    • 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 306, 1370-1373 (2004).
    • (2004) Science , vol.306 , pp. 1370-1373
    • Ando, R.1    Mizuno, H.2    Miyawaki, A.3
  • 20
    • 33646572554 scopus 로고    scopus 로고
    • A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy
    • Kogure, T. et al. A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy. Nat. Biotechnol. 24, 577-581 (2006).
    • (2006) Nat. Biotechnol. , vol.24 , pp. 577-581
    • Kogure, T.1
  • 21
    • 11144357587 scopus 로고    scopus 로고
    • GFP-like proteins as ubiquitous metazoan superfamily: Evolution of functional features and structural complexity
    • Shagin, D.A. et al. GFP-like proteins as ubiquitous metazoan superfamily: evolution of functional features and structural complexity. Mol. Biol. Evol. 21, 841-850 (2004).
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 841-850
    • Shagin, D.A.1
  • 22
    • 50549091558 scopus 로고    scopus 로고
    • Diversity and evolution of coral fluorescent proteins
    • Alieva, N.O. et al. Diversity and evolution of coral fluorescent proteins. PLoS ONE 3, e2680 (2008).
    • (2008) PLoS ONE , vol.3
    • Alieva, N.O.1
  • 23
    • 67749127839 scopus 로고    scopus 로고
    • Development of GFP-based biosensors possessing the binding properties of antibodies
    • Pavoor, T.V., Cho, Y.K. & Shusta, E.V. Development of GFP-based biosensors possessing the binding properties of antibodies. Proc. Natl. Acad. Sci. USA 106, 11895-11900 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 11895-11900
    • Pavoor, T.V.1    Cho, Y.K.2    Shusta, E.V.3
  • 24
    • 10044227172 scopus 로고    scopus 로고
    • Evolution of new nonantibody proteins via iterative somatic hypermutation
    • Wang, L., Jackson, W.C., Steinbach, P.A. & Tsien, R.Y. Evolution of new nonantibody proteins via iterative somatic hypermutation. Proc. Natl. Acad. Sci. USA 101, 16745-16749 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16745-16749
    • Wang, L.1    Jackson, W.C.2    Steinbach, P.A.3    Tsien, R.Y.4
  • 25
    • 38349092971 scopus 로고    scopus 로고
    • Protein evolution by hypermutation and selection in the B cell line DT40
    • Arakawa, H. et al. Protein evolution by hypermutation and selection in the B cell line DT40. Nucleic Acids Res. 36, e1 (2008).
    • (2008) Nucleic Acids Res. , vol.36
    • Arakawa, H.1
  • 26
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B.P., Valdivia, R.H. & Falkow, S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173, 33-38 (1996).
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 27
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A.W. & Daugherty, P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23, 355-360 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 28
    • 33845690052 scopus 로고    scopus 로고
    • Blue fluorescent proteins with enhanced brightness and photostability from a structurally targeted library
    • Mena, M.A., Treynor, T.P., Mayo, S.L. & Daugherty, P.S. Blue fluorescent proteins with enhanced brightness and photostability from a structurally targeted library. Nat. Biotechnol. 24, 1569-1571 (2006).
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1569-1571
    • Mena, M.A.1    Treynor, T.P.2    Mayo, S.L.3    Daugherty, P.S.4
  • 29
    • 33947142436 scopus 로고    scopus 로고
    • The creation of a novel fluorescent protein by guided consensus engineering
    • Dai, M. et al. The creation of a novel fluorescent protein by guided consensus engineering. Protein Eng. Des. Sel. 20, 69-79 (2007).
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 69-79
    • Dai, M.1
  • 30
    • 77955555703 scopus 로고    scopus 로고
    • A monomeric photoconvertible fluorescent protein for imaging of dynamic protein localization
    • Hoi, H. et al. A monomeric photoconvertible fluorescent protein for imaging of dynamic protein localization. J. Mol. Biol. 401, 776-791 (2010).
    • (2010) J. Mol. Biol. , vol.401 , pp. 776-791
    • Hoi, H.1
  • 31
    • 33846102955 scopus 로고    scopus 로고
    • Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function
    • Treynor, T.P., Vizcarra, C.L., Nedelcu, D. & Mayo, S.L. Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function. Proc. Natl. Acad. Sci. USA 104, 48-53 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 48-53
    • Treynor, T.P.1    Vizcarra, C.L.2    Nedelcu, D.3    Mayo, S.L.4
  • 32
    • 78650543850 scopus 로고    scopus 로고
    • Generation of longer emission wavelength red fluorescent proteins using computationally designed libraries
    • Chica, R.A., Moore, M.M., Allen, B.D. & Mayo, S.L. Generation of longer emission wavelength red fluorescent proteins using computationally designed libraries. Proc. Natl. Acad. Sci. USA 107, 20257-20262 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 20257-20262
    • Chica, R.A.1    Moore, M.M.2    Allen, B.D.3    Mayo, S.L.4
  • 33
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer, W.P., Crameri, A., Ha, K.D., Brennan, T.M. & Heyneker, H.L. Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164, 49-53 (1995).
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 34
    • 27944480763 scopus 로고    scopus 로고
    • Construction of designed protein libraries using gene assembly mutagenesis
    • eds. Arnold, F.H. & Georgiou, G. (Humana Press,) 1st edn
    • Bessette, P.H., Mena, M.A., Nguyen, A.W. & Daugherty, P.S. Construction of designed protein libraries using gene assembly mutagenesis. In Directed Evolution Library Creation: Methods and Protocols 1st edn., Vol. 231 (eds. Arnold, F.H. & Georgiou, G.) 29-37 (Humana Press, 2003).
    • (2003) Directed Evolution Library Creation: Methods and Protocols , vol.231 , pp. 29-37
    • Bessette, P.H.1    Mena, M.A.2    Nguyen, A.W.3    Daugherty, P.S.4
  • 35
    • 0029909407 scopus 로고    scopus 로고
    • Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein
    • Yang, T.T., Cheng, L. & Kain, S.R. Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein. Nucleic Acids Res. 24, 4592-4593 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4592-4593
    • Yang, T.T.1    Cheng, L.2    Kain, S.R.3
  • 36
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 38
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M. et al. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395 (1996).
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1
  • 39
    • 0028816556 scopus 로고
    • Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction
    • Fromant, M., Blanquet, S. & Plateau, P. Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction. Anal. Biochem. 224, 347-353 (1995).
    • (1995) Anal. Biochem. , vol.224 , pp. 347-353
    • Fromant, M.1    Blanquet, S.2    Plateau, P.3
  • 40
    • 3042784274 scopus 로고    scopus 로고
    • Generating mutant libraries using error-prone PCR
    • 1st edn.,( eds. Arnold, F.H. & Georgiou, G.) (Humana Press)
    • Cirino, P.C., Mayer, K.M. & Umeno, D. Generating mutant libraries using error-prone PCR. In Directed Evolution Library Creation: Methods and Protocols 1st edn., Vol. 231 (eds. Arnold, F.H. & Georgiou, G.) 3-9 (Humana Press, 2003).
    • (2003) Directed Evolution Library Creation: Methods and Protocols , vol.231 , pp. 3-9
    • Cirino, P.C.1    Mayer, K.M.2    Umeno, D.3
  • 41
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 42
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman, K.L. & Pease, L.R. Gene splicing and mutagenesis by PCR-driven overlap extension. Nat. Protoc. 2, 924-932 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 44
    • 1642414512 scopus 로고    scopus 로고
    • Staggered extension process (StEP) in vitro recombination
    • 1st edn., (eds. Arnold, F.H. & Georgiou, G.) Humana Press
    • Aguinaldo, A.M. & Arnold, F.H. Staggered extension process (StEP) in vitro recombination. In Directed Evolution Library Creation: Methods and Protocols 1st edn., Vol. 231 (eds. Arnold, F.H. & Georgiou, G.) 105-110 (Humana Press, 2003).
    • (2003) Directed Evolution Library Creation: Methods and Protocols , vol.231 , pp. 105-110
    • Aguinaldo, A.M.1    Arnold, F.H.2
  • 45
    • 34248632787 scopus 로고    scopus 로고
    • In vitro 'sexual' evolution through the PCR-based staggered extension process (StEP)
    • Zhao, H. & Zha, W. In vitro 'sexual' evolution through the PCR-based staggered extension process (StEP). Nat. Protoc. 1, 1865-1871 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1865-1871
    • Zhao, H.1    Zha, W.2
  • 48
  • 49
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E.A., Tate, E. & Stemmer, W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315-319 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 50
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M. et al. The protein data bank. Nucleic Acids Res. 28, 235-242 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 51
    • 69749106857 scopus 로고    scopus 로고
    • A rapidly maturing far-red derivative of DsRed-Express2 for whole-cell labeling
    • Strack, R.L. et al. A rapidly maturing far-red derivative of DsRed-Express2 for whole-cell labeling. Biochemistry 48, 8279-8281 (2009).
    • (2009) Biochemistry , vol.48 , pp. 8279-8281
    • Strack, R.L.1
  • 52
    • 33847088401 scopus 로고
    • Determination of absolute fluorescence quantum efficiency of quinine bisulfate in aqueous-medium by optoacoustic spectrometry
    • Adams, M.J., Highfield, J.G. & Kirkbright, G.F. Determination of absolute fluorescence quantum efficiency of quinine bisulfate in aqueous-medium by optoacoustic spectrometry. Anal. Chem. 49, 1850-1852 (1977).
    • (1977) Anal. Chem. , vol.49 , pp. 1850-1852
    • Adams, M.J.1    Highfield, J.G.2    Kirkbright, G.F.3
  • 53
    • 33947094704 scopus 로고
    • Absolute quantum yield determination by thermal blooming
    • Brannon, J.H. & Magde, D. Absolute quantum yield determination by thermal blooming. Fluorescein. J. Phys. Chem. 82, 705-709 (1978).
    • (1978) Fluorescein. J. Phys. Chem. , vol.82 , pp. 705-709
    • Brannon, J.H.1    Magde, D.2
  • 54
    • 0346599879 scopus 로고
    • Rhodamine-B and rhodamine-101 as reference substances for fluorescence quantum yield measurements
    • Karstens, T. & Kobs, K. Rhodamine-B and rhodamine-101 as reference substances for fluorescence quantum yield measurements. J. Phys. Chem. 84, 1871-1872 (1980).
    • (1980) J. Phys. Chem. , vol.84 , pp. 1871-1872
    • Karstens, T.1    Kobs, K.2
  • 55
    • 33644622698 scopus 로고    scopus 로고
    • Biochemical and physical properties of green fluorescent protein
    • 2nd edn., (eds. Chalfie, M. & Kain, S.R.) John Wiley & Sons
    • Ward, W.W. Biochemical and physical properties of green fluorescent protein. In Green Fluorescent Protein: Properties, Applications, and Protocols 2nd edn., Vol. 47 (eds. Chalfie, M. & Kain, S.R.) 39-65 (John Wiley & Sons, 2006).
    • (2006) Green Fluorescent Protein: Properties, Applications, and Protocols , vol.47 , pp. 39-65
    • Ward, W.W.1
  • 56
    • 42349096809 scopus 로고    scopus 로고
    • Hue-shifted monomeric variants of Clavularia cyan fluorescent protein: Identification of the molecular determinants of color and applications in fluorescence imaging
    • Ai, H., Olenych, S.G., Wong, P., Davidson, M.W. & Campbell, R.E. Hue-shifted monomeric variants of Clavularia cyan fluorescent protein: identification of the molecular determinants of color and applications in fluorescence imaging. BMC Biol. 6, 13 (2008).
    • (2008) BMC Biol. , vol.6 , pp. 13
    • Ai, H.1    Olenych, S.G.2    Wong, P.3    Davidson, M.W.4    Campbell, R.E.5


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