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Volumn 589, Issue , 2017, Pages 191-219

Novel Fluorescence-Based Biosensors Incorporating Unnatural Amino Acids

Author keywords

Biosensors; Fluorescence; Fluorescent proteins; Genetic code expansion; Protein engineering; Unnatural amino acids

Indexed keywords

4 BORONOPHENYLALANINE; AMINO ACID; HYDROGEN PEROXIDE; 4-BORONOPHENYLALANINE; BORON DERIVATIVE; FLUORESCENT DYE; PHENYLALANINE; PHOTOPROTEIN;

EID: 85013356507     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/bs.mie.2017.01.012     Document Type: Chapter
Times cited : (12)

References (98)
  • 2
    • 84949796862 scopus 로고    scopus 로고
    • Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids
    • Amiram, M., Haimovich, A.D., Fan, C., Wang, Y.-S., Aerni, H.-R., Ntai, I., et al. Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids. Nature Biotechnology 33 (2015), 1272–1279.
    • (2015) Nature Biotechnology , vol.33 , pp. 1272-1279
    • Amiram, M.1    Haimovich, A.D.2    Fan, C.3    Wang, Y.-S.4    Aerni, H.-R.5    Ntai, I.6
  • 4
    • 79959923783 scopus 로고    scopus 로고
    • Development of a selective, sensitive, and reversible biosensor by the genetic incorporation of a metal-binding site into green fluorescent protein
    • Ayyadurai, N., Prabhu, N.S., Deepankumar, K., Lee, S.-G., Jeong, H.-H., Lee, C.-S., et al. Development of a selective, sensitive, and reversible biosensor by the genetic incorporation of a metal-binding site into green fluorescent protein. Angewandte Chemie (International ed. in English) 50 (2011), 6534–6537.
    • (2011) Angewandte Chemie (International ed. in English) , vol.50 , pp. 6534-6537
    • Ayyadurai, N.1    Prabhu, N.S.2    Deepankumar, K.3    Lee, S.-G.4    Jeong, H.-H.5    Lee, C.-S.6
  • 8
    • 84875143731 scopus 로고    scopus 로고
    • HyPer-3: A genetically encoded H2O2 probe with improved performance for ratiometric and fluorescence lifetime imaging
    • Bilan, D.S., Pase, L., Joosen, L., Gorokhovatsky, A.Y., Ermakova, Y.G., Gadella, T.W.J., et al. HyPer-3: A genetically encoded H2O2 probe with improved performance for ratiometric and fluorescence lifetime imaging. ACS Chemical Biology 8 (2012), 535–542.
    • (2012) ACS Chemical Biology , vol.8 , pp. 535-542
    • Bilan, D.S.1    Pase, L.2    Joosen, L.3    Gorokhovatsky, A.Y.4    Ermakova, Y.G.5    Gadella, T.W.J.6
  • 10
    • 55249115067 scopus 로고    scopus 로고
    • A promiscuous aminoacyl-tRNA synthetase that incorporates cysteine, methionine, and alanine homologs into proteins
    • Brustad, E., Bushey, M.L., Brock, A., Chittuluru, J., Schultz, P.G., A promiscuous aminoacyl-tRNA synthetase that incorporates cysteine, methionine, and alanine homologs into proteins. Bioorganic and Medicinal Chemistry Letters 18 (2008), 6004–6006.
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , pp. 6004-6006
    • Brustad, E.1    Bushey, M.L.2    Brock, A.3    Chittuluru, J.4    Schultz, P.G.5
  • 11
    • 58849110330 scopus 로고    scopus 로고
    • A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer
    • Brustad, E.M., Lemke, E.A., Schultz, P.G., Deniz, A.A., A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer. Journal of the American Chemical Society 130 (2008), 17664–17665.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 17664-17665
    • Brustad, E.M.1    Lemke, E.A.2    Schultz, P.G.3    Deniz, A.A.4
  • 12
    • 0032928678 scopus 로고    scopus 로고
    • Toward the experimental codon reassignment in vivo: Protein building with an expanded amino acid repertoire
    • Budisa, N., Minks, C., Alefelder, S., Wenger, W., Dong, F., Moroder, L., et al. Toward the experimental codon reassignment in vivo: Protein building with an expanded amino acid repertoire. FASEB Journal 13 (1999), 41–51.
    • (1999) FASEB Journal , vol.13 , pp. 41-51
    • Budisa, N.1    Minks, C.2    Alefelder, S.3    Wenger, W.4    Dong, F.5    Moroder, L.6
  • 13
    • 26444492138 scopus 로고    scopus 로고
    • Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from mycobacterium tuberculosis
    • Cabantous, S., Pedelacq, J.-D., Mark, B.L., Naranjo, C., Terwilliger, T.C., Waldo, G.S., Recent advances in GFP folding reporter and split-GFP solubility reporter technologies. Application to improving the folding and solubility of recalcitrant proteins from mycobacterium tuberculosis. Journal of Structural and Functional Genomics 6 (2005), 113–119.
    • (2005) Journal of Structural and Functional Genomics , vol.6 , pp. 113-119
    • Cabantous, S.1    Pedelacq, J.-D.2    Mark, B.L.3    Naranjo, C.4    Terwilliger, T.C.5    Waldo, G.S.6
  • 14
    • 47749109536 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy
    • Cellitti, S.E., Jones, D.H., Lagpacan, L., Hao, X., Zhang, Q., Hu, H., et al. In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society 130 (2008), 9268–9281.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 9268-9281
    • Cellitti, S.E.1    Jones, D.H.2    Lagpacan, L.3    Hao, X.4    Zhang, Q.5    Hu, H.6
  • 15
    • 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 (1994), 802–805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 17
    • 84862215205 scopus 로고    scopus 로고
    • Reaction-based genetically encoded fluorescent hydrogen sulfide sensors
    • Chen, S., Chen, Z.-J., Ren, W., Ai, H.-W., Reaction-based genetically encoded fluorescent hydrogen sulfide sensors. Journal of the American Chemical Society 134 (2012), 9589–9592.
    • (2012) Journal of the American Chemical Society , vol.134 , pp. 9589-9592
    • Chen, S.1    Chen, Z.-J.2    Ren, W.3    Ai, H.-W.4
  • 18
    • 84885584704 scopus 로고    scopus 로고
    • Genetically encoded fluorescent probe for the selective detection of peroxynitrite
    • Chen, Z.-J., Ren, W., Wright, Q.E., Ai, H.-W., Genetically encoded fluorescent probe for the selective detection of peroxynitrite. Journal of the American Chemical Society 135 (2013), 14940–14943.
    • (2013) Journal of the American Chemical Society , vol.135 , pp. 14940-14943
    • Chen, Z.-J.1    Ren, W.2    Wright, Q.E.3    Ai, H.-W.4
  • 19
    • 84908621581 scopus 로고    scopus 로고
    • Genetically encoding an electrophilic amino acid for protein stapling and covalent binding to native receptors
    • Chen, X.-H., Xiang, Z., Hu, Y.S., Lacey, V.K., Cang, H., Wang, L., Genetically encoding an electrophilic amino acid for protein stapling and covalent binding to native receptors. ACS Chemical Biology 9 (2014), 1956–1961.
    • (2014) ACS Chemical Biology , vol.9 , pp. 1956-1961
    • Chen, X.-H.1    Xiang, Z.2    Hu, Y.S.3    Lacey, V.K.4    Cang, H.5    Wang, L.6
  • 20
    • 84988044440 scopus 로고    scopus 로고
    • Super-resolution microscopy: Breaking the limits
    • Chi, K.R., Super-resolution microscopy: Breaking the limits. Nature Methods 6 (2009), 15–18.
    • (2009) Nature Methods , vol.6 , pp. 15-18
    • Chi, K.R.1
  • 22
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • Chudakov, D.M., Matz, M.V., Lukyanov, S., Lukyanov, K.A., Fluorescent proteins and their applications in imaging living cells and tissues. Physiological Reviews 90 (2010), 1103–1163.
    • (2010) Physiological Reviews , vol.90 , pp. 1103-1163
    • Chudakov, D.M.1    Matz, M.V.2    Lukyanov, S.3    Lukyanov, K.A.4
  • 24
    • 0037157082 scopus 로고    scopus 로고
    • A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins
    • Datta, D., Wang, P., Carrico, I.S., Mayo, S.L., Tirrell, D.A., A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins. Journal of the American Chemical Society 124 (2002), 5652–5653.
    • (2002) Journal of the American Chemical Society , vol.124 , pp. 5652-5653
    • Datta, D.1    Wang, P.2    Carrico, I.S.3    Mayo, S.L.4    Tirrell, D.A.5
  • 26
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu, J.M., Tanner, K.G., Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998), 5633–5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 27
    • 0035917804 scopus 로고    scopus 로고
    • Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway
    • Döring, V., Mootz, H.D., Nangle, L.A., Hendrickson, T.L., de Crécy-Lagard, V., Schimmel, P., et al. Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway. Science 292 (2001), 501–504.
    • (2001) Science , vol.292 , pp. 501-504
    • Döring, V.1    Mootz, H.D.2    Nangle, L.A.3    Hendrickson, T.L.4    de Crécy-Lagard, V.5    Schimmel, P.6
  • 28
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty, D.A., Unnatural amino acids as probes of protein structure and function. Current Opinion in Chemical Biology 4 (2000), 645–652.
    • (2000) Current Opinion in Chemical Biology , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 29
    • 70349331596 scopus 로고    scopus 로고
    • Genetically encoded biosensors based on engineered fluorescent proteins
    • Frommer, W.B., Davidson, M.W., Campbell, R.E., Genetically encoded biosensors based on engineered fluorescent proteins. Chemical Society Reviews 38 (2009), 2833–2841.
    • (2009) Chemical Society Reviews , vol.38 , pp. 2833-2841
    • Frommer, W.B.1    Davidson, M.W.2    Campbell, R.E.3
  • 30
    • 70349786384 scopus 로고    scopus 로고
    • Efforts toward the direct experimental characterization of enzyme microenvironments: Tyrosine100 in dihydrofolate reductase
    • S3478/3471-S3478/3475
    • Groff, D., Thielges, M.C., Cellitti, S., Schultz, P.G., Romesberg, F.E., Efforts toward the direct experimental characterization of enzyme microenvironments: Tyrosine100 in dihydrofolate reductase. Angewandte Chemie (International ed. in English) 48 (2009), 3478–3481 S3478/3471-S3478/3475.
    • (2009) Angewandte Chemie (International ed. in English) , vol.48 , pp. 3478-3481
    • Groff, D.1    Thielges, M.C.2    Cellitti, S.3    Schultz, P.G.4    Romesberg, F.E.5
  • 32
    • 70449597245 scopus 로고    scopus 로고
    • Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
    • S9148/9141-S9148/9123
    • Guo, J., Melancon, C.E. III, Lee, H.S., Groff, D., Schultz, P.G., Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids. Angewandte Chemie (International ed. in English) 48 (2009), 9148–9151 S9148/9141-S9148/9123.
    • (2009) Angewandte Chemie (International ed. in English) , vol.48 , pp. 9148-9151
    • Guo, J.1    Melancon, C.E.2    Lee, H.S.3    Groff, D.4    Schultz, P.G.5
  • 33
    • 52049083084 scopus 로고    scopus 로고
    • Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins
    • Guo, J., Wang, J., Lee, J.S., Schultz, P.G., Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins. Angewandte Chemie (International ed. in English) 47 (2008), 6399–6401.
    • (2008) Angewandte Chemie (International ed. in English) , vol.47 , pp. 6399-6401
    • Guo, J.1    Wang, J.2    Lee, J.S.3    Schultz, P.G.4
  • 35
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • Hanson, G.T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R.A., Tsien, R.Y., et al. Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. Journal of Biological Chemistry 279 (2004), 13044–13053.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6
  • 36
    • 0036900746 scopus 로고    scopus 로고
    • Incorporation of non-natural amino acids into proteins
    • Hohsaka, T., Sisido, M., Incorporation of non-natural amino acids into proteins. Current Opinion in Chemical Biology 6 (2002), 809–815.
    • (2002) Current Opinion in Chemical Biology , vol.6 , pp. 809-815
    • Hohsaka, T.1    Sisido, M.2
  • 37
    • 0023851252 scopus 로고
    • Tyrosine sulfation and the secretory pathway
    • Huttner, W.B., Tyrosine sulfation and the secretory pathway. Annual Review of Physiology 50 (1988), 363–376.
    • (1988) Annual Review of Physiology , vol.50 , pp. 363-376
    • Huttner, W.B.1
  • 38
    • 33846809165 scopus 로고    scopus 로고
    • Site-specific incorporation of a 19F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity
    • Jackson, J.C., Hammill, J.T., Mehl, R.A., Site-specific incorporation of a 19F-amino acid into proteins as an NMR probe for characterizing protein structure and reactivity. Journal of the American Chemical Society 129 (2007), 1160–1166.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 1160-1166
    • Jackson, J.C.1    Hammill, J.T.2    Mehl, R.A.3
  • 40
    • 84878712129 scopus 로고    scopus 로고
    • Molecular recognition of sulfotyrosine and phosphotyrosine by the Src homology 2 domain
    • Ju, T., Niu, W., Cerny, R., Bollman, J., Roy, A., Guo, J., Molecular recognition of sulfotyrosine and phosphotyrosine by the Src homology 2 domain. Molecular BioSystems 9 (2013), 1829–1832.
    • (2013) Molecular BioSystems , vol.9 , pp. 1829-1832
    • Ju, T.1    Niu, W.2    Cerny, R.3    Bollman, J.4    Roy, A.5    Guo, J.6
  • 41
    • 84987804397 scopus 로고    scopus 로고
    • Evolution of Src homology 2 (SH2) domain to recognize sulfotyrosine
    • Ju, T., Niu, W., Guo, J., Evolution of Src homology 2 (SH2) domain to recognize sulfotyrosine. ACS Chemical Biology 11 (2016), 2551–2557.
    • (2016) ACS Chemical Biology , vol.11 , pp. 2551-2557
    • Ju, T.1    Niu, W.2    Guo, J.3
  • 43
    • 84857445877 scopus 로고    scopus 로고
    • Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction
    • Lang, K., Davis, L., Torres-Kolbus, J., Chou, C., Deiters, A., Chin, J.W., Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction. Nature Chemistry 4 (2012), 298–304.
    • (2012) Nature Chemistry , vol.4 , pp. 298-304
    • Lang, K.1    Davis, L.2    Torres-Kolbus, J.3    Chou, C.4    Deiters, A.5    Chin, J.W.6
  • 44
    • 84863443015 scopus 로고    scopus 로고
    • Genetic encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-alder reactions
    • Lang, K., Davis, L., Wallace, S., Mahesh, M., Cox, D.J., Blackman, M.L., et al. Genetic encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-alder reactions. Journal of the American Chemical Society 134 (2012), 10317–10320.
    • (2012) Journal of the American Chemical Society , vol.134 , pp. 10317-10320
    • Lang, K.1    Davis, L.2    Wallace, S.3    Mahesh, M.4    Cox, D.J.5    Blackman, M.L.6
  • 45
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee, S.-R., Kwon, K.-S., Kim, S.-R., Rhee, S.G., Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. Journal of Biological Chemistry 273 (1998), 15366–15372.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 15366-15372
    • Lee, S.-R.1    Kwon, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 46
    • 67749129324 scopus 로고    scopus 로고
    • Genetic incorporation of a metal-ion chelating amino acid into proteins as a biophysical probe
    • Lee, H.S., Spraggon, G., Schultz, P.G., Wang, F., Genetic incorporation of a metal-ion chelating amino acid into proteins as a biophysical probe. Journal of the American Chemical Society 131 (2009), 2481–2483.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 2481-2483
    • Lee, H.S.1    Spraggon, G.2    Schultz, P.G.3    Wang, F.4
  • 47
    • 80053049200 scopus 로고    scopus 로고
    • Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems
    • Lippert, A.R., Van de Bittner, G.C., Chang, C.J., Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems. Accounts of Chemical Research 44 (2011), 793–804.
    • (2011) Accounts of Chemical Research , vol.44 , pp. 793-804
    • Lippert, A.R.1    Van de Bittner, G.C.2    Chang, C.J.3
  • 49
    • 84876520437 scopus 로고    scopus 로고
    • Significant expansion of the fluorescent protein chromophore through the genetic incorporation of a metal-chelating unnatural amino acid
    • Liu, X., Li, J., Hu, C., Zhou, Q., Zhang, W., Hu, M., et al. Significant expansion of the fluorescent protein chromophore through the genetic incorporation of a metal-chelating unnatural amino acid. Angewandte Chemie (International ed. in English) 52 (2013), 4805–4809.
    • (2013) Angewandte Chemie (International ed. in English) , vol.52 , pp. 4805-4809
    • Liu, X.1    Li, J.2    Hu, C.3    Zhou, Q.4    Zhang, W.5    Hu, M.6
  • 50
    • 33750865963 scopus 로고    scopus 로고
    • Recombinant expression of selectively sulfated proteins in Escherichia coli
    • Liu, C.C., Schultz, P.G., Recombinant expression of selectively sulfated proteins in Escherichia coli. Nature Biotechnology 24 (2006), 1436–1440.
    • (2006) Nature Biotechnology , vol.24 , pp. 1436-1440
    • Liu, C.C.1    Schultz, P.G.2
  • 51
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C.C., Schultz, P.G., Adding new chemistries to the genetic code. Annual Review of Biochemistry 79 (2010), 413–444.
    • (2010) Annual Review of Biochemistry , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 52
    • 84860204636 scopus 로고    scopus 로고
    • Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase
    • Liu, X., Yu, Y., Hu, C., Zhang, W., Lu, Y., Wang, J., Significant increase of oxidase activity through the genetic incorporation of a tyrosine-histidine cross-link in a myoglobin model of heme-copper oxidase. Angewandte Chemie (International ed. in English) 51 (2012), 4312–4316.
    • (2012) Angewandte Chemie (International ed. in English) , vol.51 , pp. 4312-4316
    • Liu, X.1    Yu, Y.2    Hu, C.3    Zhang, W.4    Lu, Y.5    Wang, J.6
  • 53
    • 44849120336 scopus 로고    scopus 로고
    • Genetically encoded calcium indicators
    • Mank, M., Griesbeck, O., Genetically encoded calcium indicators. Chemical Reviews 108 (2008), 1550–1564.
    • (2008) Chemical Reviews , vol.108 , pp. 1550-1564
    • Mank, M.1    Griesbeck, O.2
  • 56
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2 + based on green fluorescent proteins and calmodulin
    • Miyawaki, A., Llopis, J., Heim, R., McCaffery, J.M., Adams, J.A., Ikura, M., et al. Fluorescent indicators for Ca2 + based on green fluorescent proteins and calmodulin. Nature 388 (1997), 882–887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6
  • 59
    • 77949772551 scopus 로고    scopus 로고
    • Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome
    • Neumann, H., Wang, K., Davis, L., Garcia-Alai, M., Chin, J.W., Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome. Nature 464 (2010), 441–444.
    • (2010) Nature , vol.464 , pp. 441-444
    • Neumann, H.1    Wang, K.2    Davis, L.3    Garcia-Alai, M.4    Chin, J.W.5
  • 60
    • 79955894911 scopus 로고    scopus 로고
    • Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells
    • Newman, R.H., Fosbrink, M.D., Zhang, J., Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells. Chemical Reviews 111 (2011), 3614–3666.
    • (2011) Chemical Reviews , vol.111 , pp. 3614-3666
    • Newman, R.H.1    Fosbrink, M.D.2    Zhang, J.3
  • 61
    • 84887075652 scopus 로고    scopus 로고
    • Expanding the chemistry of fluorescent protein biosensors through genetic incorporation of unnatural amino acids
    • Niu, W., Guo, J., Expanding the chemistry of fluorescent protein biosensors through genetic incorporation of unnatural amino acids. Molecular BioSystems 9 (2013), 2961–2970.
    • (2013) Molecular BioSystems , vol.9 , pp. 2961-2970
    • Niu, W.1    Guo, J.2
  • 62
    • 84880555518 scopus 로고    scopus 로고
    • An expanded genetic code in mammalian cells with a functional quadruplet codon
    • Niu, W., Schultz, P.G., Guo, J., An expanded genetic code in mammalian cells with a functional quadruplet codon. ACS Chemical Biology 8 (2013), 1640–1645.
    • (2013) ACS Chemical Biology , vol.8 , pp. 1640-1645
    • Niu, W.1    Schultz, P.G.2    Guo, J.3
  • 63
    • 3543095148 scopus 로고    scopus 로고
    • Monitoring disulfide bond formation in the eukaryotic cytosol
    • Ostergaard, H., Tachibana, C., Winther, J.R., Monitoring disulfide bond formation in the eukaryotic cytosol. Journal of Cell Biology 166 (2004), 337–345.
    • (2004) Journal of Cell Biology , vol.166 , pp. 337-345
    • Ostergaard, H.1    Tachibana, C.2    Winther, J.R.3
  • 64
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen, C.E., Carroll, K.S., Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chemical Biology 5 (2010), 47–62.
    • (2010) ACS Chemical Biology , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 65
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling-mediated cysteine oxidation
    • Poole, L.B., Nelson, K.J., Discovering mechanisms of signaling-mediated cysteine oxidation. Current Opinion in Chemical Biology 12 (2008), 18–24.
    • (2008) Current Opinion in Chemical Biology , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 66
    • 52249104161 scopus 로고    scopus 로고
    • Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants
    • Pouwels, L.J., Zhang, L., Chan, N.H., Dorrestein, P.C., Wachter, R.M., Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants. Biochemistry 47 (2008), 10111–10122.
    • (2008) Biochemistry , vol.47 , pp. 10111-10122
    • Pouwels, L.J.1    Zhang, L.2    Chan, N.H.3    Dorrestein, P.C.4    Wachter, R.M.5
  • 67
    • 85015460086 scopus 로고
    • Proton nuclear magnetic resonance and fluorescence spectroscopic studies of segmental mobility in aequorin and a green fluorescent protein from aequorea forskalea
    • Rao, B.D., Kemple, M.D., Prendergast, F.G., Proton nuclear magnetic resonance and fluorescence spectroscopic studies of segmental mobility in aequorin and a green fluorescent protein from aequorea forskalea. Biophysical Journal 32 (1980), 630–632.
    • (1980) Biophysical Journal , vol.32 , pp. 630-632
    • Rao, B.D.1    Kemple, M.D.2    Prendergast, F.G.3
  • 68
    • 33745631769 scopus 로고    scopus 로고
    • Cell signaling. H2O2, a necessary evil for cell signaling
    • Rhee, S.G., Cell signaling. H2O2, a necessary evil for cell signaling. Science 312 (2006), 1882–1883.
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 71
    • 0037432318 scopus 로고    scopus 로고
    • Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution
    • Seifert, M.H.J., Georgescu, J., Ksiazek, D., Smialowski, P., Rehm, T., Steipe, B., et al. Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution. Biochemistry 42 (2003), 2500–2512.
    • (2003) Biochemistry , vol.42 , pp. 2500-2512
    • Seifert, M.H.J.1    Georgescu, J.2    Ksiazek, D.3    Smialowski, P.4    Rehm, T.5    Steipe, B.6
  • 72
    • 36849004028 scopus 로고    scopus 로고
    • Site-specific insertion of 3-aminotyrosine into subunit α2 of E. Coli ribonucleotide reductase: Direct evidence for involvement of Y730 and Y731 in radical propagation
    • Seyedsayamdost, M.R., Xie, J., Chan, C.T.Y., Schultz, P.G., Stubbe, J., Site-specific insertion of 3-aminotyrosine into subunit α2 of E. Coli ribonucleotide reductase: Direct evidence for involvement of Y730 and Y731 in radical propagation. Journal of the American Chemical Society 129 (2007), 15060–15071.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 15060-15071
    • Seyedsayamdost, M.R.1    Xie, J.2    Chan, C.T.Y.3    Schultz, P.G.4    Stubbe, J.5
  • 73
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N.C., Campbell, R.E., Steinbach, P.A., Giepmans, B.N.G., Palmer, A.E., Tsien, R.Y., Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nature Biotechnology 22 (2004), 1567–1572.
    • (2004) Nature Biotechnology , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.G.4    Palmer, A.E.5    Tsien, R.Y.6
  • 74
    • 85011074005 scopus 로고    scopus 로고
    • Fluorogenic protein labeling using a genetically encoded unstrained alkene
    • Shang, X., Song, X., Faller, C., Lai, R., Li, H., Cerny, R., et al. Fluorogenic protein labeling using a genetically encoded unstrained alkene. Chemical Science 8 (2017), 1141–1145, 10.1039/C1036SC03635J.
    • (2017) Chemical Science , vol.8 , pp. 1141-1145
    • Shang, X.1    Song, X.2    Faller, C.3    Lai, R.4    Li, H.5    Cerny, R.6
  • 76
    • 42249110717 scopus 로고    scopus 로고
    • A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins
    • Song, W., Wang, Y., Qu, J., Madden, M.M., Lin, Q., A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins. Angewandte Chemie (International ed. in English) 47 (2008), 2832–2835.
    • (2008) Angewandte Chemie (International ed. in English) , vol.47 , pp. 2832-2835
    • Song, W.1    Wang, Y.2    Qu, J.3    Madden, M.M.4    Lin, Q.5
  • 77
    • 67349111690 scopus 로고    scopus 로고
    • Tyrosine sulfation: An increasingly recognized post-translational modification of secreted proteins
    • Stone, M.J., Chuang, S., Hou, X., Shoham, M., Zhu, J.Z., Tyrosine sulfation: An increasingly recognized post-translational modification of secreted proteins. New Biotechnology 25 (2009), 299–317.
    • (2009) New Biotechnology , vol.25 , pp. 299-317
    • Stone, M.J.1    Chuang, S.2    Hou, X.3    Shoham, M.4    Zhu, J.Z.5
  • 78
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • Stone, J.R., Yang, S., Hydrogen peroxide: A signaling messenger. Antioxidants & Redox Signaling 8 (2006), 243–270.
    • (2006) Antioxidants & Redox Signaling , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 79
    • 33644890438 scopus 로고    scopus 로고
    • Expanding the genetic code in a mammalian cell line by the introduction of four-base codon/anticodon pairs
    • Taki, M., Matsushita, J., Sisido, M., Expanding the genetic code in a mammalian cell line by the introduction of four-base codon/anticodon pairs. Chembiochem: A European Journal of Chemical Biology 7 (2006), 425–428.
    • (2006) Chembiochem: A European Journal of Chemical Biology , vol.7 , pp. 425-428
    • Taki, M.1    Matsushita, J.2    Sisido, M.3
  • 80
    • 34249020137 scopus 로고    scopus 로고
    • A genetically encoded metallocene containing amino acid
    • Tippmann, E.M., Schultz, P.G., A genetically encoded metallocene containing amino acid. Tetrahedron 63 (2007), 6182–6184.
    • (2007) Tetrahedron , vol.63 , pp. 6182-6184
    • Tippmann, E.M.1    Schultz, P.G.2
  • 81
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y., The green fluorescent protein. Annual Review of Biochemistry 67 (1998), 509–544.
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 82
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Veal, E.A., Day, A.M., Morgan, B.A., Hydrogen peroxide sensing and signaling. Molecular Cell 26 (2007), 1–14.
    • (2007) Molecular Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 83
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Verkhusha, V.V., Lukyanov, K.A., The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nature Biotechnology 22 (2004), 289–296.
    • (2004) Nature Biotechnology , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 84
    • 84925606144 scopus 로고    scopus 로고
    • Fine-tuning interaction between aminoacyl-tRNA synthetase and tRNA for efficient synthesis of proteins containing unnatural amino acids
    • Wang, N., Ju, T., Niu, W., Guo, J., Fine-tuning interaction between aminoacyl-tRNA synthetase and tRNA for efficient synthesis of proteins containing unnatural amino acids. ACS Synthetic Biology 4 (2015), 207–212.
    • (2015) ACS Synthetic Biology , vol.4 , pp. 207-212
    • Wang, N.1    Ju, T.2    Niu, W.3    Guo, J.4
  • 85
    • 71049131212 scopus 로고    scopus 로고
    • Recent progress in strategies for the creation of protein-based fluorescent biosensors
    • Wang, H., Nakata, E., Hamachi, I., Recent progress in strategies for the creation of protein-based fluorescent biosensors. Chembiochem: A European Journal of Chemical Biology 10 (2009), 2560–2577.
    • (2009) Chembiochem: A European Journal of Chemical Biology , vol.10 , pp. 2560-2577
    • Wang, H.1    Nakata, E.2    Hamachi, I.3
  • 87
    • 84899055551 scopus 로고    scopus 로고
    • Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labeling and FRET
    • Wang, K., Sachdeva, A., Cox, D.J., Wilf, N.M., Lang, K., Wallace, S., et al. Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labeling and FRET. Nature Chemistry 6 (2014), 393–403.
    • (2014) Nature Chemistry , vol.6 , pp. 393-403
    • Wang, K.1    Sachdeva, A.2    Cox, D.J.3    Wilf, N.M.4    Lang, K.5    Wallace, S.6
  • 88
    • 84959239211 scopus 로고    scopus 로고
    • Systematic evolution and study of UAGN decoding tRNAs in a genomically recoded bacteria
    • Wang, N., Shang, X., Cerny, R., Niu, W., Guo, J., Systematic evolution and study of UAGN decoding tRNAs in a genomically recoded bacteria. Scientific Reports, 6, 2016, 21898.
    • (2016) Scientific Reports , vol.6 , pp. 21898
    • Wang, N.1    Shang, X.2    Cerny, R.3    Niu, W.4    Guo, J.5
  • 89
  • 94
    • 34548602702 scopus 로고    scopus 로고
    • A genetically encoded metabolically stable analog of phosphotyrosine in Escherichia coli
    • Xie, J., Supekova, L., Schultz, P.G., A genetically encoded metabolically stable analog of phosphotyrosine in Escherichia coli. ACS Chemical Biology 2 (2007), 474–478.
    • (2007) ACS Chemical Biology , vol.2 , pp. 474-478
    • Xie, J.1    Supekova, L.2    Schultz, P.G.3
  • 95
    • 38349107042 scopus 로고    scopus 로고
    • Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis
    • Ye, S., Koehrer, C., Huber, T., Kazmi, M., Sachdev, P., Yan, E.C.Y., et al. Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis. Journal of Biological Chemistry 283 (2008), 1525–1533.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 1525-1533
    • Ye, S.1    Koehrer, C.2    Huber, T.3    Kazmi, M.4    Sachdev, P.5    Yan, E.C.Y.6
  • 98
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer, M., Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior. Chemical Reviews 102 (2002), 759–781.
    • (2002) Chemical Reviews , vol.102 , pp. 759-781
    • Zimmer, M.1


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