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Volumn 23, Issue 3, 2008, Pages 131-141

Selective labeling of proteins with chemical probes in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FLUORESCENT DYE; LIGAND; PROTEIN;

EID: 49049095153     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00007.2008     Document Type: Review
Times cited : (65)

References (86)
  • 1
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams S, Campbell R, Gross L, Martin B, Walkup G, Yao Y, Llopis J, Tsien R. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 124: 6063-6076, 2002.
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.1    Campbell, R.2    Gross, L.3    Martin, B.4    Walkup, G.5    Yao, Y.6    Llopis, J.7    Tsien, R.8
  • 2
    • 9444247617 scopus 로고    scopus 로고
    • Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging
    • Andresen M, Schmitz-Salue R, Jakobs S. Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging. Mol Biol Cell 15: 5616-5622, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 5616-5622
    • Andresen, M.1    Schmitz-Salue, R.2    Jakobs, S.3
  • 4
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz P. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci 8: 921-929, 1999.
    • (1999) Protein Sci , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.3
  • 6
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym RA, Thompson RB, Stoddard AK, Fierke CA. Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor. ACS Chem Biol 1: 103-111, 2006.
    • (2006) ACS Chem Biol , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 7
    • 34250877975 scopus 로고    scopus 로고
    • Optimized fluorescent trimethoprim derivatives for in vivo protein labeling
    • Calloway N, Choob M, Sanz A, Sheetz M, Miller L, Cornish V. Optimized fluorescent trimethoprim derivatives for in vivo protein labeling. Chembiochem 8: 767-774, 2007.
    • (2007) Chembiochem , vol.8 , pp. 767-774
    • Calloway, N.1    Choob, M.2    Sanz, A.3    Sheetz, M.4    Miller, L.5    Cornish, V.6
  • 8
    • 34548457794 scopus 로고    scopus 로고
    • A red cy3-based biarsenical fluorescent probe targeted to a complementary binding peptide
    • Cao H, Xiong Y, Wang T, Chen B, Squier TC, Mayer MU. A red cy3-based biarsenical fluorescent probe targeted to a complementary binding peptide. J Am Chem Soc 129: 8672-8673, 2007.
    • (2007) J Am Chem Soc , vol.129 , pp. 8672-8673
    • Cao, H.1    Xiong, Y.2    Wang, T.3    Chen, B.4    Squier, T.C.5    Mayer, M.U.6
  • 9
    • 34248993985 scopus 로고    scopus 로고
    • Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins
    • Chen I, Choi YA, Ting AY. Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins. J Am Chem Soc 129: 6619-6625, 2007.
    • (2007) J Am Chem Soc , vol.129 , pp. 6619-6625
    • Chen, I.1    Choi, Y.A.2    Ting, A.Y.3
  • 11
    • 0029108642 scopus 로고    scopus 로고
    • Cornish VW, Mendel D, Schultz Probing protein structure and runction with an expanded genetic code. Angewandte Chemie Int Ed English 34: 621-633, 1995.
    • Cornish VW, Mendel D, Schultz PG. Probing protein structure and runction with an expanded genetic code. Angewandte Chemie Int Ed English 34: 621-633, 1995.
  • 12
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • Cull M, Schatz P. Biotinylation of proteins in vivo and in vitro using small peptide tags. Methods Enzymol 326: 430-440, 2000.
    • (2000) Methods Enzymol , vol.326 , pp. 430-440
    • Cull, M.1    Schatz, P.2
  • 13
    • 0034599723 scopus 로고    scopus 로고
    • Active and alkylated human AGT structures: A novel zinc site, inhibitor and extrahelical base binding
    • Daniels D, Mol C, Arvai A, Kanugula S, Pegg A, Tainer J. Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding. EMBO J 19: 1719-1730, 2000.
    • (2000) EMBO J , vol.19 , pp. 1719-1730
    • Daniels, D.1    Mol, C.2    Arvai, A.3    Kanugula, S.4    Pegg, A.5    Tainer, J.6
  • 14
  • 16
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty DA. Unnatural amino acids as probes of protein structure and function. Curr Opin Chem Biol 4: 645-652, 2000.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 17
    • 33846333918 scopus 로고    scopus 로고
    • Selective labeling of proteins by using protein farnesyltransferase
    • Duckworth BP, Zhang Z, Hosokawa A, Distefano MD. Selective labeling of proteins by using protein farnesyltransferase. Chembiochem 8: 98-105, 2007.
    • (2007) Chembiochem , vol.8 , pp. 98-105
    • Duckworth, B.P.1    Zhang, Z.2    Hosokawa, A.3    Distefano, M.D.4
  • 18
    • 0033583073 scopus 로고    scopus 로고
    • Receptor-mediated targeting of fluorescent probes in living cells
    • Farinas J, Verkman A. Receptor-mediated targeting of fluorescent probes in living cells. J Biol Chem 274: 7603-7606, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 7603-7606
    • Farinas, J.1    Verkman, A.2
  • 20
    • 0037419375 scopus 로고    scopus 로고
    • Lanthanide-binding tags as versatile protein coexpression probes
    • Franz K, Nitz M, Imperiali B. Lanthanide-binding tags as versatile protein coexpression probes. Chembiochem 4: 265-271, 2003.
    • (2003) Chembiochem , vol.4 , pp. 265-271
    • Franz, K.1    Nitz, M.2    Imperiali, B.3
  • 22
    • 0037774580 scopus 로고    scopus 로고
    • Protein semi-synthesis in living cells
    • Giriat I, Muir TW. Protein semi-synthesis in living cells. J Am Chem Soc 125: 7180-7181, 2003.
    • (2003) J Am Chem Soc , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 23
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B, Adams S, Jones J, Tsien R. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol 327: 565-578, 2000.
    • (2000) Methods Enzymol , vol.327 , pp. 565-578
    • Griffin, B.1    Adams, S.2    Jones, J.3    Tsien, R.4
  • 24
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B, Adams S, Tsien R. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281: 269-272, 1998.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.1    Adams, S.2    Tsien, R.3
  • 25
    • 33745712857 scopus 로고    scopus 로고
    • Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling
    • Gronemeyer T, Chidley C, Juillerat A, Heinis C, Johnsson K. Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling. Protein Eng Des Sel 19: 309-316, 2006.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 309-316
    • Gronemeyer, T.1    Chidley, C.2    Juillerat, A.3    Heinis, C.4    Johnsson, K.5
  • 26
    • 34247247126 scopus 로고    scopus 로고
    • 2+-dye label reveals STIM1 surface exposure
    • 2+-dye label reveals STIM1 surface exposure. Proc Natl Acad Sci USA 104: 3693-3697, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3693-3697
    • Hauser, C.1    Tsien, R.2
  • 28
    • 19644391139 scopus 로고    scopus 로고
    • Targeting quantum dots to surface proteins in living cells with biotin ligase
    • Howarth M, Takao K, Hayashi Y, Ting A. Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc Natl Acad Sci USA 102: 7583-7588, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7583-7588
    • Howarth, M.1    Takao, K.2    Hayashi, Y.3    Ting, A.4
  • 29
    • 0027230113 scopus 로고
    • Dexamethasone negatively regulates the activity of a chimeric dihydrofolate reductase/glucocorticoid receptor protein
    • Israel D, Kaufman R. Dexamethasone negatively regulates the activity of a chimeric dihydrofolate reductase/glucocorticoid receptor protein. Proc Natl Acad Sci USA 90: 4290-4294, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4290-4294
    • Israel, D.1    Kaufman, R.2
  • 30
    • 33749243938 scopus 로고    scopus 로고
    • Visualizing odorant receptor trafficking in living cells down to the single-molecule level
    • Jacquier V, Prummer M, Segura JM, Pick H, Vogel H. Visualizing odorant receptor trafficking in living cells down to the single-molecule level. Proc Natl Acad Sci USA 103: 14325-14330, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14325-14330
    • Jacquier, V.1    Prummer, M.2    Segura, J.M.3    Pick, H.4    Vogel, H.5
  • 31
    • 33947274529 scopus 로고    scopus 로고
    • Propagation of centromeric chromatin requires exit from mitosis
    • Jansen LE, Black BE, Foltz DR, Cleveland DW. Propagation of centromeric chromatin requires exit from mitosis. J Cell Biol 176: 795-805, 2007.
    • (2007) J Cell Biol , vol.176 , pp. 795-805
    • Jansen, L.E.1    Black, B.E.2    Foltz, D.R.3    Cleveland, D.W.4
  • 32
    • 1542315410 scopus 로고    scopus 로고
    • Labeling of fusion proteins of O6-alkylguanine-DNA alkyltransferase with small molecules in vivo and in vitro
    • Keppler A, Kindermann M, Gendreizig S, Pick H, Vogel H, Johnsson K. Labeling of fusion proteins of O6-alkylguanine-DNA alkyltransferase with small molecules in vivo and in vitro. Methods 32: 437-444, 2004.
    • (2004) Methods , vol.32 , pp. 437-444
    • Keppler, A.1    Kindermann, M.2    Gendreizig, S.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 35
    • 33646872862 scopus 로고    scopus 로고
    • Accumulation of FlAsH/Lumio Green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins
    • Langhorst MF, Genisyuerek S, Stuermer CA. Accumulation of FlAsH/Lumio Green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins. Histochem Cell Biol 125: 743-747, 2006.
    • (2006) Histochem Cell Biol , vol.125 , pp. 743-747
    • Langhorst, M.F.1    Genisyuerek, S.2    Stuermer, C.A.3
  • 37
    • 33646038598 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells
    • Lin C, Ting A. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J Am Chem Soc 128: 4542-4543, 2006.
    • (2006) J Am Chem Soc , vol.128 , pp. 4542-4543
    • Lin, C.1    Ting, A.2
  • 38
    • 35349022538 scopus 로고    scopus 로고
    • Label transfer chemistry for the characterization of protein-protein interactions
    • Liu B, Archer C, Burdine L, Gillette T, Kodadek T. Label transfer chemistry for the characterization of protein-protein interactions. J Am Chem Soc 129: 12348-12349, 2007.
    • (2007) J Am Chem Soc , vol.129 , pp. 12348-12349
    • Liu, B.1    Archer, C.2    Burdine, L.3    Gillette, T.4    Kodadek, T.5
  • 39
    • 34447272975 scopus 로고    scopus 로고
    • The HaloTag: A novel technology for cell imaging and protein analysis
    • Los G, Wood K. The HaloTag: a novel technology for cell imaging and protein analysis. Methods Mol Biol 356: 195-208, 2007.
    • (2007) Methods Mol Biol , vol.356 , pp. 195-208
    • Los, G.1    Wood, K.2
  • 40
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • Lummis SC, Beene DL, Lee LW, Lester HA, Broadhurst RW, Dougherty DA. Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel. Nature 438: 248-252, 2005.
    • (2005) Nature , vol.438 , pp. 248-252
    • Lummis, S.C.1    Beene, D.L.2    Lee, L.W.3    Lester, H.A.4    Broadhurst, R.W.5    Dougherty, D.A.6
  • 42
    • 0037028010 scopus 로고    scopus 로고
    • Transgenically encoded protein photoinactivation (FlAsH-FALI): Acute inactivation of synaptotagmin I
    • Marek K, Davis G. Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I. Neuron 36: 805-813, 2002.
    • (2002) Neuron , vol.36 , pp. 805-813
    • Marek, K.1    Davis, G.2
  • 43
    • 3042793777 scopus 로고    scopus 로고
    • A general approach for chemical labeling and rapid, spatially controlled protein inactivation
    • Marks K, Braun P, Nolan G. A general approach for chemical labeling and rapid, spatially controlled protein inactivation. Proc Natl Acad Sci USA 101: 9982-9987, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9982-9987
    • Marks, K.1    Braun, P.2    Nolan, G.3
  • 44
    • 3042826388 scopus 로고    scopus 로고
    • In vivo targeting of organic calcium sensors via genetically selected peptides
    • Marks K, Rosinov M, Nolan G. In vivo targeting of organic calcium sensors via genetically selected peptides. Chem Biol 11: 347-356, 2004.
    • (2004) Chem Biol , vol.11 , pp. 347-356
    • Marks, K.1    Rosinov, M.2    Nolan, G.3
  • 45
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin B, Giepmans B, Adams S, Tsien R. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat Biotechnol 23: 1308-1314, 2005.
    • (2005) Nat Biotechnol , vol.23 , pp. 1308-1314
    • Martin, B.1    Giepmans, B.2    Adams, S.3    Tsien, R.4
  • 46
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer BH, Segura JM, Martinez KL, Hovius R, George N, Johnsson K, Vogel H. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc Natl Acad Sci USA 103: 2138-2143, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.M.2    Martinez, K.L.3    Hovius, R.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 47
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir TW, Sondhi D, Cole PA. Expressed protein ligation: a general method for protein engineering. Proc Natl Acad Sci USA 95: 6705-6710, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 48
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • Muralidharan V, Muir TW. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat Methods 3: 429-438, 2006.
    • (2006) Nat Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 49
    • 33751251344 scopus 로고    scopus 로고
    • Influence of protein transduction domains on intracellular delivery of macromolecules
    • Murriel CL, Dowdy SF. Influence of protein transduction domains on intracellular delivery of macromolecules. Expert Opin Drug Deliv 3: 739-746, 2006.
    • (2006) Expert Opin Drug Deliv , vol.3 , pp. 739-746
    • Murriel, C.L.1    Dowdy, S.F.2
  • 51
    • 37549061836 scopus 로고    scopus 로고
    • Nonenzymatic covalent protein labeling using a reactive tag
    • Nonaka H, Tsukiji S, Ojida A, Hamachi I. Nonenzymatic covalent protein labeling using a reactive tag. J Am Chem Soc 129: 15777-15779, 2007.
    • (2007) J Am Chem Soc , vol.129 , pp. 15777-15779
    • Nonaka, H.1    Tsukiji, S.2    Ojida, A.3    Hamachi, I.4
  • 52
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren CJ, Anthony-Cahill SJ, Griffith MC, Schultz PG. A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244: 182-188, 1989.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 54
    • 33747613117 scopus 로고    scopus 로고
    • Oligo-Asp tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins
    • Ojida A, Honda K, Shinmi D, Kiyonaka S, Mori Y, Hamachi I. Oligo-Asp tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins. J Am Chem Soc 128: 10452-10459, 2006.
    • (2006) J Am Chem Soc , vol.128 , pp. 10452-10459
    • Ojida, A.1    Honda, K.2    Shinmi, D.3    Kiyonaka, S.4    Mori, Y.5    Hamachi, I.6
  • 55
    • 0033658004 scopus 로고    scopus 로고
    • Metabolic biotinylation of recombinant proteins in mammalian cells and in mice
    • Parrott M, Barry M. Metabolic biotinylation of recombinant proteins in mammalian cells and in mice. Mol Ther 1: 96-104, 2000.
    • (2000) Mol Ther , vol.1 , pp. 96-104
    • Parrott, M.1    Barry, M.2
  • 56
    • 0034810850 scopus 로고    scopus 로고
    • Metabolic biotinylation of secreted and cell surface proteins from mammalian cells
    • Parrott M, Barry M. Metabolic biotinylation of secreted and cell surface proteins from mammalian cells. Biochem Biophys Res Commun 281: 993-1000, 2001.
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 993-1000
    • Parrott, M.1    Barry, M.2
  • 57
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham RN. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69: 961-1004, 2000.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 59
    • 0028915619 scopus 로고
    • Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase
    • Pries F, Kingma J, Krooshof G, Jeronimus-Stratingh C, Bruins A, Janssen D. Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase. J Biol Chem 270: 10405-10411, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 10405-10411
    • Pries, F.1    Kingma, J.2    Krooshof, G.3    Jeronimus-Stratingh, C.4    Bruins, A.5    Janssen, D.6
  • 64
    • 15344350796 scopus 로고    scopus 로고
    • Dynamic fluorescent imaging of human immunodeficiency virus type 1 gag in live cells by biarsenical labeling
    • Rudner L, Nydegger S, Coren L, Nagashima K, Thali M, Ott D. Dynamic fluorescent imaging of human immunodeficiency virus type 1 gag in live cells by biarsenical labeling. J Virol 79: 4055-4065, 2005.
    • (2005) J Virol , vol.79 , pp. 4055-4065
    • Rudner, L.1    Nydegger, S.2    Coren, L.3    Nagashima, K.4    Thali, M.5    Ott, D.6
  • 65
    • 36048946776 scopus 로고    scopus 로고
    • In vivo measurement of intramolecular distances using genetically encoded reporters
    • Sandtner W, Bezanilla F, Correa AM. In vivo measurement of intramolecular distances using genetically encoded reporters. Biophys J 93: 45-47, 2007.
    • (2007) Biophys J , vol.93 , pp. 45-47
    • Sandtner, W.1    Bezanilla, F.2    Correa, A.M.3
  • 66
    • 0025361947 scopus 로고
    • Dihydrofolate reductase as a therapeutic target
    • Schweitzer B, Dicker A, Bertino J. Dihydrofolate reductase as a therapeutic target. FASEB J 4: 2441-2452, 1990.
    • (1990) FASEB J , vol.4 , pp. 2441-2452
    • Schweitzer, B.1    Dicker, A.2    Bertino, J.3
  • 68
    • 38649113240 scopus 로고    scopus 로고
    • Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species
    • Slavoff S, Chen I, Choi Y, Ting A. Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species. J Am Chem Soc 130: 1160-1162, 2008.
    • (2008) J Am Chem Soc , vol.130 , pp. 1160-1162
    • Slavoff, S.1    Chen, I.2    Choi, Y.3    Ting, A.4
  • 70
    • 0034802605 scopus 로고    scopus 로고
    • The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins
    • Stroffekova K, Proenza C, Beam K. The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins. Pflugers Arch 442: 859-866, 2001.
    • (2001) Pflugers Arch , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.3
  • 75
    • 0347568469 scopus 로고    scopus 로고
    • Genetically targeted chromophore-assisted light inactivation
    • Tour O, Meijer R, Zacharias D, Adams S, Tsien R. Genetically targeted chromophore-assisted light inactivation. Nat Biotechnol 21: 1505-1508, 2003.
    • (2003) Nat Biotechnol , vol.21 , pp. 1505-1508
    • Tour, O.1    Meijer, R.2    Zacharias, D.3    Adams, S.4    Tsien, R.5
  • 78
    • 0029590066 scopus 로고
    • Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes
    • Wagner J, Lerner R, Barbas Cr. Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science 270: 1797-1800, 1995.
    • (1995) Science , vol.270 , pp. 1797-1800
    • Wagner, J.1    Lerner, R.2    Barbas, C.3
  • 79
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L, Brock A, Herberich B, Schultz PG. Expanding the genetic code of Escherichia coli. Science 292: 498-500, 2001.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 83
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins: An expanded genetic code
    • Xie J, Schultz PG. A chemical toolkit for proteins: an expanded genetic code. Nat Rev Mol Cell Biol 7: 775-782, 2006.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 84
    • 34548602702 scopus 로고    scopus 로고
    • Xie J, Supekova L, Schultz A genetically encoded metabolically stable analogue of phosphotyrosine in Escherichia coli. ACS Chem Biol 2: 474-478, 2007.
    • Xie J, Supekova L, Schultz PG. A genetically encoded metabolically stable analogue of phosphotyrosine in Escherichia coli. ACS Chem Biol 2: 474-478, 2007.
  • 86
    • 34347368946 scopus 로고    scopus 로고
    • Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases
    • Zhou Z, Cironi P, Lin AJ, Xu Y, Hrvatin S, Golan DE, Silver PA, Walsh CT, Yin J. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. ACS Chem Biol 2: 337-346, 2007.
    • (2007) ACS Chem Biol , vol.2 , pp. 337-346
    • Zhou, Z.1    Cironi, P.2    Lin, A.J.3    Xu, Y.4    Hrvatin, S.5    Golan, D.E.6    Silver, P.A.7    Walsh, C.T.8    Yin, J.9


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