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Volumn 25, Issue 11, 2008, Pages 775-786

Expanding the genetic code of Saccharomyces cerevisiae with methionine analogues

Author keywords

Homopropargylglycine; Human superoxide dismutase; Methionine analogues; Norleucine

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; METHIONINE DERIVATIVE; NORLEUCINE; PROPARGYLGLYCINE; ALKYNE; DRUG DERIVATIVE; GLYCINE; METHIONINE; RECOMBINANT PROTEIN; SUPEROXIDE DISMUTASE;

EID: 58149328976     PISSN: 0749503X     EISSN: 10970061     Source Type: Journal    
DOI: 10.1002/yea.1632     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0020410218 scopus 로고
    • Molecular aspects of the in vivo and in vitro effects of ethionine, an analog of methionine
    • Alix JH. 1982. Molecular aspects of the in vivo and in vitro effects of ethionine, an analog of methionine. Microbiol Rev 46: 281-295.
    • (1982) Microbiol Rev , vol.46 , pp. 281-295
    • Alix, J.H.1
  • 2
    • 2442659130 scopus 로고    scopus 로고
    • An expanded genetic code with a functional quadruplet codon
    • Anderson JC, Wu N, Santoro SW, et al. 2004. An expanded genetic code with a functional quadruplet codon. Proc Natl Acad Sci USA 101: 7566-7571.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7566-7571
    • Anderson, J.C.1    Wu, N.2    Santoro, S.W.3
  • 4
    • 33751201853 scopus 로고    scopus 로고
    • Fluorescence visualization of newly synthesized proteins in mammalian cells
    • Beatty KE, Liu JC, Xie F, et al. 2006. Fluorescence visualization of newly synthesized proteins in mammalian cells. Angew Chem Int Ed Engl 45: 7364-7367.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 7364-7367
    • Beatty, K.E.1    Liu, J.C.2    Xie, F.3
  • 5
    • 26844472243 scopus 로고    scopus 로고
    • Selective dye-labelling of newly synthesized proteins in bacterial cells
    • Beatty KE, Xie F, Wang Q, et al. 2005. Selective dye-labelling of newly synthesized proteins in bacterial cells. J Am Chem Soc 127: 14150-14151.
    • (2005) J Am Chem Soc , vol.127 , pp. 14150-14151
    • Beatty, K.E.1    Xie, F.2    Wang, Q.3
  • 6
    • 0029153552 scopus 로고
    • The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae
    • Bonetti B, Fu L, Moon J, et al. 1995. The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae. J Mol Biol 251: 334-345.
    • (1995) J Mol Biol , vol.251 , pp. 334-345
    • Bonetti, B.1    Fu, L.2    Moon, J.3
  • 7
    • 33646809781 scopus 로고    scopus 로고
    • The sulphur-containing amino acids: An overview
    • Brosnan JT, Brosnan ME. 2006. The sulphur-containing amino acids: an overview. J Nutr 136: 1636S-1640S.
    • (2006) J Nutr , vol.136
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 8
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa N, Steipe B, Demange P, et al. 1995. High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur J Biochem 230: 788-796.
    • (1995) Eur J Biochem , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3
  • 9
    • 0035157217 scopus 로고    scopus 로고
    • Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II
    • Bushnell DA, Cramer P, Kornberg RD. 2001. Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II. Structure 9: R11-R14.
    • (2001) Structure , vol.9
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 10
    • 0025251693 scopus 로고
    • Purification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae
    • Chang YH, Teichert U, Smith JA. 1990. Purification and characterization of a methionine aminopeptidase from Saccharomyces cerevisiae. J Biol Chem 265: 19892-19897.
    • (1990) J Biol Chem , vol.265 , pp. 19892-19897
    • Chang, Y.H.1    Teichert, U.2    Smith, J.A.3
  • 11
    • 34447093548 scopus 로고    scopus 로고
    • An improved system for the generation and analysis of mutant proteins containing unnatural amino acids in Saccharomyces cerevisiae
    • Chen S, Schultz PG, Brock A. 2007. An improved system for the generation and analysis of mutant proteins containing unnatural amino acids in Saccharomyces cerevisiae. J Mol Biol 371: 112-122.
    • (2007) J Mol Biol , vol.371 , pp. 112-122
    • Chen, S.1    Schultz, P.G.2    Brock, A.3
  • 12
    • 0041520960 scopus 로고    scopus 로고
    • An expanded eukaryotic genetic code
    • Chin JW, Cropp TA, Anderson JC, et al. 2003. An expanded eukaryotic genetic code. Science 301: 964-967.
    • (2003) Science , vol.301 , pp. 964-967
    • Chin, J.W.1    Cropp, T.A.2    Anderson, J.C.3
  • 13
    • 0016750477 scopus 로고
    • Biochemical and regulatory effects of methionine analogues in Saccharomyces cerevisiae
    • Colombani F, Cherest H, de Robichon-Szulmajster H. 1975. Biochemical and regulatory effects of methionine analogues in Saccharomyces cerevisiae. J Bacteriol 122: 375-384.
    • (1975) J Bacteriol , vol.122 , pp. 375-384
    • Colombani, F.1    Cherest, H.2    de Robichon-Szulmajster, H.3
  • 14
    • 33847035549 scopus 로고    scopus 로고
    • Non-canonical amino acids in protein polymer design
    • Connor RE, Tirrell DA. 2007. Non-canonical amino acids in protein polymer design. Polymer Rev 47: 9-28.
    • (2007) Polymer Rev , vol.47 , pp. 9-28
    • Connor, R.E.1    Tirrell, D.A.2
  • 15
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley SD. 2003. Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr Opin Chem Biol 7: 265-272.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 16
    • 38449100431 scopus 로고    scopus 로고
    • Reprogramming the amino-acid substrate specificity of orthogonal aminoacyl-tRNA synthetases to expand the genetic code of eukaryotic cells
    • Cropp TA, Anderson JC, Chin JW. 2007. Reprogramming the amino-acid substrate specificity of orthogonal aminoacyl-tRNA synthetases to expand the genetic code of eukaryotic cells. Nat Protocols 2: 2590-2600.
    • (2007) Nat Protocols , vol.2 , pp. 2590-2600
    • Cropp, T.A.1    Anderson, J.C.2    Chin, J.W.3
  • 17
    • 0141732270 scopus 로고    scopus 로고
    • Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae
    • Deiters A, Cropp TA, Mukherji M, et al. 2003. Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. J Am Chem Soc 125: 11782-11783.
    • (2003) J Am Chem Soc , vol.125 , pp. 11782-11783
    • Deiters, A.1    Cropp, T.A.2    Mukherji, M.3
  • 18
    • 7044260692 scopus 로고    scopus 로고
    • Site-specific PEGylation of proteins containing unnatural amino acids
    • Deiters A, Cropp TA, Summerer D, et al. 2004. Site-specific PEGylation of proteins containing unnatural amino acids. Bioorg Med Chem Lett 14: 5743-5745.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 5743-5745
    • Deiters, A.1    Cropp, T.A.2    Summerer, D.3
  • 19
    • 34347218266 scopus 로고    scopus 로고
    • Labelling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging
    • Dieterich DC, Lee JJ, Link AJ, et al. 2007. Labelling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging. Nat Protocols 2: 532-540.
    • (2007) Nat Protocols , vol.2 , pp. 532-540
    • Dieterich, D.C.1    Lee, J.J.2    Link, A.J.3
  • 20
    • 57849149951 scopus 로고    scopus 로고
    • Convenient synthesis of homopropargylglycine
    • Dong S, Merkel L, Budisa N, et al. 2008. Convenient synthesis of homopropargylglycine. J Pept Sci 14: 1148-1150.
    • (2008) J Pept Sci , vol.14 , pp. 1148-1150
    • Dong, S.1    Merkel, L.2    Budisa, N.3
  • 21
    • 37249074786 scopus 로고    scopus 로고
    • Oxidative modification to cysteine sulphonic acid of Cys111 in human copper-zinc superoxide dismutase
    • Fujiwara N, Nakano M, Kato S, et al. 2007. Oxidative modification to cysteine sulphonic acid of Cys111 in human copper-zinc superoxide dismutase. J Biol Chem 282: 35933-35944.
    • (2007) J Biol Chem , vol.282 , pp. 35933-35944
    • Fujiwara, N.1    Nakano, M.2    Kato, S.3
  • 22
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • Walker JM ed, Humana: Totowa, NJ;
    • Gasteiger E, Hoogland C, Gattiker A, et al. 2005. Protein identification and analysis tools on the ExPASy server. In The Proteomics Protocols Handbook, Walker JM (ed.). Humana: Totowa, NJ; 571-607.
    • (2005) The Proteomics Protocols Handbook , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2    Gattiker, A.3
  • 23
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/ single-stranded carrier DNA/polyethylene glycol method
    • Gietz RD, Woods RA. 2002. Transformation of yeast by lithium acetate/ single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol 350: 87-96.
    • (2002) Methods Enzymol , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 24
    • 0021010421 scopus 로고
    • Immunochemical identification of membrane proteins after sodium dodecyl sulphate-polyacrylamide gel electrophoresis
    • Haid A, Suissa M. 1983. Immunochemical identification of membrane proteins after sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Methods Enzymol 96: 192-205.
    • (1983) Methods Enzymol , vol.96 , pp. 192-205
    • Haid, A.1    Suissa, M.2
  • 25
    • 0026335854 scopus 로고
    • Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines
    • Hallewell RA, Imlay KC, Lee P, et al. 1991. Thermostabilization of recombinant human and bovine CuZn superoxide dismutases by replacement of free cysteines. Biochem Biophys Res Commun 181: 474-480.
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 474-480
    • Hallewell, R.A.1    Imlay, K.C.2    Lee, P.3
  • 26
    • 0023113744 scopus 로고
    • Amino terminal acetylation of authentic human Cu,Zn superoxide dismutase produced in yeast
    • Hallewell RA, Mills R, Tekamp-Olson P, et al. 1987. Amino terminal acetylation of authentic human Cu,Zn superoxide dismutase produced in yeast. Biotechnology (N Y) 5: 363-366.
    • (1987) Biotechnology (N Y) , vol.5 , pp. 363-366
    • Hallewell, R.A.1    Mills, R.2    Tekamp-Olson, P.3
  • 27
    • 43049128964 scopus 로고    scopus 로고
    • An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides
    • Hartman MCT, Josephson K, Lin C-W, et al. 2007. An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides. PLoS ONE 2: e972.
    • (2007) PLoS ONE , vol.2
    • Hartman, M.C.T.1    Josephson, K.2    Lin, C.-W.3
  • 28
    • 43949102724 scopus 로고    scopus 로고
    • Unnatural amino acid replacement in a yeast G protein-coupled receptor in its native environment
    • Huang L-Y, Umanah G, Hauser M, et al. 2008. Unnatural amino acid replacement in a yeast G protein-coupled receptor in its native environment. Biochemistry 47: 5638-5648.
    • (2008) Biochemistry , vol.47 , pp. 5638-5648
    • Huang, L.-Y.1    Umanah, G.2    Hauser, M.3
  • 29
    • 0034674281 scopus 로고    scopus 로고
    • Expanding the scope of protein biosynthesis by altering the methionyl-tRNA synthetase activity of a bacterial expression host
    • Kiick KL, van Hest JCM, Tirrell DA. 2000. Expanding the scope of protein biosynthesis by altering the methionyl-tRNA synthetase activity of a bacterial expression host. Angew Chem Int Ed Engl 39: 2148-2152.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 2148-2152
    • Kiick, K.L.1    van Hest, J.C.M.2    Tirrell, D.A.3
  • 30
    • 0035958733 scopus 로고    scopus 로고
    • Identification of an expanded set of translationally active methionine analogues in Escherichia coli
    • Kiick KL, Weberskirch R, Tirrell DA. 2001. Identification of an expanded set of translationally active methionine analogues in Escherichia coli. FEBS Lett 502: 25-30.
    • (2001) FEBS Lett , vol.502 , pp. 25-30
    • Kiick, K.L.1    Weberskirch, R.2    Tirrell, D.A.3
  • 31
    • 0014602483 scopus 로고
    • Influence of methionine pool composition on the formation of methyl-deficient transfer ribonucleic acid in Saccharomyces cerevisiae
    • Kjellin-Stråby K. 1969. Influence of methionine pool composition on the formation of methyl-deficient transfer ribonucleic acid in Saccharomyces cerevisiae. J Bacteriol 100: 687-694.
    • (1969) J Bacteriol , vol.100 , pp. 687-694
    • Kjellin-Stråby, K.1
  • 32
    • 0013784786 scopus 로고
    • Studies on microbial RNA, 3. Formation of submethylated sRNA in Saccharomyces cerevisiae
    • Kjellin-Stråby K, Boman HG. 1965. Studies on microbial RNA, 3. Formation of submethylated sRNA in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 53: 1346-1352.
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 1346-1352
    • Kjellin-Stråby, K.1    Boman, H.G.2
  • 33
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • Kolb HC, Sharpless KB. 2003. The growing impact of click chemistry on drug discovery. Drug Discov Today 8: 1128-1137.
    • (2003) Drug Discov Today , vol.8 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0036008516 scopus 로고    scopus 로고
    • Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris
    • Larsson AM, Ståhlberg J, Jones TA. 2002. Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris. Acta Crystallogr D Biol Crystallogr 58: 346-348.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 346-348
    • Larsson, A.M.1    Ståhlberg, J.2    Jones, T.A.3
  • 36
    • 11144224207 scopus 로고    scopus 로고
    • Gene silencing pathway RNA-dependent RNA polymerase of Neurospora crassa: Yeast expression and crystallization of selenomethionated QDE-1 protein
    • Laurila MRL, Salgado PS, Makeyev EV, et al. 2005. Gene silencing pathway RNA-dependent RNA polymerase of Neurospora crassa: yeast expression and crystallization of selenomethionated QDE-1 protein. J Struct Biol 149: 111-115.
    • (2005) J Struct Biol , vol.149 , pp. 111-115
    • Laurila, M.R.L.1    Salgado, P.S.2    Makeyev, E.V.3
  • 37
    • 34249856231 scopus 로고    scopus 로고
    • Blocking S-adenosylmethionine synthesis in yeast allows selenomethionine incorporation and multiwavelength anomalous dispersion phasing
    • Malkowski MG, Quartley E, Friedman AE, et al. 2007. Blocking S-adenosylmethionine synthesis in yeast allows selenomethionine incorporation and multiwavelength anomalous dispersion phasing. Proc Natl Acad Sci USA 104: 6678-6683.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6678-6683
    • Malkowski, M.G.1    Quartley, E.2    Friedman, A.E.3
  • 38
    • 38849157944 scopus 로고    scopus 로고
    • In vivo chemoenzymatic control of N-terminal processing in recombinant human epidermal growth factor
    • Merkel L, Cheburkin Y, Wiltschi B, et al. 2007. In vivo chemoenzymatic control of N-terminal processing in recombinant human epidermal growth factor. Chembiochem 8: 2227-2232.
    • (2007) Chembiochem , vol.8 , pp. 2227-2232
    • Merkel, L.1    Cheburkin, Y.2    Wiltschi, B.3
  • 39
    • 0026711256 scopus 로고
    • Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
    • Parge HE, Hallewell RA, Tainer JA. 1992. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc Natl Acad Sci USA 89: 6109-6113.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6109-6113
    • Parge, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 40
    • 0000326822 scopus 로고
    • The effect of amino acid analogues on growth and protein synthesis in microorganisms
    • Richmond MH. 1962. The effect of amino acid analogues on growth and protein synthesis in microorganisms. Microbiol Mol Biol Rev 26: 398-420.
    • (1962) Microbiol Mol Biol Rev , vol.26 , pp. 398-420
    • Richmond, M.H.1
  • 41
    • 0020998506 scopus 로고
    • Import of proteins into mitochondria: A 70 kDa outer membrane protein with a large carboxy-terminal deletion is still transported to the outer membrane
    • Riezman H, Hase T, van Loon AP, et al. 1983. Import of proteins into mitochondria: a 70 kDa outer membrane protein with a large carboxy-terminal deletion is still transported to the outer membrane. EMBO J 2: 2161-2168.
    • (1983) EMBO J , vol.2 , pp. 2161-2168
    • Riezman, H.1    Hase, T.2    van Loon, A.P.3
  • 42
    • 0036849244 scopus 로고    scopus 로고
    • Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells
    • Sakamoto K, Hayashi A, Sakamoto A, et al. 2002. Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells. Nucleic Acids Res 30: 4692-4699.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4692-4699
    • Sakamoto, K.1    Hayashi, A.2    Sakamoto, A.3
  • 43
    • 39749146396 scopus 로고    scopus 로고
    • Introduction of plasmid DNA into cells. Curr Protoc Mol Biol
    • Unit 1.8.1-1.8.10
    • Seidman CE, Struhl K, Sheen J, et al. 2001. Introduction of plasmid DNA into cells. Curr Protoc Mol Biol Chapter 1: Unit 1.8.1-1.8.10.
    • (2001) Chapter , vol.1
    • Seidman, C.E.1    Struhl, K.2    Sheen, J.3
  • 44
    • 0018231898 scopus 로고
    • Methionine analogs and cell division regulation in the yeast Saccharomyces cerevisiae
    • Singer RA, Johnston GC, Bedard D. 1978. Methionine analogs and cell division regulation in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA 75: 6083-6087.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 6083-6087
    • Singer, R.A.1    Johnston, G.C.2    Bedard, D.3
  • 45
    • 42949178439 scopus 로고    scopus 로고
    • Unnatural amino acid incorporation into virus-like particles
    • Strable E, Prasuhn DE, Udit AK, et al. 2008. Unnatural amino acid incorporation into virus-like particles. Bioconjug Chem 19: 866-875.
    • (2008) Bioconjug Chem , vol.19 , pp. 866-875
    • Strable, E.1    Prasuhn, D.E.2    Udit, A.K.3
  • 46
    • 0034003659 scopus 로고    scopus 로고
    • Efficient incorporation of unsaturated methionine analogs into proteins in vivo
    • van Hest JC, Kiick KL, Tirrell DA. 2000. Efficient incorporation of unsaturated methionine analogs into proteins in vivo. J Am Chem Soc 122: 1282-1288.
    • (2000) J Am Chem Soc , vol.122 , pp. 1282-1288
    • van Hest, J.C.1    Kiick, K.L.2    Tirrell, D.A.3
  • 47
    • 0028307059 scopus 로고
    • Endocytosis and degradation of the yeast uracil permease under adverse conditions
    • Volland C, Urban-Grimal D, Geraud G, et al. 1994. Endocytosis and degradation of the yeast uracil permease under adverse conditions. J Biol Chem 269: 9833-9841.
    • (1994) J Biol Chem , vol.269 , pp. 9833-9841
    • Volland, C.1    Urban-Grimal, D.2    Geraud, G.3
  • 48
    • 38849132058 scopus 로고    scopus 로고
    • Processing of N-terminal unnatural amino acids in recombinant human interferon-β in Escherichia coli
    • Wang A, Winblade Nairn N, Johnson RS, et al. 2008. Processing of N-terminal unnatural amino acids in recombinant human interferon-β in Escherichia coli. Chembiochem 9: 324-330.
    • (2008) Chembiochem , vol.9 , pp. 324-330
    • Wang, A.1    Winblade Nairn, N.2    Johnson, R.S.3
  • 49
    • 34447342528 scopus 로고    scopus 로고
    • Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion
    • Wang K, Neumann H, Peak-Chew SY, et al. 2007. Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion. Nat Biotechnol 25: 770-777.
    • (2007) Nat Biotechnol , vol.25 , pp. 770-777
    • Wang, K.1    Neumann, H.2    Peak-Chew, S.Y.3
  • 50
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L, Brock A, Herberich B, et al. 2001. Expanding the genetic code of Escherichia coli. Science 292: 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3
  • 51
    • 0037454346 scopus 로고    scopus 로고
    • Wang Q, Chan TR, Hilgraf R, et al. 2003. Bioconjugation by copper(I)-catalysed azide-alkyne [3 + 2] cycloaddition. J Am Chem Soc 125: 3192-3193.
    • Wang Q, Chan TR, Hilgraf R, et al. 2003. Bioconjugation by copper(I)-catalysed azide-alkyne [3 + 2] cycloaddition. J Am Chem Soc 125: 3192-3193.
  • 52
    • 0037131560 scopus 로고    scopus 로고
    • Nutrient-regulated protein kinases in budding yeast
    • Wilson WA, Roach PJ. 2002. Nutrient-regulated protein kinases in budding yeast. Cell 111: 155-158.
    • (2002) Cell , vol.111 , pp. 155-158
    • Wilson, W.A.1    Roach, P.J.2
  • 53
    • 33847302452 scopus 로고    scopus 로고
    • Natural history and experimental evolution of the genetic code
    • Wiltschi B, Budisa N. 2007. Natural history and experimental evolution of the genetic code. Appl Microbiol Biotechnol 74: 739-753.
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 739-753
    • Wiltschi, B.1    Budisa, N.2
  • 54
    • 7744222751 scopus 로고    scopus 로고
    • A genetically encoded photocaged amino acid
    • Wu N, Deiters A, Cropp TA, et al. 2004. A genetically encoded photocaged amino acid. J Am Chem Soc 126: 14306-14307.
    • (2004) J Am Chem Soc , vol.126 , pp. 14306-14307
    • Wu, N.1    Deiters, A.2    Cropp, T.A.3


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