메뉴 건너뛰기




Volumn 110, Issue 13, 2013, Pages 4992-4997

Mutant methionyl-tRNA synthetase from bacteria enables site-selective N-terminal labeling of proteins expressed in mammalian cells

Author keywords

Protein engineering; Protein synthesis; Proteomics; Translational profiling

Indexed keywords

BACTERIAL ENZYME; BACTERIAL RNA; METHIONINE TRANSFER RNA LIGASE; METHIONYL AMINOPEPTIDASE; PROTEIN P53; TRANSFER RNA;

EID: 84875523875     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1216375110     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 0032437667 scopus 로고    scopus 로고
    • Control of translation initiation in animals
    • Gray NK, Wickens M (1998) Control of translation initiation in animals. Annu Rev Cell Dev Biol 14:399-458.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 399-458
    • Gray, N.K.1    Wickens, M.2
  • 2
  • 3
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhäusser B, Gossen M, Dittmar G, Selbach M (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9(1):205-209.
    • (2009) Proteomics , vol.9 , Issue.1 , pp. 205-209
    • Schwanhäusser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 4
    • 80053013322 scopus 로고    scopus 로고
    • Noncanonical amino acids in the interrogation of cellular protein synthesis
    • Ngo JT, Tirrell DA (2011) Noncanonical amino acids in the interrogation of cellular protein synthesis. Acc Chem Res 44(9):677-685.
    • (2011) Acc Chem Res , vol.44 , Issue.9 , pp. 677-685
    • Ngo, J.T.1    Tirrell, D.A.2
  • 5
    • 33745464039 scopus 로고    scopus 로고
    • Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
    • Dieterich DC, Link AJ, Graumann J, Tirrell DA, Schuman EM (2006) Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT). Proc Natl Acad Sci USA 103(25):9482-9487.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.25 , pp. 9482-9487
    • Dieterich, D.C.1    Link, A.J.2    Graumann, J.3    Tirrell, D.A.4    Schuman, E.M.5
  • 6
    • 84862908426 scopus 로고    scopus 로고
    • Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin
    • Liu J, Xu Y, Stoleru D, Salic A (2012) Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin. Proc Natl Acad Sci USA 109(2):413-418.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.2 , pp. 413-418
    • Liu, J.1    Xu, Y.2    Stoleru, D.3    Salic, A.4
  • 7
    • 79952901680 scopus 로고    scopus 로고
    • Enhancer function: New insights into the regulation of tissue-specific gene expression
    • Ong C-T, Corces VG (2011) Enhancer function: New insights into the regulation of tissue-specific gene expression. Nat Rev Genet 12(4):283-293.
    • (2011) Nat Rev Genet , vol.12 , Issue.4 , pp. 283-293
    • Ong, C.-T.1    Corces, V.G.2
  • 8
    • 70349327398 scopus 로고    scopus 로고
    • Cell-selective metabolic labeling of proteins
    • Ngo JT, et al. (2009) Cell-selective metabolic labeling of proteins. Nat Chem Biol 5(10): 715-717.
    • (2009) Nat Chem Biol , vol.5 , Issue.10 , pp. 715-717
    • Ngo, J.T.1
  • 9
    • 70349320611 scopus 로고    scopus 로고
    • Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo
    • Tanrikulu IC, Schmitt E, Mechulam Y, Goddard WA, 3rd, Tirrell DA (2009) Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo. Proc Natl Acad Sci USA 106(36):15285-15290.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.36 , pp. 15285-15290
    • Tanrikulu, I.C.1    Schmitt, E.2    Mechulam, Y.3    Goddard III, W.A.4    Tirrell, D.A.5
  • 10
    • 78650590308 scopus 로고    scopus 로고
    • Cleavable biotin probes for labeling of biomolecules via azide-alkyne cycloaddition
    • Szychowski J, et al. (2010) Cleavable biotin probes for labeling of biomolecules via azide-alkyne cycloaddition. J Am Chem Soc 132(51):18351-18360.
    • (2010) J Am Chem Soc , vol.132 , Issue.51 , pp. 18351-18360
    • Szychowski, J.1
  • 11
    • 26844472243 scopus 로고    scopus 로고
    • Selective dye-labeling of newly synthesized proteins in bacterial cells
    • Beatty KE, Xie F, Wang Q, Tirrell DA (2005) Selective dye-labeling of newly synthesized proteins in bacterial cells. J Am Chem Soc 127(41):14150-14151.
    • (2005) J Am Chem Soc , vol.127 , Issue.41 , pp. 14150-14151
    • Beatty, K.E.1    Xie, F.2    Wang, Q.3    Tirrell, D.A.4
  • 12
    • 33751201853 scopus 로고    scopus 로고
    • Fluorescence visualization of newly synthesized proteins in mammalian cells
    • Beatty KE, et al. (2006) Fluorescence visualization of newly synthesized proteins in mammalian cells. Angew Chem Int Ed Engl 45(44):7364-7367.
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.44 , pp. 7364-7367
    • Beatty, K.E.1
  • 13
    • 77955575354 scopus 로고    scopus 로고
    • Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection
    • Grammel M, Zhang MM, Hang HC (2010) Orthogonal alkynyl amino acid reporter for selective labeling of bacterial proteomes during infection. Angew Chem Int Ed Engl 49(34):5970-5974.
    • (2010) Angew Chem Int Ed Engl , vol.49 , Issue.34 , pp. 5970-5974
    • Grammel, M.1    Zhang, M.M.2    Hang, H.C.3
  • 14
    • 0015852075 scopus 로고
    • The mechanism of action of methioninetRNA synthetase: 2. Interaction of the enzyme with specific and unspecific tRNAs
    • Blanquet S, Petrissant G, Waller JP (1973) The mechanism of action of methioninetRNA synthetase: 2. Interaction of the enzyme with specific and unspecific tRNAs. Eur J Biochem 36(1):227-233.
    • (1973) Eur J Biochem , vol.36 , Issue.1 , pp. 227-233
    • Blanquet, S.1    Petrissant, G.2    Waller, J.P.3
  • 15
    • 0031952186 scopus 로고    scopus 로고
    • Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis
    • Drabkin HJ, Estrella M, Rajbhandary UL (1998) Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis. Mol Cell Biol 18(3):1459-1466.
    • (1998) Mol Cell Biol , vol.18 , Issue.3 , pp. 1459-1466
    • Drabkin, H.J.1    Estrella, M.2    Rajbhandary, U.L.3
  • 16
    • 0014966553 scopus 로고
    • Roles of methionine transfer RNAs in protein synthesis in rabbit reticulocytes
    • Gupta NK, Chatterjee KK, Bose S, Chung A (1970) Roles of methionine transfer RNAs in protein synthesis in rabbit reticulocytes. J Mol Biol 54(1):145-154.
    • (1970) J Mol Biol , vol.54 , Issue.1 , pp. 145-154
    • Gupta, N.K.1    Chatterjee, K.K.2    Bose, S.3    Chung, A.4
  • 17
    • 0026674275 scopus 로고
    • Involvement of the size and sequence of the anticodon loop in tRNA recognition by mammalian and E. coli methionyltRNA synthetases
    • Meinnel T, Mechulam Y, Fayat G, Blanquet S (1992) Involvement of the size and sequence of the anticodon loop in tRNA recognition by mammalian and E. coli methionyltRNA synthetases. Nucleic Acids Res 20(18):4741-4746.
    • (1992) Nucleic Acids Res , vol.20 , Issue.18 , pp. 4741-4746
    • Meinnel, T.1    Mechulam, Y.2    Fayat, G.3    Blanquet, S.4
  • 18
    • 0016000962 scopus 로고
    • Specific aminoacylation of the methionine-specific tRNA's of eukaryotes
    • Stanley WM, Jr. (1974) Specific aminoacylation of the methionine-specific tRNA's of eukaryotes. Methods Enzymol 29:530-547.
    • (1974) Methods Enzymol , vol.29 , pp. 530-547
    • Stanley Jr., W.M.1
  • 19
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak M (1983) Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev 47(1):1-45.
    • (1983) Microbiol Rev , vol.47 , Issue.1 , pp. 1-45
    • Kozak, M.1
  • 20
    • 0014951549 scopus 로고
    • Cytoplasmic methionine transfer RNAs from eukaryotes
    • Smith AE, Marcker KA (1970) Cytoplasmic methionine transfer RNAs from eukaryotes. Nature 226(5246):607-610.
    • (1970) Nature , vol.226 , Issue.5246 , pp. 607-610
    • Smith, A.E.1    Marcker, K.A.2
  • 21
    • 0015513046 scopus 로고
    • Recognition of eukaryotic initiator tRNA by an initiation factor and the transfer of the methionine moiety into peptide linkage
    • Dettman GL, Stanley WM, Jr. (1972) Recognition of eukaryotic initiator tRNA by an initiation factor and the transfer of the methionine moiety into peptide linkage. Biochim Biophys Acta 287(1):124-133.
    • (1972) Biochim Biophys Acta , vol.287 , Issue.1 , pp. 124-133
    • Dettman, G.L.1    Stanley Jr., W.M.2
  • 22
    • 0034768617 scopus 로고    scopus 로고
    • Preparation and activity of synthetic unmodified mammalian tRNAi(Met) in initiation of translation in vitro
    • Pestova TV, Hellen CUT (2001) Preparation and activity of synthetic unmodified mammalian tRNAi(Met) in initiation of translation in vitro. RNA 7(10):1496-1505.
    • (2001) RNA , vol.7 , Issue.10 , pp. 1496-1505
    • Pestova, T.V.1    Hellen, C.U.T.2
  • 23
    • 36749028242 scopus 로고    scopus 로고
    • Copper-free click chemistry for dynamic in vivo imaging
    • Baskin JM, et al. (2007) Copper-free click chemistry for dynamic in vivo imaging. Proc Natl Acad Sci USA 104(43):16793-16797.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.43 , pp. 16793-16797
    • Baskin, J.M.1
  • 24
    • 72449154666 scopus 로고    scopus 로고
    • Analysis and optimization of coppercatalyzed azide-alkyne cycloaddition for bioconjugation
    • Hong V, Presolski SI, Ma C, Finn MG (2009) Analysis and optimization of coppercatalyzed azide-alkyne cycloaddition for bioconjugation. Angew Chem Int Ed Engl 48(52):9879-9883.
    • (2009) Angew Chem Int Ed Engl , vol.48 , Issue.52 , pp. 9879-9883
    • Hong, V.1    Presolski, S.I.2    Ma, C.3    Finn, M.G.4
  • 25
    • 72149099119 scopus 로고    scopus 로고
    • Aza-dibenzocyclooctynes for fast and efficient enzyme PEGylation via copper-free (3+2) cycloaddition
    • Debets MF, et al. (2010) Aza-dibenzocyclooctynes for fast and efficient enzyme PEGylation via copper-free (3+2) cycloaddition. Chem Commun (Camb) 46(1):97-99.
    • (2010) Chem Commun (Camb) , vol.46 , Issue.1 , pp. 97-99
    • Debets, M.F.1
  • 26
    • 84858741572 scopus 로고    scopus 로고
    • Preventing thiol-yne addition improves the specificity of strain-promoted azide-alkyne cycloaddition
    • van Geel R, Pruijn GJ, van Delft FL, Boelens WC (2012) Preventing thiol-yne addition improves the specificity of strain-promoted azide-alkyne cycloaddition. Bioconjug Chem 23(3):392-398.
    • (2012) Bioconjug Chem , vol.23 , Issue.3 , pp. 392-398
    • Van Geel, R.1    Pruijn, G.J.2    Van Delft, F.L.3    Boelens, W.C.4
  • 27
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: A functional node in cell biology
    • Bernstein BW, Bamburg JR (2010) ADF/cofilin: A functional node in cell biology. Trends Cell Biol 20(4):187-195.
    • (2010) Trends Cell Biol , vol.20 , Issue.4 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 28
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and N alpha-acetyl transferase families
    • Bradshaw RA, Brickey WW, Walker KW (1998) N-terminal processing: The methionine aminopeptidase and N alpha-acetyl transferase families. Trends Biochem Sci 23(7): 263-267.
    • (1998) Trends Biochem Sci , vol.23 , Issue.7 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 29
    • 38849132058 scopus 로고    scopus 로고
    • Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli
    • Wang A, Winblade Nairn N, Johnson RS, Tirrell DA, Grabstein K (2008) Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli. ChemBioChem 9(2):324-330.
    • (2008) ChemBioChem , vol.9 , Issue.2 , pp. 324-330
    • Wang, A.1    Winblade Nairn, N.2    Johnson, R.S.3    Tirrell, D.A.4    Grabstein, K.5
  • 30
    • 60349090901 scopus 로고    scopus 로고
    • Fine tuning the N-terminal residue excision with methionine analogues
    • Wiltschi B, Merkel L, Budisa N (2009) Fine tuning the N-terminal residue excision with methionine analogues. ChemBioChem 10(2):217-220.
    • (2009) ChemBioChem , vol.10 , Issue.2 , pp. 217-220
    • Wiltschi, B.1    Merkel, L.2    Budisa, N.3
  • 31
    • 0016691755 scopus 로고
    • Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro
    • Pestana A, Pitot HC (1975) Acetylation of nascent polypeptide chains on rat liver polyribosomes in vivo and in vitro. Biochemistry 14(7):1404-1412.
    • (1975) Biochemistry , vol.14 , Issue.7 , pp. 1404-1412
    • Pestana, A.1    Pitot, H.C.2
  • 32
    • 66249126298 scopus 로고    scopus 로고
    • Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans
    • Arnesen T, et al. (2009) Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc Natl Acad Sci USA 106(20):8157-8162.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.20 , pp. 8157-8162
    • Arnesen, T.1
  • 33
    • 0036898897 scopus 로고    scopus 로고
    • Histone mRNA expression: Multiple levels of cell cycle regulation and important developmental consequences
    • Marzluff WF, Duronio RJ (2002) Histone mRNA expression: Multiple levels of cell cycle regulation and important developmental consequences. CurrOpin CellBiol 14(6):692-699.
    • (2002) CurrOpin CellBiol , vol.14 , Issue.6 , pp. 692-699
    • Marzluff, W.F.1    Duronio, R.J.2
  • 34
    • 3042870747 scopus 로고
    • Histone mRNA concentrations are regulated at the level of transcription and mRNA degradation
    • Sittman DB, Graves RA, Marzluff WF (1983) Histone mRNA concentrations are regulated at the level of transcription and mRNA degradation. Proc Natl Acad Sci USA 80(7):1849-1853.
    • (1983) Proc Natl Acad Sci USA , vol.80 , Issue.7 , pp. 1849-1853
    • Sittman, D.B.1    Graves, R.A.2    Marzluff, W.F.3
  • 35
    • 0018539353 scopus 로고
    • Fate of newly synthesized histones shortly after interruption of DNA replication
    • Senshu T, Ohashi M (1979) Fate of newly synthesized histones shortly after interruption of DNA replication. J Biochem 86(5):1259-1267.
    • (1979) J Biochem , vol.86 , Issue.5 , pp. 1259-1267
    • Senshu, T.1    Ohashi, M.2
  • 36
    • 0015890741 scopus 로고
    • Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme
    • Atkin CL, Thelander L, Reichard P, Lang G (1973) Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme. J Biol Chem 248(21):7464-7472.
    • (1973) J Biol Chem , vol.248 , Issue.21 , pp. 7464-7472
    • Atkin, C.L.1    Thelander, L.2    Reichard, P.3    Lang, G.4
  • 37
    • 70349438994 scopus 로고    scopus 로고
    • Tumour suppression by p53: A role for the DNA damage response?
    • Meek DW (2009) Tumour suppression by p53: A role for the DNA damage response? Nat Rev Cancer 9(10):714-723.
    • (2009) Nat Rev Cancer , vol.9 , Issue.10 , pp. 714-723
    • Meek, D.W.1
  • 39
    • 77952996319 scopus 로고    scopus 로고
    • Genome-wide kinetics of nucleosome turnover determined by metabolic labeling of histones
    • Deal RB, Henikoff JG, Henikoff S (2010) Genome-wide kinetics of nucleosome turnover determined by metabolic labeling of histones. Science 328(5982):1161-1164.
    • (2010) Science , vol.328 , Issue.5982 , pp. 1161-1164
    • Deal, R.B.1    Henikoff, J.G.2    Henikoff, S.3
  • 40
    • 77952486777 scopus 로고    scopus 로고
    • Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation
    • Tcherkezian J, Brittis PA, Thomas F, Roux PP, Flanagan JG (2010) Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation. Cell 141(4):632-644.
    • (2010) Cell , vol.141 , Issue.4 , pp. 632-644
    • Tcherkezian, J.1    Brittis, P.A.2    Thomas, F.3    Roux, P.P.4    Flanagan, J.G.5
  • 41
    • 77954095160 scopus 로고    scopus 로고
    • In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons
    • Dieterich DC, et al. (2010) In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nat Neurosci 13(7):897-905.
    • (2010) Nat Neurosci , vol.13 , Issue.7 , pp. 897-905
    • Dieterich, D.C.1
  • 42
    • 84857275266 scopus 로고    scopus 로고
    • Local translation of extranuclear lamin B promotes axon maintenance
    • Yoon BC, et al. (2012) Local translation of extranuclear lamin B promotes axon maintenance. Cell 148(4):752-764.
    • (2012) Cell , vol.148 , Issue.4 , pp. 752-764
    • Yoon, B.C.1
  • 43
    • 84865380837 scopus 로고    scopus 로고
    • Dopaminergic modulation of the hippocampal neuropil proteome identified by bioorthogonal noncanonical amino acid tagging (BONCAT)
    • 10.1002/pmic.201200112
    • Hodas JJ, et al. (2012) Dopaminergic modulation of the hippocampal neuropil proteome identified by bioorthogonal noncanonical amino acid tagging (BONCAT). Proteomics 12(15-16):2464-2476, 10.1002/pmic.201200112.
    • (2012) Proteomics , vol.12 , Issue.15-16 , pp. 2464-2476
    • Hodas, J.J.1
  • 44
    • 84856064801 scopus 로고    scopus 로고
    • Non-canonical amino acid labeling in vivo to visualize and affinity purify newly synthesized proteins in larval zebrafish
    • Hinz FI, Dieterich DC, Tirrell DA, Schuman EM (2012) Non-canonical amino acid labeling in vivo to visualize and affinity purify newly synthesized proteins in larval zebrafish. ACS Chem Neurosci 3(1):40-49.
    • (2012) ACS Chem Neurosci , vol.3 , Issue.1 , pp. 40-49
    • Hinz, F.I.1    Dieterich, D.C.2    Tirrell, D.A.3    Schuman, E.M.4
  • 45
    • 55449107738 scopus 로고    scopus 로고
    • A translational profiling approach for the molecular characterization of CNS cell types
    • Heiman M, et al. (2008) A translational profiling approach for the molecular characterization of CNS cell types. Cell 135(4):738-748.
    • (2008) Cell , vol.135 , Issue.4 , pp. 738-748
    • Heiman, M.1
  • 46
    • 69549113277 scopus 로고    scopus 로고
    • Cell-type-specific isolation of ribosome-associated mRNA from complex tissues
    • Sanz E, et al. (2009) Cell-type-specific isolation of ribosome-associated mRNA from complex tissues. Proc Natl Acad Sci USA 106(33):13939-13944.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13939-13944
    • Sanz, E.1
  • 47
    • 67349288523 scopus 로고    scopus 로고
    • TU-tagging: Cell type-specific RNA isolation from intact complex tissues
    • Miller MR, Robinson KJ, Cleary MD, Doe CQ (2009) TU-tagging: Cell type-specific RNA isolation from intact complex tissues. Nat Methods 6(6):439-441.
    • (2009) Nat Methods , vol.6 , Issue.6 , pp. 439-441
    • Miller, M.R.1    Robinson, K.J.2    Cleary, M.D.3    Doe, C.Q.4
  • 49
    • 3042662113 scopus 로고    scopus 로고
    • In silico proteome analysis to facilitate proteomics experiments using mass spectrometry
    • Cagney G, Amiri S, Premawaradena T, Lindo M, Emili A (2003) In silico proteome analysis to facilitate proteomics experiments using mass spectrometry. Proteome Sci 1(1):5-20.
    • (2003) Proteome Sci , vol.1 , Issue.1 , pp. 5-20
    • Cagney, G.1    Amiri, S.2    Premawaradena, T.3    Lindo, M.4    Emili, A.5
  • 50
    • 67650403796 scopus 로고    scopus 로고
    • Selective enrichment of azide-containing peptides from complex mixtures
    • Nessen MA, et al. (2009) Selective enrichment of azide-containing peptides from complex mixtures. J Proteome Res 8(7):3702-3711.
    • (2009) J Proteome Res , vol.8 , Issue.7 , pp. 3702-3711
    • Nessen, M.A.1
  • 51
    • 80053604348 scopus 로고    scopus 로고
    • Selecting protein N-terminal peptides by combined fractional diagonal chromatography
    • Staes A, et al. (2011) Selecting protein N-terminal peptides by combined fractional diagonal chromatography. Nat Protoc 6(8):1130-1141.
    • (2011) Nat Protoc , vol.6 , Issue.8 , pp. 1130-1141
    • Staes, A.1
  • 53
    • 23044460011 scopus 로고    scopus 로고
    • N-terminal labeling of proteins using initiator tRNA
    • Olejnik J, Gite S, Mamaev S, Rothschild KJ (2005) N-terminal labeling of proteins using initiator tRNA. Methods 36(3):252-260.
    • (2005) Methods , vol.36 , Issue.3 , pp. 252-260
    • Olejnik, J.1    Gite, S.2    Mamaev, S.3    Rothschild, K.J.4
  • 54
    • 0842281352 scopus 로고    scopus 로고
    • Cell-free N-terminal protein labeling using initiator suppressor tRNA
    • Mamaev S, Olejnik J, Olejnik EK, Rothschild KJ (2004) Cell-free N-terminal protein labeling using initiator suppressor tRNA. Anal Biochem 326(1):25-32.
    • (2004) Anal Biochem , vol.326 , Issue.1 , pp. 25-32
    • Mamaev, S.1    Olejnik, J.2    Olejnik, E.K.3    Rothschild, K.J.4
  • 55
    • 0034653964 scopus 로고    scopus 로고
    • Ultrasensitive fluorescence-based detection of nascent proteins in gels
    • Gite S, Mamaev S, Olejnik J, Rothschild K (2000) Ultrasensitive fluorescence-based detection of nascent proteins in gels. Anal Biochem 279(2):218-225.
    • (2000) Anal Biochem , vol.279 , Issue.2 , pp. 218-225
    • Gite, S.1    Mamaev, S.2    Olejnik, J.3    Rothschild, K.4
  • 57
    • 84857451064 scopus 로고    scopus 로고
    • Designer proteins: Applications of genetic code expansion in cell biology
    • Davis L, Chin JW (2012) Designer proteins: Applications of genetic code expansion in cell biology. Nat Rev Mol Cell Biol 13(3):168-182.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.3 , pp. 168-182
    • Davis, L.1    Chin, J.W.2
  • 58
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • Carrico IS, Carlson BL, Bertozzi CR (2007) Introducing genetically encoded aldehydes into proteins. Nat Chem Biol 3(6):321-322.
    • (2007) Nat Chem Biol , vol.3 , Issue.6 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.