메뉴 건너뛰기




Volumn 10, Issue 1, 1999, Pages 64-70

tRNA-mediated protein engineering

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; STABLE ISOTOPE; TRANSFER RNA;

EID: 0032935859     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)80012-3     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0009849775 scopus 로고
    • Nucleic acid synthesis in the study of the genetic code
    • New York: Elsevier-North Holland
    • Khorana HG: Nucleic acid synthesis in the study of the genetic code. In Nobel Lectures: Physiology or Medicine. New York: Elsevier-North Holland; 1977:303-333.
    • (1977) In Nobel Lectures: Physiology or Medicine , pp. 303-333
    • Khorana, H.G.1
  • 2
    • 0001358802 scopus 로고
    • RNA codewords and protein synthesis
    • Nirenberg MW, Leder P RNA codewords and protein synthesis. Science. 145:1964;1399-1407.
    • (1964) Science , vol.145 , pp. 1399-1407
    • Nirenberg, M.W.1    Leder, P.2
  • 3
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • Krieg UC, Walter P, Johnson AE Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc Natl Acad Sci USA. 83:1986;8604-8608.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 4
    • 0024425706 scopus 로고
    • Protein translocation across the endoplasmic reticulum membrane: Identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel
    • Krieg UC, Johnson AE, Walter P Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel. J Cell Biol. 109:1989;2033-2043.
    • (1989) J Cell Biol , vol.109 , pp. 2033-2043
    • Krieg, U.C.1    Johnson, A.E.2    Walter, P.3
  • 5
    • 0026061020 scopus 로고
    • A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation
    • Thrift RN, Andrews DW, Walter P, Johnson AE A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation. J Cell Biol. 112:1991;809-821.
    • (1991) J Cell Biol , vol.112 , pp. 809-821
    • Thrift, R.N.1    Andrews, D.W.2    Walter, P.3    Johnson, A.E.4
  • 6
    • 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. 244:1989;182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 8
  • 9
    • 0032516767 scopus 로고    scopus 로고
    • Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine
    • This paper describes the crystal structure of modified glutathione transferase where all the tyrosine residues are replaced by its analog 3-fluorotyrosine. This is one of the first reports of analysis of a protein structure with such a fluorotyrosine substitution.
    • Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine. J Mol Biol. 281:1998;323-339. This paper describes the crystal structure of modified glutathione transferase where all the tyrosine residues are replaced by its analog 3-fluorotyrosine. This is one of the first reports of analysis of a protein structure with such a fluorotyrosine substitution.
    • (1998) J Mol Biol , vol.281 , pp. 323-339
    • Xiao, G.1    Parsons, J.F.2    Tesh, K.3    Armstrong, R.N.4    Gilliland, G.L.5
  • 10
    • 0031929949 scopus 로고    scopus 로고
    • Residue specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: Structure and stability of the per-thiaproline mutant of annexin V
    • This paper describes a procedure for preparing recombinant protein by in vivo synthesis using an auxotropic strain of E. coli and special growth media, where all the proline residues in the protein are replaced by the proline analog thiaproline. Such proteins are very useful for biophysical analysis.
    • Budisa N, Minks C, Medrano FJ, Lutz J, Huber R, Moroder L Residue specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: structure and stability of the per-thiaproline mutant of annexin V. Proc Natl Acad Sci USA. 95:1998;455-459. This paper describes a procedure for preparing recombinant protein by in vivo synthesis using an auxotropic strain of E. coli and special growth media, where all the proline residues in the protein are replaced by the proline analog thiaproline. Such proteins are very useful for biophysical analysis.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 455-459
    • Budisa, N.1    Minks, C.2    Medrano, F.J.3    Lutz, J.4    Huber, R.5    Moroder, L.6
  • 11
    • 0030784822 scopus 로고    scopus 로고
    • Exploiting unassigned codons in Micrococcus fluteus for tRNA-based amino acid mutagenesis
    • The authors highlight the use of unassigned codons for site-directed incorporation of non-native amino acids into proteins without the use of a stop codon. The model system described is based on the use of one of the six unassigned codons in M. luteus.
    • Kowal AK, Oliver JS Exploiting unassigned codons in Micrococcus fluteus for tRNA-based amino acid mutagenesis. Nucleic Acids Res. 25:1997;4685-4689. The authors highlight the use of unassigned codons for site-directed incorporation of non-native amino acids into proteins without the use of a stop codon. The model system described is based on the use of one of the six unassigned codons in M. luteus.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4685-4689
    • Kowal, A.K.1    Oliver, J.S.2
  • 12
    • 0030482172 scopus 로고    scopus 로고
    • Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids
    • Cload ST, Liu DR, Froland WA, Schultz PG Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids. Chem Biol. 3:1996;1033-1038.
    • (1996) Chem Biol , vol.3 , pp. 1033-1038
    • Cload, S.T.1    Liu, D.R.2    Froland, W.A.3    Schultz, P.G.4
  • 15
    • 0028099585 scopus 로고
    • Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices
    • Cornish VW, Kaplan MI, Veenstra DL, Kollman PA, Schultz PG Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices. Biochemistry. 33:1994;12022-12031.
    • (1994) Biochemistry , vol.33 , pp. 12022-12031
    • Cornish, V.W.1    Kaplan, M.I.2    Veenstra, D.L.3    Kollman, P.A.4    Schultz, P.G.5
  • 17
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G In vitro synthesis of protein in microbial systems. Annu Rev Genet. 7:1973;267-287.
    • (1973) Annu Rev Genet , vol.7 , pp. 267-287
    • Zubay, G.1
  • 18
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB A continuous cell-free translation system capable of producing polypeptides in high yield. Science. 242:1988;1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 19
    • 0032010706 scopus 로고    scopus 로고
    • Cell-free protein synthesis systems
    • Nakano H, Yamane T Cell-free protein synthesis systems. Biotechnol Adv. 16:1998;367-384.
    • (1998) Biotechnol Adv , vol.16 , pp. 367-384
    • Nakano, H.1    Yamane, T.2
  • 20
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim DM, Kigawa T, Choi CY, Yokoyama S A highly efficient cell-free protein synthesis system from Escherichia coli. Eur J Biochem. 239:1996;881-886.
    • (1996) Eur J Biochem , vol.239 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Choi, C.Y.3    Yokoyama, S.4
  • 21
    • 0031921676 scopus 로고    scopus 로고
    • E. coli-based in vitro transcription/translation: In vivo-specific synthesis rates and high yields in a batch system
    • Patnaik R, Swartz JR E. coli-based in vitro transcription/translation: in vivo-specific synthesis rates and high yields in a batch system. Biotechniques. 24:1998;862-868.
    • (1998) Biotechniques , vol.24 , pp. 862-868
    • Patnaik, R.1    Swartz, J.R.2
  • 23
    • 0032036838 scopus 로고    scopus 로고
    • Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis
    • This paper describes two methods for stable isotope labeling of proteins using cell-free translation. One special feature of this work is the utilization of a high yield optimized cell-free translation system. For example, 2.2 mg of site-directed isotope labeled (SDIL) c-Ha-Ras protein was synthesized from a 30 ml reaction system for the purpose of NMR analysis.
    • Yabuki T, Kigawa T, Dohmae N, Takio K, Terada T, Ito Y, Laue ED, Cooper JA, Kainosho M, Yokoyama S Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis. J Biomol NMR. 11:1998;295-306. This paper describes two methods for stable isotope labeling of proteins using cell-free translation. One special feature of this work is the utilization of a high yield optimized cell-free translation system. For example, 2.2 mg of site-directed isotope labeled (SDIL) c-Ha-Ras protein was synthesized from a 30 ml reaction system for the purpose of NMR analysis.
    • (1998) J Biomol NMR , vol.11 , pp. 295-306
    • Yabuki, T.1    Kigawa, T.2    Dohmae, N.3    Takio, K.4    Terada, T.5    Ito, Y.6    Laue, E.D.7    Cooper, J.A.8    Kainosho, M.9    Yokoyama, S.10
  • 24
    • 0030776931 scopus 로고    scopus 로고
    • Synthesis of region labeled proteins for MNR studies by in vitro translation of column-coupled mRNAs
    • This paper describes a novel method of in vitro translation that permits the isotope labeling of specific regions of a protein (region-directed isotope labeling). The translation is carried out using column bound mRNA and a specialized translation mix which is designed for labeling the particular region of the protein.
    • Pavlov MY, Freistroffer DV, Ehrenberg M Synthesis of region labeled proteins for MNR studies by in vitro translation of column-coupled mRNAs. Biochimie. 79:1997;415-422. This paper describes a novel method of in vitro translation that permits the isotope labeling of specific regions of a protein (region-directed isotope labeling). The translation is carried out using column bound mRNA and a specialized translation mix which is designed for labeling the particular region of the protein.
    • (1997) Biochimie , vol.79 , pp. 415-422
    • Pavlov, M.Y.1    Freistroffer, D.V.2    Ehrenberg, M.3
  • 25
    • 0032311418 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system
    • This report describes in vivo SNAAR using the Xenopus oocyte system. The authors also address the feasibility of incorporating non-native amino acids into ion channels and membrane receptors in mammalian cells.
    • Nowak MW, Gallivan JP, Silverman SK, Labarca CG, Dougherty DA, Lester HA In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system. Methods Enzymol. 293:1998;504-529. This report describes in vivo SNAAR using the Xenopus oocyte system. The authors also address the feasibility of incorporating non-native amino acids into ion channels and membrane receptors in mammalian cells.
    • (1998) Methods Enzymol , vol.293 , pp. 504-529
    • Nowak, M.W.1    Gallivan, J.P.2    Silverman, S.K.3    Labarca, C.G.4    Dougherty, D.A.5    Lester, H.A.6
  • 26
    • 0030984176 scopus 로고    scopus 로고
    • Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo
    • This article describes the construction of a novel tRNA-aminoacyl-tRNA synthetase pair by genetic manipulation and its use for in vivo site-specific incorporation of non-native amino acids into proteins.
    • Liu DR, Magliery TJ, Pastrnak M, Schultz PG Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo. Proc Natl Acad Sci USA. 94:1997;10092-10097. This article describes the construction of a novel tRNA-aminoacyl-tRNA synthetase pair by genetic manipulation and its use for in vivo site-specific incorporation of non-native amino acids into proteins.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10092-10097
    • Liu, D.R.1    Magliery, T.J.2    Pastrnak, M.3    Schultz, P.G.4
  • 28
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluoro phenylalanine incorporation in Escherichia coli
    • Pheamb/phenylalanyl-tRNA-synthetase pair expressed in an analogue-resistant E. coli strain.
    • Pheamb/phenylalanyl-tRNA-synthetase pair expressed in an analogue-resistant E. coli strain.
    • (1998) Protein Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 29
    • 0027383208 scopus 로고
    • Protein translocation across the ER membrane: A fluorescent light at the end of the tunnel
    • Johnson AE Protein translocation across the ER membrane: a fluorescent light at the end of the tunnel. Trends Biochem Sci. 18:1993;456-458.
    • (1993) Trends Biochem Sci , vol.18 , pp. 456-458
    • Johnson, A.E.1
  • 31
    • 0031042616 scopus 로고    scopus 로고
    • In vitro site-specific incorporation of fluorescent probes into β-galactosidase
    • This paper describes the incorporation of fluorescent amino acid analogs into β-galactosidase using a translation system derived from a special E. coli strain that is defective in one of the release factors. The authors describe how such a system may improve suppression efficiency for SNAAR.
    • Steward LE, Collins CS, Gilmore MA, Carlson JE, Ross JBA, Chamberlin AR In vitro site-specific incorporation of fluorescent probes into β-galactosidase. J Am Chem Soc. 119:1997;6-11. This paper describes the incorporation of fluorescent amino acid analogs into β-galactosidase using a translation system derived from a special E. coli strain that is defective in one of the release factors. The authors describe how such a system may improve suppression efficiency for SNAAR.
    • (1997) J Am Chem Soc , vol.119 , pp. 6-11
    • Steward, L.E.1    Collins, C.S.2    Gilmore, M.A.3    Carlson, J.E.4    Ross, J.B.A.5    Chamberlin, A.R.6
  • 32
    • 0032239857 scopus 로고    scopus 로고
    • Protein engineering with nonstandard amino acids
    • Steward LE, Chamberlin AR Protein engineering with nonstandard amino acids. Methods Mol Biol. 77:1998;325-354.
    • (1998) Methods Mol Biol , vol.77 , pp. 325-354
    • Steward, L.E.1    Chamberlin, A.R.2
  • 33
    • 0031391109 scopus 로고    scopus 로고
    • Fluorescent labeling of NK2 receptor at specific sites in vivo and fluorescence energy transfer analysis of NK2 ligand-receptor complexes
    • Turcatti G, Nemeth K, Edgerton MD, Knowles J, Vogel H, Chollet A Fluorescent labeling of NK2 receptor at specific sites in vivo and fluorescence energy transfer analysis of NK2 ligand-receptor complexes. Recept Channels. 5:1997;201-207.
    • (1997) Recept Channels , vol.5 , pp. 201-207
    • Turcatti, G.1    Nemeth, K.2    Edgerton, M.D.3    Knowles, J.4    Vogel, H.5    Chollet, A.6
  • 34
    • 0029838186 scopus 로고    scopus 로고
    • Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites
    • Turcatti G, Nemeth K, Edgerton MD, Meseth U, Talabot F, Peitsch M, Knowles J, Vogel H, Chollet A Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites. J Biol Chem. 271:1996;19991-19998.
    • (1996) J Biol Chem , vol.271 , pp. 19991-19998
    • Turcatti, G.1    Nemeth, K.2    Edgerton, M.D.3    Meseth, U.4    Talabot, F.5    Peitsch, M.6    Knowles, J.7    Vogel, H.8    Chollet, A.9
  • 35
    • 0031260274 scopus 로고    scopus 로고
    • Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins
    • The authors describe the use of biotin residues incorporated by SNAAR into the nicotinic acetylcholine receptor for probing surface-exposed regions. This approach should be very useful to explore the topology of a wide range of receptors and serve as an alternative to more conventional strategies, such as the cysteine substitution approach.
    • Gallivan JP, Lester HA, Dougherty DA Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins. Chem Biol. 4:1997;739-749. The authors describe the use of biotin residues incorporated by SNAAR into the nicotinic acetylcholine receptor for probing surface-exposed regions. This approach should be very useful to explore the topology of a wide range of receptors and serve as an alternative to more conventional strategies, such as the cysteine substitution approach.
    • (1997) Chem Biol , vol.4 , pp. 739-749
    • Gallivan, J.P.1    Lester, H.A.2    Dougherty, D.A.3
  • 36
    • 0001633622 scopus 로고
    • Construction of a light-activated protein by unnatural amino acid mutagenesis
    • Mendel D, Ellman JA, Schultz PG Construction of a light-activated protein by unnatural amino acid mutagenesis. J Am Chem Soc. 113:1991;2758-2760.
    • (1991) J Am Chem Soc , vol.113 , pp. 2758-2760
    • Mendel, D.1    Ellman, J.A.2    Schultz, P.G.3
  • 37
    • 0030923523 scopus 로고    scopus 로고
    • Site-specific, photochemical proteolysis applied to ion channels in vivo
    • This report describes the incorporation of 2-nitro-phenylglycine into membrane channel proteins at specific sites. This amino acid has the special property that upon irradiation it causes site-specific cleavage of the polypeptide chain.
    • England PM, Lester HA, Davidson N, Dougherty DA Site-specific, photochemical proteolysis applied to ion channels in vivo. Proc Natl Acad Sci USA. 94:1997;11025-11030. This report describes the incorporation of 2-nitro-phenylglycine into membrane channel proteins at specific sites. This amino acid has the special property that upon irradiation it causes site-specific cleavage of the polypeptide chain.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11025-11030
    • England, P.M.1    Lester, H.A.2    Davidson, N.3    Dougherty, D.A.4
  • 38
    • 0032495762 scopus 로고    scopus 로고
    • Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogs
    • Killian JA, Van Cleave MD, Shayo YF, Hecht SM Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogs. J Am Chem Soc. 120:1998;3032-3042.
    • (1998) J Am Chem Soc , vol.120 , pp. 3032-3042
    • Killian, J.A.1    Van Cleave, M.D.2    Shayo, Y.F.3    Hecht, S.M.4
  • 39
    • 0029743320 scopus 로고    scopus 로고
    • Firefly luciferase: Alteration of the color of emitted light resulting from substitutions at position 286
    • Mamaev SV, Laikhter AL, Arslan T, Hecht SM Firefly luciferase: alteration of the color of emitted light resulting from substitutions at position 286. J Am Chem Soc. 118:1996;7243-7244.
    • (1996) J Am Chem Soc , vol.118 , pp. 7243-7244
    • Mamaev, S.V.1    Laikhter, A.L.2    Arslan, T.3    Hecht, S.M.4
  • 40
    • 0023857532 scopus 로고
    • TRNA-mediated labeling of proteins with biotin: A nonradioactive method for the detection of cell-free translation products
    • Kurzchalia TV, Wiedmann M, Breter H, Zimmermann W, Bauschke E, Rapoport TA tRNA-mediated labeling of proteins with biotin: a nonradioactive method for the detection of cell-free translation products. Eur J Biochem. 172:1988;663-668.
    • (1988) Eur J Biochem , vol.172 , pp. 663-668
    • Kurzchalia, T.V.1    Wiedmann, M.2    Breter, H.3    Zimmermann, W.4    Bauschke, E.5    Rapoport, T.A.6
  • 42
    • 0031324890 scopus 로고    scopus 로고
    • Use of biotinylated-cysteinyl-tRNA as a non-RI probe in protein synthesis
    • Ohtsuka H, Yokogawa T, Asahara H, Nishikawa K Use of biotinylated-cysteinyl-tRNA as a non-RI probe in protein synthesis. Nucleic Acids Symp Ser. 37:1997;125-126.
    • (1997) Nucleic Acids Symp Ser , vol.37 , pp. 125-126
    • Ohtsuka, H.1    Yokogawa, T.2    Asahara, H.3    Nishikawa, K.4
  • 43
    • 0004944299 scopus 로고    scopus 로고
    • Promega: Protein translation in vitro
    • Wisconsin: Promega Corporation
    • Promega: Protein translation in vitro. In Protocols and Application Guide, edn 3. Wisconsin: Promega Corporation; 1996:261-276.
    • (1996) In Protocols and Application Guide, Edn 3. , pp. 261-276
  • 44
    • 0002229790 scopus 로고
    • Translation suppresion: When two wrongs do make a right
    • D. Soll, & U.L. RajBhandary. Washington DC: ASM Press
    • Murgola EJ Translation suppresion: when two wrongs do make a right. Soll D, RajBhandary UL tRNA: Structure, Biosynthesis and Function. 1995;491-509 ASM Press, Washington DC.
    • (1995) TRNA: Structure, Biosynthesis and Function , pp. 491-509
    • Murgola, E.J.1
  • 45
    • 0001359519 scopus 로고
    • Aminoacyl-tRNA synthetase: Occurrence, structure and function
    • D. Soll, & U.L. RajBhandary. Washington DC: ASM Press
    • Meinnel T, Mechulam Y, Blanquet S Aminoacyl-tRNA synthetase: occurrence, structure and function. Soll D, RajBhandary UL tRNA: Structure, Biosynthesis and Function. 1995;251-292 ASM Press, Washington DC.
    • (1995) TRNA: Structure, Biosynthesis and Function , pp. 251-292
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 46
    • 85030354168 scopus 로고    scopus 로고
    • US Patent 1997, no 5 654 722. Methods are disclosed for the non-radioactive labeling, detection, quantitation and isolation of nascent proteins translated in a cellular or cell-free translation system. Use of misaminoacylated tRNA molecules facilitates the detection and isolation of nascent protein from other components of the translation system
    • Rothschild KJ, Olejnik J, Sonar S: Methods for the detection and isolation of proteins. US Patent 1997, no 5 654 722. Methods are disclosed for the non-radioactive labeling, detection, quantitation and isolation of nascent proteins translated in a cellular or cell-free translation system. Use of misaminoacylated tRNA molecules facilitates the detection and isolation of nascent protein from other components of the translation system.
    • Methods for the Detection and Isolation of Proteins
    • Rothschild, K.J.1    Olejnik, J.2    Sonar, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.