메뉴 건너뛰기




Volumn 100, Issue 3, 2000, Pages 311-321

The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CRYSTAL STRUCTURE; HUMAN; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN SYNTHESIS; SIGNAL TRANSDUCTION; STOP CODON; TRANSCRIPTION TERMINATION;

EID: 0034603210     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80667-4     Document Type: Article
Times cited : (396)

References (58)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of the bovine mitochondrial F1 ATPase
    • Abrahams, J.P., and Leslie, A.G.W. (1996). Methods used in the structure determination of the bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30-42.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 3
    • 0030466725 scopus 로고    scopus 로고
    • The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1
    • Andjelkovic, N., Zolnierowicz, S., Van Hoof, C., Goris, J., and Hemmings, B.A. (1996). The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15, 7156-7167.
    • (1996) EMBO J. , vol.15 , pp. 7156-7167
    • Andjelkovic, N.1    Zolnierowicz, S.2    Van Hoof, C.3    Goris, J.4    Hemmings, B.A.5
  • 4
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton, G.J. (1990). Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183, 403-428.
    • (1990) Methods Enzymol. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: A tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 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., and Bedwell, D.M. (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    Bedwell, D.M.4
  • 7
    • 0028559880 scopus 로고
    • Direct recognition of mRNA stop signals by Escherichia coli polypeptide chain release factor 2
    • Brown, C.M., and Tate, W.P. (1994). Direct recognition of mRNA stop signals by Escherichia coli polypeptide chain release factor 2. J. Biol. Chem. 269, 33164-33170.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33164-33170
    • Brown, C.M.1    Tate, W.P.2
  • 8
    • 0025315173 scopus 로고
    • The signal for the termination of protein synthesis in prokaryotes
    • Brown, C.M., Stockwell, P.A., Trotman, C.N., and Tate, W.P. (1990). The signal for the termination of protein synthesis in prokaryotes. Nucleic Acids Res. 18, 2079-2086.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2079-2086
    • Brown, C.M.1    Stockwell, P.A.2    Trotman, C.N.3    Tate, W.P.4
  • 11
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structures of 70S ribosome functional complexes
    • Cate, J.H., Yusupov, M.M., Yusupova, G.Z., Earnest, T.N., and Noller, H.F. (1999). X-ray crystal structures of 70S ribosome functional complexes. Science 285, 2095-2104.
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 12
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project no.4.) (1994). The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 13
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modifiation calculations
    • Cowtan, K., and Main, P. (1996). Phase combination and cross validation in iterated density-modifiation calculations. Acta Crystallogr. D 52, 43-48.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 43-48
    • Cowtan, K.1    Main, P.2
  • 14
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski, J., Wang, J., Steitz, T.A., and Moore, P.B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 15
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameters refinement in the MIR and MAD methods
    • De la Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameters refinement in the MIR and MAD methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De la Fortelle, E.1    Bricogne, G.2
  • 16
    • 0023770831 scopus 로고
    • Transfer RNA-mediated suppression of termination codons in E. coli
    • Eggertsson, G., and Soll, P. (1988). Transfer RNA-mediated suppression of termination codons in E. coli. Microbiol. Rev. 52, 354-379.
    • (1988) Microbiol. Rev. , vol.52 , pp. 354-379
    • Eggertsson, G.1    Soll, P.2
  • 17
    • 0032937983 scopus 로고    scopus 로고
    • The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
    • Eurwilaichitr, L., Graves, F.M., Stansfield, I., and Tuite, M.F. (1999). The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol. Microbiol. 32, 485-496.
    • (1999) Mol. Microbiol. , vol.32 , pp. 485-496
    • Eurwilaichitr, L.1    Graves, F.M.2    Stansfield, I.3    Tuite, M.F.4
  • 18
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer, D.V., Pavlov, M.Y., MacDougall, J., Buckingham, R.H., and Ehrenberg, M. (1997). Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 16, 4126-4133.
    • (1997) EMBO J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 20
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome dependent guanosine triphosphatase
    • Frolova, L., Goff, X.L., Zhouravleva, G., Davydova, E., Philippe, M., and Kisselev, L. (1996). Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome dependent guanosine triphosphatase. RNA 2, 334-341.
    • (1996) RNA , vol.2 , pp. 334-341
    • Frolova, L.1    Goff, X.L.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 21
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • Frolova, L.Y., Tsivkovskii, R.Y., Sivolobova, G.F., Oparina, N.Y., Serpinsky, O.I., Blinov, V.M., Tatkov, S.I., and Kisselev, L.L. (1999). Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5, 1014-1020.
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6    Tatkov, S.I.7    Kisselev, L.L.8
  • 24
    • 0030995429 scopus 로고    scopus 로고
    • Ribosomal binding site of release factors RF1 and RF2. A new translational termination assay in vitro
    • Grentzmann, G., and Kelly, P.J. (1997). Ribosomal binding site of release factors RF1 and RF2. A new translational termination assay in vitro. J. Biol. Chem. 272, 12300-12304.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12300-12304
    • Grentzmann, G.1    Kelly, P.J.2
  • 26
    • 0029975504 scopus 로고    scopus 로고
    • Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis
    • Ito, K., Ebihara, K., Uno, M., and Nakamura, Y. (1996). Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc. Natl. Acad. Sci. USA 93, 5443-5448.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5443-5448
    • Ito, K.1    Ebihara, K.2    Uno, M.3    Nakamura, Y.4
  • 27
    • 0031857784 scopus 로고    scopus 로고
    • The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast
    • Ito, K., Ebihara, K., and Nakamura, Y. (1998). The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. RNA 4, 958-972.
    • (1998) RNA , vol.4 , pp. 958-972
    • Ito, K.1    Ebihara, K.2    Nakamura, Y.3
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 489-501.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 489-501
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0017744989 scopus 로고
    • Characterization of reticulocyte release factor
    • Konecki, D.S., Aune, K.C., Tate, W., and Caskey, C.T. (1977). Characterization of reticulocyte release factor. J. Biol. Chem. 252, 4514-4520.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4514-4520
    • Konecki, D.S.1    Aune, K.C.2    Tate, W.3    Caskey, C.T.4
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. App. Crystallog. 24, 946-950.
    • (1991) J. App. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0031848912 scopus 로고    scopus 로고
    • Efficient in vitro translation termination in E. coli is constrained by the orientations of the release factor, stop signal and peptidly-tRNA within the termination complex
    • McCaughan, K.K., Poole, E.S., Pel, H.J., Mansell, J.B., Mannering, S.A., and Tate, W.P. (1998). Efficient in vitro translation termination in E. coli is constrained by the orientations of the release factor, stop signal and peptidly-tRNA within the termination complex. Biol. Chem. 379, 857-866.
    • (1998) Biol. Chem. , vol.379 , pp. 857-866
    • McCaughan, K.K.1    Poole, E.S.2    Pel, H.J.3    Mansell, J.B.4    Mannering, S.A.5    Tate, W.P.6
  • 32
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merit, E.A., and Murphy, M.E.P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merit, E.A.1    Murphy, M.E.P.2
  • 33
    • 0032969177 scopus 로고    scopus 로고
    • C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction
    • Merkulova, T.I., Frolova, L.Y., Lazar, M., Camonis, J., and Kisselev, L.L. (1999). C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction. FEBS Lett. 443, 41-47.
    • (1999) FEBS Lett. , vol.443 , pp. 41-47
    • Merkulova, T.I.1    Frolova, L.Y.2    Lazar, M.3    Camonis, J.4    Kisselev, L.L.5
  • 36
    • 0022671052 scopus 로고
    • Nuclear-mitochondrial-interactions in yeast: Mitochondrial mutations compensating respiratory deficiency of sup1 and sup2 mutants
    • Russia
    • Mironova, L.N., Zelenaya, O.A., and Ter-Avanesyan, M.D. (1986). Nuclear-mitochondrial-interactions in yeast: Mitochondrial mutations compensating respiratory deficiency of sup1 and sup2 mutants. Genetica (Russia) 22, 200-208.
    • (1986) Genetica , vol.22 , pp. 200-208
    • Mironova, L.N.1    Zelenaya, O.A.2    Ter-Avanesyan, M.D.3
  • 37
    • 0028305727 scopus 로고
    • A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity
    • Moffat, J.G., and Tate, W.P. (1994). A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity. J. Biol. Chem. 269, 18899-18903.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18899-18903
    • Moffat, J.G.1    Tate, W.P.2
  • 38
    • 0032189779 scopus 로고    scopus 로고
    • The influence of the 5′ codon context on translation termination in Saccharomyces cerevisiae
    • Mottagui-Tabar, S., Tuite, M.F., and Isaksson, L.A. (1998). The influence of the 5′ codon context on translation termination in Saccharomyces cerevisiae. Eur. J. Biochem. 257, 249-254.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 249-254
    • Mottagui-Tabar, S.1    Tuite, M.F.2    Isaksson, L.A.3
  • 39
    • 0028990057 scopus 로고
    • The RNP domain: A sequence-specific RNA-binding domain involved in processing and transport of RNA
    • Nagai, K., Oubridge, C., Ito, N., Avis, J., and Evans, P. (1995). The RNP domain: A sequence-specific RNA-binding domain involved in processing and transport of RNA. Trends Biochem. Sci. 20, 235-240.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 40
    • 0031901175 scopus 로고    scopus 로고
    • How protein reads the stop codon and terminates translation
    • Nakamura, Y., and Ito, K. (1998). How protein reads the stop codon and terminates translation. Genes Cells 3, 265-278.
    • (1998) Genes Cells , vol.3 , pp. 265-278
    • Nakamura, Y.1    Ito, K.2
  • 41
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 43
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl-transferase to protein extraction procedures
    • Noller, H.F., Hoffarth, V., and Zimniak, L. (1992). Unusual resistance of peptidyl-transferase to protein extraction procedures. Science 256, 1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 44
    • 0032562586 scopus 로고    scopus 로고
    • Visualisation of the cysteinyl-phosphate intermediate of a protein tyrosine phosphatase by X-ray crystallography
    • Pannifer, A.D., Flint, A.J., Tonks, N.K., and Barford, D. (1998). Visualisation of the cysteinyl-phosphate intermediate of a protein tyrosine phosphatase by X-ray crystallography. J. Biol. Chem. 273, 10454-10462.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10454-10462
    • Pannifer, A.D.1    Flint, A.J.2    Tonks, N.K.3    Barford, D.4
  • 45
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy-atom parameters
    • Proceedings of the CCP4 Study Weekend, 25-26, W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Warrington, UK: SERC Daresbury Laboratory)
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy-atom parameters. In Isomorphous Replacement and Anomalous Scattering. Proceedings of the CCP4 Study Weekend, 25-26, W. Wolf, P.R. Evans, and A.G.W. Leslie, eds. (Warrington, UK: SERC Daresbury Laboratory), pp. 80-86.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 46
    • 0028821311 scopus 로고
    • The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli
    • Poole, E.S., Brown, C.M., and Tate, W.P. (1995). The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli. EMBO J. 14, 151-158.
    • (1995) EMBO J. , vol.14 , pp. 151-158
    • Poole, E.S.1    Brown, C.M.2    Tate, W.P.3
  • 47
    • 0030842711 scopus 로고    scopus 로고
    • Decoding the translational termination signal: The polypeptide chain release factor in Escherichia coli crosslinks to the base following the stop codon
    • Poole, E.S., Brimacombe, R., and Tate, W.P. (1997). Decoding the translational termination signal: The polypeptide chain release factor in Escherichia coli crosslinks to the base following the stop codon. RNA 3, 974-982.
    • (1997) RNA , vol.3 , pp. 974-982
    • Poole, E.S.1    Brimacombe, R.2    Tate, W.P.3
  • 48
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, C.T., Graziano, V., Lee, P.J., and Sweet, R.M. (1993). Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, C.T.2    Graziano, V.3    Lee, P.J.4    Sweet, R.M.5
  • 49
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 50
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek, K., Ahmadian, M.R., Kabsch, W., Wiesmuller, L., Lautwein, A., Schmitz, F., and Wittinghofer, A. (1997). The Ras-RasGap complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 227, 333-338.
    • (1997) Science , vol.227 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5    Schmitz, F.6    Wittinghofer, A.7
  • 52
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 54
    • 0028946816 scopus 로고
    • A mutant allele of the SUP45 (SAL4) gene of Saccharomyces cerevisiae shows temperature-dependent allosuppressor and omnipotent suppressor phenotypes
    • Stansfield, I., Akhmaloka, and Tuite, M.F. (1995b). A mutant allele of the SUP45 (SAL4) gene of Saccharomyces cerevisiae shows temperature-dependent allosuppressor and omnipotent suppressor phenotypes. Curr. Genet. 27, 417-426.
    • (1995) Curr. Genet. , vol.27 , pp. 417-426
    • Stansfield, I.1    Akhmaloka2    Tuite, M.F.3
  • 55
    • 0029992246 scopus 로고    scopus 로고
    • Depletion in the levels of the release factor eRF1 causes a reduction in the efficiency of translation termination in yeast
    • Stansfield, I., Eurwilaichitr, L., Akhmaloka, and Tuite, M.F. (1996). Depletion in the levels of the release factor eRF1 causes a reduction in the efficiency of translation termination in yeast. Mol. Microbiol. 20, 1135-1143.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1135-1143
    • Stansfield, I.1    Eurwilaichitr, L.2    Akhmaloka3    Tuite, M.F.4
  • 56
    • 0030957794 scopus 로고    scopus 로고
    • A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae
    • Stansfield, I., Kushnirov, V.V., Jones, K.M., and Tuite, M.F. (1997). A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 245, 557-563.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 557-563
    • Stansfield, I.1    Kushnirov, V.V.2    Jones, K.M.3    Tuite, M.F.4
  • 57
    • 0025092680 scopus 로고
    • Codon recognition in polypeptide chain termination: Site directed crosslinking of termination codons to Escherichia coli release factor 2
    • Tate, W., Greuer, B., and Brimacombe, R. (1990). Codon recognition in polypeptide chain termination: Site directed crosslinking of termination codons to Escherichia coli release factor 2. Nucleic Acids Res. 18, 6537-6544.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6537-6544
    • Tate, W.1    Greuer, B.2    Brimacombe, R.3
  • 58
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva, G., Frolova, L., Le Goff, X., Le Guellec, R., Inge-Vechtomov, S., Kisselev, L., and Philippe, M. (1995). Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 14, 4065-4072.
    • (1995) EMBO J. , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1    Frolova, L.2    Le Goff, X.3    Le Guellec, R.4    Inge-Vechtomov, S.5    Kisselev, L.6    Philippe, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.