메뉴 건너뛰기




Volumn 41, Issue 8, 2013, Pages 4573-4586

Two-step model of stop codon recognition by eukaryotic release factor eRF1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MESSENGER RNA; MUTANT PROTEIN; NUCLEOTIDE; PROTEIN ERF1; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 84877301308     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt113     Document Type: Article
Times cited : (46)

References (62)
  • 1
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev, L., Ehrenberg, M. and Frolova, L. (2003) Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J., 22, 175-182.
    • (2003) EMBO J , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.3
  • 3
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing, T.M. and Ramakrishnan, V. (2009) What recent ribosome structures have revealed about the mechanism of translation. Nature, 461, 1234-1242.
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 4
    • 77952928661 scopus 로고    scopus 로고
    • Ribosome structure and dynamics during translocation and termination
    • Dunkle, J.A. and Cate, J.H. (2010) Ribosome structure and dynamics during translocation and termination. Ann. Rev. Biophys., 39, 227-244.
    • (2010) Ann. Rev. Biophys , vol.39 , pp. 227-244
    • Dunkle, J.A.1    Cate, J.H.2
  • 5
    • 79955662779 scopus 로고    scopus 로고
    • Molecular recognition and catalysis in translation termination complexes
    • Klaholz, B.P. (2011) Molecular recognition and catalysis in translation termination complexes. Trends Biochem. Sci., 36, 282-292.
    • (2011) Trends Biochem. Sci , vol.36 , pp. 282-292
    • Klaholz, B.P.1
  • 6
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song, H., Mugnier, P., Das, A.K., Webb, H.M., Evans, D.R., Tuite, M.F., Hemmings, B.A. and Barford, D. (2000) The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell, 100, 311-321.
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8
  • 7
    • 0034069537 scopus 로고    scopus 로고
    • Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains
    • Frolova, L.Y., Merkulova, T.I. and Kisselev, L.L. (2000) Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains. RNA, 6, 381-390.
    • (2000) RNA , vol.6 , pp. 381-390
    • Frolova, L.Y.1    Merkulova, T.I.2    Kisselev, L.L.3
  • 8
    • 0033827056 scopus 로고    scopus 로고
    • Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
    • Bertram, G., Bell, H.A., Ritchie, D.W., Fullerton, G. and Stansfield, I. (2000) Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition. RNA, 6, 1236-1247.
    • (2000) RNA , vol.6 , pp. 1236-1247
    • Bertram, G.1    Bell, H.A.2    Ritchie, D.W.3    Fullerton, G.4    Stansfield, I.5
  • 9
    • 0035910449 scopus 로고    scopus 로고
    • Molecular mechanism of stop codon recognition by eRF1: A wobble hypothesis for peptide anticodons
    • Muramatsu, T., Heckmann, K., Kitanaka, C. and Kuchino, Y. (2001) Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons. FEBS Lett., 488, 105-109.
    • (2001) FEBS Lett , vol.488 , pp. 105-109
    • Muramatsu, T.1    Heckmann, K.2    Kitanaka, C.3    Kuchino, Y.4
  • 10
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova, L., Seit-Nebi, A. and Kisselev, L. (2002) Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1. RNA, 8, 129-136.
    • (2002) RNA , vol.8 , pp. 129-136
    • Frolova, L.1    Seit-Nebi, A.2    Kisselev, L.3
  • 11
    • 0037079664 scopus 로고    scopus 로고
    • Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: The evolution of stop codon specificity
    • Inagaki, Y., Blouin, C., Doolittle, W.F. and Roger, A.J. (2002) Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity. Nucleic Acids Res., 30, 532-544.
    • (2002) Nucleic Acids Res , vol.30 , pp. 532-544
    • Inagaki, Y.1    Blouin, C.2    Doolittle, W.F.3    Roger, A.J.4
  • 12
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • Seit-Nebi, A., Frolova, L. and Kisselev, L. (2002) Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1. EMBO Rep., 3, 881-886.
    • (2002) EMBO Rep , vol.3 , pp. 881-886
    • Seit-Nebi, A.1    Frolova, L.2    Kisselev, L.3
  • 13
    • 0043168057 scopus 로고    scopus 로고
    • Stop codons and UGG promote efficient binding of the polypeptide release factor eRF1 to the ribosomal A site
    • Chavatte, L., Frolova, L., Laugǎa, P., Kisselev, L. and Favre, A. (2003) Stop codons and UGG promote efficient binding of the polypeptide release factor eRF1 to the ribosomal A site. J. Mol. Biol., 331, 745-758.
    • (2003) J. Mol. Biol , vol.331 , pp. 745-758
    • Chavatte, L.1    Frolova, L.2    Laugǎa, P.3    Kisselev, L.4    Favre, A.5
  • 14
    • 14744303845 scopus 로고    scopus 로고
    • Newly sequenced eRF1s from ciliates: The diversity of stop codon usage and the molecular surfaces that are important for stop codon interactions
    • Kim, O.T., Yura, K., Go, N. and Harumoto, T. (2005) Newly sequenced eRF1s from ciliates: the diversity of stop codon usage and the molecular surfaces that are important for stop codon interactions. Gene, 346, 277-286.
    • (2005) Gene , vol.346 , pp. 277-286
    • Kim, O.T.1    Yura, K.2    Go, N.3    Harumoto, T.4
  • 16
    • 18844421633 scopus 로고    scopus 로고
    • Decoding the decoding region: Analysis of eukaryotic release factor (eRF1) stop codon-binding residues
    • Liang, H., Wong, J.Y., Bao, Q., Cavalcanti, A.R. and Landweber, L.F. (2005) Decoding the decoding region: analysis of eukaryotic release factor (eRF1) stop codon-binding residues. J. Mol. Evol., 60, 337-344.
    • (2005) J. Mol. Evol , vol.60 , pp. 337-344
    • Liang, H.1    Wong, J.Y.2    Bao, Q.3    Cavalcanti, A.R.4    Landweber, L.F.5
  • 17
    • 34547414394 scopus 로고    scopus 로고
    • Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors
    • Lekomtsev, S., Kolosov, P., Bidou, L., Frolova, L., Rousset, J.P. and Kisselev, L. (2007) Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors. Proc. Natl Acad. Sci. USA, 104, 10824-10829.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10824-10829
    • Lekomtsev, S.1    Kolosov, P.2    Bidou, L.3    Frolova, L.4    Rousset, J.P.5    Kisselev, L.6
  • 18
    • 84861385710 scopus 로고    scopus 로고
    • Identification of eRF1 residues that play critical and complementary roles in stop codon recognition
    • Conard, S.E., Buckley, J., Dang, M., Bedwell, G.J., Carter, R.L., Khass, M. and Bedwell, D.M. (2012) Identification of eRF1 residues that play critical and complementary roles in stop codon recognition. RNA, 18, 1210-1221.
    • (2012) RNA , vol.18 , pp. 1210-1221
    • Conard, S.E.1    Buckley, J.2    Dang, M.3    Bedwell, G.J.4    Carter, R.L.5    Khass, M.6    Bedwell, D.M.7
  • 19
    • 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
  • 20
    • 0035476654 scopus 로고    scopus 로고
    • Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition
    • Seit-Nebi, A., Frolova, L., Justesen, J. and Kisselev, L. (2001) Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition. Nucleic Acids Res., 29, 3982-3987.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 22
    • 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
  • 23
    • 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
  • 24
    • 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
  • 26
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov, A.V., Buckingham, R.H. and Ehrenberg, M. (2001) A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell, 107, 115-124.
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 27
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov, A.V., Mora, L., Buckingham, R.H. and Ehrenberg, M. (2002) Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell, 10, 789-798.
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 28
    • 36249001733 scopus 로고    scopus 로고
    • Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits
    • Gao, N., Zavialov, A.V., Ehrenberg, M. and Frank, J. (2007) Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits. J. Mol. Biol., 374, 1345-1358.
    • (2007) J. Mol. Biol , vol.374 , pp. 1345-1358
    • Gao, N.1    Zavialov, A.V.2    Ehrenberg, M.3    Frank, J.4
  • 29
    • 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
  • 30
    • 4344677977 scopus 로고    scopus 로고
    • GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination
    • Salas-Marco, J. and Bedwell, D.M. (2004) GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol. Cell. Biol., 24, 7769-7778.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7769-7778
    • Salas-Marco, J.1    Bedwell, D.M.2
  • 31
    • 33744993160 scopus 로고    scopus 로고
    • In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva, E.Z., Pisarev, A.V., Frolova, L.Y., Kisselev, L.L. and Pestova, T.V. (2006) In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell, 12, 1125-1136.
    • (2006) Cell , vol.12 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 33
    • 77955431163 scopus 로고    scopus 로고
    • Recognition of the amber UAG stop codon by release factor RF1
    • Korostelev, A., Zhu, J., Asahara, H. and Noller, H.F. (2010) Recognition of the amber UAG stop codon by release factor RF1. EMBO J., 29, 2577-2585.
    • (2010) EMBO J , vol.29 , pp. 2577-2585
    • Korostelev, A.1    Zhu, J.2    Asahara, H.3    Noller, H.F.4
  • 34
    • 29244487090 scopus 로고    scopus 로고
    • Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon
    • Petry, S., Brodersen, D.E., Murphy, F.V., Dunham, C.M., Selmer, M., Tarry, M.J., Kelley, A.C. and Ramakrishnan, V. (2005) Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon. Cell, 123, 1255-1266.
    • (2005) Cell , vol.123 , pp. 1255-1266
    • Petry, S.1    Brodersen, D.E.2    Murphy, F.V.3    Dunham, C.M.4    Selmer, M.5    Tarry, M.J.6    Kelley, A.C.7    Ramakrishnan, V.8
  • 36
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem, A., Jenner, L., Yusupova, G. and Yusupov, M. (2010) Crystal structure of the eukaryotic ribosome. Science, 330, 1203-1209.
    • (2010) Science , vol.330 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 38
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl, J., Leibundgut, M., Ataide, S.F., Haag, A. and Ban, N. (2011) Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science, 331, 730-736.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 39
    • 0036792666 scopus 로고    scopus 로고
    • The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome
    • Chavatte, L., Seit-Nebi, A., Dubovaya, V. and Favre, A. (2002) The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBO J., 21, 5302-5311.
    • (2002) EMBO J , vol.21 , pp. 5302-5311
    • Chavatte, L.1    Seit-Nebi, A.2    Dubovaya, V.3    Favre, A.4
  • 41
    • 0033784538 scopus 로고    scopus 로고
    • Functional sites of interaction between release factor RF1 and the ribosome
    • Wilson, K.S., Ito, K., Noller, H.F. and Nakamura, Y. (2000) Functional sites of interaction between release factor RF1 and the ribosome. Nat. Struct. Biol., 7, 866-870.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 866-870
    • Wilson, K.S.1    Ito, K.2    Noller, H.F.3    Nakamura, Y.4
  • 42
    • 0037173091 scopus 로고    scopus 로고
    • Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1
    • Ito, K., Frolova, L., Seit-Nebi, A., Karamyshev, A., Kisselev, L. and Nakamura, Y. (2002) Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1. Proc. Natl Acad. Sci. USA, 99, 8494-8499.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8494-8499
    • Ito, K.1    Frolova, L.2    Seit-Nebi, A.3    Karamyshev, A.4    Kisselev, L.5    Nakamura, Y.6
  • 44
    • 78650923220 scopus 로고    scopus 로고
    • Functional characterization of polypeptide release factor 1b in the ciliate Euplotes
    • Wang, Y., Chai, B., Wang, W. and Liang, A. (2010) Functional characterization of polypeptide release factor 1b in the ciliate Euplotes. Biosci. Rep., 30, 425-431.
    • (2010) Biosci. Rep , vol.30 , pp. 425-431
    • Wang, Y.1    Chai, B.2    Wang, W.3    Liang, A.4
  • 46
    • 84863226738 scopus 로고    scopus 로고
    • Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1
    • Wong, L.E., Li, Y., Pillay, S., Frolova, L. and Pervushin, K. (2012) Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1. Nucleic Acids Res., 40, 5751-5765.
    • (2012) Nucleic Acids Res , vol.40 , pp. 5751-5765
    • Wong, L.E.1    Li, Y.2    Pillay, S.3    Frolova, L.4    Pervushin, K.5
  • 48
    • 79551484186 scopus 로고    scopus 로고
    • A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity
    • Eliseev, B., Kryuchkova, P., Alkalaeva, E. and Frolova, L. (2011) A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity. Nucleic Acids Res., 39, 599-608.
    • (2011) Nucleic Acids Res , vol.39 , pp. 599-608
    • Eliseev, B.1    Kryuchkova, P.2    Alkalaeva, E.3    Frolova, L.4
  • 49
    • 0016017204 scopus 로고
    • Mammalian release factor: In vitro assay and purification
    • Caskey, C.N., Beaudet, A.L. and Tate, W.P. (1974) Mammalian release factor: in vitro assay and purification. Methods Enzymol., 30, 293-303.
    • (1974) Methods Enzymol , vol.30 , pp. 293-303
    • Caskey, C.N.1    Beaudet, A.L.2    Tate, W.P.3
  • 52
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1-and ribosome-dependent guanosine triphosphatase
    • Frolova, L., Le Goff, X., 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    Le Goff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 53
    • 15244354879 scopus 로고    scopus 로고
    • Translation toeprinting assays using fluorescently labeled primers and capillary electrophoresis
    • Gould, P.S., Bird, H. and Easton, A.J. (2005) Translation toeprinting assays using fluorescently labeled primers and capillary electrophoresis. Biotechniques, 38, 397-400.
    • (2005) Biotechniques , vol.38 , pp. 397-400
    • Gould, P.S.1    Bird, H.2    Easton, A.J.3
  • 55
    • 38649111610 scopus 로고    scopus 로고
    • The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome
    • Andreev, D., Hauryliuk, V., Terenin, I., Dmitriev, S., Ehrenberg, M. and Shatsky, I. (2008) The bacterial toxin RelE induces specific mRNA cleavage in the A site of the eukaryote ribosome. RNA, 14, 233-239.
    • (2008) RNA , vol.14 , pp. 233-239
    • Andreev, D.1    Hauryliuk, V.2    Terenin, I.3    Dmitriev, S.4    Ehrenberg, M.5    Shatsky, I.6
  • 57
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan, R. and Totrov, M. (1994) Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol., 235, 983-1002.
    • (1994) J. Mol. Biol , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 59
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C. and van der Spoel, D. (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput., 4, 435-447.
    • (2008) J. Chem. Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3
  • 61
    • 0345146926 scopus 로고    scopus 로고
    • Stop codon selection in eukaryotic translation termination: Comparison of the discriminating potential between human and ciliate eRF1s
    • Chavatte, L., Kervestin, S., Favre, A. and Jean-Jean, O. (2003) Stop codon selection in eukaryotic translation termination: comparison of the discriminating potential between human and ciliate eRF1s. EMBO J., 22, 1644-1653.
    • (2003) EMBO J , vol.22 , pp. 1644-1653
    • Chavatte, L.1    Kervestin, S.2    Favre, A.3    Jean-Jean, O.4
  • 62
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia, N.T., Lareau, L.F. and Weissman, J.S. (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell, 147, 789-802.
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.