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Volumn 18, Issue 5, 2011, Pages 589-600

Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE; ANTIINFECTIVE AGENT; BACTERIOCIN; ELONGATION FACTOR G; EVERNINOMICIN; INITIATION FACTOR 2; MICROCOCCIN; PEPTIDE; THIOSTREPTON;

EID: 79957467219     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.03.010     Document Type: Article
Times cited : (37)

References (80)
  • 1
    • 0034426125 scopus 로고    scopus 로고
    • Presence of variations in ribosomal protein L16 corresponding to susceptibility of enterococci to oligosaccharides (avilamycin and evernimicin)
    • DOI 10.1128/AAC.44.12.3425-3427.2000
    • F.M. Aarestrup, and L.B. Jensen Presence of variations in ribosomal protein L16 corresponding to susceptibility of enterococci to oligosaccharides (Avilamycin and evernimicin) Antimicrob. Agents Chemother. 44 2000 3425 3427 (Pubitemid 33009504)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.12 , pp. 3425-3427
    • Aarestrup, F.M.1    Jensen, L.B.2
  • 3
    • 0033996649 scopus 로고    scopus 로고
    • Mutations in ribosomal protein L16 conferring reduced susceptibility to evernimicin (SCH27899): Implications for mechanism of action
    • DOI 10.1128/AAC.44.3.732-738.2000
    • P.V. Adrian, W. Zhao, T.A. Black, K.J. Shaw, R.S. Hare, and K.P. Klugman Mutations in ribosomal protein L16 conferring reduced susceptibility to evernimicin (SCH27899): implications for mechanism of action Antimicrob. Agents Chemother. 44 2000 732 738 (Pubitemid 30117970)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.3 , pp. 732-738
    • Adrian, P.V.1    Zhao, W.2    Black, T.A.3    Shaw, K.J.4    Hare, R.S.5    Klugman, K.P.6
  • 4
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • DOI 10.1016/j.cell.2005.03.023, PII S0092867405002953
    • G.S. Allen, A. Zavialov, R. Gursky, M. Ehrenberg, and J. Frank The cryo-EM structure of a translation initiation complex from Escherichia coli Cell 121 2005 703 712 (Pubitemid 40797593)
    • (2005) Cell , vol.121 , Issue.5 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 5
    • 33745763700 scopus 로고    scopus 로고
    • How initiation factors tune the rate of initiation of protein synthesis in bacteria
    • DOI 10.1038/sj.emboj.7601140, PII 7601140
    • A. Antoun, M.Y. Pavlov, M. Lovmar, and M. Ehrenberg How initiation factors tune the rate of initiation of protein synthesis in bacteria EMBO J. 25 2006 2539 2550 (Pubitemid 44012236)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2539-2550
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 9
    • 77953718212 scopus 로고    scopus 로고
    • Probing translation with small-molecule inhibitors
    • S.C. Blanchard, B.S. Cooperman, and D.N. Wilson Probing translation with small-molecule inhibitors Chem. Biol. 17 2010 633 645
    • (2010) Chem. Biol. , vol.17 , pp. 633-645
    • Blanchard, S.C.1    Cooperman, B.S.2    Wilson, D.N.3
  • 11
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • DOI 10.1016/S0022-2836(02)00235-8
    • D.M. Cameron, J. Thompson, P.E. March, and A.E. Dahlberg Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome J. Mol. Biol. 319 2002 27 35 (Pubitemid 34729484)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 12
    • 0344443255 scopus 로고    scopus 로고
    • Ribosomal Protection Proteins and Their Mechanism of Tetracycline Resistance
    • DOI 10.1128/AAC.47.12.3675-3681.2003
    • S.R. Connell, D.M. Tracz, K.H. Nierhaus, and D.E. Taylor Ribosomal protection proteins and their mechanism of tetracycline resistance Antimicrob. Agents Chemother. 47 2003 3675 3681 (Pubitemid 37484970)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.12 , pp. 3675-3681
    • Connell, S.R.1    Tracz, D.M.2    Nierhaus, K.H.3    Taylor, D.E.4
  • 16
    • 0019483431 scopus 로고
    • Concerning the mode of action of micrococcin upon bacterial protein synthesis
    • DOI 10.1111/j.1432-1033.1981.tb05484.x
    • E. Cundliffe, and J. Thompson Concerning the mode of action of micrococcin upon bacterial protein synthesis Eur. J. Biochem. 118 1981 47 52 (Pubitemid 11023719)
    • (1981) European Journal of Biochemistry , vol.118 , Issue.1 , pp. 47-52
    • Cundliffe, E.1    Thompson, J.2
  • 17
    • 0031876998 scopus 로고    scopus 로고
    • Binding interaction between Tet(M) and the ribosome: Requirements for binding
    • K.A. Dantley, H.K. Dannelly, and V. Burdett Binding interaction between Tet(M) and the ribosome: requirements for binding J. Bacteriol. 180 1998 4089 4092 (Pubitemid 28373510)
    • (1998) Journal of Bacteriology , vol.180 , Issue.16 , pp. 4089-4092
    • Dantley, K.A.1    Dannelly, H.K.2    Burdett, V.3
  • 18
    • 28444441961 scopus 로고    scopus 로고
    • Interaction of the G′ domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM
    • DOI 10.1016/j.molcel.2005.10.028, PII S1097276505017235
    • P.P. Datta, M.R. Sharma, L. Qi, J. Frank, and R.K. Agrawal Interaction of the G′ domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM Mol. Cell 20 2005 723 731 (Pubitemid 41740694)
    • (2005) Molecular Cell , vol.20 , Issue.5 , pp. 723-731
    • Datta, P.P.1    Sharma, M.R.2    Qi, L.3    Frank, J.4    Agrawal, R.K.5
  • 19
    • 50249130207 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium BipA exhibits two distinct ribosome binding modes
    • M.A. deLivron, and V.L. Robinson Salmonella enterica serovar Typhimurium BipA exhibits two distinct ribosome binding modes J. Bacteriol. 190 2008 5944 5952
    • (2008) J. Bacteriol. , vol.190 , pp. 5944-5952
    • Delivron, M.A.1    Robinson, V.L.2
  • 20
    • 70449431778 scopus 로고    scopus 로고
    • A novel domain in translational GTPase BipA mediates interaction with the 70S ribosome and influences GTP hydrolysis
    • M.A. deLivron, H.S. Makanji, M.C. Lane, and V.L. Robinson A novel domain in translational GTPase BipA mediates interaction with the 70S ribosome and influences GTP hydrolysis Biochemistry 48 2009 10533 10541
    • (2009) Biochemistry , vol.48 , pp. 10533-10541
    • Delivron, M.A.1    Makanji, H.S.2    Lane, M.C.3    Robinson, V.L.4
  • 21
    • 21244465843 scopus 로고    scopus 로고
    • Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTpase activation
    • DOI 10.1016/j.cell.2005.04.015, PII S0092867405003958
    • M. Diaconu, U. Kothe, F. Schlunzen, N. Fischer, J.M. Harms, A.G. Tonevitsky, H. Stark, M.V. Rodnina, and M.C. Wahl Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation Cell 121 2005 991 1004 (Pubitemid 40884392)
    • (2005) Cell , vol.121 , Issue.7 , pp. 991-1004
    • Diaconu, M.1    Kothe, U.2    Schlunzen, F.3    Fischer, N.4    Harms, J.M.5    Tonevitsky, A.G.6    Stark, H.7    Rodnina, M.V.8    Wahl, M.C.9
  • 22
    • 0022518007 scopus 로고
    • Lep operon proximal gene is not required for growth or secretion by Escherichia coli
    • N.J. Dibb, and P.B. Wolfe lep operon proximal gene is not required for growth or secretion by Escherichia coli J. Bacteriol. 166 1986 83 87 (Pubitemid 16043284)
    • (1986) Journal of Bacteriology , vol.166 , Issue.1 , pp. 83-87
    • Dibb, N.J.1    Wolfe, P.B.2
  • 24
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Y.G. Gao, M. Selmer, C.M. Dunham, A. Weixlbaumer, A.C. Kelley, and V. Ramakrishnan The structure of the ribosome with elongation factor G trapped in the posttranslocational state Science 326 2009 694 699
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1    Selmer, M.2    Dunham, C.M.3    Weixlbaumer, A.4    Kelley, A.C.5    Ramakrishnan, V.6
  • 25
    • 36248958685 scopus 로고    scopus 로고
    • Thiostrepton inhibition of tRNA delivery to the ribosome
    • DOI 10.1261/rna.499407
    • R.L. Gonzalez Jr., S. Chu, and J.D. Puglisi Thiostrepton inhibition of tRNA delivery to the ribosome RNA 13 2007 2091 2097 (Pubitemid 350127551)
    • (2007) RNA , vol.13 , Issue.12 , pp. 2091-2097
    • Gonzalez Jr., R.L.1    Chu, S.2    Puglisi, J.D.3
  • 26
    • 34748843156 scopus 로고    scopus 로고
    • A Quantitative Kinetic Scheme for 70S Translation Initiation Complex Formation
    • DOI 10.1016/j.jmb.2007.07.032, PII S002228360700959X
    • C. Grigoriadou, S. Marzi, S. Kirillov, C.O. Gualerzi, and B.S. Cooperman A quantitative kinetic scheme for 70 S translation initiation complex formation J. Mol. Biol. 373 2007 562 572 (Pubitemid 47488388)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.3 , pp. 562-572
    • Grigoriadou, C.1    Marzi, S.2    Kirillov, S.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 27
    • 0009673347 scopus 로고
    • Inhibition by thiostrepton of the IF-2-dependent ribosomal GTPase
    • M. Grunberg-Manago, J. Dondon, and M. Graffe Inhibition by thiostrepton of the IF-2-dependent ribosomal GTPase FEBS Lett. 22 1972 217 221
    • (1972) FEBS Lett. , vol.22 , pp. 217-221
    • Grunberg-Manago, M.1    Dondon, J.2    Graffe, M.3
  • 28
    • 0015500284 scopus 로고
    • Requirement of an E. coli 50S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate
    • E. Hamel, M. Koka, and T. Nakamoto Requirement of an E. coli 50S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate J. Biol. Chem. 247 1972 805 814
    • (1972) J. Biol. Chem. , vol.247 , pp. 805-814
    • Hamel, E.1    Koka, M.2    Nakamoto, T.3
  • 29
    • 41549163979 scopus 로고    scopus 로고
    • Translational Regulation via L11: Molecular Switches on the Ribosome Turned On and Off by Thiostrepton and Micrococcin
    • DOI 10.1016/j.molcel.2008.01.009, PII S1097276508000440
    • J.M. Harms, D.N. Wilson, F. Schluenzen, S.R. Connell, T. Stachelhaus, Z. Zaborowska, C.M. Spahn, and P. Fucini Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin Mol. Cell 30 2008 26 38 (Pubitemid 351470144)
    • (2008) Molecular Cell , vol.30 , Issue.1 , pp. 26-38
    • Harms, J.M.1    Wilson, D.N.2    Schluenzen, F.3    Connell, S.R.4    Stachelhaus, T.5    Zaborowska, Z.6    Spahn, C.M.T.7    Fucini, P.8
  • 30
    • 33751532962 scopus 로고    scopus 로고
    • The Ribosomal Stalk Binds to Translation Factors IF2, EF-Tu, EF-G and RF3 via a Conserved Region of the L12 C-terminal Domain
    • DOI 10.1016/j.jmb.2006.10.025, PII S0022283606013635
    • M. Helgstrand, C.S. Mandava, F.A. Mulder, A. Liljas, S. Sanyal, and M. Akke The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain J. Mol. Biol. 365 2007 468 479 (Pubitemid 44838724)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.2 , pp. 468-479
    • Helgstrand, M.1    Mandava, C.S.2    Mulder, F.A.A.3    Liljas, A.4    Sanyal, S.5    Akke, M.6
  • 31
    • 77953082717 scopus 로고    scopus 로고
    • The ribosomal stalk plays a key role in IF2-mediated association of the ribosomal subunits
    • C. Huang, C.S. Mandava, and S. Sanyal The ribosomal stalk plays a key role in IF2-mediated association of the ribosomal subunits J. Mol. Biol. 399 2010 145 153
    • (2010) J. Mol. Biol. , vol.399 , pp. 145-153
    • Huang, C.1    Mandava, C.S.2    Sanyal, S.3
  • 32
    • 35648951171 scopus 로고    scopus 로고
    • From amino acids to heteroaromatics - Thiopeptide antibiotics, nature's heterocyclic peptides
    • DOI 10.1002/anie.200700728
    • R.A. Hughes, and C.J. Moody From amino acids to heteroaromatics - thiopeptide antibiotics, nature's heterocyclic peptides Angew. Chem. Int. Ed. Engl. 46 2007 7930 7954 (Pubitemid 350033464)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.42 , pp. 7930-7954
    • Hughes, R.A.1    Moody, C.J.2
  • 33
    • 0015215464 scopus 로고
    • Reconstitution of a GTPase activity by a 50S ribosomal protein from E. coli
    • K. Kischa, W. Möller, and G. Stöffler Reconstitution of a GTPase activity by a 50S ribosomal protein from E. coli Nat. New Biol. 233 1971 62 63
    • (1971) Nat. New Biol. , vol.233 , pp. 62-63
    • Kischa, K.1    Möller, W.2    Stöffler, G.3
  • 34
    • 13444252553 scopus 로고    scopus 로고
    • Characterization of the tRNA and ribosome-dependent pppGpp-synthesis by recombinant stringent factor from Escherichia coli
    • R.M. Knutsson Jenvert, and L. Holmberg Schiavone Characterization of the tRNA and ribosome-dependent pppGpp-synthesis by recombinant stringent factor from Escherichia coli FEBS J. 272 2005 685 695
    • (2005) FEBS J. , vol.272 , pp. 685-695
    • Knutsson Jenvert, R.M.1    Holmberg Schiavone, L.2
  • 35
    • 0036839695 scopus 로고    scopus 로고
    • Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA
    • DOI 10.1128/AAC.46.11.3339-3342.2002
    • C.B. Kofoed, and B. Vester Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA Antimicrob. Agents Chemother. 46 2002 3339 3342 (Pubitemid 35192894)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.11 , pp. 3339-3342
    • Kofoed, C.B.1    Vester, B.2
  • 36
    • 1242339673 scopus 로고    scopus 로고
    • Interaction of Helix D of Elongation Factor Tu with Helices 4 and 5 of Protein L7/12 on the Ribosome
    • DOI 10.1016/j.jmb.2003.12.080
    • U. Kothe, H.J. Wieden, D. Mohr, and M.V. Rodnina Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome J. Mol. Biol. 336 2004 1011 1021 (Pubitemid 38229693)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.5 , pp. 1011-1021
    • Kothe, U.1    Wieden, H.-J.2    Mohr, D.3    Rodnina, M.V.4
  • 39
    • 70349786238 scopus 로고    scopus 로고
    • Total synthesis and stereochemical assignment of micrococcin P1
    • D. Lefranc, and M.A. Ciufolini Total synthesis and stereochemical assignment of micrococcin P1 Angew. Chem. Int. Ed. Engl. 48 2009 4198 4201
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 4198-4201
    • Lefranc, D.1    Ciufolini, M.A.2
  • 40
    • 0042415065 scopus 로고    scopus 로고
    • Structural basis for contrasting activities of ribosome binding thiazole antibiotics
    • DOI 10.1016/S1074-5521(03)00173-X
    • G. Lentzen, R. Klinck, N. Matassova, F. Aboul-ela, and A. Murchie Structural basis for contrasting activities of ribosome binding thiazole antibiotics Chem. Biol. 10 2003 769 778 (Pubitemid 37089852)
    • (2003) Chemistry and Biology , vol.10 , Issue.8 , pp. 769-778
    • Lentzen, G.1    Klinck, R.2    Matassova, N.3    Aboul-Ela, F.4    Murchie, A.I.H.5
  • 41
    • 77649273875 scopus 로고    scopus 로고
    • Interrupted catalysis: The EF4 (LepA) effect on back-translocation
    • H. Liu, D. Pan, M. Pech, and B.S. Cooperman Interrupted catalysis: the EF4 (LepA) effect on back-translocation J. Mol. Biol. 396 2010 1043 1052
    • (2010) J. Mol. Biol. , vol.396 , pp. 1043-1052
    • Liu, H.1    Pan, D.2    Pech, M.3    Cooperman, B.S.4
  • 44
    • 0031030313 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton
    • DOI 10.1074/jbc.272.4.2046
    • G.A. McConkey, M.J. Rogers, and T.F. McCutchan Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton J. Biol. Chem. 272 1997 2046 2049 (Pubitemid 27058476)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.4 , pp. 2046-2049
    • McConkey, G.A.1    Rogers, M.J.2    McCutchan, T.F.3
  • 45
    • 0034052755 scopus 로고    scopus 로고
    • Evernimicin binds exclusively to the 50S ribosomal subunit and inhibits translation in cell-free systems derived from both gram-positive and gram- negative bacteria
    • DOI 10.1128/AAC.44.5.1121-1126.2000
    • P.M. McNicholas, D.J. Najarian, P.A. Mann, D. Hesk, R.S. Hare, K.J. Shaw, and T.A. Black Evernimicin binds exclusively to the 50S ribosomal subunit and inhibits translation in cell-free systems derived from both Gram-positive and Gram-negative bacteria Antimicrob. Agents Chemother. 44 2000 1121 1126 (Pubitemid 30228282)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.5 , pp. 1121-1126
    • Mcnicholas, P.M.1    Najarian, D.J.2    Mann, P.A.3    Hesk, D.4    Hare, R.S.5    Shaw, K.J.6    Black, T.A.7
  • 47
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • DOI 10.1038/342142a0
    • D. Moazed, and H.F. Noller Intermediate states in the movement of transfer RNA in the ribosome Nature 342 1989 142 148 (Pubitemid 19277015)
    • (1989) Nature , vol.342 , Issue.6246 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 48
    • 0015100638 scopus 로고
    • Inhibition by siomycin and thiostrepton of both aminoacyl-tRNA and factor G binding to ribosomes
    • J. Modolell, B. Cabrer, A. Parmeggiani, and D. Vazquez Inhibition by siomycin and thiostrepton of both aminoacyl-tRNA and factor G binding to ribosomes Proc. Natl. Acad. Sci. USA 68 1971 1796 1800
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1796-1800
    • Modolell, J.1    Cabrer, B.2    Parmeggiani, A.3    Vazquez, D.4
  • 49
    • 0037108102 scopus 로고    scopus 로고
    • GTPase activation of elongation factors Tu and G on the ribosome
    • D. Mohr, W. Wintermeyer, and M.V. Rodnina GTPase activation of elongation factors Tu and G on the ribosome Biochemistry 41 2002 12520 12528
    • (2002) Biochemistry , vol.41 , pp. 12520-12528
    • Mohr, D.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 52
    • 37549007641 scopus 로고    scopus 로고
    • Functional interactions between the G′ subdomain of bacterial translation factor EF-G and ribosomal protein L7/L12
    • R. Nechifor, M. Murataliev, and K.S. Wilson Functional interactions between the G′ subdomain of bacterial translation factor EF-G and ribosomal protein L7/L12 J. Biol. Chem. 282 2007 36998 37005
    • (2007) J. Biol. Chem. , vol.282 , pp. 36998-37005
    • Nechifor, R.1    Murataliev, M.2    Wilson, K.S.3
  • 56
    • 0016269146 scopus 로고
    • Micrococcin: Acceptor-site-specific inhibitor of protein synthesis
    • T. Otaka, and A. Kaji Micrococcin: acceptor-site-specific inhibitor of protein synthesis Eur. J. Biochem. 50 1974 101 106
    • (1974) Eur. J. Biochem. , vol.50 , pp. 101-106
    • Otaka, T.1    Kaji, A.2
  • 57
    • 4444325711 scopus 로고    scopus 로고
    • A dedicated translation factor controls the synthesis of the global regulator Fis
    • DOI 10.1038/sj.emboj.7600343
    • R.M. Owens, G. Pritchard, P. Skipp, M. Hodey, S.R. Connell, K.H. Nierhaus, and C.D. O'Connor A dedicated translation factor controls the synthesis of the global regulator Fis EMBO J. 23 2004 3375 3385 (Pubitemid 39209161)
    • (2004) EMBO Journal , vol.23 , Issue.16 , pp. 3375-3385
    • Owens, R.M.1    Pritchard, G.2    Skipp, P.3    Hodey, M.4    Connell, S.R.5    Nierhaus, K.H.6    O'Connor, C.D.7
  • 58
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically Competent Intermediates in the Translocation Step of Protein Synthesis
    • DOI 10.1016/j.molcel.2007.01.014, PII S1097276507000366
    • D. Pan, S.V. Kirillov, and B.S. Cooperman Kinetically competent intermediates in the translocation step of protein synthesis Mol. Cell 25 2007 519 529 (Pubitemid 46274443)
    • (2007) Molecular Cell , vol.25 , Issue.4 , pp. 519-529
    • Pan, D.1    Kirillov, S.V.2    Cooperman, B.S.3
  • 59
    • 0014941703 scopus 로고
    • Thiostrepton: A ribosomal inhibitor of translocation
    • S. Pestka Thiostrepton: a ribosomal inhibitor of translocation Biochem. Biophys. Res. Commun. 40 1970 667 674
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 667-674
    • Pestka, S.1
  • 60
    • 0015240599 scopus 로고
    • Studies on the formation of transfer ribonucleic acid-ribosome complexes. IV. Effect of antibiotics on steps of bacterial protein synthesis: Some new ribosomal inhibitors of translocation
    • S. Pestka, and N. Brot Studies on the formation of transfer ribonucleic acid-ribosome complexes. IV. Effect of antibiotics on steps of bacterial protein synthesis: some new ribosomal inhibitors of translocation J. Biol. Chem. 246 1971 7715 7722
    • (1971) J. Biol. Chem. , vol.246 , pp. 7715-7722
    • Pestka, S.1    Brot, N.2
  • 61
    • 33750799914 scopus 로고    scopus 로고
    • The Highly Conserved LepA Is a Ribosomal Elongation Factor that Back-Translocates the Ribosome
    • DOI 10.1016/j.cell.2006.09.037, PII S0092867406012980
    • Y. Qin, N. Polacek, O. Vesper, E. Staub, E. Einfeldt, D.N. Wilson, and K.H. Nierhaus The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome Cell 127 2006 721 733 (Pubitemid 44716253)
    • (2006) Cell , vol.127 , Issue.4 , pp. 721-733
    • Qin, Y.1    Polacek, N.2    Vesper, O.3    Staub, E.4    Einfeldt, E.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 63
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • DOI 10.1038/385037a0
    • M.V. Rodnina, A. Savelsbergh, V.I. Katunin, and W. Wintermeyer Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome Nature 385 1997 37 41 (Pubitemid 27024544)
    • (1997) Nature , vol.385 , Issue.6611 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 65
    • 0033966203 scopus 로고    scopus 로고
    • Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12
    • DOI 10.1074/jbc.275.2.890
    • A. Savelsbergh, D. Mohr, B. Wilden, W. Wintermeyer, and M.V. Rodnina Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12 J. Biol. Chem. 275 2000 890 894 (Pubitemid 30051131)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 890-894
    • Savelsbergh, A.1    Mohr, D.2    Wilden, B.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 66
    • 0038433302 scopus 로고    scopus 로고
    • An Elongation Factor G-Induced Ribosome Rearrangement Precedes tRNA-mRNA Translocation
    • DOI 10.1016/S1097-2765(03)00230-2
    • A. Savelsbergh, V.I. Katunin, D. Mohr, F. Peske, M.V. Rodnina, and W. Wintermeyer An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation Mol. Cell 11 2003 1517 1523 (Pubitemid 36776538)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 67
    • 29244445859 scopus 로고    scopus 로고
    • Control of phosphate release from elongation factor G by ribosomal protein L7/12
    • DOI 10.1038/sj.emboj.7600884
    • A. Savelsbergh, D. Mohr, U. Kothe, W. Wintermeyer, and M.V. Rodnina Control of phosphate release from elongation factor G by ribosomal protein L7/12 EMBO J. 24 2005 4316 4323 (Pubitemid 41828906)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4316-4323
    • Savelsbergh, A.1    Mohr, D.2    Kothe, U.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 68
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • T.M. Schmeing, and V. Ramakrishnan What recent ribosome structures have revealed about the mechanism of translation Nature 461 2009 1234 1242
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 69
    • 33644542727 scopus 로고    scopus 로고
    • EF-G-dependent GTPase on the ribosome. Conformational change and fusidic acid inhibition
    • H.S. Seo, S. Abedin, D. Kamp, D.N. Wilson, K.H. Nierhaus, and B.S. Cooperman EF-G-dependent GTPase on the ribosome. Conformational change and fusidic acid inhibition Biochemistry 45 2006 2504 2514
    • (2006) Biochemistry , vol.45 , pp. 2504-2514
    • Seo, H.S.1    Abedin, S.2    Kamp, D.3    Wilson, D.N.4    Nierhaus, K.H.5    Cooperman, B.S.6
  • 71
    • 70349464324 scopus 로고    scopus 로고
    • Enhanced SnapShot: Antibiotic inhibition of protein synthesis II
    • D. Sohmen, J.M. Harms, F. Schlünzen, and D.N. Wilson Enhanced SnapShot: antibiotic inhibition of protein synthesis II Cell 139 2009 212-212.e1
    • (2009) Cell , vol.139
    • Sohmen, D.1    Harms, J.M.2    Schlünzen, F.3    Wilson, D.N.4
  • 72
    • 70349464324 scopus 로고    scopus 로고
    • SnapShot: Antibiotic inhibition of protein synthesis i
    • D. Sohmen, J.M. Harms, F. Schlünzen, and D.N. Wilson SnapShot: antibiotic inhibition of protein synthesis I Cell 138 2009 1248.e1
    • (2009) Cell , vol.138
    • Sohmen, D.1    Harms, J.M.2    Schlünzen, F.3    Wilson, D.N.4
  • 76
    • 49849110756 scopus 로고
    • Inhibition by thiostrepton of the formation of a ribosome-bound guanine nucleotide complex
    • B. Weisblum, and V. Demohn Inhibition by thiostrepton of the formation of a ribosome-bound guanine nucleotide complex FEBS Lett. 11 1970 149 152
    • (1970) FEBS Lett. , vol.11 , pp. 149-152
    • Weisblum, B.1    Demohn, V.2
  • 77
    • 70450233600 scopus 로고    scopus 로고
    • The A-Z of bacterial translation inhibitors
    • D.N. Wilson The A-Z of bacterial translation inhibitors Crit. Rev. Biochem. Mol. Biol. 44 2009 393 433
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 393-433
    • Wilson, D.N.1
  • 78
    • 0015822062 scopus 로고
    • Avilamycin, an inhibitor of the 30S ribosomal subunits function
    • H. Wolf Avilamycin, an inhibitor of the 30S ribosomal subunits function FEBS Lett. 36 1973 181 186
    • (1973) FEBS Lett. , vol.36 , pp. 181-186
    • Wolf, H.1
  • 79
    • 0018679519 scopus 로고
    • 50-S subunit from Escherichia coli ribosomes. Isolation of active ribosomal proteins and protein complexes
    • DOI 10.1111/j.1432-1033.1979.tb02038.x
    • G. Wystup, H. Teraoka, H. Schulze, H. Hampl, and K.H. Nierhaus 50S subunit from Escherichia coli ribosomes. Isolation of active ribosomal proteins and protein complexes Eur. J. Biochem. 100 1979 101 113 (Pubitemid 10237742)
    • (1979) European Journal of Biochemistry , vol.100 , Issue.1 , pp. 101-113
    • Wystup, G.1    Teraoka, H.2    Schulze, H.3
  • 80
    • 0036838794 scopus 로고    scopus 로고
    • Mutations in ribosomal protein L16 and in 23S rRNA in Enterococcus strains for which evernimicin MICs differ
    • DOI 10.1128/AAC.46.11.3657-3659.2002
    • M. Zarazaga, C. Tenorio, R. Del Campo, F. Ruiz-Larrea, and C. Torres Mutations in ribosomal protein L16 and in 23S rRNA in Enterococcus strains for which evernimicin MICs differ Antimicrob. Agents Chemother. 46 2002 3657 3659 (Pubitemid 35192947)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.11 , pp. 3657-3659
    • Zarazaga, M.1    Tenorio, C.2    Del Campo, R.3    Ruiz-Larrea, F.4    Torres, C.5


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