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Volumn 44, Issue 6, 2009, Pages 393-433

The A-Z of bacterial translation inhibitors

Author keywords

Antibiotics; Inhibitors; Protein synthesis; Resistance; Ribosome; Translation

Indexed keywords

1 METHYLMOCIMYCIN; AMIKACIN; AMINOGLYCOSIDE ANTIBIOTIC AGENT; ANISOMYCIN; ANTIBIOTIC AGENT; AVILAMYCIN; AZITHROMYCIN; BLASTICIDIN S; CARBOMYCIN; CETHROMYCIN; CHLORAMPHENICOL; CLARITHROMYCIN; DALFOPRISTIN PLUS QUINUPRISTIN; EDEINE; ERYTHROMYCIN; EVERNIMICIN; FUSIDIC ACID; GE 2270A; GE 81112; GENTAMICIN; KASUGAMYCIN; KASUMIN; LINCOSAMIDE DERIVATIVE; LINEZOLID; MOCIMYCIN; PACTAMYCIN; PROTEIN SYNTHESIS INHIBITOR; PULVOMYCIN; PUROMYCIN; SB 280080; SB 571519; SPARSOMYCIN; SPECTINOMYCIN; STREPTOMYCIN; TETRACYCLINE DERIVATIVE; TIGECYCLINE; TOBRAMYCIN SULFATE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 70450233600     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409230903307311     Document Type: Review
Times cited : (270)

References (362)
  • 1
    • 0034426125 scopus 로고    scopus 로고
    • Presence of variations in ribos-omal protein L16 corresponding to susceptibility of enterococci to oligosaccharides (Avilamycin and evernimicin)
    • Aarestrup FM and Jensen LB. 2000. Presence of variations in ribos-omal protein L16 corresponding to susceptibility of enterococci to oligosaccharides (Avilamycin and evernimicin). Antimicrob Agents Chemother 44:3425-3427.
    • (2000) Antimicrob Agents Chemother , vol.44 , 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
    • Adrian P V, Zhao W, Black TA, Shaw KJ, Hare RS and Klugman KP. 2000b. Mutations in ribosomal protein L16 conferring reduced susceptibility to evernimicin (SCH27899): implications for mechanism of action. Antimicrob Agents Chemother 44:732-738.
    • (2000) Antimicrob Agents Chemother , vol.44 , 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
  • 5
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: Te mechanism of translocation
    • Agrawal R, Penczek P, Grassucci R and Frank J. 1998. Visualization of elongation factor G on the Escherichia coli 70S ribosome: Te mechanism of translocation. Proc Natl Acad Sci USA 95:6134-6138.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6134-6138
    • Agrawal, R.1    Penczek, P.2    Grassucci, R.3    Frank, J.4
  • 6
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal RK, Heagle AB, Penczek P, Grassucci RA and Frank J. 1999. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nature Struct Biol 6:643-647.
    • (1999) Nature Struct Biol , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 7
    • 0035943352 scopus 로고    scopus 로고
    • Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation
    • Agrawal RK, Linde J, Sengupta J, Nierhaus KH and Frank J. 2001. Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation. J Mol Biol 311:777-787.
    • (2001) J Mol Biol , vol.311 , pp. 777-787
    • Agrawal, R.K.1    Linde, J.2    Sengupta, J.3    Nierhaus, K.H.4    Frank, J.5
  • 8
    • 20444365142 scopus 로고    scopus 로고
    • Te cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen G, Zavialov A, Gursky R, Ehrenberg M and Frank J. 2005. Te cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121:703-712.
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 11
    • 19544367992 scopus 로고    scopus 로고
    • Antimycobacterial agents difer with respect to their bacteriostatic versus bactericidal activities in relation to time of exposure, mycobacterial growth phase, and their use in combination
    • Bakker-Woudenberg IA, van Vianen W, van Soolingen D, Verbrugh HA and van Agtmael MA. 2005. Antimycobacterial agents difer with respect to their bacteriostatic versus bactericidal activities in relation to time of exposure, mycobacterial growth phase, and their use in combination. Antimicrob Agents Chemother 49:2387-2398.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2387-2398
    • Bakker-Woudenberg, I.A.1    Van Vianen, W.2    Van Soolingen, D.3    Verbrugh, H.A.4    Van Agtmael, M.A.5
  • 12
    • 0026569497 scopus 로고
    • Unusual ribosome binding properties of messenger RNA encoding bac-teriophage lambda repressor
    • Balakin AG, Skripkin EA, Shatsky IN and Bogdanov AA. 1992. Unusual ribosome binding properties of messenger RNA encoding bac-teriophage lambda repressor. Nucl Acids Res 20:563-571.
    • (1992) Nucl Acids Res , vol.20 , pp. 563-571
    • Balakin, A.G.1    Skripkin, E.A.2    Shatsky, I.N.3    Bogdanov, A.A.4
  • 13
    • 0016166350 scopus 로고
    • 3H) anisomycin binding to eukary-otic ribosomes
    • Barbacid M and Vazquez D. 1974. (3H)anisomycin binding to eukary-otic ribosomes. J Mol Biol 84:603-623.
    • (1974) J Mol Biol , vol.84 , pp. 603-623
    • Barbacid, M.1    Vazquez, D.2
  • 16
    • 3042810717 scopus 로고    scopus 로고
    • 2+ cleavage of 16S rRNA
    • Bauer G, Berens C, Projan S and Hillen W. 2004. Comparison of tetracycline and tigecycline binding to ribosomes mapped by dimethylsulphate and drug-directed Fe2+ cleavage of 16S rRNA. J Antimicrob Chemother 53:592-599.
    • (2004) J Antimicrob Chemother , vol.53 , pp. 592-599
    • Bauer, G.1    Berens, C.2    Projan, S.3    Hillen, W.4
  • 17
    • 0035957387 scopus 로고    scopus 로고
    • A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit
    • Belova L, Tenson T, Xiong LQ, McNicholas PM and Mankin AS. 2001. A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit. Proc Natl Acad Sci USA 98:3726-3731.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3726-3731
    • Belova, L.1    Tenson, T.2    Xiong, L.Q.3    McNicholas, P.M.4    Mankin, A.S.5
  • 19
    • 34247589630 scopus 로고    scopus 로고
    • Te ribosomal peptidyl trans-ferase
    • Beringer M and Rodnina MV. 2007. Te ribosomal peptidyl trans-ferase. Mol Cell 26:311-321.
    • (2007) Mol Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 21
    • 0038492422 scopus 로고    scopus 로고
    • Structural insight into the antibiotic action of telithromycin on resistant mutants
    • Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen H, Fucini P and Yonath A. 2003a. Structural insight into the antibiotic action of telithromycin on resistant mutants. J Bact 185:4276-4279.
    • (2003) J Bact , vol.185 , pp. 4276-4279
    • Berisio, R.1    Harms, J.2    Schluenzen, F.3    Zarivach, R.4    Hansen, H.5    Fucini, P.6    Yonath, A.7
  • 23
    • 0037243625 scopus 로고    scopus 로고
    • Molecular analysis of fusidic acid resistance in Staphylococcus aureus
    • Besier S, Ludwig A, Brade V and Wichelhaus TA. 2003. Molecular analysis of fusidic acid resistance in Staphylococcus aureus. Mol Microbiol 47:463-469.
    • (2003) Mol Microbiol , vol.47 , pp. 463-469
    • Besier, S.1    Ludwig, A.2    Brade, V.3    Wichelhaus, T.A.4
  • 24
    • 16244419018 scopus 로고    scopus 로고
    • Compensatory adaptation to the loss of biological ftness associated with acquisition of fusidic acid resistance in Staphylococcus aureus
    • Besier S, Ludwig A, Brade V and Wichelhaus TA. 2005. Compensatory adaptation to the loss of biological ftness associated with acquisition of fusidic acid resistance in Staphylococcus aureus. Antimicrob Agents Chemother 49:1426-1431.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1426-1431
    • Besier, S.1    Ludwig, A.2    Brade, V.3    Wichelhaus, T.A.4
  • 25
    • 0014117610 scopus 로고
    • Pactamycin, an antibiotic that inhibits protein synthesis
    • Bhuyan BK. 1967. Pactamycin, an antibiotic that inhibits protein synthesis. Biochem Pharmacol 16:1411-1420.
    • (1967) Biochem Pharmacol , vol.16 , pp. 1411-1420
    • Bhuyan, B.K.1
  • 27
    • 43449093704 scopus 로고    scopus 로고
    • Mutations outside the anisomycin-binding site can make ribos-omes drug-resistant
    • Blaha G, Gurel G, Schroeder SJ, Moore PB and Steitz TA. 2008. Mutations outside the anisomycin-binding site can make ribos-omes drug-resistant. J Mol Biol 379:505-519.
    • (2008) J Mol Biol , vol.379 , pp. 505-519
    • Blaha, G.1    Gurel, G.2    Schroeder, S.J.3    Moore, P.B.4    Steitz, T.A.5
  • 29
    • 0036718512 scopus 로고    scopus 로고
    • Characterization of a novel antibacterial agent that inhibits bacterial translation
    • Boddeker N, Bahador G, Gibbs C, Mabery E, Wolf J, Xu L and Watson J. 2002. Characterization of a novel antibacterial agent that inhibits bacterial translation. RNA 8:1120-1128.
    • (2002) RNA , vol.8 , pp. 1120-1128
    • Boddeker, N.1    Bahador, G.2    Gibbs, C.3    Mabery, E.4    Wolf, J.5    Xu, L.6    Watson, J.7
  • 30
    • 0014687949 scopus 로고
    • Formation of the ribosome-G factor-GDP complex in the presence of fusidic acid
    • Bodley JW, Zieve FJ, Lin L and Zieve ST. 1969. Formation of the ribosome-G factor-GDP complex in the presence of fusidic acid. Biochem Biophys Res Commun 37:437-443.
    • (1969) Biochem Biophys Res Commun , vol.37 , pp. 437-443
    • Bodley, J.W.1    Zieve, F.J.2    Lin, L.3    Zieve, S.T.4
  • 31
    • 40449123425 scopus 로고    scopus 로고
    • Mutation from gua-nine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae
    • Bommakanti AS, Lindahl L and Zengel JM. 2008. Mutation from gua-nine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae. RNA 14:460-464.
    • (2008) RNA , vol.14 , pp. 460-464
    • Bommakanti, A.S.1    Lindahl, L.2    Zengel, J.M.3
  • 34
    • 47949110827 scopus 로고    scopus 로고
    • Structural basis for hygromycin B inhibition of protein biosynthesis
    • Borovinskaya MA, Shoji S, Fredrick K and Cate JH. 2008. Structural basis for hygromycin B inhibition of protein biosynthesis. RNA 14:1590-1599.
    • (2008) RNA , vol.14 , pp. 1590-1599
    • Borovinskaya, M.A.1    Shoji, S.2    Fredrick, K.3    Cate, J.H.4
  • 35
    • 0041922660 scopus 로고    scopus 로고
    • Resistance to the peptidyl transferase inhibitor tiamulin caused by mutation of ribosomal protein L3
    • Bosling J, Poulsen SM, Vester B and Long KS. 2003. Resistance to the peptidyl transferase inhibitor tiamulin caused by mutation of ribosomal protein L3. Antimicrob Agents Chemother 47:2892-2896.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2892-2896
    • Bosling, J.1    Poulsen, S.M.2    Vester, B.3    Long, K.S.4
  • 37
    • 33745608210 scopus 로고    scopus 로고
    • Characterization of GE82832, a peptide inhibitor of translocation interacting with bacterial 30S ribos-omal subunits
    • Brandi L, Fabbretti A, Di Stefano M, Lazzarini A, Abbondi M and Gualerzi CO. 2006a. Characterization of GE82832, a peptide inhibitor of translocation interacting with bacterial 30S ribos-omal subunits. RNA 12:1262-1270.
    • (2006) RNA , vol.12 , pp. 1262-1270
    • Brandi, L.1    Fabbretti, A.2    Di Stefano, M.3    Lazzarini, A.4    Abbondi, M.5    Gualerzi, C.O.6
  • 40
    • 0028359389 scopus 로고
    • Spectinomycin interacts specifcally with the residues G(1064) and C(1192) in 16S rRNA, thereby potentially freezing this molecule into an inactive conformation
    • Brink MF, Brink G, Verbeet MP and Deboer HA. 1994. Spectinomycin interacts specifcally with the residues G(1064) and C(1192) in 16S rRNA, thereby potentially freezing this molecule into an inactive conformation. Nucleic Acids Res 22:325-331.
    • (1994) Nucleic Acids Res , vol.22 , pp. 325-331
    • Brink, M.F.1    Brink, G.2    Verbeet, M.P.3    Deboer, H.A.4
  • 41
    • 0034704217 scopus 로고    scopus 로고
    • Te structural basis for the action of the antibiotics tetracycline, pactamy-cin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen DE, Clemons WM, Carter AP, Morgan-Warren RJ, Wimberly BT and Ramakrishnan V. 2000. Te structural basis for the action of the antibiotics tetracycline, pactamy-cin, and hygromycin B on the 30S ribosomal subunit. Cell 103:1143-1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 43
    • 42249112442 scopus 로고    scopus 로고
    • Interaction of 23S ribosomal RNA helices 89 and 91 of Escherichia coli contributes to the activity of IF2 but is insignifcant for elongation factors functioning
    • Burakovskii DE, Smirnova AS, Lesniak D V, Kiparisov S V, Leonov AA, Sergiev PV, Bogdanov AA and Dontsova OA. 2007. Interaction of 23S ribosomal RNA helices 89 and 91 of Escherichia coli contributes to the activity of IF2 but is insignifcant for elongation factors functioning. Mol Biol (Mosk) 41:1031-1041.
    • (2007) Mol Biol (Mosk) , vol.41 , pp. 1031-1041
    • Burakovskii, D.E.1    Smirnova, A.S.2    Lesniak, D.V.3    Kiparisov, S.V.4    Leonov, A.A.5    Sergiev, P.V.6    Bogdanov, A.A.7    Dontsova, O.A.8
  • 44
    • 0032549507 scopus 로고    scopus 로고
    • On the target of a novel class of antibiotics, oxazolidinones, active against multidrug-resistant Gram-positive bacteria
    • Burghardt H, Schimz KL and Muller M. 1998. On the target of a novel class of antibiotics, oxazolidinones, active against multidrug-resistant Gram-positive bacteria. FEBS Lett 425:40-44.
    • (1998) FEBS Lett , vol.425 , pp. 40-44
    • Burghardt, H.1    Schimz, K.L.2    Muller, M.3
  • 45
    • 0018168389 scopus 로고
    • Inhibition of ribosomal translocation by aminoglycoside antibiotics
    • Cabanas MJ, Vazquez D and Modolell J. 1978. Inhibition of ribosomal translocation by aminoglycoside antibiotics. Biochem Biophys Res Commun 83:991-997.
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 991-997
    • Cabanas, M.J.1    Vazquez, D.2    Modolell, J.3
  • 47
    • 0035428052 scopus 로고    scopus 로고
    • Overcoming bacterial resistance by dual target inhibition: The case of streptogramins
    • Canu A and Leclercq R. 2001. Overcoming bacterial resistance by dual target inhibition: the case of streptogramins. Curr Drug Targets Infect Disord 1:215-225.
    • (2001) Curr Drug Targets Infect Disord , vol.1 , pp. 215-225
    • Canu, A.1    Leclercq, R.2
  • 48
    • 0015463161 scopus 로고
    • Survey of inhibitors in diferent steps of protein synthesis by mammalian ribosomes
    • Carrasco L and Vazquez D. 1972. Survey of inhibitors in diferent steps of protein synthesis by mammalian ribosomes. J Antibiot (Tokyo) 25:732-737.
    • (1972) J Antibiot (Tokyo) , vol.25 , pp. 732-737
    • Carrasco, L.1    Vazquez, D.2
  • 50
    • 0000195026 scopus 로고
    • Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribos-omes
    • Celma ML, Monro RE and Vazquez D. 1970. Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribos-omes. FEBS Lett 6:273-277.
    • (1970) FEBS Lett , vol.6 , pp. 273-277
    • Celma, M.L.1    Monro, R.E.2    Vazquez, D.3
  • 51
    • 0001350056 scopus 로고
    • Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes: Binding of UACCA-leu to 50S subunits
    • Celma ML, Monro RE and Vazquez D. 1971. Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes: binding of UACCA-leu to 50S subunits. FEBS Lett 13:247-251.
    • (1971) FEBS Lett , vol.13 , pp. 247-251
    • Celma, M.L.1    Monro, R.E.2    Vazquez, D.3
  • 52
    • 0035342162 scopus 로고    scopus 로고
    • Bacterial ribosomal subunit synthesis: A novel antibiotic target
    • Champney WS. 2001. Bacterial ribosomal subunit synthesis: a novel antibiotic target. Curr Drug Targets Infect Disord 1:19-36.
    • (2001) Curr Drug Targets Infect Disord , vol.1 , pp. 19-36
    • Champney, W.S.1
  • 53
    • 33845443409 scopus 로고    scopus 로고
    • Te other target for ribosomal antibiotics: Inhibition of bacterial ribosomal subunit formation
    • Champney WS. 2006. Te other target for ribosomal antibiotics: inhibition of bacterial ribosomal subunit formation. Infect Disord Drug Targets 6:377-390.
    • (2006) Infect Disord Drug Targets , vol.6 , pp. 377-390
    • Champney, W.S.1
  • 54
    • 0027442084 scopus 로고
    • Resistance of lambda cI translation to antibiotics that inhibit translation initiation
    • Chin K, Shean CS and Gottesman ME. 1993. Resistance of lambda cI translation to antibiotics that inhibit translation initiation. J Bacteriol 175:7471-7473.
    • (1993) J Bacteriol , vol.175 , pp. 7471-7473
    • Chin, K.1    Shean, C.S.2    Gottesman, M.E.3
  • 55
    • 0021167328 scopus 로고
    • Te action of virginiamycin M on the acceptor, donor, and catalytic sites of peptidyltrans-ferase
    • Chinali G, Moureau P and Cocito C. 1984. Te action of virginiamycin M on the acceptor, donor, and catalytic sites of peptidyltrans-ferase. J Biol Chem 259:9563-9568.
    • (1984) J Biol Chem , vol.259 , pp. 9563-9568
    • Chinali, G.1    Moureau, P.2    Cocito, C.3
  • 56
    • 0023736089 scopus 로고
    • Action of erythromycin and virginiamycin S on polypeptide synthesis in cell-free systems
    • Chinali G, Nyssen E, Di Giambattista M and Cocito C. 1988a. Action of erythromycin and virginiamycin S on polypeptide synthesis in cell-free systems. Biochim Biophys Acta 951:42-52.
    • (1988) Biochim Biophys Acta , vol.951 , pp. 42-52
    • Chinali, G.1    Nyssen, E.2    Di Giambattista, M.3    Cocito, C.4
  • 57
    • 0023850435 scopus 로고
    • Inhibition of polypeptide synthesis in cell-free systems by vir-giniamycin S and erythromycin Evidence for a common mode of action of type B synergimycins and 14-membered macrolides
    • Chinali G, Nyssen E, Di Giambattista M and Cocito C. 1988b. Inhibition of polypeptide synthesis in cell-free systems by vir-giniamycin S and erythromycin. Evidence for a common mode of action of type B synergimycins and 14-membered macrolides. Biochim Biophys Acta 949:71-78.
    • (1988) Biochim Biophys Acta , vol.949 , pp. 71-78
    • Chinali, G.1    Nyssen, E.2    Di Giambattista, M.3    Cocito, C.4
  • 58
    • 0028148698 scopus 로고
    • Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli
    • Chittum HS and Champney WS. 1994. Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli. J Bacteriol 176:6192-6198.
    • (1994) J Bacteriol , vol.176 , pp. 6192-6198
    • Chittum, H.S.1    Champney, W.S.2
  • 59
    • 0036619713 scopus 로고    scopus 로고
    • New developments in tetracycline antibiotics: Gly-cylcyclines and tetracycline efux pump inhibitors
    • Chopra I. 2002. New developments in tetracycline antibiotics: gly-cylcyclines and tetracycline efux pump inhibitors. Drug Resist Updates 5:119-125.
    • (2002) Drug Resist Updates , vol.5 , pp. 119-125
    • Chopra, I.1
  • 60
    • 0034973583 scopus 로고    scopus 로고
    • Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance
    • Chopra I and Roberts M. 2001. Tetracycline antibiotics: mode of action, applications, molecular biology, and epidemiology of bacterial resistance. Microbiol Mol Biol Rev 65:232-260.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 232-260
    • Chopra, I.1    Roberts, M.2
  • 63
    • 33748414041 scopus 로고    scopus 로고
    • Non-ribosomal factors in ribos-ome subunit assembly are emerging targets for new antibacterial drugs
    • Comartin DJ and Brown ED. 2006. Non-ribosomal factors in ribos-ome subunit assembly are emerging targets for new antibacterial drugs. Curr Opin Pharmacol 6:453-458.
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 453-458
    • Comartin, D.J.1    Brown, E.D.2
  • 64
    • 0036035221 scopus 로고    scopus 로고
    • Te tetracycline resistance protein Tet(O) perturbs the conformation of the ribosomal decoding centre
    • Connell SR, Trieber CA, Stelzl U, Einfeldt E, Taylor DE and Nierhaus KH. 2002. Te tetracycline resistance protein Tet(O) perturbs the conformation of the ribosomal decoding centre. Mol Microbiol 45:1463-1472.
    • (2002) Mol Microbiol , vol.45 , pp. 1463-1472
    • Connell, S.R.1    Trieber, C.A.2    Stelzl, U.3    Einfeldt, E.4    Taylor, D.E.5    Nierhaus, K.H.6
  • 68
    • 55349106559 scopus 로고    scopus 로고
    • Mechanistic insight into the ribosome biogenesis functions of the ancient protein KsgA
    • Connolly K, Rife JP and Culver G. 2008. Mechanistic insight into the ribosome biogenesis functions of the ancient protein KsgA. Mol Microbiol 70:1062-1075.
    • (2008) Mol Microbiol , vol.70 , pp. 1062-1075
    • Connolly, K.1    Rife, J.P.2    Culver, G.3
  • 69
    • 0017363068 scopus 로고
    • Cooperative and antagonistic interactions of peptidyl-tRNA and antibiotics with bacterial ribosomes
    • Contreras A and Vazquez D. 1977. Cooperative and antagonistic interactions of peptidyl-tRNA and antibiotics with bacterial ribosomes. Eur J Biochem 74:539-547.
    • (1977) Eur J Biochem , vol.74 , pp. 539-547
    • Contreras, A.1    Vazquez, D.2
  • 74
    • 58549118714 scopus 로고    scopus 로고
    • Structural basis for cross-resistance to ribosomal PTC antibiotics
    • Davidovich C, Bashan A and Yonath A. 2008. Structural basis for cross-resistance to ribosomal PTC antibiotics. Proc Natl Acad Sci USA 105:20665-20670.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20665-20670
    • Davidovich, C.1    Bashan, A.2    Yonath, A.3
  • 75
    • 0032546747 scopus 로고    scopus 로고
    • Ribosomal proteins S5 and L6: High-resolution crystal structures and roles in protein synthesis and antibiotic resistance
    • Davies C, Bussiere DE, Golden BL, Porter SJ, Ramakrishnan V and White SW. 1998. Ribosomal proteins S5 and L6: High-resolution crystal structures and roles in protein synthesis and antibiotic resistance. J Mol Biol 279:873-888.
    • (1998) J Mol Biol , vol.279 , pp. 873-888
    • Davies, C.1    Bussiere, D.E.2    Golden, B.L.3    Porter, S.J.4    Ramakrishnan, V.5    White, S.W.6
  • 76
    • 0025143632 scopus 로고
    • What are antibiotics? Archaic functions for modern activities
    • Davies J. 1990. What are antibiotics? Archaic functions for modern activities. Mol Microbiol 4:1227-1232.
    • (1990) Mol Microbiol , vol.4 , pp. 1227-1232
    • Davies, J.1
  • 77
    • 0043144142 scopus 로고
    • Inhibition of protein synthesis by spectinomycin
    • Davies J, Anderson P and Davis BD. 1965. Inhibition of protein synthesis by spectinomycin. Science 149:1096-1098.
    • (1965) Science , vol.149 , pp. 1096-1098
    • Davies, J.1    Anderson, P.2    Davis, B.D.3
  • 78
    • 0023615466 scopus 로고
    • Mechanism of bactericidal action of aminoglyco-sides
    • Davis BD. 1987. Mechanism of bactericidal action of aminoglyco-sides. Microbiol Rev 51:341-350.
    • (1987) Microbiol Rev , vol.51 , pp. 341-350
    • Davis, B.D.1
  • 79
    • 0035170204 scopus 로고    scopus 로고
    • Mutation in 23S rRNA responsible for resistance to 16-membered macrolides and streptogramins in Streptococcus pneumoniae
    • Depardieu F and Courvalin P. 2001. Mutation in 23S rRNA responsible for resistance to 16-membered macrolides and streptogramins in Streptococcus pneumoniae. Antimicrob Agents Chemother 45:319-323.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 319-323
    • Depardieu, F.1    Courvalin, P.2
  • 81
    • 0024453356 scopus 로고
    • Te molecular basis of the inhibitory activities of type A and type B synergimycins and related antibiotics on ribosomes
    • Di Giambattista M, Chinali G and Cocito C. 1989. Te molecular basis of the inhibitory activities of type A and type B synergimycins and related antibiotics on ribosomes. J Antimicrob Chemother 24:485-507.
    • (1989) J Antimicrob Chemother , vol.24 , pp. 485-507
    • Di Giambattista, M.1    Chinali, G.2    Cocito, C.3
  • 82
    • 1642564526 scopus 로고    scopus 로고
    • Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: The universally conserved residues G693 and C795 regulate P-site tRNA binding
    • Dinos G, Wilson DN, Teraoka Y, Szafarski W, Fucini P, Kalpaxis D and Nierhaus KH. 2004. Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site tRNA binding. Mol Cell 13:113-124.
    • (2004) Mol Cell , vol.13 , pp. 113-124
    • Dinos, G.1    Wilson, D.N.2    Teraoka, Y.3    Szafarski, W.4    Fucini, P.5    Kalpaxis, D.6    Nierhaus, K.H.7
  • 83
    • 0018162344 scopus 로고
    • Te efects of tiamulin, a semi-synthetic pleuromutilin derivative, on bacterial polypeptide chain initiation
    • Dornhelm P and Hogenauer G. 1978. Te efects of tiamulin, a semi-synthetic pleuromutilin derivative, on bacterial polypeptide chain initiation. Eur J Biochem 91:465-473.
    • (1978) Eur J Biochem , vol.91 , pp. 465-473
    • Dornhelm, P.1    Hogenauer, G.2
  • 84
    • 0026660662 scopus 로고
    • Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA
    • Douthwaite S. 1992. Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA. Nucleic Acids Res 20:4717-4720.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4717-4720
    • Douthwaite, S.1
  • 85
    • 0034115717 scopus 로고    scopus 로고
    • Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA
    • Douthwaite S, Hansen LH and Mauvais P. 2000. Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA. Mol Microbiol 36:183-193.
    • (2000) Mol Microbiol , vol.36 , pp. 183-193
    • Douthwaite, S.1    Hansen, L.H.2    Mauvais, P.3
  • 86
    • 1842471295 scopus 로고    scopus 로고
    • Te tylosin-re-sistance methyltransferase RlmA(II) (TlrB) modifes the N-1 position of 23S rRNA nucleotide G748
    • Douthwaite S, Crain P, Liu M and Poehlsgaard J. 2004. Te tylosin-re-sistance methyltransferase RlmA(II) (TlrB) modifes the N-1 position of 23S rRNA nucleotide G748. J Mol Biol 337:1073-1077.
    • (2004) J Mol Biol , vol.337 , pp. 1073-1077
    • Douthwaite, S.1    Crain, P.2    Liu, M.3    Poehlsgaard, J.4
  • 88
    • 0023748768 scopus 로고
    • Mechanism of action of DuP 721: Inhibition of an early event during initiation of protein synthesis
    • Eustice DC, Feldman PA, Zajac I and Slee AM. 1988. Mechanism of action of DuP 721: inhibition of an early event during initiation of protein synthesis. Antimicrob Agents Chemother 32:1218-1222.
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 1218-1222
    • Eustice, D.C.1    Feldman, P.A.2    Zajac, I.3    Slee, A.M.4
  • 89
    • 0015220211 scopus 로고
    • Substrate-and antibiotic-binding sites at the peptidyl transferase centre of e coli ribosomes. Studies on the chloram-phenicol, lincomycin and erythromycin sites
    • Fernandez-Munoz R, Monro RE, Torres-Pinedo R and Vazquez D. 1971. Substrate-and antibiotic-binding sites at the peptidyl transferase centre of E coli ribosomes. Studies on the chloram-phenicol, lincomycin and erythromycin sites. Eur J Biochem 23:185-193.
    • (1971) Eur J Biochem , vol.23 , pp. 185-193
    • Fernandez-Munoz, R.1    Monro, R.E.2    Torres-Pinedo, R.3    Vazquez, D.4
  • 90
    • 0029825658 scopus 로고    scopus 로고
    • Structure of the A-site of E. coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic
    • Fourmy D, Recht MI, Blanchard SC and Puglisi JD. 1996. Structure of the A-site of E. coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic. Science 274:1367-1371.
    • (1996) Science , vol.274 , pp. 1367-1371
    • Fourmy, D.1    Recht, M.I.2    Blanchard, S.C.3    Puglisi, J.D.4
  • 91
    • 0032571359 scopus 로고    scopus 로고
    • Paromomycin binding induces a local conformational change in the A-Site of 16S rRNA
    • Fourmy D, Yoshizawa S and Puglisi JD. 1998. Paromomycin binding induces a local conformational change in the A-Site of 16S rRNA. J Mol Biol 277:333-345.
    • (1998) J Mol Biol , vol.277 , pp. 333-345
    • Fourmy, D.1    Yoshizawa, S.2    Puglisi, J.D.3
  • 92
    • 33644610182 scopus 로고    scopus 로고
    • Structure-based drug design meets the ribosome
    • Franceschi F and Dufy EM. 2006. Structure-based drug design meets the ribosome. Biochem Pharmacol 71:1016-1025.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1016-1025
    • Franceschi, F.1    Dufy, E.M.2
  • 93
    • 0038286524 scopus 로고    scopus 로고
    • Catalysis of ribosomal translocation by sparsomycin
    • Fredrick K and Noller HF. 2003. Catalysis of ribosomal translocation by sparsomycin. Science 300:1159-1162.
    • (2003) Science , vol.300 , pp. 1159-1162
    • Fredrick, K.1    Noller, H.F.2
  • 94
    • 0019448670 scopus 로고
    • Cloning of yeast gene for trichode-rmin resistance and ribosomal protein L3
    • Fried HM and Warner JR. 1981. Cloning of yeast gene for trichode-rmin resistance and ribosomal protein L3. Proc Natl Acad Sci USA 78:238-242.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 238-242
    • Fried, H.M.1    Warner, J.R.2
  • 95
    • 0007571942 scopus 로고
    • Te molecular basis for rRNA-dependent spectinomycin resistance in Nicotiana chloroplasts
    • Fromm H, Efelman M, Aviv D and Galun E. 1987. Te molecular basis for rRNA-dependent spectinomycin resistance in Nicotiana chloroplasts. EMBO J 6:3233-3237.
    • (1987) EMBO J , vol.6 , pp. 3233-3237
    • Fromm, H.1    Efelman, M.2    Aviv, D.3    Galun, E.4
  • 96
    • 0015253480 scopus 로고
    • Ribosomal proteins: XXVII Localization of the amino acid exchanges in protein S5 from 2 E. coli mutants resistant to spectinomycin
    • Funatsu G, Schilitz E and Wittmann HG. 1971. Ribosomal proteins: XXVII. Localization of the amino acid exchanges in protein S5 from 2 E. coli mutants resistant to spectinomycin. Molec Gen Genet 114:106-111.
    • (1971) Molec Gen Genet , vol.114 , pp. 106-111
    • Funatsu, G.1    Schilitz, E.2    Wittmann, H.G.3
  • 98
    • 37549054020 scopus 로고    scopus 로고
    • In vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specifc antibiotic thiostrepton
    • Garcia-Marcos A, Morreale A, Guarinos E, Briones E, Remacha M, Ortiz AR and Ballesta JP. 2007. In vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specifc antibiotic thiostrepton. Nucleic Acids Res 35:7109-7117.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7109-7117
    • Garcia-Marcos, A.1    Morreale, A.2    Guarinos, E.3    Briones, E.4    Remacha, M.5    Ortiz, A.R.6    Ballesta, J.P.7
  • 99
    • 0038135144 scopus 로고    scopus 로고
    • Macrolide antibiotics: Binding site, mechanism of action, resistance
    • Gaynor M and Mankin A. 2003. Macrolide antibiotics: binding site, mechanism of action, resistance. Curr Top Med Chem 3:949-961.
    • (2003) Curr Top Med Chem , vol.3 , pp. 949-961
    • Gaynor, M.1    Mankin, A.2
  • 100
    • 0025678448 scopus 로고
    • Signifcance of the third tRNA binding site, the e Site, on E. coli ribosomes for the accuracy of translation: An occupied e site prevents the binding of non-cognate aminoacyl-transfer RNA to the A site
    • Geigenmüller U and Nierhaus KH. 1990. Signifcance of the third tRNA binding site, the E Site, on E. coli ribosomes for the accuracy of translation: an occupied E site prevents the binding of non-cognate aminoacyl-transfer RNA to the A site. EMBO J 9:4527-4533.
    • (1990) EMBO J , vol.9 , pp. 4527-4533
    • Geigenmüller, U.1    Nierhaus, K.H.2
  • 102
    • 0000882601 scopus 로고
    • Fucidin: A new orally active antibiotic
    • Godtfredsen W, Roholt K and Tybring L. 1962a. Fucidin: a new orally active antibiotic. Lancet 1:928-931.
    • (1962) Lancet , vol.1 , pp. 928-931
    • Godtfredsen, W.1    Roholt, K.2    Tybring, L.3
  • 105
    • 36248958685 scopus 로고    scopus 로고
    • Tiostrepton inhibition of tRNA delivery to the ribosome
    • Gonzalez Jr RL, Chu S and Puglisi JD. 2007. Tiostrepton inhibition of tRNA delivery to the ribosome. RNA 13:2091-2097.
    • (2007) RNA , vol.13 , pp. 2091-2097
    • Gonzalez Jr, R.L.1    Chu, S.2    Puglisi, J.D.3
  • 106
    • 0033014076 scopus 로고    scopus 로고
    • Erythromycin resistance mutations in ribosomal proteins L22 und L4 perturb the higher order structure of 23S ribosomal RNA
    • Gregory ST and Dahlberg AE. 1999. Erythromycin resistance mutations in ribosomal proteins L22 und L4 perturb the higher order structure of 23S ribosomal RNA. J Mol Biol 289:827-834.
    • (1999) J Mol Biol , vol.289 , pp. 827-834
    • Gregory, S.T.1    Dahlberg, A.E.2
  • 107
    • 34748843156 scopus 로고    scopus 로고
    • A quantitative kinetic scheme for 70 S translation initiation complex formation
    • Grigoriadou C, Marzi S, Kirillov S, Gualerzi CO and Cooperman BS. 2007. A quantitative kinetic scheme for 70 S translation initiation complex formation. J Mol Biol 373:562-572.
    • (2007) J Mol Biol , vol.373 , pp. 562-572
    • Grigoriadou, C.1    Marzi, S.2    Kirillov, S.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 108
    • 1842420639 scopus 로고    scopus 로고
    • Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome
    • Gromadski KB and Rodnina MV. 2004. Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome. Nat Struct Mol Biol 11:316-322.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 316-322
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 109
    • 0025365804 scopus 로고
    • Initiation of messenger-RNA translation in prokaryotes
    • Gualerzi CO and Pon CL. 1990. Initiation of messenger-RNA translation in prokaryotes. Biochemistry 29:5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 110
    • 0019023614 scopus 로고
    • Hygromycin A, a novel inhibitor of ribosomal peptidyltransferase
    • Guerrero MD and Modolell J. 1980. Hygromycin A, a novel inhibitor of ribosomal peptidyltransferase. Eur J Biochem 107:409-414.
    • (1980) Eur J Biochem , vol.107 , pp. 409-414
    • Guerrero, M.D.1    Modolell, J.2
  • 111
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N and Peitsch MC. 1997. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 112
    • 67349260439 scopus 로고    scopus 로고
    • U2504 determines the species specifcity of the A-site cleft antibiotics:the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome
    • Gurel G, Blaha G, Moore PB and Steitz TA. 2009. U2504 determines the species specifcity of the A-site cleft antibiotics:the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome. J Mol Biol 389:146-156.
    • (2009) J Mol Biol , vol.389 , pp. 146-156
    • Gurel, G.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 113
    • 0037664152 scopus 로고
    • Actinospectacin, a new antibiotic. II. Microbiological assay
    • Hanka LJ, Mason DJ and Sokolski W T. 1961. Actinospectacin, a new antibiotic. II. Microbiological assay. Antibiot Chemother 11:123-126.
    • (1961) Antibiot Chemother , vol.11 , pp. 123-126
    • Hanka, L.J.1    Mason, D.J.2    Sokolski, W.T.3
  • 114
    • 0036342198 scopus 로고    scopus 로고
    • Te structures of four macrolide antibiotics bound to the large ribosomal subunit
    • Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB and Steitz TA. 2002a. Te structures of four macrolide antibiotics bound to the large ribosomal subunit. Mol Cell 10:117-128.
    • (2002) Mol Cell , vol.10 , pp. 117-128
    • Hansen, J.L.1    Ippolito, J.A.2    Ban, N.3    Nissen, P.4    Moore, P.B.5    Steitz, T.A.6
  • 116
    • 0038013670 scopus 로고    scopus 로고
    • Structures of fve antibiotics bound at the peptidyl transferase center of the large ribos-omal subunit
    • Hansen JL, Moore PB and Steitz TA. 2003. Structures of fve antibiotics bound at the peptidyl transferase center of the large ribos-omal subunit. J Mol Biol 330:1061-1075.
    • (2003) J Mol Biol , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 117
    • 0032950956 scopus 로고    scopus 로고
    • Te macrolide-ke-tolide antibiotic binding site is formed by structures in domains II and v of 23S ribosomal RNA
    • Hansen LH, Mauvais P and Douthwaite S. 1999. Te macrolide-ke-tolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA. Mol Microbiol 31:623-631.
    • (1999) Mol Microbiol , vol.31 , pp. 623-631
    • Hansen, L.H.1    Mauvais, P.2    Douthwaite, S.3
  • 118
    • 3242712966 scopus 로고    scopus 로고
    • Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfo-pristin and quinupristin
    • Harms J, Schluenzen F, Fucini P, Bartels H and Yonath A. 2004. Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfo-pristin and quinupristin. BMC Biol 2:4.
    • (2004) BMC Biol , vol.2 , pp. 4
    • Harms, J.1    Schluenzen, F.2    Fucini, P.3    Bartels, H.4    Yonath, A.5
  • 120
    • 0023405923 scopus 로고
    • Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors
    • Hausner TP, Atmadja J and Nierhaus KH. 1987. Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors. Biochimie 69:911-923.
    • (1987) Biochimie , vol.69 , pp. 911-923
    • Hausner, T.P.1    Atmadja, J.2    Nierhaus, K.H.3
  • 121
    • 0023741257 scopus 로고
    • Te allos-teric three site model for the ribosomal elongation cycle. New insights into the inhibition mechanisms of aminoglycosides, thiostrepton, and viomycin
    • Hausner TP, Geigenmüller U and Nierhaus KH. 1988. Te allos-teric three site model for the ribosomal elongation cycle. New insights into the inhibition mechanisms of aminoglycosides, thiostrepton, and viomycin. J Biol Chem 263:13103-13111.
    • (1988) J Biol Chem , vol.263 , pp. 13103-13111
    • Hausner, T.P.1    Geigenmüller, U.2    Nierhaus, K.H.3
  • 122
    • 0030850832 scopus 로고    scopus 로고
    • Structure-activity relationships of hygromycin A and its analogs: Protein synthesis inhibition activity in a cell free system
    • Hayashi SF, Norcia LJL, Seibel SB and Silvia AM. 1997. Structure-activity relationships of hygromycin A and its analogs: Protein synthesis inhibition activity in a cell free system. J. Antibiot. 50: 514-521.
    • (1997) J. Antibiot , vol.50 , pp. 514-521
    • Hayashi, S.F.1    Norcia, L.J.L.2    Seibel, S.B.3    Silvia, A.M.4
  • 123
    • 0034635128 scopus 로고    scopus 로고
    • Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: Atomic basis for GE2270A inhibition of EF-Tu
    • Hefron SE and Jurnak F. 2000. Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu. Biochemistry 39: 37-45.
    • (2000) Biochemistry , vol.39 , pp. 37-45
    • Hefron, S.E.1    Jurnak, F.2
  • 124
    • 70450236663 scopus 로고    scopus 로고
    • Garrett RA, Douthwaite SR, Liljas A, Matheson AT, Moore PB and Noller HF, eds Te Ribosome. Structure, Function, Antibiotics, and Cellular Interactions, Washington, DC: ASM press
    • Hilgenfeld R, Mesters J and Hogg T. 2000. Insights into the GTPase mechanism of EF-Tu from structural studies, pp. 347-357. In: Garrett RA, Douthwaite SR, Liljas A, Matheson AT, Moore PB and Noller HF, eds Te Ribosome. Structure, Function, Antibiotics, and Cellular Interactions, Washington, DC: ASM press.
    • (2000) Insights into the GTPase Mechanism of EF-Tu from Structural Studies , pp. 347-357
    • Hilgenfeld, R.1    Mesters, J.2    Hogg, T.3
  • 126
    • 23644456851 scopus 로고    scopus 로고
    • Te role of ribosome recycling factor in dissociation of 70S ribos-omes into subunits
    • Hirokawa G, Nijman R, Raj V, Kaji H, Igarashi K and Kaji A. 2005. Te role of ribosome recycling factor in dissociation of 70S ribos-omes into subunits. RNA 11:1317-11128
    • (2005) RNA , vol.11 , pp. 1317-11128
    • Hirokawa, G.1    Nijman, R.2    Raj, V.3    Kaji, H.4    Igarashi, K.5    Kaji, A.6
  • 127
    • 0016203943 scopus 로고
    • Te mode of action of pleuromu-tilin derivatives. Efect on cell-free polypeptide synthesis
    • Hodgin LA and Hogenauer G. 1974. Te mode of action of pleuromu-tilin derivatives. Efect on cell-free polypeptide synthesis. Eur J Biochem 47:527-533.
    • (1974) Eur J Biochem , vol.47 , pp. 527-533
    • Hodgin, L.A.1    Hogenauer, G.2
  • 128
    • 0016733664 scopus 로고
    • Te production of dihydrospec-tinomycin by Streptomyces spectabilis
    • Hoeksema H and Knight JC. 1975. Te production of dihydrospec-tinomycin by Streptomyces spectabilis. J Antibiot (Tokyo) 28:240-241.
    • (1975) J Antibiot (Tokyo) , vol.28 , pp. 240-241
    • Hoeksema, H.1    Knight, J.C.2
  • 129
    • 0016668072 scopus 로고
    • Te mode of action of pleuromutilin derivatives. Location and properties of the pleuromutilin binding site on Escherichia coli ribosomes
    • Hogenauer G. 1975. Te mode of action of pleuromutilin derivatives. Location and properties of the pleuromutilin binding site on Escherichia coli ribosomes. Eur J Biochem 52:93-98.
    • (1975) Eur J Biochem , vol.52 , pp. 93-98
    • Hogenauer, G.1
  • 130
    • 0035999878 scopus 로고    scopus 로고
    • Inhibitory mechanisms of antibiotics targeting elongation factor Tu
    • Hogg T, Mesters JR and Hilgenfeld R. 2002. Inhibitory mechanisms of antibiotics targeting elongation factor Tu. Curr Protein Pept Sci 3:121-131.
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 121-131
    • Hogg, T.1    Mesters, J.R.2    Hilgenfeld, R.3
  • 131
    • 35648951171 scopus 로고    scopus 로고
    • From amino acids to heteroaro-matics--thiopeptide antibiotics, nature's heterocyclic peptides
    • Hughes RA and Moody CJ. 2007. From amino acids to heteroaro-matics-- thiopeptide antibiotics, nature's heterocyclic peptides. Angew Chem Int Ed Engl 46:7930-7954.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 7930-7954
    • Hughes, R.A.1    Moody, C.J.2
  • 132
    • 0023139432 scopus 로고
    • 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80 S ribosome targeted antibiotic anisomycin
    • Hummel H and Boeck A. 1987a. 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80 S ribosome targeted antibiotic anisomycin. Nucleic Acids Res 15:2431-2443.
    • (1987) Nucleic Acids Res , vol.15 , pp. 2431-2443
    • Hummel, H.1    Boeck, A.2
  • 133
    • 0023544379 scopus 로고
    • Tiostrepton resistance mutations in the gene for 23S ribosomal RNA of halobacteria
    • Hummel H and Boeck A. 1987b. Tiostrepton resistance mutations in the gene for 23S ribosomal RNA of halobacteria. Biochimie 69:857-861.
    • (1987) Biochimie , vol.69 , pp. 857-861
    • Hummel, H.1    Boeck, A.2
  • 135
    • 0031553990 scopus 로고    scopus 로고
    • Determination of eukaryotic peptidyltransferase activity by pseudo-frst-order kinetic analysis
    • Ioannou M, Coutsogeorgopoulos C and Drainas D. 1997. Determination of eukaryotic peptidyltransferase activity by pseudo-frst-order kinetic analysis. Anal Biochem 247:115-122.
    • (1997) Anal Biochem , vol.247 , pp. 115-122
    • Ioannou, M.1    Coutsogeorgopoulos, C.2    Drainas, D.3
  • 137
    • 58149142988 scopus 로고    scopus 로고
    • Multidrug-resistant to extensively drug resistant tuberculosis: What is next?
    • Jain A and Dixit P. 2008. Multidrug-resistant to extensively drug resistant tuberculosis: what is next? J Biosci 33:605-616.
    • (2008) J Biosci , vol.33 , pp. 605-616
    • Jain, A.1    Dixit, P.2
  • 138
    • 33746106088 scopus 로고    scopus 로고
    • Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2?-O-methylations in 16S and 23S rRNAs
    • Johansen SK, Maus CE, Plikaytis BB and Douthwaite S. 2006. Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2?-O-methylations in 16S and 23S rRNAs. Mol Cell 23:173-182.
    • (2006) Mol Cell , vol.23 , pp. 173-182
    • Johansen, S.K.1    Maus, C.E.2    Plikaytis, B.B.3    Douthwaite, S.4
  • 139
    • 0028944493 scopus 로고
    • A new mutation in 16S rRNA of Escherichia coli conferring spectinomycin resistance
    • Johanson U and Hughes D. 1995. A new mutation in 16S rRNA of Escherichia coli conferring spectinomycin resistance. Nucleic Acids Res 23:464-466.
    • (1995) Nucleic Acids Res , vol.23 , pp. 464-466
    • Johanson, U.1    Hughes, D.2
  • 140
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translo-case
    • Jorgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG and Andersen GR. 2003. Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translo-case. Nat Struct Biol 10:379-385.
    • (2003) Nat Struct Biol , vol.10 , pp. 379-385
    • Jorgensen, R.1    Ortiz, P.A.2    Carr-Schmid, A.3    Nissen, P.4    Kinzy, T.G.5    Andersen, G.R.6
  • 141
    • 0032488918 scopus 로고    scopus 로고
    • Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis
    • Justice MC, Hsu MJ, Tse B, Ku T, Balkovec J, Schmatz D and Nielsen J. 1998. Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J Biol Chem 273:3148-3151.
    • (1998) J Biol Chem , vol.273 , pp. 3148-3151
    • Justice, M.C.1    Hsu, M.J.2    Tse, B.3    Ku, T.4    Balkovec, J.5    Schmatz, D.6    Nielsen, J.7
  • 142
    • 58649086299 scopus 로고    scopus 로고
    • An unexpected type of ribosomes induced by kasugamycin: A look into ancestral times of protein synthesis?
    • Kaberdina AC, Szafarski W, Nierhaus KH and Moll I. 2009. An unexpected type of ribosomes induced by kasugamycin: a look into ancestral times of protein synthesis? Mol Cell 33:227-236.
    • (2009) Mol Cell , vol.33 , pp. 227-236
    • Kaberdina, A.C.1    Szafarski, W.2    Nierhaus, K.H.3    Moll, I.4
  • 144
    • 0032706754 scopus 로고    scopus 로고
    • Slow sequential confor-mational changes in Escherichia coli ribosomes induced by lin-comycin: Kinetic evidence
    • Kallia-Raftopoulos S and Kalpaxis DL. 1999. Slow sequential confor-mational changes in Escherichia coli ribosomes induced by lin-comycin: kinetic evidence. Mol Pharmacol 56:1042-1046.
    • (1999) Mol Pharmacol , vol.56 , pp. 1042-1046
    • Kallia-Raftopoulos, S.1    Kalpaxis, D.L.2
  • 145
    • 0027988447 scopus 로고
    • Dissociation rate of cognate pep-tidyl-tRNA from the A-site of hyper-accurate and error-prone ribosomes
    • Karimi R and Ehrenberg M. 1994. Dissociation rate of cognate pep-tidyl-tRNA from the A-site of hyper-accurate and error-prone ribosomes. Eur J Biochem 226:355-360.
    • (1994) Eur J Biochem , vol.226 , pp. 355-360
    • Karimi, R.1    Ehrenberg, M.2
  • 146
    • 14844357497 scopus 로고    scopus 로고
    • Translation and protein synthesis: Mac-rolides
    • Katz L and Ashley GW. 2005. Translation and protein synthesis: mac-rolides. Chem Rev 105:499-528.
    • (2005) Chem Rev , vol.105 , pp. 499-528
    • Katz, L.1    Ashley, G.W.2
  • 147
    • 34250157042 scopus 로고    scopus 로고
    • Mutations in 16S rRNA and ribos-omal protein S5 associated with high-level spectinomycin resistance in Pasteurella multocida
    • Kehrenberg C and Schwarz S. 2007. Mutations in 16S rRNA and ribos-omal protein S5 associated with high-level spectinomycin resistance in Pasteurella multocida. Antimicrob Agents Chemother 51:2244-2246.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2244-2246
    • Kehrenberg, C.1    Schwarz, S.2
  • 148
    • 23744453392 scopus 로고    scopus 로고
    • A new mechanism for chloramphenicol, forfenicol and clindamy-cin resistance: Methylation of 23S ribosomal RNA at A2503
    • Kehrenberg C, Schwarz S, Jacobsen L, Hansen L and Vester B. 2005. A new mechanism for chloramphenicol, forfenicol and clindamy-cin resistance: methylation of 23S ribosomal RNA at A2503. Mol Microbiol 57:1064-1073.
    • (2005) Mol Microbiol , vol.57 , pp. 1064-1073
    • Kehrenberg, C.1    Schwarz, S.2    Jacobsen, L.3    Hansen, L.4    Vester, B.5
  • 149
    • 0033584879 scopus 로고    scopus 로고
    • Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl trans-ferase center
    • Kloss P, Xiong L, Shinabarger DL and Mankin AS. 1999. Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl trans-ferase center. J Mol Biol 294:93-101.
    • (1999) J Mol Biol , vol.294 , pp. 93-101
    • Kloss, P.1    Xiong, L.2    Shinabarger, D.L.3    Mankin, A.S.4
  • 150
    • 0036839695 scopus 로고    scopus 로고
    • Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA
    • Kofoed CB and Vester B. 2002. Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA. Antimicrob Agents Chemother 46:3339-3342.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3339-3342
    • Kofoed, C.B.1    Vester, B.2
  • 151
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski MA, Dwyer DJ, Hayete B, Lawrence CA and Collins JJ. 2007. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130:797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 152
    • 55449126342 scopus 로고    scopus 로고
    • Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death
    • Kohanski MA, Dwyer DJ, Wierzbowski J, Cottarel G and Collins JJ. 2008. Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Cell 135:679-690.
    • (2008) Cell , vol.135 , pp. 679-690
    • Kohanski, M.A.1    Dwyer, D.J.2    Wierzbowski, J.3    Cottarel, G.4    Collins, J.J.5
  • 153
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • Kosolapov A and Deutsch C. 2009. Tertiary interactions within the ribosomal exit tunnel. Nat Struct Mol Biol 16:405-411.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 154
    • 33747348387 scopus 로고    scopus 로고
    • Unraveling new features of clindamycin interaction with functional ribosomes and dependence of the drug potency on polyamines
    • Kouvela EC, Petropoulos AD and Kalpaxis DL. 2006. Unraveling new features of clindamycin interaction with functional ribosomes and dependence of the drug potency on polyamines. J Biol Chem 281:23103-23110.
    • (2006) J Biol Chem , vol.281 , pp. 23103-23110
    • Kouvela, E.C.1    Petropoulos, A.D.2    Kalpaxis, D.L.3
  • 155
    • 0000190405 scopus 로고    scopus 로고
    • Neidhardt FC, ed. Escherichia coli and Salmonella, Cellular and Molecular Biology, Washington DC: ASM Press
    • Kurland CG, Hughes D and Ehrenberg M. 1996. Limitations of translational accuracy, pp. 979-1004. In: Neidhardt FC, ed. Escherichia coli and Salmonella, Cellular and Molecular Biology, Washington DC: ASM Press.
    • (1996) Limitations of Translational Accuracy , pp. 979-1004
    • Kurland, C.G.1    Hughes, D.2    Ehrenberg, M.3
  • 156
    • 0015043629 scopus 로고
    • Altered methylation of ribosomal RNA in an erythromycin-resistant strain of Staphylococcus aureus
    • Lai CJ and Weisblum B. 1971. Altered methylation of ribosomal RNA in an erythromycin-resistant strain of Staphylococcus aureus. Proc Natl Acad Sci USA 68:856-860.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 856-860
    • Lai, C.J.1    Weisblum, B.2
  • 158
    • 0033369771 scopus 로고    scopus 로고
    • Quinupristin/dalfopristin: A review of its use in the management of serious Gram-positive infections
    • Lamb HM, Figgitt DP and Faulds D. 1999. Quinupristin/dalfopristin: a review of its use in the management of serious gram-positive infections. Drugs 58:1061-1097. (Pubitemid 30055047)
    • (1999) Drugs , vol.58 , Issue.6 , pp. 1061-1097
    • Lamb, H.M.1    Figgitt, D.P.2    Faulds, D.3
  • 159
    • 0026561004 scopus 로고
    • Inhibition of bacterial protein synthesis by elongation-factor-Tu-binding antibiotics MDL-62,879 and Efrotomycin
    • Landini P, Bandera M, Goldstein BP, Ripamonti F, Sofentini A, Islam K and Denaro M. 1992. Inhibition of bacterial protein synthesis by elongation-factor-Tu-binding antibiotics MDL-62,879 and Efrotomycin. Biochem J 283:649-652.
    • (1992) Biochem J , vol.283 , pp. 649-652
    • Landini, P.1    Bandera, M.2    Goldstein, B.P.3    Ripamonti, F.4    Sofentini, A.5    Islam, K.6    Denaro, M.7
  • 160
    • 0034903857 scopus 로고    scopus 로고
    • Initiation factor if 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA
    • La Teana A, Gualerzi CO and Dahlberg AE. 2001. Initiation factor IF 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA. RNA 7:1173-1179.
    • (2001) RNA , vol.7 , pp. 1173-1179
    • La Teana, A.1    Gualerzi, C.O.2    Dahlberg, A.E.3
  • 163
    • 0025999638 scopus 로고
    • Chemical, biochemical and genetic endeavours characterizing the interaction of sparsomycin with the ribosome
    • Lazaro E, Van dBL, San FA, Ottenheijm HC and Ballesta JP. 1991a. Chemical, biochemical and genetic endeavours characterizing the interaction of sparsomycin with the ribosome. Biochimie 73:1137-1143.
    • (1991) Biochimie , vol.73 , pp. 1137-1143
    • Lazaro, E.1    Van, D.B.L.2    San, F.A.3    Ottenheijm, H.C.4    Ballesta, J.P.5
  • 164
    • 0026008858 scopus 로고
    • Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes
    • Lazaro E, Vandenbroek LAGM, Felix AS, Ottenheijm HCJ and Ballesta JPG. 1991b. Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes. Biochemistry 30:9642-9648.
    • (1991) Biochemistry , vol.30 , pp. 9642-9648
    • Lazaro, E.1    Lagm, V.2    Felix, A.S.3    Ottenheijm, H.C.J.4    Ballesta, J.P.G.5
  • 165
    • 0030590237 scopus 로고    scopus 로고
    • A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modifcation at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA
    • Lazaro E, Rodriguezfonseca C, Porse B, Urena D, Garrett RA and Ballesta JPG. 1996. A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modifcation at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA. J Mol Biol 261:231-238.
    • (1996) J Mol Biol , vol.261 , pp. 231-238
    • Lazaro, E.1    Rodriguezfonseca, C.2    Porse, B.3    Urena, D.4    Garrett, R.A.5    Ballesta, J.P.G.6
  • 167
    • 35549006992 scopus 로고
    • Actinospectacin, a new antibiotic. III in vitro and in vivo evaluation
    • Lewis C and Clapp HW. 1961. Actinospectacin, a new antibiotic. III. In vitro and in vivo evaluation. Antibiot Chemother 11:127-133.
    • (1961) Antibiot Chemother , vol.11 , pp. 127-133
    • Lewis, C.1    Clapp, H.W.2
  • 168
    • 60549109637 scopus 로고    scopus 로고
    • Tiopeptide biosynthesis featuring ribosoma-lly synthesized precursor peptides and conserved posttransla-tional modifcations
    • Liao R, Duan L, Lei C, Pan H, Ding Y, Zhang Q, Chen D, Shen B, Yu Y and Liu W. 2009. Tiopeptide biosynthesis featuring ribosoma-lly synthesized precursor peptides and conserved posttransla-tional modifcations. Chem Biol 16:141-147.
    • (2009) Chem Biol , vol.16 , pp. 141-147
    • Liao, R.1    Duan, L.2    Lei, C.3    Pan, H.4    Ding, Y.5    Zhang, Q.6    Chen, D.7    Shen, B.8    Yu, Y.9    Liu, W.10
  • 169
    • 0015947011 scopus 로고
    • Structural basis for inhibition of protein synthesis by the aminoacyl-aminohexosyl-cyto-sine group of antibiotics
    • Lichtenthaler F and Trummlitz G. 1974. Structural basis for inhibition of protein synthesis by the aminoacyl-aminohexosyl-cyto-sine group of antibiotics. FEBS Lett 38:237-242.
    • (1974) FEBS Lett , vol.38 , pp. 237-242
    • Lichtenthaler, F.1    Trummlitz, G.2
  • 171
    • 0030773903 scopus 로고    scopus 로고
    • Te oxazo-lidinone eperezolid binds to the 50S ribosomal subunit and competes with binding of chloramphenicol and lincomycin
    • Lin AH, Murray RW, Vidmar TJ and Marotti KR. 1997. Te oxazo-lidinone eperezolid binds to the 50S ribosomal subunit and competes with binding of chloramphenicol and lincomycin. Antimicrob Agents Chemother 41:2127-2131.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2127-2131
    • Lin, A.H.1    Murray, R.W.2    Vidmar, T.J.3    Marotti, K.R.4
  • 172
    • 0017165021 scopus 로고
    • Dual actions of viomycin on the ribos-omal functions
    • Liou Y and Tanaka N. 1976. Dual actions of viomycin on the ribos-omal functions. Biochem Biophys Res Commun 71:477-483.
    • (1976) Biochem Biophys Res Commun , vol.71 , pp. 477-483
    • Liou, Y.1    Tanaka, N.2
  • 173
    • 0141890246 scopus 로고    scopus 로고
    • Recombination profciency infuences frequency and locus of mutational resistance to linezolid in Enterococcus faecalis
    • Lobritz M, Hutton-Tomas R, Marshall S and Rice LB. 2003. Recombination profciency infuences frequency and locus of mutational resistance to linezolid in Enterococcus faecalis. Antimicrob Agents Chemother 47:3318-3320.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3318-3320
    • Lobritz, M.1    Hutton-Tomas, R.2    Marshall, S.3    Rice, L.B.4
  • 175
    • 33645767206 scopus 로고    scopus 로고
    • Interaction of pleuromutilin derivatives with the ribosomal peptidyl trans-ferase center
    • Long KS, Hansen LH, Jakobsen L and Vester B. 2006. Interaction of pleuromutilin derivatives with the ribosomal peptidyl trans-ferase center. Antimicrob Agents Chemother 50:1458-1462.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1458-1462
    • Long, K.S.1    Hansen, L.H.2    Jakobsen, L.3    Vester, B.4
  • 176
    • 60649086618 scopus 로고    scopus 로고
    • Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket
    • Long KS, Poehlsgaard J, Hansen LH, Hobbie SN, Bottger EC and Vester B. 2009. Single 23S rRNA mutations at the ribosomal peptidyl transferase centre confer resistance to valnemulin and other antibiotics in Mycobacterium smegmatis by perturbation of the drug binding pocket. Mol Microbiol 71:1218-1227.
    • (2009) Mol Microbiol , vol.71 , pp. 1218-1227
    • Long, K.S.1    Poehlsgaard, J.2    Hansen, L.H.3    Hobbie, S.N.4    Bottger, E.C.5    Vester, B.6
  • 178
    • 28544449949 scopus 로고    scopus 로고
    • Folding zones inside the ribosomal exit tunnel
    • Lu J and Deutsch C. 2005. Folding zones inside the ribosomal exit tunnel. Nat Struct Mol Biol 12:1123-1129.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1123-1129
    • Lu, J.1    Deutsch, C.2
  • 179
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu J and Deutsch C. 2008. Electrostatics in the ribosomal tunnel modulate chain elongation rates. J Mol Biol 384:73-86.
    • (2008) J Mol Biol , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 180
    • 0037229886 scopus 로고    scopus 로고
    • Comparison of x-ray crystal structure of the 30S subunit-antibiotic complex with NMR structure of decoding site oligonucleotide-paromomycin complex
    • Lynch SR, Gonzalez Jr, RL, and Puglisi JD. 2003. Comparison of x-ray crystal structure of the 30S subunit-antibiotic complex with NMR structure of decoding site oligonucleotide-paromomycin complex. Structure 11:43-53.
    • (2003) Structure , vol.11 , pp. 43-53
    • Lynch, S.R.1    Gonzalez Jr, R.L.2    Puglisi, J.D.3
  • 181
    • 63849261309 scopus 로고    scopus 로고
    • Inhibition of bacterial ribosome assembly: A suitable drug target?
    • Maguire BA. 2009. Inhibition of bacterial ribosome assembly: a suitable drug target? Microbiol Mol Biol Rev 73:22-35.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 22-35
    • Maguire, B.A.1
  • 182
    • 0035385073 scopus 로고    scopus 로고
    • Ribosomal antibiotics
    • Mankin AS. 2001. Ribosomal antibiotics. Molecular Biology 35:509-520.
    • (2001) Molecular Biology , vol.35 , pp. 509-520
    • Mankin, A.S.1
  • 184
    • 0028134851 scopus 로고
    • Cross-hypersensitivity efects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding
    • Mankin AS, Leviev I and Garrett RA. 1994. Cross-hypersensitivity efects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding. J Mol Biol 244:151-157.
    • (1994) J Mol Biol , vol.244 , pp. 151-157
    • Mankin, A.S.1    Leviev, I.2    Garrett, R.A.3
  • 186
    • 0034786898 scopus 로고    scopus 로고
    • EmtA, a rRNA methyltransferase conferring high-level evernim-icin resistance
    • FM, Goering RV, Black TA, Hare RS and McNicholas PM. 2001. EmtA, a rRNA methyltransferase conferring high-level evernim-icin resistance. Mol Microbiol 41:1349-1356.
    • (2001) Mol Microbiol , vol.41 , pp. 1349-1356
    • Fm Goering, R.V.1    Black, T.A.2    Hare, R.S.3    McNicholas, P.M.4
  • 188
    • 0000482768 scopus 로고
    • Actinospectacin, a new antibiotic I. Discovery and biological properties
    • Mason DJ, Dietz A and Smith RM. 1961. Actinospectacin, a new antibiotic. I. Discovery and biological properties. Antibiot Chemother 11:118-122.
    • (1961) Antibiot Chemother , vol.11 , pp. 118-122
    • Mason, D.J.1    Dietz, A.2    Smith, R.M.3
  • 190
    • 23044445646 scopus 로고    scopus 로고
    • Molecular analysis of cross-resistance to capreomycin, kanamycin, amikacin, and viomycin in Mycobacterium tuberculosis
    • Maus CE, Plikaytis BB and Shinnick TM. 2005. Molecular analysis of cross-resistance to capreomycin, kanamycin, amikacin, and viomycin in Mycobacterium tuberculosis. Antimicrob Agents Chemother 49:3192-3197.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3192-3197
    • Maus, C.E.1    Plikaytis, B.B.2    Shinnick, T.M.3
  • 191
    • 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
    • McNicholas PM, Najarian DJ, Mann PA, Hesk D, Hare RS, Shaw KJ and Black TA. 2000. 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 44:1121-1126.
    • (2000) Antimicrob Agents Chemother , vol.44 , 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
  • 193
    • 0020322533 scopus 로고
    • Erythromycin, carbomycin and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes
    • Menninger J and Otto D. 1982. Erythromycin, carbomycin and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes. Antimicrob Agents Chemother 21:811-818.
    • (1982) Antimicrob Agents Chemother , vol.21 , pp. 811-818
    • Menninger, J.1    Otto, D.2
  • 194
    • 33947240700 scopus 로고    scopus 로고
    • Ribosomal protein L3: Gatekeeper to the A site
    • Meskauskas A and Dinman JD. 2007. Ribosomal protein L3: gatekeeper to the A site. Mol Cell 25:877-888.
    • (2007) Mol Cell , vol.25 , pp. 877-888
    • Meskauskas, A.1    Dinman, J.D.2
  • 195
    • 28544434886 scopus 로고    scopus 로고
    • Identifcation of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis
    • Meskauskas A, Petrov AN and Dinman JD. 2005. Identifcation of functionally important amino acids of ribosomal protein L3 by saturation mutagenesis. Mol Cell Biol 25:10863-10874.
    • (2005) Mol Cell Biol , vol.25 , pp. 10863-10874
    • Meskauskas, A.1    Petrov, A.N.2    Dinman, J.D.3
  • 196
    • 0035476599 scopus 로고    scopus 로고
    • Methylation of the nucleobases in RNA oligonucle-otides mediates duplex-hairpin conversion
    • Micura R, Pils W, Hobartner C, Grubmayr K, Ebert M and Jaun B. 2001. Methylation of the nucleobases in RNA oligonucle-otides mediates duplex-hairpin conversion. Nucleic Acids Res 29:3997-4005.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3997-4005
    • Micura, R.1    Pils, W.2    Hobartner, C.3    Grubmayr, K.4    Ebert, M.5    Jaun, B.6
  • 197
    • 42949109089 scopus 로고    scopus 로고
    • Linezolid and tiamulin cross-resistance in Staphylococcus aureus mediated by point mutations in the peptidyl transferase center
    • Miller K, Dunsmore CJ, Fishwick CW and Chopra I. 2008. Linezolid and tiamulin cross-resistance in Staphylococcus aureus mediated by point mutations in the peptidyl transferase center. Antimicrob Agents Chemother 52:1737-1742.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1737-1742
    • Miller, K.1    Dunsmore, C.J.2    Fishwick, C.W.3    Chopra, I.4
  • 198
    • 0018078433 scopus 로고
    • Interaction of kanamycin and related antibiotics with the large subunit of ribosomes and the inhibition of translocation
    • Misumi M, Nishimura T, Komai T and Tanaka N. 1978. Interaction of kanamycin and related antibiotics with the large subunit of ribosomes and the inhibition of translocation. Biochem Biophys Res Commun 84:358-365.
    • (1978) Biochem Biophys Res Commun , vol.84 , pp. 358-365
    • Misumi, M.1    Nishimura, T.2    Komai, T.3    Tanaka, N.4
  • 199
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA
    • Moazed D and Noller HF. 1987a. Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie 69:879-884.
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 200
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed D and Noller HF. 1987b. Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327:389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 201
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23S rRNA in the ribosomal A, P, and e sites
    • Moazed D and Noller HF. 1989. Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites. Cell 57:585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 202
    • 0023722010 scopus 로고
    • Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA
    • Moazed D, Robertson JM and Noller HF. 1988. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA. Nature 334:362-364.
    • (1988) Nature , vol.334 , pp. 362-364
    • Moazed, D.1    Robertson, J.M.2    Noller, H.F.3
  • 203
    • 0017730231 scopus 로고
    • Te inhibition of ribosomal translo-cation by viomycin
    • Modolell J and Vazquez D. 1977. Te inhibition of ribosomal translo-cation by viomycin. Eur J Biochem 81:491-497.
    • (1977) Eur J Biochem , vol.81 , pp. 491-497
    • Modolell, J.1    Vazquez, D.2
  • 204
    • 0031566186 scopus 로고    scopus 로고
    • Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora rosea has an unexpected resistance profle against EF-Tu targeted antibiotics
    • Mohrle VG, Tieleman LN and Kraal B. 1997. Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora rosea has an unexpected resistance profle against EF-Tu targeted antibiotics. Biochem Biophys Res Commun 230:320-326.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 320-326
    • Mohrle, V.G.1    Tieleman, L.N.2    Kraal, B.3
  • 205
    • 0036035334 scopus 로고    scopus 로고
    • Diferential inhibition of 30S and 70S translation initiation complexes on leaderless mRNA by kasugamy-cin
    • Moll I and Bläsi U. 2002. Diferential inhibition of 30S and 70S translation initiation complexes on leaderless mRNA by kasugamy-cin. Biochem Biophys Res Comm 297:1021-1026.
    • (2002) Biochem Biophys Res Comm , vol.297 , pp. 1021-1026
    • Moll, I.1    Bläsi, U.2
  • 206
    • 3042690803 scopus 로고    scopus 로고
    • Translation initiation with 70S ribosomes: An alternative pathway for leader-less mRNAs
    • Moll I, Hirokawa G, Kiel MC, Kaji A and Blasi U. 2004. Translation initiation with 70S ribosomes: an alternative pathway for leader-less mRNAs. Nucleic Acids Res 32:3354-3363.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3354-3363
    • Moll, I.1    Hirokawa, G.2    Kiel, M.C.3    Kaji, A.4    Blasi, U.5
  • 207
    • 0014691601 scopus 로고
    • Action of sparsomycin on ribosome-catalysed peptidyl transfer
    • Monro RE, Celma ML and Vazquez D. 1969. Action of sparsomycin on ribosome-catalysed peptidyl transfer. Nature 222:356-358.
    • (1969) Nature , vol.222 , pp. 356-358
    • Monro, R.E.1    Celma, M.L.2    Vazquez, D.3
  • 208
    • 0043268903 scopus 로고    scopus 로고
    • Te structural basis of large ribosomal subunit function
    • Moore P and Steitz T. 2003. Te structural basis of large ribosomal subunit function. Annu Rev Biochem 72:813-850.
    • (2003) Annu Rev Biochem , vol.72 , pp. 813-850
    • Moore, P.1    Steitz, T.2
  • 209
    • 14844365696 scopus 로고    scopus 로고
    • Streptogramins, oxazolidinones, and other inhibitors of bacterial protein synthesis
    • Mukhtar TA and Wright GD. 2005. Streptogramins, oxazolidinones, and other inhibitors of bacterial protein synthesis. Chem Rev 105:529-542.
    • (2005) Chem Rev , vol.105 , pp. 529-542
    • Mukhtar, T.A.1    Wright, G.D.2
  • 213
    • 58249108035 scopus 로고    scopus 로고
    • Recent advances in the chemistry and biology of naturally occurring antibiotics
    • Nicolaou KC, Chen JS, Edmonds DJ and Estrada AA. 2009. Recent advances in the chemistry and biology of naturally occurring antibiotics. Angew Chem Int Ed Engl 48:660-719.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 660-719
    • Nicolaou, K.C.1    Chen, J.S.2    Edmonds, D.J.3    Estrada, A.A.4
  • 215
    • 0034637161 scopus 로고    scopus 로고
    • Te structural basis of ribosome activity in peptide bond synthesis
    • Nissen P, Hansen J, Ban N, Moore PB and Steitz TA. 2000. Te structural basis of ribosome activity in peptide bond synthesis. Science 289:920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 216
    • 0024446773 scopus 로고
    • Analysis of the reversible binding of virginiamycin M to ribosome and particle functions after removal of the antibiotic
    • Nyssen E, Di Giambattista M and Cocito C. 1989. Analysis of the reversible binding of virginiamycin M to ribosome and particle functions after removal of the antibiotic. Biochim Biophys Acta 1009:39-46.
    • (1989) Biochim Biophys Acta , vol.1009 , pp. 39-46
    • Nyssen, E.1    Di Giambattista, M.2    Cocito, C.3
  • 218
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle JM, Murphy FV, Tarry MJ and Ramakrishnan V. 2002. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111:721-732.
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 219
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • Ogle J, Carter A and Ramakrishnan V. 2003. Insights into the decoding mechanism from recent ribosome structures. TIBS 28:259-266.
    • (2003) TIBS , vol.28 , pp. 259-266
    • Ogle, J.1    Carter, A.2    Ramakrishnan, V.3
  • 220
    • 0014961204 scopus 로고
    • Complex formation of fusidic acid with G factor, ribosome and guanosine nucleotide
    • Okura A, Kinoshita T and Tanaka N. 1970. Complex formation of fusidic acid with G factor, ribosome and guanosine nucleotide. Biochem Biophys Res Comm 41:1545-1550.
    • (1970) Biochem Biophys Res Comm , vol.41 , pp. 1545-1550
    • Okura, A.1    Kinoshita, T.2    Tanaka, N.3
  • 221
    • 0016710554 scopus 로고
    • Release of (oligo)peptidyl-tRNA from ribosomes by erythromycin A
    • Otaka T and Kaji A. 1975. Release of (oligo)peptidyl-tRNA from ribosomes by erythromycin A. Proc Natl Acad Sci USA 72:2649-2652.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2649-2652
    • Otaka, T.1    Kaji, A.2
  • 222
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically competent intermediates in the translocation step of protein synthesis
    • Pan D, Kirillov SV and Cooperman BS. 2007. Kinetically competent intermediates in the translocation step of protein synthesis. Mol Cell 25:519-529.
    • (2007) Mol Cell , vol.25 , pp. 519-529
    • Pan, D.1    Kirillov, S.V.2    Cooperman, B.S.3
  • 223
    • 0033961143 scopus 로고    scopus 로고
    • Conformational switch in the decoding region of 16S rRNA during aminoacyl-tRNA selection on the ribosome
    • Pape T, Wintermeyer W and Rodnina MV. 2000. Conformational switch in the decoding region of 16S rRNA during aminoacyl-tRNA selection on the ribosome. Nat Struct Bio 7:104-107.
    • (2000) Nat Struct Bio , vol.7 , pp. 104-107
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 224
    • 0019143485 scopus 로고
    • Lasting damage to bacterial ribosomes by reversibly bound virginiamycin M
    • Parfait R and Cocito C. 1980. Lasting damage to bacterial ribosomes by reversibly bound virginiamycin M. Proc Natl Acad Sci USA 77:5492-5496.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5492-5496
    • Parfait, R.1    Cocito, C.2
  • 225
    • 0018087547 scopus 로고
    • A spectrofluorimetric study of the interaction between virginiamycin S and bacterial ribosomes
    • Parfait R, de Bethune MP and Cocito C. 1978. A spectrofuorimetric study of the interaction between virginiamycin S and bacterial ribosomes. Mol Gen Genet 166:45-51. (Pubitemid 9047092)
    • (1978) Molecular and General Genetics , vol.166 , Issue.1 , pp. 45-51
    • Parfait, R.1    De Bethune, M.P.2    Cocito, C.3
  • 226
    • 0019407040 scopus 로고
    • Competition between erythromycin and virginiamycin for in vitro binding to the large ribosomal subunit
    • Parfait R, Di Giambattista M and Cocito C. 1981. Competition between erythromycin and virginiamycin for in vitro binding to the large ribosomal subunit. Biochim Biophys Acta 654:236-241.
    • (1981) Biochim Biophys Acta , vol.654 , pp. 236-241
    • Parfait, R.1    Di Giambattista, M.2    Cocito, C.3
  • 227
    • 42649103317 scopus 로고    scopus 로고
    • Retapamulin: A new topical antibiotic for the treatment of uncomplicated skin infections
    • Parish LC and Parish JL. 2008. Retapamulin: a new topical antibiotic for the treatment of uncomplicated skin infections. Drugs Today (Barc) 44:91-102.
    • (2008) Drugs Today (Barc) , vol.44 , pp. 91-102
    • Parish, L.C.1    Parish, J.L.2
  • 228
    • 33746882485 scopus 로고    scopus 로고
    • Elongation factor Tu-targeted antibiotics: Four diferent structures, two mechanisms of action
    • Parmeggiani A and Nissen P. 2006b. Elongation factor Tu-targeted antibiotics: four diferent structures, two mechanisms of action. FEBS Lett 580:4576-4581.
    • (2006) FEBS Lett , vol.580 , pp. 4576-4581
    • Parmeggiani, A.1    Nissen, P.2
  • 229
    • 33646231052 scopus 로고    scopus 로고
    • Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics
    • Parmeggiani A, Krab IM, Watanabe T, Nielsen RC, Dahlberg C, Nyborg J and Nissen P. 2006. Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics. J Biol Chem 281:2893-2900.
    • (2006) J Biol Chem , vol.281 , pp. 2893-2900
    • Parmeggiani, A.1    Krab, I.M.2    Watanabe, T.3    Nielsen, R.C.4    Dahlberg, C.5    Nyborg, J.6    Nissen, P.7
  • 231
    • 6344252614 scopus 로고    scopus 로고
    • During elongation factor G-dependent tRNA-mRNA transloca-tion
    • during elongation factor G-dependent tRNA-mRNA transloca-tion. J Mol Biol 343:1183-1194.
    • J Mol Biol , vol.343 , pp. 1183-1194
  • 232
    • 0014678722 scopus 로고
    • Studies on the formation of transfer ribonucleic acid-ribosome complexes. X. Phenylalanyl-oligonucleotide binding to ribosomes and the mechanism of chloramphenicol action
    • Pestka S. 1969a. Studies on the formation of transfer ribonucleic acid-ribosome complexes. X. Phenylalanyl-oligonucleotide binding to ribosomes and the mechanism of chloramphenicol action. Biochem Biophys Res Commun 36:589-595.
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 589-595
    • Pestka, S.1
  • 234
    • 2942705913 scopus 로고    scopus 로고
    • Polyamines afect diversely the antibiotic potency: Insight gained from kinetic studies of the blasticidin S and spiramycin interactions with functional ribosomes
    • Petropoulos AD, Xaplanteri MA, Dinos GP, Wilson DN and Kalpaxis DL. 2004. Polyamines afect diversely the antibiotic potency: insight gained from kinetic studies of the blasticidin S and spiramycin interactions with functional ribosomes. J Biol Chem 279:26518-26525.
    • (2004) J Biol Chem , vol.279 , pp. 26518-26525
    • Petropoulos, A.D.1    Xaplanteri, M.A.2    Dinos, G.P.3    Wilson, D.N.4    Kalpaxis, D.L.5
  • 236
    • 0142075322 scopus 로고    scopus 로고
    • The molecular basis for A-site mutations conferring aminoglycoside resistance: Relationship between ribosomal susceptibility and X-ray crystal structures
    • DOI 10.1002/cbic.200300657
    • Pfster P, Hobbie S, Vicens Q, Bottger E and Westhof E. 2003. Te molecular basis for A-site mutations conferring aminoglycoside resistance: relationship between ribosomal susceptibility and X-ray crystal structures. Chembiochem 4:1078-1088. (Pubitemid 37267597)
    • (2003) ChemBioChem , vol.4 , Issue.10 , pp. 1078-1088
    • Pfister, P.1    Hobbie, S.2    Vicens, Q.3    Bottger, E.C.4    Westhof, E.5
  • 238
    • 77958029293 scopus 로고
    • Hygromycin I. Preliminary studies in the production and biologic activity on a new antibiotic
    • Pittenger RC, Wolfe RN, Hoehn PN, Daily WA and McGuire JM. 1953. Hygromycin. I. Preliminary studies in the production and biologic activity on a new antibiotic. Antibiot Chemother 3:1268-1278.
    • (1953) Antibiot Chemother , vol.3 , pp. 1268-1278
    • Pittenger, R.C.1    Wolfe, R.N.2    Hoehn, P.N.3    Daily, W.A.4    McGuire, J.M.5
  • 239
    • 0037303518 scopus 로고    scopus 로고
    • Macrolide antibiotic interaction and resistance on the bacterial ribosome
    • Poehlsgaard J and Douthwaite S. 2003. Macrolide antibiotic interaction and resistance on the bacterial ribosome. Curr Opin Investig Drugs 4:140-148.
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 140-148
    • Poehlsgaard, J.1    Douthwaite, S.2
  • 241
    • 31344478504 scopus 로고    scopus 로고
    • Te ribosomal peptidyl transferase center: Structure, function, evolution, inhibition
    • Polacek N and Mankin AS. 2005. Te ribosomal peptidyl transferase center: structure, function, evolution, inhibition. Crit Rev Biochem Mol Biol 40:285-311.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 285-311
    • Polacek, N.1    Mankin, A.S.2
  • 242
    • 0033582599 scopus 로고    scopus 로고
    • Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms
    • Porse BT and Garrett RA. 1999. Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms. J Mol Biol 286:375-387.
    • (1999) J Mol Biol , vol.286 , pp. 375-387
    • Porse, B.T.1    Garrett, R.A.2
  • 243
    • 0029403050 scopus 로고
    • Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity
    • Porse B, Rodriguez-Fonseca C, Leviev I and Garrett R. 1995. Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. Biochem Cell Biol 73:877-885.
    • (1995) Biochem Cell Biol , vol.73 , pp. 877-885
    • Porse, B.1    Rodriguez-Fonseca, C.2    Leviev, I.3    Garrett, R.4
  • 244
    • 0032548821 scopus 로고    scopus 로고
    • Te antibiotic thiostrepon inhibits a functional transition within protein L11 at the ribosomal GTPase centre
    • Porse BT, Leviev I, Mankin AS and Garrett RA. 1998. Te antibiotic thiostrepon inhibits a functional transition within protein L11 at the ribosomal GTPase centre. J Mol Biol 276:391-404.
    • (1998) J Mol Biol , vol.276 , pp. 391-404
    • Porse, B.T.1    Leviev, I.2    Mankin, A.S.3    Garrett, R.A.4
  • 245
    • 0033583095 scopus 로고    scopus 로고
    • Te antibiotic micrococ-cin acts on protein L11 at the ribosomal GTPase centre
    • Porse BT, Cundlife E and Garrett RA. 1999a. Te antibiotic micrococ-cin acts on protein L11 at the ribosomal GTPase centre. J Mol Biol 287:33-45.
    • (1999) J Mol Biol , vol.287 , pp. 33-45
    • Porse, B.T.1    Cundlife, E.2    Garrett, R.A.3
  • 246
    • 0033529799 scopus 로고    scopus 로고
    • Direct crosslinking of the antitumor antibiotic spar-somycin, and its derivatives, to A2602 in the peptidyl transferase center of 23S-like rRNA within ribosome-tRNA complexes
    • Porse BT, Kirillov SV, Awayez MJ, Ottenheijm HC and Garrett RA. 1999b. Direct crosslinking of the antitumor antibiotic spar-somycin, and its derivatives, to A2602 in the peptidyl transferase center of 23S-like rRNA within ribosome-tRNA complexes. Proc Natl Acad Sci USA 96:9003-9008.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9003-9008
    • Porse, B.T.1    Kirillov, S.V.2    Awayez, M.J.3    Ottenheijm, H.C.4    Garrett, R.A.5
  • 248
    • 0034406527 scopus 로고    scopus 로고
    • Inhibition of the ribos-omal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin
    • Poulsen SM, Kofoed C and Vester B. 2000. Inhibition of the ribos-omal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin. J Mol Biol 304:471-481.
    • (2000) J Mol Biol , vol.304 , pp. 471-481
    • Poulsen, S.M.1    Kofoed, C.2    Vester, B.3
  • 249
    • 9644301282 scopus 로고    scopus 로고
    • Mutations in ribosomal protein L3 and 23S ribosomal RNA at the pepti-dyl transferase centre are associated with reduced susceptibility to tiamulin in Brachyspira spp. isolates
    • Pringle M, Poehlsgaard J, Vester B and Long KS. 2004. Mutations in ribosomal protein L3 and 23S ribosomal RNA at the pepti-dyl transferase centre are associated with reduced susceptibility to tiamulin in Brachyspira spp. isolates. Mol Microbiol 54:1295-1306.
    • (2004) Mol Microbiol , vol.54 , pp. 1295-1306
    • Pringle, M.1    Poehlsgaard, J.2    Vester, B.3    Long, K.S.4
  • 251
    • 33750799914 scopus 로고    scopus 로고
    • Te highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin Y, Polacek N, Vesper O, Staub E, Einfeldt E, Wilson DN and Nierhaus KH. 2006. Te highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127:721-733.
    • (2006) Cell , vol.127 , 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
  • 252
    • 41149135521 scopus 로고    scopus 로고
    • RRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance
    • Rakauskaite R and Dinman JD. 2008. rRNA mutants in the yeast peptidyltransferase center reveal allosteric information networks and mechanisms of drug resistance. Nucleic Acids Res 36:1497-1507.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1497-1507
    • Rakauskaite, R.1    Dinman, J.D.2
  • 253
    • 60349100340 scopus 로고    scopus 로고
    • Programmed drug-dependent ribosome stalling
    • Ramu H, Mankin A and Vazquez-Laslop N. 2009. Programmed drug-dependent ribosome stalling. Mol Microbiol 71:811-824.
    • (2009) Mol Microbiol , vol.71 , pp. 811-824
    • Ramu, H.1    Mankin, A.2    Vazquez-Laslop, N.3
  • 254
    • 0028275776 scopus 로고
    • Inhibition of protein synthesis occurring on tetracycline-resistant, TetM-protected ribosomes by a novel class of tetracyclines, the glycylcyclines
    • Rasmussen BA, Gluzman Y and Tally FP. 1994. Inhibition of protein synthesis occurring on tetracycline-resistant, TetM-protected ribosomes by a novel class of tetracyclines, the glycylcyclines. Antimicrob Agents Chemother 38:1658-1660.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1658-1660
    • Rasmussen, B.A.1    Gluzman, Y.2    Tally, F.P.3
  • 255
    • 0025151914 scopus 로고
    • Partial release of AcPhe-Phe-transfer RNA from ribosomes during Poly(U)-dependent Poly(Phe) synthesis and the efects of chloramphenicol
    • Rheinberger HJ and Nierhaus KH. 1990. Partial release of AcPhe-Phe-transfer RNA from ribosomes during Poly(U)-dependent Poly(Phe) synthesis and the efects of chloramphenicol. Eur J Biochem 193:643-650.
    • (1990) Eur J Biochem , vol.193 , pp. 643-650
    • Rheinberger, H.J.1    Nierhaus, K.H.2
  • 256
    • 0032526960 scopus 로고    scopus 로고
    • Te structure of a methylated tetraloop in 16S ribosomal RNA
    • Rife JP and Moore PB. 1998. Te structure of a methylated tetraloop in 16S ribosomal RNA. Structure 6:747-756.
    • (1998) Structure , vol.6 , pp. 747-756
    • Rife, J.P.1    Moore, P.B.2
  • 258
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca C, Amils R and Garrett RA. 1995. Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J Mol Biol 247:224-235.
    • (1995) J Mol Biol , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 259
    • 0031917769 scopus 로고    scopus 로고
    • Te antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite
    • Rogers MJ, Cundlife E and McCutchan TF. 1998. Te antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite. Antimicrob Agents Chemother 42:715-716.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 715-716
    • Rogers, M.J.1    Cundlife, E.2    McCutchan, T.F.3
  • 260
    • 0028355760 scopus 로고
    • Te antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A
    • Rosendahl G and Douthwaite S. 1994. Te antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A. Nucleic Acids Res 22:357-363.
    • (1994) Nucleic Acids Res , vol.22 , pp. 357-363
    • Rosendahl, G.1    Douthwaite, S.2
  • 261
    • 0031862823 scopus 로고    scopus 로고
    • 16S rRNA mutation associated with tetracycline resistance in a gram-positive bacterium
    • Ross JI, Eady EA, Cove JH and Cunlife WJ. 1998. 16S rRNA mutation associated with tetracycline resistance in a gram-positive bacterium. Antimicrob Agents Chemother 42:1702-1705.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1702-1705
    • Ross, J.I.1    Eady, E.A.2    Cove, J.H.3    Cunlife, W.J.4
  • 263
    • 0026771498 scopus 로고
    • Novel mutants of 23S RNA-characterization of functional properties
    • Saarma U and Remme J. 1992. Novel mutants of 23S RNA-characterization of functional properties. Nucleic Acids Res 20:3147-3152.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3147-3152
    • Saarma, U.1    Remme, J.2
  • 264
    • 27644502679 scopus 로고    scopus 로고
    • Simulating movement of tRNA into the ribosome during decoding
    • Sanbonmatsu KY, Joseph S and Tung CS. 2005. Simulating movement of tRNA into the ribosome during decoding. Proc Natl Acad Sci USA 102:15854-15859.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15854-15859
    • Sanbonmatsu, K.Y.1    Joseph, S.2    Tung, C.S.3
  • 265
    • 0036886952 scopus 로고    scopus 로고
    • Ribosomal and non-ribosomal resistance to oxazolidi-nones: Species-specifc idiosyncrasy of ribosomal alterations
    • Sander P, Belova L, Kidan YG, Pfster P, Mankin AS and Bottger EC. 2002. Ribosomal and non-ribosomal resistance to oxazolidi-nones: species-specifc idiosyncrasy of ribosomal alterations. Mol Microbiol 46:1295-1304.
    • (2002) Mol Microbiol , vol.46 , pp. 1295-1304
    • Sander, P.1    Belova, L.2    Kidan, Y.G.3    Pfster, P.4    Mankin, A.S.5    Bottger, E.C.6
  • 266
    • 65249164177 scopus 로고    scopus 로고
    • Distinct functions of elongation factor G in ribosome recycling and translo-cation
    • Savelsbergh A, Rodnina MV and Wintermeyer W. 2009. Distinct functions of elongation factor G in ribosome recycling and translo-cation. RNA 15:772-780.
    • (2009) RNA , vol.15 , pp. 772-780
    • Savelsbergh, A.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 268
    • 0037166262 scopus 로고    scopus 로고
    • Codon-anticodon interaction at the P Site is a prerequisite for tRNA interaction with the small ribosomal subunit
    • Schäfer MA, Tastan AO, Patzke S, Blaha G, Spahn CM, Wilson DN and Nierhaus KH. 2002. Codon-anticodon interaction at the P Site is a prerequisite for tRNA interaction with the small ribosomal subunit. J Biol Chem 277:19095-19105.
    • (2002) J Biol Chem , vol.277 , pp. 19095-19105
    • Schäfer, M.A.1    Tastan, A.O.2    Patzke, S.3    Blaha, G.4    Spahn, C.M.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 271
    • 9644281855 scopus 로고    scopus 로고
    • Inhibition of peptide bond formation by pleuromutilins: The structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin
    • Schlünzen F, Pyetan E, Fucini P, Yonath A and Harms J. 2004. Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin. Mol Microbiol 54:1287-1294.
    • (2004) Mol Microbiol , vol.54 , pp. 1287-1294
    • Schlünzen, F.1    Pyetan, E.2    Fucini, P.3    Yonath, A.4    Harms, J.5
  • 274
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2? hydroxyl of the P site tRNA in the peptidyl transferase reaction
    • Schmeing TM, Huang KS, Kitchen DE, Strobel SA and Steitz TA. 2005a. Structural insights into the roles of water and the 2? hydroxyl of the P site tRNA in the peptidyl transferase reaction. Mol Cell 20:437-448.
    • (2005) Mol Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 275
    • 28544452248 scopus 로고    scopus 로고
    • An induced-ft mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing TM, Huang KS, Strobel SA and Steitz TA. 2005b. An induced-ft mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438:520-524.
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 279
    • 33644542727 scopus 로고    scopus 로고
    • EF-G-dependent GTPase on the ribos-ome Conformational change and fusidic acid inhibition
    • Seo H, Abedin S, Kamp D, Wilson DN, Nierhaus KH and Cooperman BS. 2006. EF-G-dependent GTPase on the ribos-ome. Conformational change and fusidic acid inhibition. Biochemistry 45:2504-2514.
    • (2006) Biochemistry , vol.45 , pp. 2504-2514
    • Seo, H.1    Abedin, S.2    Kamp, D.3    Wilson, D.N.4    Nierhaus, K.H.5    Cooperman, B.S.6
  • 280
    • 0035135564 scopus 로고    scopus 로고
    • Species-specific inhibition of fungal protein synthesis by sordarin: Identification of a sordarin-specificity region in eukaryotic elongation factor 2
    • Shastry M, Nielsen J, Ku T, Hsu MJ, Liberator P, Anderson J, Schmatz D and Justice MC. 2001. Species-specifc inhibition of fungal protein synthesis by sordarin: identifcation of a sordarin-spe-cifcity region in eukaryotic elongation factor 2. Microbiology 147:383-390. (Pubitemid 32156814)
    • (2001) Microbiology , vol.147 , Issue.2 , pp. 383-390
    • Shastry, M.1    Nielsen, J.2    Ku, T.3    Hsu, M.-J.4    Liberator, P.5    Anderson, J.6    Schmatz, D.7    Justice, M.C.8
  • 282
    • 33845631049 scopus 로고    scopus 로고
    • Reverse translocation of tRNA in the ribosome
    • Shoji S, Walker SE and Fredrick K. 2006. Reverse translocation of tRNA in the ribosome. Mol Cell 24:931-942.
    • (2006) Mol Cell , vol.24 , pp. 931-942
    • Shoji, S.1    Walker, S.E.2    Fredrick, K.3
  • 283
    • 0343417099 scopus 로고
    • Erythromycin resistance due to a mutation in a ribosomal RNA operon of Escherichia coli
    • Sigmund CD and Morgan EA. 1982. Erythromycin resistance due to a mutation in a ribosomal RNA operon of Escherichia coli. Proc Natl Acad Sci USA 79:5602-5606.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5602-5606
    • Sigmund, C.D.1    Morgan, E.A.2
  • 284
    • 59749083182 scopus 로고    scopus 로고
    • Erythromycin-and chloramphenicol-induced ribosomal assembly defects are secondary efects of protein synthesis inhibition
    • Siibak T, Peil L, Xiong L, Mankin A, Remme J and Tenson T. 2009. Erythromycin-and chloramphenicol-induced ribosomal assembly defects are secondary efects of protein synthesis inhibition. Antimicrob Agents Chemother 53:563-571.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 563-571
    • Siibak, T.1    Peil, L.2    Xiong, L.3    Mankin, A.4    Remme, J.5    Tenson, T.6
  • 286
    • 0021064473 scopus 로고
    • Site of action of a ribos-omal RNA methylase responsible for resistance to erythromycin and other antibiotics
    • Skinner R, Cundlife E and Schmidt FJ. 1983. Site of action of a ribos-omal RNA methylase responsible for resistance to erythromycin and other antibiotics. J Biol Chem 258:12702-12706.
    • (1983) J Biol Chem , vol.258 , pp. 12702-12706
    • Skinner, R.1    Cundlife, E.2    Schmidt, F.J.3
  • 288
    • 0029745623 scopus 로고    scopus 로고
    • Trowing a spanner in the works: Antibiotics and the translational apparatus
    • Spahn CMT and Prescott CD. 1996. Trowing a spanner in the works: antibiotics and the translational apparatus. J Mol Med 74:423-439.
    • (1996) J Mol Med , vol.74 , pp. 423-439
    • Spahn, C.M.T.1    Prescott, C.D.2
  • 290
    • 34548339675 scopus 로고    scopus 로고
    • Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome
    • Spiegel PC, Ermolenko DN and Noller HF. 2007. Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome. RNA 13:1473-1482.
    • (2007) RNA , vol.13 , pp. 1473-1482
    • Spiegel, P.C.1    Ermolenko, D.N.2    Noller, H.F.3
  • 291
    • 9744275238 scopus 로고    scopus 로고
    • Lincosamides: Chemical structure, biosynthesis, mechanism of action, resistance, and applications
    • Spizek J, Novotna J and Rezanka T. 2004. Lincosamides: chemical structure, biosynthesis, mechanism of action, resistance, and applications. Adv Appl Microbiol 56:121-154.
    • (2004) Adv Appl Microbiol , vol.56 , pp. 121-154
    • Spizek, J.1    Novotna, J.2    Rezanka, T.3
  • 292
    • 0030770467 scopus 로고    scopus 로고
    • Visualization of elongation factor Tu on the Escherichia coli ribosome
    • DOI 10.1038/38770
    • Stark H, Rodnina MV, Rinkeappel J, Brimacombe R, Wintermeyer W and Vanheel M. 1997. Visualization of Elongation Factor Tu On the Escherichia Coli Ribosome. Nature 389:403-406. (Pubitemid 27415225)
    • (1997) Nature , vol.389 , Issue.6649 , pp. 403-406
    • Stark, H.1    Rodnina, M.V.2    Rinke-Appel, J.3    Brimacombe, R.4    Wintermeyer, W.5    Van Heel, M.6
  • 293
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz TA. 2008. A structural understanding of the dynamic ribosome machine. Nat Rev Mol Cell Biol 9:242-253.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 294
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • Stirpe F and Battelli MG. 2006. Ribosome-inactivating proteins: progress and problems. Cell Mol Life Sci 63:1850-1866.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 295
    • 70450282089 scopus 로고
    • Nucleoside Antibiotics, NY: Wiley
    • Suhadolnik R. 1970. Nucleoside Antibiotics, NY: Wiley.
    • (1970)
    • Suhadolnik, R.1
  • 296
    • 25144480034 scopus 로고    scopus 로고
    • Improving on nature: Antibiotics that target the ribosome
    • Sutclife JA. 2005. Improving on nature: antibiotics that target the ribosome. Curr Opin Microbiol 8:534-542.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 534-542
    • Sutclife, J.A.1
  • 297
    • 0025783792 scopus 로고
    • Mutation Proximal to the Transfer-RNA Binding Region of the Nicotiana Plastid 16S rRNA Confers Resistance to Spectinomycin
    • Svab Z and Maliga P. 1991. Mutation Proximal to the Transfer-RNA Binding Region of the Nicotiana Plastid 16S rRNA Confers Resistance to Spectinomycin. Mol Gen Genet 228:316-319.
    • (1991) Mol Gen Genet , vol.228 , pp. 316-319
    • Svab, Z.1    Maliga, P.2
  • 298
  • 299
    • 44649171519 scopus 로고    scopus 로고
    • New features of the ribosome and ribosomal inhibitors: Non-enzymatic recycling, misreading and back-transloca-tion
    • Szafarski W, Vesper O, Teraoka Y, Plitta B, Wilson DN and Nierhaus KH. 2008. New features of the ribosome and ribosomal inhibitors: non-enzymatic recycling, misreading and back-transloca-tion. J Mol Biol 380:193-205.
    • (2008) J Mol Biol , vol.380 , pp. 193-205
    • Szafarski, W.1    Vesper, O.2    Teraoka, Y.3    Plitta, B.4    Wilson, D.N.5    Nierhaus, K.H.6
  • 300
    • 0016210059 scopus 로고
    • Selective action of erythro-mycin on initiating ribosomes
    • Tai P-C, Wallace BJ and Davis BD. 1974. Selective action of erythro-mycin on initiating ribosomes. Biochemistry 13:4653-4659.
    • (1974) Biochemistry , vol.13 , pp. 4653-4659
    • Tai, P.-C.1    Wallace, B.J.2    Davis, B.D.3
  • 301
    • 0038474136 scopus 로고    scopus 로고
    • Structural consideration of macrolide antibiotics in relation to the ribosomal interaction and drug design
    • Takashima H. 2003. Structural consideration of macrolide antibiotics in relation to the ribosomal interaction and drug design. Curr Top Med Chem 3:991-999.
    • (2003) Curr Top Med Chem , vol.3 , pp. 991-999
    • Takashima, H.1
  • 303
    • 0030590258 scopus 로고    scopus 로고
    • Mutations in the pepti-dyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation
    • Tan GT, Deblasio A and Mankin AS. 1996. Mutations in the pepti-dyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation. J Mol Biol 261:222-230.
    • (1996) J Mol Biol , vol.261 , pp. 222-230
    • Tan, G.T.1    Deblasio, A.2    Mankin, A.S.3
  • 304
    • 0037040406 scopus 로고    scopus 로고
    • Regulatory nascent peptides in the ribosomal tunnel
    • Tenson T and Ehrenberg M. 2002. Regulatory nascent peptides in the ribosomal tunnel. Cell 108:591-594.
    • (2002) Cell , vol.108 , pp. 591-594
    • Tenson, T.1    Ehrenberg, M.2
  • 305
    • 0034817784 scopus 로고    scopus 로고
    • Short peptides conferring resistance to macrolide antibiotics
    • Tenson T and Mankin A. 2001. Short peptides conferring resistance to macrolide antibiotics. Peptides 22:1661-1668.
    • (2001) Peptides , vol.22 , pp. 1661-1668
    • Tenson, T.1    Mankin, A.2
  • 306
    • 0038690158 scopus 로고    scopus 로고
    • Te mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome
    • Tenson T, Lovmar M and Ehrenberg M. 2003. Te mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome. J Mol Biol 330:1005-1014.
    • (2003) J Mol Biol , vol.330 , pp. 1005-1014
    • Tenson, T.1    Lovmar, M.2    Ehrenberg, M.3
  • 307
    • 0020468991 scopus 로고
    • Biochemical characterization of resistance determinants cloned from antibiotic-producing streptomycetes
    • Tompson CJ, Skinner RH, Tompson J, Ward JM, Hopwood DA and Cundlife E. 1982. Biochemical characterization of resistance determinants cloned from antibiotic-producing streptomycetes. J Bacteriol 151:678-685.
    • (1982) J Bacteriol , vol.151 , pp. 678-685
    • Tompson, C.J.1    Skinner, R.H.2    Tompson, J.3    Ward, J.M.4    Hopwood, D.A.5    Cundlife, E.6
  • 308
    • 0018497597 scopus 로고
    • Binding of thiostrep-ton to a complex of 23S rRNA with ribosomal protein L11
    • Tompson J, Cundlife E and Stark M. 1979. Binding of thiostrep-ton to a complex of 23S rRNA with ribosomal protein L11. Eur J Biochem 98:261-265.
    • (1979) Eur J Biochem , vol.98 , pp. 261-265
    • Tompson, J.1    Cundlife, E.2    Stark, M.3
  • 309
    • 0023689001 scopus 로고
    • Site-directed muta-genesis of Escherichia coli 23S ribosomal RNA at position 1067 within the GTP hydrolysis center
    • Tompson J, Cundlife E and Dahlberg AE. 1988. Site-directed muta-genesis of Escherichia coli 23S ribosomal RNA at position 1067 within the GTP hydrolysis center. J Mol Biol 203:457-465.
    • (1988) J Mol Biol , vol.203 , pp. 457-465
    • Tompson, J.1    Cundlife, E.2    Dahlberg, A.E.3
  • 310
    • 0036384314 scopus 로고    scopus 로고
    • Te protein synthesis inhibitors, oxazolidinones and chlorampheni-col, cause extensive translational inaccuracy in vivo
    • Tompson J, O'Connor M, Mills JA and Dahlberg AE. 2002. Te protein synthesis inhibitors, oxazolidinones and chlorampheni-col, cause extensive translational inaccuracy in vivo. J Mol Biol 322:273-279.
    • (2002) J Mol Biol , vol.322 , pp. 273-279
    • Tompson, J.1    O'connor, M.2    Mills, J.A.3    Dahlberg, A.E.4
  • 311
    • 9644265316 scopus 로고    scopus 로고
    • Efects of a number of classes of 50S inhibitors on stop codon readthrough during protein synthesis
    • Tompson J, Pratt CA and Dahlberg AE. 2004. Efects of a number of classes of 50S inhibitors on stop codon readthrough during protein synthesis. Antimicrob Agents Chemother 48:4889-4891.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4889-4891
    • Tompson, J.1    Pratt, C.A.2    Dahlberg, A.E.3
  • 312
    • 67651158789 scopus 로고    scopus 로고
    • Conformational changes in switch i of EF-G drive its directional cycling on and of the ribosome
    • Ticu C, Nechifor R, Nguyen B, Desrosiers M and Wilson KS. 2009. Conformational changes in switch I of EF-G drive its directional cycling on and of the ribosome. EMBO J 28: 2053-2065.
    • (2009) EMBO J , vol.28 , pp. 2053-2065
    • Ticu, C.1    Nechifor, R.2    Nguyen, B.3    Desrosiers, M.4    Wilson, K.S.5
  • 313
    • 0036204635 scopus 로고    scopus 로고
    • Mutations in the 16S rRNA genes of Helicobacter pylori mediate resistance to tetracycline
    • Trieber CA and Taylor DE. 2002. Mutations in the 16S rRNA genes of Helicobacter pylori mediate resistance to tetracycline. J Bacteriol 184:2131-2140.
    • (2002) J Bacteriol , vol.184 , pp. 2131-2140
    • Trieber, C.A.1    Taylor, D.E.2
  • 314
    • 0032493758 scopus 로고    scopus 로고
    • Ketolide resistance conferred by short peptides
    • Tripathi S, Kloss PS and Mankin AS. 1998. Ketolide resistance conferred by short peptides. J Biol Chem 273:20073-20077.
    • (1998) J Biol Chem , vol.273 , pp. 20073-20077
    • Tripathi, S.1    Kloss, P.S.2    Mankin, A.S.3
  • 315
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu D, Blaha G, Moore P and Steitz T. 2005. Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 121:257-270.
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.3    Steitz, T.4
  • 316
    • 0018186765 scopus 로고
    • Cooperative binding of 3? fragments of tRNA to the peptidyltransferase centre of E. coli ribosomes
    • Ulbrich B, Mertens G and Nierhaus KH. 1978. Cooperative binding of 3? fragments of tRNA to the peptidyltransferase centre of E. coli ribosomes. Arch Biochem Biophys 190:149-154.
    • (1978) Arch Biochem Biophys , vol.190 , pp. 149-154
    • Ulbrich, B.1    Mertens, G.2    Nierhaus, K.H.3
  • 317
    • 66449107983 scopus 로고    scopus 로고
    • Accuracy modulating mutations of the ribosomal protein S4-S5 interface do not necessarily destabilize the rps4-rps5 protein-protein interaction
    • Vallabhaneni H and Farabaugh PJ. 2009. Accuracy modulating mutations of the ribosomal protein S4-S5 interface do not necessarily destabilize the rps4-rps5 protein-protein interaction. RNA 15:1100-1109.
    • (2009) RNA , vol.15 , pp. 1100-1109
    • Vallabhaneni, H.1    Farabaugh, P.J.2
  • 320
    • 0026671180 scopus 로고
    • Te role of rRNA bases in the interaction of peptidyltransferase inhibitors with bacterial ribosomes
    • Vannufel P, Digiambattista M and Cocito C. 1992. Te role of rRNA bases in the interaction of peptidyltransferase inhibitors with bacterial ribosomes. J Biol Chem 267.
    • (1992) J Biol Chem 267
    • Vannufel, P.1    Digiambattista, M.2    Cocito, C.3
  • 321
    • 0028099297 scopus 로고
    • Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl-transferase domain
    • Vannufel P, Digiambattista M and Cocito C. 1994. Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl-transferase domain. Nucleic Acids Res 22:4449-4453.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4449-4453
    • Vannufel, P.1    Digiambattista, M.2    Cocito, C.3
  • 322
    • 70450269809 scopus 로고
    • Inhibitors of Protein Synthesis, Berlin, Heidelberg, New York: Springer
    • Vasquez D. 1979. Inhibitors of Protein Synthesis, Berlin, Heidelberg, New York: Springer.
    • (1979)
    • Vasquez, D.1
  • 323
    • 0035160878 scopus 로고    scopus 로고
    • Macrolide resistance conferred by base substitutions in 23S rRNA
    • Vester B and Douthwaite S. 2001. Macrolide resistance conferred by base substitutions in 23S rRNA. Antimicrob Agents Chemother 45:1-12.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1-12
    • Vester, B.1    Douthwaite, S.2
  • 324
    • 0034886697 scopus 로고    scopus 로고
    • Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site
    • Vicens Q and Westhof E. 2001. Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site. Structure (Camb) 9:647-658.
    • (2001) Structure (Camb) , vol.9 , pp. 647-658
    • Vicens, Q.1    Westhof, E.2
  • 325
    • 0042337397 scopus 로고    scopus 로고
    • Molecular recognition of aminoglyco-side antibiotics by ribosomal RNA and resistance enzymes: An analysis of x-ray crystal structures
    • Vicens Q and Westhof E. 2003. Molecular recognition of aminoglyco-side antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures. Biopolymers 70:42-57.
    • (2003) Biopolymers , vol.70 , pp. 42-57
    • Vicens, Q.1    Westhof, E.2
  • 326
    • 0033569631 scopus 로고    scopus 로고
    • Isolation of kasugamycin resistant mutants in the 16 S ribosomal RNA of Escherichia coli
    • Vila-Sanjurjo A, Squires CL and Dahlberg AE. 1999. Isolation of kasugamycin resistant mutants in the 16 S ribosomal RNA of Escherichia coli. J Mol Biol 293:1-8.
    • (1999) J Mol Biol , vol.293 , pp. 1-8
    • Vila-Sanjurjo, A.1    Squires, C.L.2    Dahlberg, A.E.3
  • 328
    • 6344275448 scopus 로고    scopus 로고
    • Peptide-mediated macrolide resistance reveals possible specifc interactions in the nascent peptide exit tunnel
    • Vimberg V, Xiong L, Bailey M, Tenson T and Mankin A. 2004. Peptide-mediated macrolide resistance reveals possible specifc interactions in the nascent peptide exit tunnel. Mol Microbiol 54:376-385.
    • (2004) Mol Microbiol , vol.54 , pp. 376-385
    • Vimberg, V.1    Xiong, L.2    Bailey, M.3    Tenson, T.4    Mankin, A.5
  • 329
    • 0035907234 scopus 로고    scopus 로고
    • Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox
    • Vogeley L, Palm GJ, Mesters JR and Hilgenfeld R. 2001. Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox. J. Biol. Chem. 276: 17149-17155.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17149-17155
    • Vogeley, L.1    Palm, G.J.2    Mesters, J.R.3    Hilgenfeld, R.4
  • 331
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • Walsh C. 2000. Molecular mechanisms that confer antibacterial drug resistance. Nature 406:775-781.
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.1
  • 332
    • 0020382746 scopus 로고
    • New polyenic antibiotics active against gram-positive and -negative bacteria. I. Isolation and purification of antibiotics produced by Gluconobacter sp. W-315
    • Watanabe T, Izaki K and Takahashi H. 1982. New polyenic antibiotics active against Gram-positive and-negative bacteria. I. Isolation and purifcation of antibiotics produced by Gluconobacter sp. W-315. J Antibiot (Tokyo) 35:1141-1147. (Pubitemid 13256009)
    • (1982) Journal of Antibiotics , vol.35 , Issue.9 , pp. 1141-1147
    • Watanabe, T.1    Izaki, K.2    Takahashi, H.3
  • 333
    • 0026534154 scopus 로고
    • New polyenic antibiotics active against gram-positive and gram-negative bacteria. IV. Structural elucidation of enacyloxin IIa
    • Watanabe T, Sugiyama T, Takahashi M, Shima J, Yamashita K, Izaki K, Furihata K and Seto H. 1992. New polyenic antibiotics active against gram-positive and gram-negative bacteria. IV. Structural elucidation of enacyloxin IIa. J Antibiot (Tokyo) 45:470-475.
    • (1992) J Antibiot (Tokyo) , vol.45 , pp. 470-475
    • Watanabe, T.1    Sugiyama, T.2    Takahashi, M.3    Shima, J.4    Yamashita, K.5    Izaki, K.6    Furihata, K.7    Seto, H.8
  • 334
    • 0028914553 scopus 로고
    • Insights into erythromycin action from studies of its activity as inducer of resistance
    • Weisblum B. 1995. Insights into erythromycin action from studies of its activity as inducer of resistance. Antimicrob Agents Chemother 39:797-805.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 797-805
    • Weisblum, B.1
  • 335
    • 0032856049 scopus 로고    scopus 로고
    • Fusidic acid in the treatment of methicillin-resist-ant Staphylococcus aureus
    • Whitby M. 1999. Fusidic acid in the treatment of methicillin-resist-ant Staphylococcus aureus. Int J Antimicrob Agents 12 Suppl 2:S67-71.
    • (1999) Int J Antimicrob Agents , vol.2 , Issue.12 SUPPL.
    • Whitby, M.1
  • 336
    • 62449284698 scopus 로고    scopus 로고
    • Tirteen posttranslational modifcations convert a 14-residue peptide into the antibiotic thiocillin
    • Wieland Brown LC, Acker MG, Clardy J, Walsh CT and Fischbach MA. 2009. Tirteen posttranslational modifcations convert a 14-residue peptide into the antibiotic thiocillin. Proc Natl Acad Sci USA 106:2549-2553.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2549-2553
    • Wieland Brown, L.C.1    Acker, M.G.2    Clardy, J.3    Walsh, C.T.4    Fischbach, M.A.5
  • 337
    • 70450242281 scopus 로고
    • Trobicin (actinospectacin), a new injectable antibiotic in the treatment of gonorrhoea
    • Willcox RR. 1962. Trobicin (actinospectacin), a new injectable antibiotic in the treatment of gonorrhoea. Br J Vener Dis 38:150-153.
    • (1962) Br J Vener Dis , vol.38 , pp. 150-153
    • Willcox, R.R.1
  • 338
    • 0016737059 scopus 로고
    • Some characteristics of and structural requirements for the interaction of 24,25-dihydrofusidic acid with ribosome-elongation factor g Complexes
    • Willie GR, Richman N, Godtfredsen WP and Bodley JW. 1975. Some characteristics of and structural requirements for the interaction of 24,25-dihydrofusidic acid with ribosome-elongation factor g Complexes. Biochemistry 14:1713-1718.
    • (1975) Biochemistry , vol.14 , pp. 1713-1718
    • Willie, G.R.1    Richman, N.2    Godtfredsen, W.P.3    Bodley, J.W.4
  • 339
    • 84955162315 scopus 로고    scopus 로고
    • Nierhaus K and Wilson D, eds, Protein Synthesis and Ribosome Structure, Weinheim: Wiley-VCH
    • Wilson DN. 2004. Antibiotics and the inhibition of ribosome function, pp. 449-527. In: Nierhaus K and Wilson D, eds, Protein Synthesis and Ribosome Structure, Weinheim: Wiley-VCH.
    • (2004) Antibiotics and the Inhibition of Ribosome Function , pp. 449-527
    • Wilson, D.N.1
  • 340
    • 33845484606 scopus 로고    scopus 로고
    • Te E-site Story: Te importance of maintaining two tRNAs on the ribosome during protein synthesis
    • Wilson DN and Nierhaus KH. 2006. Te E-site Story: Te importance of maintaining two tRNAs on the ribosome during protein synthesis. Cell Mol Life Sci 63:2725-2737.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2725-2737
    • Wilson, D.N.1    Nierhaus, K.H.2
  • 341
    • 34250377197 scopus 로고    scopus 로고
    • Te weird and wonderful world of bacterial ribosome regulation
    • Wilson DN and Nierhaus KH. 2007. Te weird and wonderful world of bacterial ribosome regulation. Crit Rev Biochem Mol Biol 42:187-219.
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 187-219
    • Wilson, D.N.1    Nierhaus, K.H.2
  • 342
    • 29044436081 scopus 로고    scopus 로고
    • Species-specifc antibiotic-ribosome interactions: Implications for drug development
    • Wilson DN, Harms JM, Nierhaus KH, Schlünzen F and Fucini P. 2005. Species-specifc antibiotic-ribosome interactions: Implications for drug development. Biol Chem 386:1239-1252.
    • (2005) Biol Chem , vol.386 , pp. 1239-1252
    • Wilson, D.N.1    Harms, J.M.2    Nierhaus, K.H.3    Schlünzen, F.4    Fucini, P.5
  • 343
    • 51649117099 scopus 로고    scopus 로고
    • Te oxazolidinone antibiotics perturb the ribos-omal peptidyl-transferase center and efect tRNA positioning
    • Wilson DN, Schluenzen F, Harms JM, Starosta AL, Connell SR and Fucini P. 2008. Te oxazolidinone antibiotics perturb the ribos-omal peptidyl-transferase center and efect tRNA positioning. Proc Natl Acad Sci USA 105:13339-13344.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13339-13344
    • Wilson, D.N.1    Schluenzen, F.2    Harms, J.M.3    Starosta, A.L.4    Connell, S.R.5    Fucini, P.6
  • 344
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the A site of the ribosome
    • Wilson JE, Pestova T V, Hellen CUT and Sarnow P. 2000. Initiation of protein synthesis from the A site of the ribosome. Cell 102:511-520.
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.T.3    Sarnow, P.4
  • 345
    • 0015745765 scopus 로고
    • Biochemical and genetic studies on two diferent types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins
    • Wittmann HG, Stofer G, Apirion D, Rosen L, Tanaka K, Tamaki M, Takata R, Dekio S and Otaka E. 1973. Biochemical and genetic studies on two diferent types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins. Mol Gen Genet 127:175-189.
    • (1973) Mol Gen Genet , vol.127 , pp. 175-189
    • Wittmann, H.G.1    Stofer, G.2    Apirion, D.3    Rosen, L.4    Tanaka, K.5    Tamaki, M.6    Takata, R.7    Dekio, S.8    Otaka, E.9
  • 346
    • 0025799785 scopus 로고
    • Interaction of antibiotics with A-and P-site-specifc bases in 16S ribosomal RNA
    • Woodcock J, Moazed D, Cannon M, Davies J and Noller HF. 1991. Interaction of antibiotics with A-and P-site-specifc bases in 16S ribosomal RNA. EMBO J 10:3099-3103.
    • (1991) EMBO J , vol.10 , pp. 3099-3103
    • Woodcock, J.1    Moazed, D.2    Cannon, M.3    Davies, J.4    Noller, H.F.5
  • 347
    • 48749139837 scopus 로고
    • Te mechanism of action of the cytotoxic nucle-ase a-sarcin and its use to analyse ribosome structure
    • Wool IG. 1984. Te mechanism of action of the cytotoxic nucle-ase a-sarcin and its use to analyse ribosome structure. TIBS 9:14-17.
    • (1984) TIBS , vol.9 , pp. 14-17
    • Wool, I.G.1
  • 348
    • 0026690643 scopus 로고
    • Ribotoxin recognition of ribos-omal RNA and a proposal for the mechanism of translocation
    • Wool IG, Gluck A and Endo Y. 1992. Ribotoxin recognition of ribos-omal RNA and a proposal for the mechanism of translocation. Trends Biochem Sci 17:266-269.
    • (1992) Trends Biochem Sci , vol.17 , pp. 266-269
    • Wool, I.G.1    Gluck, A.2    Endo, Y.3
  • 349
    • 0035173131 scopus 로고    scopus 로고
    • Recent developments on ketolides and mac-rolides
    • Wu YJ and Su WG. 2001. Recent developments on ketolides and mac-rolides. Curr Med Chem 8:1727-1758.
    • (2001) Curr Med Chem , vol.8 , pp. 1727-1758
    • Wu, Y.J.1    Su, W.G.2
  • 350
    • 0020583413 scopus 로고
    • Te inhibition pattern of antibiotics on the extent and accuracy of tRNA
    • Wurmbach P and Nierhaus KH. 1983. Te inhibition pattern of antibiotics on the extent and accuracy of tRNA binding to the ribos-ome, and their efect on the subsequent steps in chain elongation. Eur J Biochem 130:9-12.
    • (1983) Eur J Biochem , vol.130 , pp. 9-12
    • Wurmbach, P.1    Nierhaus, K.H.2
  • 351
    • 0030020855 scopus 로고    scopus 로고
    • Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11
    • Xing YY and Draper DE. 1996. Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11. Biochemistry 35:1581-1588.
    • (1996) Biochemistry , vol.35 , pp. 1581-1588
    • Xing, Y.Y.1    Draper, D.E.2
  • 352
    • 0032904341 scopus 로고    scopus 로고
    • A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre
    • Xiong L, Shah S, Mauvais P and Mankin AS. 1999. A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre. Mol Microbiol 31:633-639.
    • (1999) Mol Microbiol , vol.31 , pp. 633-639
    • Xiong, L.1    Shah, S.2    Mauvais, P.3    Mankin, A.S.4
  • 353
    • 0018165088 scopus 로고
    • Resistance to viomycin conferred by RNA of either ribosomal subunit
    • Yamada T, Mizugichi Y, Nierhaus KH and Wittmann HG. 1978. Resistance to viomycin conferred by RNA of either ribosomal subunit. Nature 275:460-461.
    • (1978) Nature , vol.275 , pp. 460-461
    • Yamada, T.1    Mizugichi, Y.2    Nierhaus, K.H.3    Wittmann, H.G.4
  • 354
    • 0016636406 scopus 로고
    • Isolation and purifcation of blasticidin S deaminase from Aspergillus terreus
    • Yamaguchi I, Shibata H, Seto H and Misato T. 1975. Isolation and purifcation of blasticidin S deaminase from Aspergillus terreus. J Antibiot (Tokyo) 28:7-14.
    • (1975) J Antibiot (Tokyo) , vol.28 , pp. 7-14
    • Yamaguchi, I.1    Shibata, H.2    Seto, H.3    Misato, T.4
  • 355
    • 34548236988 scopus 로고    scopus 로고
    • Potential new antibiotic sites in the ribosome revealed by deleterious mutations in RNA of the large ribosomal subunit
    • Yassin A and Mankin AS. 2007. Potential new antibiotic sites in the ribosome revealed by deleterious mutations in RNA of the large ribosomal subunit. J Biol Chem 282:24329-24342.
    • (2007) J Biol Chem , vol.282 , pp. 24329-24342
    • Yassin, A.1    Mankin, A.S.2
  • 356
    • 28044462415 scopus 로고    scopus 로고
    • Deleterious mutations in small subunit ribosomal RNA identify functional sites and potential targets for antibiotics
    • Yassin A, Fredrick K and Mankin AS. 2005. Deleterious mutations in small subunit ribosomal RNA identify functional sites and potential targets for antibiotics. Proc Natl Acad Sci USA 102:16620-16625.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16620-16625
    • Yassin, A.1    Fredrick, K.2    Mankin, A.S.3
  • 358
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: Lessons from protein synthesis
    • Zaher HS and Green R. 2009a. Fidelity at the molecular level: lessons from protein synthesis. Cell 136:746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 359
    • 58149354143 scopus 로고    scopus 로고
    • Quality control by the ribosome following peptide bond formation
    • Zaher HS and Green R. 2009b. Quality control by the ribosome following peptide bond formation. Nature 457:161-166.
    • (2009) Nature , vol.457 , pp. 161-166
    • Zaher, H.S.1    Green, R.2
  • 360
    • 0036838794 scopus 로고    scopus 로고
    • Mutations in ribosomal protein L16 and in 23S rRNA in Enterococcus strains for which evernimicin MICs difer
    • Zarazaga M, Tenorio C, Del Campo R, Ruiz-Larrea F and Torres C. 2002. Mutations in ribosomal protein L16 and in 23S rRNA in Enterococcus strains for which evernimicin MICs difer. Antimicrob Agents Chemother 46:3657-3659.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3657-3659
    • Zarazaga, M.1    Tenorio, C.2    Del Campo, R.3    Ruiz-Larrea, F.4    Torres, C.5
  • 362
    • 0015116013 scopus 로고
    • Alteration of a 30S ribosomal protein accompanying the ram mutation in Escherichia coli
    • Zimmermann RA, Garvin RT and Gorini L. 1971. Alteration of a 30S ribosomal protein accompanying the ram mutation in Escherichia coli. Proc Natl Acad Sci USA 68:2263-2267.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 2263-2267
    • Zimmermann, R.A.1    Garvin, R.T.2    Gorini, L.3


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