The bacterial ribosome as a target for antibiotics

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327

The Structural Basis of Ribosome Activity in Peptide Bond Synthesis

Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269

Structure of the 30S ribosomal subunit

Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035

Crystal structure of the ribosome at 5.5 Å resolution

Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

Carter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615

The Molecular Basis of Antibiotic Action

Gale, E. F. (1981) · Medical Entomology and Zoology · Cited by 1,217

Recognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit

Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162

Interaction of antibiotics with functional sites in 16S ribosomal RNA

Moazed, D., & Noller, H. F. (1987) · Nature · doi:10.1038/327389a0 · Cited by 1,150

Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,059

Erythromycin resistance by ribosome modification

Weisblum, B. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.3.577 · Cited by 1,008

Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979

The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit

Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950

High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 901

Structure of the A Site of Escherichia coli 16 S Ribosomal RNA Complexed with an Aminoglycoside Antibiotic

Fourmy, D., Recht, M. I., Blanchard, S. C., & Puglisi, J. D. (1996) · Science · doi:10.1126/science.274.5291.1367 · Cited by 829

Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures

Noller, H. F., Hoffarth, V., & Zimniak, L. (1992) · Science · doi:10.1126/science.1604315 · Cited by 728

The Path of Messenger RNA through the Ribosome

Yusupova, G. Z., Yusupov, M. M., Cate, J. H. D., & Noller, H. F. (2001) · Cell · doi:10.1016/s0092-8674(01)00435-4 · Cited by 600

The Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit

Hansen, J. L., Ippolito, J. A., Ban, N., Nissen, P., Moore, P. B., & Steitz, T. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00570-1 · Cited by 568

Macrolide Resistance Conferred by Base Substitutions in 23S rRNA

Vester, B., & Douthwaite, S. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.1.1-12.2001 · Cited by 556

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3

Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1829 · Cited by 527

The Ribosome : structure, function, and evolution

Hill, W. E. (1990) · Medical Entomology and Zoology · Cited by 521

The ribosome: Structure, function and evolution

Edward, B., & Baden, H. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90126-g · Cited by 508

mRNA Helicase Activity of the Ribosome

Takyar, S., Hickerson, R. P., & Noller, H. F. (2005) · Cell · doi:10.1016/j.cell.2004.11.042 · Cited by 494

The Mechanism of Action of Macrolides, Lincosamides and Streptogramin B Reveals the Nascent Peptide Exit Path in the Ribosome

Tenson, T., Lovmar, M., & Ehrenberg, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00662-4 · Cited by 461

Structures of MLSBK Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance

Tu, D., Blaha, G., Moore, P. B., & Steitz, T. A. (2005) · Cell · doi:10.1016/j.cell.2005.02.005 · Cited by 433

The Roles of Ribosomal Proteins in the Structure Assembly, and Evolution of the Large Ribosomal Subunit

Klein, D. J., Moore, P. B., & Steitz, T. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.076 · Cited by 422

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., & Ban, N. (2004) · Nature · doi:10.1038/nature02899 · Cited by 418

Structures of Five Antibiotics Bound at the Peptidyl Transferase Center of the Large Ribosomal Subunit

Hansen, J. L., Moore, P. B., & Steitz, T. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00668-5 · Cited by 393

Structural origins of gentamicin antibiotic action

Yoshizawa, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6437 · Cited by 374

Crystal Structure of Paromomycin Docked into the Eubacterial Ribosomal Decoding A Site

Vicens, Q., & Westhof, E. (2001) · Structure · doi:10.1016/s0969-2126(01)00629-3 · Cited by 373

Insights into the decoding mechanism from recent ribosome structures

Ogle, J. M., Carter, A. P., & Ramakrishnan, V. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00066-5 · Cited by 371

The ribosome as an entropy trap

Sievers, A., Beringer, M., Rodnina, M. V., & Wolfenden, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402488101 · Cited by 357

The Active Site of the Ribosome Is Composed of Two Layers of Conserved Nucleotides with Distinct Roles in Peptide Bond Formation and Peptide Release

Youngman, E. M., Brunelle, J. L., Kochaniak, A. B., & Green, R. (2004) · Cell · doi:10.1016/s0092-8674(04)00411-8 · Cited by 335

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Valle, M., Zavialov, A., Li, W., Stagg, S. M., Sengupta, J., Nielsen, R. C., Nissen, P., Harvey, S. C., Ehrenberg, M., & Frank, J. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb1003 · Cited by 333

Structure of Functionally Activated Small Ribosomal Subunit

Schluenzen, F., Tocilj, A., Zarivach, R., et al. (2000) · Cited by 331

The Ribosome, Structure, Function, Antibiotics, and Cellular Interactions

Garrett, R. A. (2000) · Research at the University of Copenhagen (University of Copenhagen) · Cited by 325

Inhibitors of protein biosynthesis

(2006) · Biochemistry and Molecular Biology of Antimicrobial Drug Action · doi:10.1007/0-387-27566-5_5 · Cited by 318

Peptide bond formation by in vitro selected ribozymes

Zhang, B., & Cech, T. R. (1997) · Nature · doi:10.1038/36375 · Cited by 299

Ribosome structure determined by electron microscopy of Escherichia coli small subunits, large subunits and monomeric ribosomes

Lake, J. A. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90200-x · Cited by 295

The macrolide–ketolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA

Hansen, L. H., Mauvais, P., & Douthwaite, S. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01202.x · Cited by 291

Fine-Tuning of RNA Functions by Modification and Editing

(2005) · Topics in Current Genetics · doi:10.1007/b95147 · Cited by 289

Structural Basis of the Ribosomal Machinery for Peptide Bond Formation, Translocation, and Nascent Chain Progression

Bashan, A., Agmon, I., Zarivach, R., Schluenzen, F., Harms, J., Berisio, R., Bartels, H., Franceschi, F., Auerbach, T., Hansen, H. A. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00009-1 · Cited by 286

Mutations in 23S rRNA and Ribosomal Protein L4 Account for Resistance in Pneumococcal Strains Selected In Vitro by Macrolide Passage

Tait-Kamradt, A., Davies, T., Cronan, M., Jacobs, M. R., Appelbaum, P. C., & Sutcliffe, J. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.8.2118-2125.2000 · Cited by 281

Insights into erythromycin action from studies of its activity as inducer of resistance

Weisblum, B. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.4.797 · Cited by 267

Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics.

Skinner, R., Cundliffe, E., & Schmidt, F. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44232-3 · Cited by 263

Crystal Structure of a Complex between the Aminoglycoside Tobramycin and an Oligonucleotide Containing the Ribosomal Decoding A Site

Vicens, Q., & Westhof, E. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00153-9 · Cited by 242

Regulatory Nascent Peptides in the Ribosomal Tunnel

Tenson, T., & Ehrenberg, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00669-4 · Cited by 240

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., & Harms, J. M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04346.x · Cited by 240

Recognition of the Codon-Anticodon Helix by Ribosomal RNA

Yoshizawa, S., Fourmy, D., & Puglisi, J. D. (1999) · Science · doi:10.1126/science.285.5434.1722 · Cited by 238

Inhibitors of Protein Biosynthesis

Vázquez, D. (1979) · Molecular Biology Biochemistry and Biophysics · doi:10.1007/978-3-642-81309-2 · Cited by 238

Instruction of Translating Ribosome by Nascent Peptide

Gong, F., & Yanofsky, C. (2002) · Science · doi:10.1126/science.1073997 · Cited by 233

Structural Basis for the Antibiotic Activity of Ketolides and Azalides

Schlünzen, F., Harms, J. M., Franceschi, F., Hansen, H. A. S., Bartels, H., Zarivach, R., & Yonath, A. (2003) · Structure · doi:10.1016/s0969-2126(03)00022-4 · Cited by 231

An Active Role for tRNA in Decoding Beyond Codon:Anticodon Pairing

Cochella, L., & Green, R. (2005) · Science · doi:10.1126/science.1111408 · Cited by 213

Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl transferase center 1 1Edited by D. E. Draper

Kloss, P., Xiong, L., Shinabarger, D. L., & Mankin, A. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3247 · Cited by 213

The Polypeptide Tunnel System in the Ribosome and Its Gating in Erythromycin Resistance Mutants of L4 and L22

Gabashvili, I. S., Gregory, S. T., Valle, M., Grassucci, R., Worbs, M., Wahl, M. C., Dahlberg, A. E., & Frank, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00293-3 · Cited by 201

Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome

Rodnina, M. V., Savelsbergh, A., Matassova, N. B., Katunin, V. I., Semenkov, Y. P., & Wintermeyer, W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9586 · Cited by 186

Drugs targeting the ribosome

Hermann, T. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.05.001 · Cited by 182

Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides

Beauclerk, A. A. D., & Cundliffe, E. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90349-4 · Cited by 181

Crystal Structure of Geneticin Bound to a Bacterial 16S Ribosomal RNA A Site Oligonucleotide

Vicens, Q., & Westhof, E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01435-3 · Cited by 180

Structural insight into the role of the ribosomal tunnel in cellular regulation

Berisio, R., Schluenzen, F., Harms, J., Bashan, A., Auerbach, T., Baram, D., & Yonath, A. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb915 · Cited by 178

Translation and Protein Synthesis: Macrolides

Katz, L., & Ashley, G. W. (2005) · Chemical Reviews · doi:10.1021/cr030107f · Cited by 177

Throwing a spanner in the works: antibiotics and the translation apparatus

Spahn, C. M. T., & Prescott, C. D. (1996) · Journal of Molecular Medicine · doi:10.1007/bf00217518 · Cited by 171

Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin

Harms, J. M., Schlünzen, F., Fucini, P., Bartels, H., & Yonath, A. (2004) · BMC Biology · doi:10.1186/1741-7007-2-4 · Cited by 171

Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins

Wittmann, H. G., Stöffler, G., Apirion, D., Rosen, L., Tanaka, K., Tamaki, M., Takata, R., Dekio, S., Otaka, E., & Osawa, S. (1973) · Molecular and General Genetics MGG · doi:10.1007/bf00333665 · Cited by 169

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., & Mankin, A. S. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01203.x · Cited by 169

Architecture of the Escherichia coli ribosome as determined by immune electron microscopy.

Tischendorf, G. W., Zeichhardt, H., & Stöffler, G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.12.4820 · Cited by 168

Structural Insight into the Antibiotic Action of Telithromycin against Resistant Mutants

Berisio, R., Harms, J., Schluenzen, F., Zarivach, R., Hansen, H. A. S., Fucini, P., & Yonath, A. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.14.4276-4279.2003 · Cited by 165

Macrolides, chemistry, pharmacology and clinical uses

Vanderhaeghe, H., & Hoogmartens, J. (1993) · Cited by 165

The Structural Basis of Large Ribosomal Subunit Function

Moore, P. B., & Steitz, T. A. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.110601.135450 · Cited by 163

Visualizing tmRNA Entry into a Stalled Ribosome

Valle, M., Gillet, R., Kaur, S., Henne, A., Ramakrishnan, V., & Frank, J. (2003) · Science · doi:10.1126/science.1081798 · Cited by 154

Throwing a spanner in the works: antibiotics and the translation apparatus

Spahn, C. M. T., & Prescott, C. D. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050044 · Cited by 154

Erythromycin Resistance Mutations in Ribosomal Proteins L22 and L4 Perturb the Higher Order Structure of 23 S Ribosomal RNA

Gregory, S. T., & Dahĺberg, A. E. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2839 · Cited by 139

Translation and Protein Synthesis: Macrolides

Katz, L., & Ashley, G. W. (2005) · ChemInform · doi:10.1002/chin.200524271 · Cited by 138

Binding Site of Macrolide Antibiotics on the Ribosome: New Resistance Mutation Identifies a Specific Interaction of Ketolides with rRNA

Garza‐Ramos, G., Xiong, L., Zhong, P., & Mankin, A. S. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.23.6898-6907.2001 · Cited by 136

Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli

Chittum, H. S., & Champney, W. S. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.20.6192-6198.1994 · Cited by 134

Resistance to Macrolide, Lincosamide, Streptogramin, Ketolide, and Oxazolidinone Antibiotics

Roberts, M. C. (2004) · Molecular Biotechnology · doi:10.1385/mb:28:1:47 · Cited by 134

Characterization and preliminary attempts for derivatization of crystals of large ribosomal subunits from Haloarcula marismortui diffracting to 3 Å resolution

von Böhlen, K., Makowski, I., Hansen, H. A. S., Bartels, H., BERKOVITCH‐YELLIN, Z., Zaytzev-Bashan, A., Meyer, S., Paulke, C., Franceschi, F. J., & Yonath, A. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90730-t · Cited by 130

Ketolides—telithromycin, an example of a new class of antibacterial agents

Bryskier, A. (2000) · Clinical Microbiology and Infection · doi:10.1046/j.1469-0691.2000.00185.x · Cited by 127

Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin

Poulsen, S. M., Kofoed, C. B., & Vester, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4229 · Cited by 123

Mutations in ribosomal protein L3 and 23S ribosomal RNA at the peptidyl transferase centre are associated with reduced susceptibility to tiamulin in Brachyspira spp. isolates

Pringle, M., Poehlsgaard, J., Vester, B., & Long, K. S. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04373.x · Cited by 120

Resistance to the macrolide antibiotic tylosin is conferred by single methylations at 23S rRNA nucleotides G748 and A2058 acting in synergy

Liu, M., & Douthwaite, S. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232580599 · Cited by 112

The role of tRNA as a molecular spring in decoding, accommodation, and peptidyl transfer

Frank, J., Sengupta, J., Gao, H., Li, W., Valle, M., Zavialov, A. V., & Ehrenberg, M. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.10.105 · Cited by 107

The Protein Synthesis Inhibitors, Oxazolidinones and Chloramphenicol, Cause Extensive Translational Inaccuracy in Vivo

Thompson, J., O'Connor, M., Mills, J. A., & Dahĺberg, A. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00784-2 · Cited by 104

Activity of the Ketolide Telithromycin Is Refractory to Erm Monomethylation of Bacterial rRNA

Liu, M., & Douthwaite, S. R. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.6.1629-1633.2002 · Cited by 104

X-ray crystal structures of the WT and a hyper-accurate ribosome from Escherichia coli

Vila‐Sanjurjo, A., Ridgeway, W. K., Seymaner, V., Zhang, W., Santoso, S., Yu, K., & Cate, J. H. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1133380100 · Cited by 101

A novel site of antibiotic action in the ribosome: Interaction of evernimicin with the large ribosomal subunit

Belova, L., Tenson, T., Xiong, L., McNicholas, P. M., & Mankin, A. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071527498 · Cited by 99

The driving force for molecular evolution of translation

NOLLER, H. F. (2004) · RNA · doi:10.1261/rna.7142404 · Cited by 96

RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli

Semrad, K., Green, R., & Schroeder, R. (2004) · RNA · doi:10.1261/rna.7121704 · Cited by 91

Erythromycin Binding is Reduced in Ribosomes with Conformational Alterations in the 23 S rRNA Peptidyl Transferase Loop

Douthwaite, S. R., & Aagaard, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1426 · Cited by 86

Chemical engineering of the peptidyl transferase center reveals an important role of the 2'-hydroxyl group of A2451

Erlacher, M. D. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki308 · Cited by 86

Methylation of 23S rRNA caused by tlrA (ermSF), a tylosin resistance determinant from Streptomyces fradiae

Zalacaín, M., & Cundliffe, E. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.8.4254-4260.1989 · Cited by 84

Ribosome-Catalyzed Peptide-Bond Formation with an A-Site Substrate Covalently Linked to 23 S Ribosomal RNA

Green, R., Switzer, C., & Noller, H. F. (1998) · Science · doi:10.1126/science.280.5361.286 · Cited by 83

Control of SecA and SecM translation by protein secretion

Nakatogawa, H., Murakami, A., & Ito, K. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.01.001 · Cited by 81

23S rRNA base pair 2057–2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A→G

Pfister, P., Corti, N., Hobbie, S. N., Bruell, C. M., Zarivach, R., Yonath, A., & Böttger, E. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501598102 · Cited by 81

In Vitro Activities of Telithromycin, Linezolid, and Quinupristin-Dalfopristin against Streptococcus pneumoniae with Macrolide Resistance Due to Ribosomal Mutations

Farrell, D. J., Morrissey, I., Bakker, S., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.3169-3171.2004 · Cited by 80

Intact Aminoacyl-tRNA Is Required To Trigger GTP Hydrolysis by Elongation Factor Tu on the Ribosome

Piepenburg, O., Pape, T., Pleiss, J. A., et al. (2000) · Biochemistry · doi:10.1021/bi992331y · Cited by 76

Structural aspects of protein synthesis

Liljas, A., & Al‐Karadaghi, S. (1997) · Nature Structural Biology · doi:10.1038/nsb1097-767 · Cited by 72

Molecular Recognition by Glycoside Pseudo Base Pairs and Triples in an Apramycin–RNA Complex

Han, Q., Zhao, Q., Fish, S., Simonsen, K. B., Vourloumis, D., Froelich, J. M., Wall, D., & Hermann, T. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500028 · Cited by 70

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, P. M., Najarian, D. J., Mann, P. A., Hesk, D., Hare, R. S., Shaw, K. J., & Black, T. A. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.5.1121-1126.2000 · Cited by 66

Mutagenesis of 16S rRNA C1409-G1491 Base-pair Differentiates Between 6′OH and 6′NH3+ Aminoglycosides

Pfister, P., Hobbie, S. N., Bruell, C. M., Corti, N., Vasella, A. T., Westhof, É., & Böttger, E. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.073 · Cited by 65

Parameters for crystal growth of ribosomal subunits

Yonath, A., Müssig, J., & Wittmann, H. G. (1982) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240190205 · Cited by 64

Cloning of tlrD, a fourth resistance gene, from the tyiosin producer, Streptomyces fradiae

Zalacaín, M., & Cundliffe, E. (1991) · Gene · doi:10.1016/0378-1119(91)90021-3 · Cited by 63

Ribosomal Crystallography: Initiation, Peptide Bond Formation, and Amino Acid Polymerization are Hampered by Antibiotics

Yonath, A., & Bashan, A. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123822 · Cited by 60

Binding Site of the Bridged Macrolides in the Escherichia coli Ribosome

Xiong, L., Korkhin, Y., & Mankin, A. S. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.1.281-288.2005 · Cited by 60

Short peptides conferring resistance to macrolide antibiotics

Tenson, T., & Mankin, A. S. (2001) · Peptides · doi:10.1016/s0196-9781(01)00501-0 · Cited by 55

Bacterial Ribosomal Subunit Assembly is an Antibiotic Target

Champney, W. S. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033452186 · Cited by 54

Structural studies of the translational apparatus

Agrawal, R. K., & Frank, J. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80031-1 · Cited by 53

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Brandi, L., Marzi, S., Fabbretti, A., Fleischer, C., Hill, W. E., Gualerzi, C. O., & Lodmell, J. S. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.067 · Cited by 48

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Davydova, N., Streltsov, V. A., Wilce, M. C. J., Liljas, A., & Garber, M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00772-6 · Cited by 48

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Treede, I., Jakobsen, L. A., Kirpekar, F., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03558.x · Cited by 47

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Sutcliffe, J. A., & Leclercq, R. (2002) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8105-0_17 · Cited by 46

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Bowen, W. S., Dyke, N. V., Murgola, E. J., Lodmell, J. S., & Hill, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407008200 · Cited by 43

Properties of ribosomes from erythromycin resistant mutants of Escherichia coli

Pardo, D., & Rosset, R. (1977) · Molecular and General Genetics MGG · doi:10.1007/bf00267181 · Cited by 43

Interaction of Avilamycin with Ribosomes and Resistance Caused by Mutations in 23S rRNA

Kofoed, C. B., & Vester, B. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.11.3339-3342.2002 · Cited by 42

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Novotny, G. W., Jakobsen, L. A., Andersen, N. M., Poehlsgaard, J., & Douthwaite, S. R. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.10.3677-3683.2004 · Cited by 32

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Awan, A., Brennan, R., Regan, A. C., & Barber, J. (2000) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/b003000g · Cited by 31

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Yusupov, M., Garber, M. B., Vasiliev, V. D., & Spirin, A. S. (1991) · Biochimie · doi:10.1016/0300-9084(91)90130-s · Cited by 23

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