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Chapter 17 : Inhibitors of the 30S Ribosomal Subunit

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Inhibitors of the 30S Ribosomal Subunit, Page 1 of 2

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Abstract:

The aminoglycoside group of antibiotics are multifunctional hydrophilic carbohydrates that possess two or more amino monosaccharides connected by glycosidic bonds to an aminocyclitol nucleus. Most aminoglycosides contain a 2-deoxystreptamine cyclitol. The aminoglycoside antibiotics have several features justifying their continued clinical use, including their rapid and potent bactericidal activity, long-lasting postantibiotic effect, and synergy with other antibiotics. The emerging structural data now have the potential to be exploited in the design of specific inhibitors of enzyme activity. The challenge is to use this information to synthesize effective and potent inhibitors that will overcome antibiotic resistance produced by the aminoglycoside-modifying enzymes. The tetracyclines are a group of antibiotics with an identical basic skeleton of four linearly fused six-membered rings, named 1,4,4a,5,5a,6,11,12-octahydronaphthacene and differing from each other chemically only by substituent variation at positions 5, 6, and 7. It has been found that there are two binding sites for tetracycline within the small ribosomal subunit. Bacterial resistance results from the selective pressure exerted on bacteria during the administration of tetracyclines for chemotherapy. Resistance to tetracycline may be mediated by one of three different mechanisms: (i) an energy-dependent efflux of tetracyclines carried out by transmembrane spanning proteins, which results in reduction of the concentration of tetracycline in the cytosol; (ii) ribosomal protection, whereby the tetracyclines no longer bind productively to the bacterial ribosome; or (iii) chemical modification, requiring oxygen and NADPH and catalysis by enzymes. Since the chemical alteration mechanism occurs rarely, this discussion focuses on the major mechanisms of tetracycline resistance.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Figures

Image of Figure 17.1
Figure 17.1

Classification of aminoglycoside antibiotics based on the chemical structure of the aminocyclitol: streptidine, streptamine, or 2-deoxystreptamine, including those in which the amino sugars are linked at the 4- and 5-hydroxyl groups and those substituted at the 4- and 6-hydroxyl positions.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.2
Figure 17.2

Chemical structures of streptomycin and dihydrostreptomycin.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.3
Figure 17.3

Chemical structure of spectinomycin chlorhydrate drawn conformationally and planar. At the right is the 3-keto form, which is hydrated in aqueous medium, forming a diol group as shown.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.4
Figure 17.4

Chemical structures of neomycin B, paromomycin, and ribostamycin, with the atomic and ring-numbering systems denoted in arabic and roman numerals, respectively.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.5
Figure 17.5

Chemical structures of kanamycins A, B, and C, amikacin, dibekacin, and tobramycin.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.6
Figure 17.6

Chemical structures of gentamicins C1, C2, and C1a.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.7
Figure 17.7

Chemical structures of sisomicin and netilmicin.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.8
Figure 17.8

Secondary structure of E. coli 16S rRNA . This four-domain structure is 46% base paired, highlighting the decoding region A site. Nucleotides conserved in more than 95% of ribosomal sequences are shown in outline. Adapted from M. O'Connor, M. Bayfield, S. T. Gregory, W.-C. M. Lee, J. S. Lodmell, A. Mankad, J. R. Thompson, A. Vila-Sanjurjo, C. L. Squires, and A. E. Dahlberg, p. 217–227, in R. A. Garrett, S. R. Douthwaite, A. Liljas, A. T. Matheson, P. B. Moore, and H. F. Noller (ed.), The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions (ASM Press, Washington, D.C., 2000), with permission from the publisher.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.9
Figure 17.9

Secondary structure of the 27-mer A-site RNA oligonucleotide, as derived by NMR. Watson-Crick base pairs are denoted by solid lines, while mismatched base pairs are denoted by dashed lines. Bases present in E. coli 16S rRNA are depicted in bold type and are numbered as in 16S rRNA. The aminoglycoside-binding site, as revealed by NMR and footprinting studies, is as indicated. Reprinted from M. Kaul and D. S. Pilch, Biochemistry 41:7695–7706, 2002, with permission from the publisher.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.10
Figure 17.10

The streptomycin-binding site. For details, see the text. Adapted from A. P. Carter, W. M. Clemons, D. E. Brodersen, R. J. Morgan-Warren, B. T. Wimberly, and V. Ramakrishnan, Nature 407:340–348, 2000, with permission from the publisher.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.11
Figure 17.11

Enzymatic inactivation of kanamycin B. Not all resistant bacteria exhibit every reaction shown.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.12
Figure 17.12

Chemical structure of isepamicin compared to that of amikacin.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.13
Figure 17.13

Chemical structure of arbekacin.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.14
Figure 17.14

Chemical structures of seven clinically important tetracyclines (for an explanation, see the text).

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.15
Figure 17.15

Chemical structure of tetracycline hydrochloride.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.16
Figure 17.16

Chemical instability of tetracycline under acidic and basic conditions. Note that the 6β-hydroxy group participates in these degradation reactions.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.17
Figure 17.17

Epimerization of the tetracycline subsituents at C-4 in acidic medium (pH 2 to 6).

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.18
Figure 17.18

Diagrammatic representation of tetracycline accumulation in sensitive (top) and resistant (bottom) bacterial cells. Sensitive cells show a net active uptake, while resistant cells show a net active efflux. T, tetracycline. Reprinted from L. E. Bryan (ed.), Antimicrobial Drug Resistance (Academic Press, Inc., New York, N.Y., 1984), with permission from the publisher.

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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Image of Figure 17.19
Figure 17.19

Chemical structure of N,N-dimethylglycylamido derivatives of 9- aminominocycline (DMG-MINO) and 9-amino-6-demethyl-6-deoxytetracycline (DMGDMDOT).

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
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References

/content/book/10.1128/9781555817794.chap17
1. Wright, G. D.,, A. M. Berghuis,, and S. Mobashery,. 1998. Aminoglycoside antibiotics, p. 2769. In B. P. Rosen, and S. Mobashery (ed.), Resolving the Antibiotic Paradox. Kluwer Academic/Plenum Publishers, New York, N.Y.
2. Carter, A. P.,, W. M. Clemons,, D. E. Brodersen,, R. J. Morgan-Warren,, B. T. Wimberly,, and V. Ramakrishnan. 2000. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407:340348.
3. Fourmy, D.,, M. I. Recht,, S. C. Blanchard,, and J. D. Puglisi. 1996. Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic. Science 274:13671372.
4. Fourmy, D.,, M. I. Recht,, and J. D. Puglisi. 1998. Binding of neomycin-class aminoglycoside antibiotics to the A-site of 16S rRNA. J. Mol. Biol. 277:347362.
5. Fourmy, D.,, S. Yoshizawa,, and J. D. Puglisi. 1998. Paromomycin binding induces a local conformational change in the A-site of 16S rRNA. J. Mol. Biol. 277:333345.
6. Kaul, M.,, and D. S. Pilch. 2002. Thermodynamics of aminoglycosides- rRNA recognition: the binding of neomycin-class aminoglycosides to the A site of 16S rRNA. Biochemistry 41:76957706.
7. Kotra, L. P.,, J. Haddad,, and S. Mobashery. 2000. Aminoglycosides: perspectives on mechanisms of action and resistance and strategies to counter resistance. Antimicrob. Agents Chemother. 44:32493256.
8. Mehta, R.,, and W. S. Champney. 2002. 30S ribosomal subunit assembly is a target for inhibition by aminoglycosides in Escherichia coli. Antimicrob. Agents Chemother. 46:15461549.
9. Moazed, D.,, and H. F. Noller. 1987. Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327:389394.
10. Ryu, D. H.,, A. Litovchick,, and R. R. Rando. 2002. Stereospecificity of aminoglycoside-ribosomal interactions. Biochemistry 41:1049910509.
11. Wang, H.,, and Y. Tor. 1998. RNA-aminoglycoside interactions: design, synthesis, and binding of “amino-aminoglycosides” to RNA. Angew. Chem. Int. Ed. 37:109111.
12. Wong, C. H.,, M. Hendrix,, E. S. Priestley,, and W. A. Greenberg. 1998. Specificity of aminoglycoside antibiotics for the A-site of the decoding region of ribosomal RNA. Chem. Biol. 5:397406.
13. Yoshizawa, S.,, D. Fourmy,, and J. D. Puglisi. 1998. Structural origins of gentamicin antibiotic action. EMBO J. 17:64376448.
14. Davies, J.,, and G. D. Wright. 1997. Bacterial resistance to aminoglycoside antibiotics. Trends Microbiol. 5:234240.
15. Mingeot-Leclercq, M. P.,, Y. Glupczynski,, and P. M. Tulkens. 1999. Aminoglycosides: activity and resistance. Antimicrob. Agents Chemother. 43:727737.
16. Shaw, K. J.,, P. N. Rather,, R. S. Hare,, and G. M. Miller. 1993. Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57:138163.
17. Azucena, E.,, and S. Mobashery. 2001. Aminoglycosidemodifying enzymes: mechanism of catalytic processes and inhibition. Drug Resist. Updates 4:106117.
18. Wright, G. D. 1999. Aminoglycoside-modifing enzymes. Curr. Opin. Microbiol. 2:499503.
19. Chung, L.,, G. Kaloyanides,, R. McDaniel,, A. McLaughlin,, and S. McLaughlin. 1985. Interaction of gentamicin and spermine with bilayer membranes containing negatively-charged phospholipids. Biochemistry 24:442452.
20. Taber, H. W.,, J. P. Mueller,, P. F. Miller,, and A. S. Arrow. 1987. Bacterial uptake of aminoglycoside antibiotics. Microbiol. Rev. 51:439457.
21. Hon, W. C.,, G. A. McKay,, P. R. Thompson,, R. M. Sweet,, D. S. C. Yang,, G. D. Wright,, and A. M. Berghuis. 1997. Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89:887895.
22. Pedersen, L. C.,, M. M. Benning,, and H. M. Holden. 1995. Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34:1330513311.
23. Sakon, J.,, H. H. Liao,, A. M. Kanikula,, M. M. Benning,, I. Rayment,, and H. M. Holden. 1993. Molecular structure of kanamycin nucleotidyl transferase determined to 3 Å resolution. Biochemistry 32:1197711984.
24. Vetting, M. W.,, S. S. Hegde,, F. Javid-Majd,, J. S. Blanchard,, and S. L. Roderick. 2002. Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycosides substrates. Nat. Struct. Biol. 9:653658.
25. Wolf, E.,, A. Vassilev,, Y. Makino,, A. Sali,, Y. Nakatani,, and S. K. Burley. 1998. Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase Cell 94:439449.
26. Wybenga-Groot, L. E.,, K. Draker,, G. D. Wright,, and A. M. Berghuis. 1999. Crystal structure of an aminoglycoside 6'-Nacetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7:497507.
27. Mingeot-Leclercq, M. P.,, and P. M. Tulkens. 1999. Aminoglycosides: nephrotoxicity. Antimicrob. Agents Chemother. 43:10031012.
28. American Medical Association. 1996. Drug Evaluations Annual 1995 , p. 15371558. American Medical Association, Chicago, Ill.
29. Dworkin, R. J. 1999. Aminoglycosides for the treatment of gram-negative infections: therapeutic use, resistance and future outlook. Drug Resist. Updates 2:173179.
30. Kucers, A.,, S. M. Crowe,, M. L. Grayson,, and J. F. Hoy. 1997. The Use of Antibiotics , 5th ed., p. 428541. Butterworth- Heinemann, Oxford, United Kingdom.
31. Maurin, M.,, and D. Raoult. 2001. Use of aminoglycosides in treatment of infection due to intracellular bacteria. Antimicrob. Agents Chemother. 45:29772986.
32. Reese, R. E.,, R. F. Betts,, and B. Gumustop. 2000. Handbook of Antibiotics , 3rd ed., p. 415434. Lippincott Williams & Wilkins, Philadelphia, Pa.
33. Jones, R. N. 1995. Isepamicin (SCH 21420, 1-N-HAPA gentamicin B): microbiological characteristics including antimicrobial potency and spectrum of activity. J. Chemother. 7(Suppl. 2):716.
34. Miller, G. H.,, F. J. Sabatelli,, L. Naples,, R. S. Hare,, and K. J. Shaw. 1995. The changing nature of aminoglycoside resistance mechanisms and the role of isepamicin. A new broad spectrum aminoglycoside. J. Chemother. 7(Suppl. 2):3144.
35. Hotta, K.,, C. B. Zhu,, and T. Ogata. 1996. Enzymatic 2'-Nacetylation of arbekacin and antibiotic activity of its product. J. Antibiot. 49:458464.
36. Lambert, T.,, G. Gerbaud,, M. Galimand,, and P. Courvalin. 1993. Characterization of Acinetobacter haemolyticus aac(6')-Ig gene encoding an aminoglycoside 6'-N-acetyltransferase which modifies amikacin. Antimicrob. Agents Chemother.37:20932100.
37. Chopra, I.,, P. M. Hawkey,, and M. Hinton. 1992. Tetracyclines, molecular and clinical aspects. J. Antimicrob. Chemother. 29:245277.
38. Chopra, I.,, and M. Roberts. 2001. Tetracycline antibiotics: mode of action, applications, molecular biology, and epidemiology of bacterial resistance. Microbiol. Mol. Biol. Rev. 65:232260.
39. Hlavka, J. J.,, G. A. Ellestad,, and I. Chopra,. 1993. Tetracyclines, p. 562577. In M. Howe-Grant (ed.), Chemotherapeutics and Disease Control. John Wiley & Sons, Inc., New York, N.Y.
40. Brodersen, D. E.,, W. M. Clemons,, A. P. Carter,, R. J. Morgan-Warren,, B. T. Wimberly,, and V. Ramakrishnan. 2000. The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell 103:11431154.
41. Pioletti, M.,, F. Schlünzen,, J. Harms,, R. Zarivach,, M. Glühmann,, H. Avila,, A. Bashan,, H. Bartels,, T. Auerbach,, C. Jacobi,, T. Hartsch,, A. Yonat,, and F. Franceschi. 2001. Crystal structures of complexes of the small ribosomal unit with tetracycline, edeine and IF3. EMBO J. 20:18291839.
42. Levy, S. B.,, L. M. McMurry,, T. M. Barbosa,, V. Burdett,, P. Courvalin,, W. Hillen,, M. C. Roberts,, J. I. Rood,, and D. E. Taylor. 1999. Nomenclature for new tetracycline resistance determinants. Antimicrob. Agents Chemother. 40:15.
43. Levy, S. B.,, L. M. McMurry,, V. Burdett,, P. Courvalin,, W. Hillen,, M. C. Roberts,, and D. E. Taylor. 1989. Nomenclature for tetracycline resistance determinants. Antimicrob. Agents Chemother. 33:13731374.
44. Roberts, M. C. 1994. Epidemiology of tetracycline-resistance determinants. Trends Microbiol. 2:353357.
45. Speer, B. S.,, N. B. Shoemaker,, and A. A. Salyers. 1992. Bacterial resistance to tetracycline: mechanisms, transfer, and clinical significance. Clin. Microbiol. Rev. 5:387399.
46. Taylor, D. E.,, and A. Chau. 1996. Tetracycline resistance mediated by ribosomal protection. Antimicrob. Agents Chemother. 33:13731374.
47. Borges-Walmsley, M. I.,, and A. R. Walmsley. 2001. The structure and function of drug pumps. Trends Microbiol. 9:7179.
48. Koronakis, V.,, A. Sharff,, E. Koronakis,, B. Luisi,, and C. Hughes. 2000. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914919.
49. Levy, S. B. 1992. Active efflux mechanisms for antimicrobial resistance. Antimicrob. Agents Chemother. 36:695703.
50. American Medical Association. 1996. Drug Evaluations Annual, 1995 , p. 15191528. American Medical Association, Chicago, Ill.
51. Kucers, A.,, S. M. Grove,, M. L. Grayson,, and J. F. Hoy. 1997. The Use of Antibiotics , 5th ed., p. 719762. Butterworth-Heinemann, Oxford, United Kingdom.
52. Scholar, E. M.,, and W. B. Pratt. 2000. The Antimicrobial Drugs , p. 184197. Oxford University Press, Oxford, United Kingdom.
53. Bergeron, J.,, M. Ammirati,, D. Danley,, L. James,, M. Norcia,, J. Retsema,, C. A. Strick,, W. G. Su,, J. Sutcliffe,, and L. Wondrack. 1996. Glycylcyclines bind to the high-affinity tetracycline ribosomal binding site and evade Tet(M)- and Tet(O)-mediated ribosomal protection. Antimicrob. Agents Chemother. 40:22262228.
54. Sum, P. E.,, V. J. Lee,, R. T. Testa,, J. J. Hlavka,, G. A. Ellestad,, J. D. Bloom,, Y. Gluzman,, and F. P. Tally. 1994. Glycylcyclines. 1. A new generation of potent antibacterial agents through modifications of 9-aminotetracyclines. J. Med. Chem. 37:184188.
55. Tally, F. P.,, G. A. Ellestad,, and R. T. Testa. 1995. Glycylcyclines: a new generation of tetracyclines. J. Antimicrob. Chemother. 35:449452.

Tables

Generic image for table
Table 17.1

Typical enzymes modifying clinically used aminoglycosides

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
Generic image for table
Table 17.2

Generic and common trade names of aminoglycosides, the preparations available, and manufacturers in the United States

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
Generic image for table
Table 17.3

Classification of tetracycline resistance determinants according to their mechanism of resistance a

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17
Generic image for table
Table 17.4

List of generic and common trade names of tetracyclines, the preparations available, and manufacturers in the United States

Citation: Mascaretti O. 2003. Inhibitors of the 30S Ribosomal Subunit, p 229-246. In Bacteria versus Antibacterial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555817794.ch17

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