RNA as a target for small-molecule therapeutics

Bibliography

• HERMANN T, WESTHOF E: RNA as a drug target: chemical, modelling and evolutionary tools. Curr. Opin. BiotechnoL (1998) 9:66–73.
   PubMed Web of Science ®Google Scholar
• HERMANN T: Strategies for the design of drugs targeting RNA and RNA—protein complexes. Angelo. Chem. Int. Ed. (2000) 39:1890–1904.
   PubMed Web of Science ®Google Scholar
• TORY: Targeting RNA with small molecules. Chembiochem (2003) 4:998–1007.
   PubMed Web of Science ®Google Scholar
• MANUAL M, BREAKER RR: Gene regulation by riboswitches. Nat. Rev. Mol. Cell Biol. (2004) 5:451–463.
   PubMed Web of Science ®Google Scholar
• NUDLER E, MIRONOV AS: The riboswitch control of bacterial metabolism. Trends Biochem. Sci. (2004) 29:11–17.
   PubMed Web of Science ®Google Scholar
• AUERBACH T, BASHAN A, SCHLUENZEN J et al.: Antibiotics targeting ribosomes: crystallographic studies. Curr. Drug Targets Infect. Disord. (2002) 2:169–186.
   PubMedGoogle Scholar
• HERMANN T: Chemical and functional diversity of small molecule ligands for RNA. Biopolymers (2003) 70:4–18.
   PubMed Web of Science ®Google Scholar
• •Up-to-date overview on the chemical diversity of natural small-molecule ligands for RNA, focusing on bacterial ribosomal RNA targets and related 3D structural data.
   Google Scholar
• GRIFFEY RH, SWAYZE EE: RNA -targeted therapeutics: prospects and promise. Expert Opin. Ther. Patents (2002) 12:1367–1374.
   Web of Science ®Google Scholar
• VICENS Q, WESTHOF E: RNA as a drugtarget: the case of aminoglycosides. Chembiochem (2003) 4:1018–1023.
   PubMed Web of Science ®Google Scholar
• POEHLSGAARD J, DOUTHWAITE S: Macrolide antibiotic interaction and resistance on the bacterial ribosome. Curr. Opin. Investig Drugs (2003) 4:140–148.
   PubMedGoogle Scholar
• DRYSDALE MJ, LENTZEN G, MATASSOVA N, MURCHIE Al, ABOUL-ELA F, AFSHAR M: RNA as a drug target. Prog. Med. Chem. (2002) 39:73–119.
   PubMedGoogle Scholar
• HADDAD J, KOTRA LP, LLANO -SOLETO B et al.: Design of novel antibiotics that bind to the ribosomal acyltransferase site. J. Am. Chem. Soc. (2002) 124:3229–3237.
   Google Scholar
• RUSSELL RJ, MURRAY JB, LENTZEN G, HADDAD J, MOBASHERY S: The complex of a designer antibiotic with a model aminoacyl site of the 30S ribosomal subunit revealed by X-ray crystallography. J. Am. Chem. Soc. (2003) 125:3410–3411.
   PubMed Web of Science ®Google Scholar
• •First published crystal structure of a designed aminoglycoside derivative in complex with its RNA target. The conception, synthesis and identification of the compound is outlined in [12].
   Google Scholar
• FRIDMAN M, BELAKHOV V, YARON S, BAASOV T: A new class of branched aminoglycosides: pseudo-pentasaccharide dervatives of beomycin B. Org. Lett. (2003) 5:3575–3578.
   PubMed Web of Science ®Google Scholar
• DINGY, HOFSTADLER SA, SWAYZE EE, GRIFFEY RH: An efficient synthesis of mimetics of neamine for RNA recognition. Org. Lett. (2001) 3:1621–1623.
   PubMed Web of Science ®Google Scholar
• DINGY, HOFSTADLER SA, SWAYZE EE, RISEN L, GRIFFEY RH: Design and synthesis of paromomycin-related heterocycle-substituted aminoglycoside mimetics based on a mass spectrometry RNA-binding assay. Angew. Chem. Int. Ed. (2003) 42:3409–3412.
   PubMed Web of Science ®Google Scholar
• YAO S, SGARBI PW, MARBY KA et al.:Glyco-optimization of aminoglycosides: new aminoglycosides as novel anti-infective agents. Bioorg. Med. Chem. Lett. (2004) 14:3733–3738.
   PubMed Web of Science ®Google Scholar
• VOURLOUMIS D, TAKAHASHI M, WINTERS GC et al.: Novel 2,5-dideoxystreptamine derivatives taregting the ribosomal decoding site RNA. Bioorg. Med. Chem. Lett. (2002) 12:3367–3372.
   PubMed Web of Science ®Google Scholar
• SIMONSEN KB, AYIDA BK, VOURLOUMIS D et al.: Novel paromamine derivatives exploring shallow-groove recognition of ribosomal-decoding-site RNA. Chembiochem (2002) 3:1223–1228.
   PubMed Web of Science ®Google Scholar
• VOURLOUMIS D, WINTERS GC, TAKAHASHI M et al.: Novel acyclic deoxystreptamine mimetics targeting the ribosomal decoding site. Chembiochem (2003) 4:879–885.
   PubMed Web of Science ®Google Scholar
• SIMONSEN KB, AYIDA BK, VOURLOUMIS D et al.: Piperidine glycosides targeting the ribosomal decoding site. Chembiochem (2003) 4:886–890.
   PubMed Web of Science ®Google Scholar
• BARLUENGA S, SIMONSEN KB, LITTLEFIELD ES et al.: Rational design of azepane-glycoside antibiotics targteing the bacterial ribosome. Bioorg. Med. Chem. Lett. (2004) 14:713–718.
   PubMed Web of Science ®Google Scholar
• •Use of crystal structure data for the design of an aminoglycoside mimetic in which the key 2-deoxystreptamine scaffold of the natural antibiotics was replaced by a heterocyclic system aimed at utilising a target-bound water molecule.
   Google Scholar
• VICENS Q, WESTHOF E: Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of X-ray crystal structures. Chembiochem (2003) 4:1018–1023.
   PubMed Web of Science ®Google Scholar
• WU B, YANG J, ROBINSON D et aL: Synthesis of linked carbohydrates and evaluation of their binding for 16S RNA by mass spectrometry. Bioorg. Med. Chem. Lett. (2003) 13:3915–3918.
   PubMed Web of Science ®Google Scholar
• AGNELLI F, SUCHECK SJ, MARBY KA et al.: Dimeric aminoglycosides as antibiotics. Angelo Chem. Int. Ed. (2004) 43:1562–1566.
   PubMed Web of Science ®Google Scholar
• CHOU CH, WU CS, CHEN CH et al.:Regioselective glycosylation of neamine core: a facile entry to kanamycin B related analogues. Org. Lett. (2004) 6:585–588.
   PubMed Web of Science ®Google Scholar
• HEY, YANG J, WU B et al.: Synthesis andevaluation of novel bacterial rRNA-binding benzimidazoles by mass spectrometry. Bioorg. Med. Chem. Lett. (2004) 14:695–699.
   PubMed Web of Science ®Google Scholar
• SWAYZE EE, JEFFERSON EA, SANNES-LOWERY KA et al.: SAR by MS: A ligand based technique for drug lead discovery against structured RNA targets. J. Med. Chem. (2002) 45:3816–3819.
   PubMed Web of Science ®Google Scholar
• •Extension of a mass spectrometry-based affinity assay for RNA targets to establish SAR and to guide lead improvement (SAR by MS).
   Google Scholar
• YU L, OOST TK, SCHKERYANTZ JM, YANG J, JANOWICK D, FESIK SW: Discovery of aminoglycoside mimetics by NMR-based screening of Escherichia coli A-site RNA. J. Am. Chem. Soc. (2003) 125:4444–4450.
   Google Scholar
• ••First publication of an NMR-basedscreening approach for an RNA target, yielding a series of novel scaffolds for molecular recognition of the bacterial decoding site.
   Google Scholar
• JOHNSON EC, FEHER VA, PENG JW, MOORE JM, WILLIAMSON JR: Application of NMR SHAPES screening to an RNA target. J. Am. Chem. Soc. (2003) 125:15724–15725.
   PubMed Web of Science ®Google Scholar
• FOLOPPE N, CHEN I-J, DAVIS B, HOLD A, MORLEY D, HOWES R: A structure-based strategy to identify new molecular scaffolds targeting the bacterial ribosomal A-site. Bioorg. Med. Chem. (2004) 12:935–947.
   PubMed Web of Science ®Google Scholar
• ••Comprehensive description of a leaddiscovery campaign for the bacterial decoding site, including computational screening, biochemical assaying and NMR-based characterisation of compounds. Data are provided for 30 hits out of the discovery effort.
   Google Scholar
• DISNEY MD, SEEBERGER PH: Aminoglycoside microarrays to explore interactions of antibiotics with RNAs and proteins. Chemistry (2004) 10:3308–3314.
   PubMed Web of Science ®Google Scholar
• KAUL M, BARBIERI CM, PILCH DS: Fluorescence-based approach for detecting and characterizing antibiotic-induced conformational changes in ribosomal RNA: comparing aminoglycoside binding to prokaryotic and eukaryotic ribosomal RNA sequences. J. Am. Chem. Soc. (2004) 126:3447–3453.
   PubMed Web of Science ®Google Scholar
• SHANDRICK S, ZHAO Q, HAN Q et aL: Monitoring molecular recognition of the ribosomal decoding site. Angelo. Chem. Int. Ed. (2004) 43:3177–3182.
   PubMed Web of Science ®Google Scholar
• MATASSOVA NB, RODNINA MV, ENDERMANN R et al: Ribosomal RNA is the target for oxazolidinones, a novel class of translation inhibitors. RNA (1999) 5:939–946.
   PubMed Web of Science ®Google Scholar
• ZHOU CC, SWANEY SM, SHINABARGER DL, STOCKMAN BJ: 1H Nuclear magnetic resonance study of oxazolidinone binding to bacterial ribosomes. Antimicrob. Agents Chemother. (2002) 46:625–629.
   PubMed Web of Science ®Google Scholar
• AOKI H, KE L, POPPE SM et al.: Oxazolidinone antibiotics target the P site on Escherichia coli ribosomes. Antimicrob. Agents Chemother. (2002) 46:1080–1085.
   PubMed Web of Science ®Google Scholar
• HANSEN JL, IPPOLITO JA, BAN N, NISSEN P, MOORE PB, STEITZ TA: The structures of four macrolide antibiotics bound to the large ribosomal subunit. Molecular Cell (2002) 10:117–128.
   PubMed Web of Science ®Google Scholar
• LENTZEN G, KLINCK R, MATASSOVA N, ABOUL-ELA F: Structural basis for contrasting activities of ribosome binding thiazole antibiotics. Chem. Biol (2003) 10:769–778.
   PubMed Web of Science ®Google Scholar
• BOWER J, DRYSDALE M, HEBDON R et al.: Structure-based design of agents targeting the bacterial ribosome. Bioorg. Med. Chem. Lett. (2003) 13:2455–2458.
   PubMed Web of Science ®Google Scholar
• LEE J, KWON M, LEE KH et al.: An approach to enhance specificity against RNA targets using heteroconjugates of aminoglycosides and chloramphenicol (or linezolid). J. Am. Chem. Soc. (2004) 126:1956–1957.
   PubMed Web of Science ®Google Scholar
• CARRIERE M, VIJAYABASKAR APPLEFIELD D et al.: Inhibition of protein synthesis by aminoglycoside-arginine conjugates. RNA (2002) 8:1267–1279.
   Google Scholar
• DANDLIKER PJ, PRATT SD, NILIUS AMet al: Novel antibacterial class. Antimicrob. Agents Chemother (2003) 47:3831–3839.
   PubMed Web of Science ®Google Scholar
• JEFFERSON EA, ARAKAWA S, BLYN LB et al.: New inhibitors of bacterial protein synthesis from a combinatorial library of macrocycles. J. Med. Chem. (2002) 45:3430–3439.
   PubMed Web of Science ®Google Scholar
• PRATT SD, DAVID CA, BLACK -SCIAEFER C et al.: A strategy for discovery of novel broad-spectrum antibacterials using a high-throughput Streptococcus pneumoniae transcription/ translation screen. J. Biomol. Screen. (2004) 9:3–11.
   Google Scholar
• CLARK RF, WANG S, MA, Z et al.: Novel inhibitors of bacterial protein synthesis: structure-activity relationships for 1,8-naphtyridine derivatives incorporating position 3 and 4 variants. Bioorg Med. Chem. Lett. (2004) 14:3299–3302.
   PubMed Web of Science ®Google Scholar
• JEFFERSON EA, ARAKAWA S, BLYN LB et al.: New inhibitors of bacterial protein synthesis from a combinatorial library of macrocycles. J. Med. Chem. (2002) 45:3430–3439.
   PubMed Web of Science ®Google Scholar
• VIOQUE A, DE LA CRUZ J: Trans-translation and protein synthesis inhibitors. FEMS Microbiol Lett. (2003) 218:9–14.
   PubMed Web of Science ®Google Scholar
• CORVAISIER S, BORDEAU V, FELDEN B: Inhibition of transfer messenger RNA aminoacylation and trans-translation by aminoglycoside antibiotics. J. Biol. Chem. (2003) 278:14788–14797.
   PubMed Web of Science ®Google Scholar
• TAKAHASHI T, KONNO T, MUTO A, HIMENO H: Various effects of paromomycin on tmRNA-directed trans-translation. J. Biol. Chem. (2003) 278:27672–27680.
   PubMed Web of Science ®Google Scholar
• KONNO T, TAKAHASHI T, KURITA D, MUTO A, HIMENO H: A minimum structure of aminoglycosides that causes an initiation shift trans-translation. Nucleic Acids Res. (2004) 32:4119–4126.
   PubMed Web of Science ®Google Scholar
• MIKKELSEN NE, BRANNVALL M, VIRTANEN A, KIRSEBOM LA: Inhibition of RNAse P RNA cleavage by aminoglycosides. Proc. Natl. Acad. Sci. USA (1999) 96:6155–6160.
   PubMed Web of Science ®Google Scholar
• EDER PS, HATFIELD C, VIOQUE A. GOPALAN V: Bacterial RNase P as a potential target for novel anti-infectives. Curr. Opin. Investig. Drugs (2003) 4:937–943.
   Google Scholar
• EUBANK TD, BISWAS R, JOVANOVIC M, LITOVCHICK A, LAPIDOT A. GOPALAN V: Inhibition of bacterial RNase P by aminoglycoside-arginine conjugates. FEBS Lett. (2002) 511:107–112.
   Google Scholar
• ZAPP ML, STERN S, GREEN MR: Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production. Cell (1993) 74:969–978.
   PubMed Web of Science ®Google Scholar
• WERSTUCK G, ZAPP ML, GREEN MR: A non-canonical base pair within the human immunodeficiency virus rev-responsive element is involved in both rev and small molecule recognition. Chem. Biol. (1996) 3:129–137.
   PubMedGoogle Scholar
• MET HY MACK DP, GALAN AA et aL: Discovery of selective, small-molecule inhibitors of RNA complexes I. The Tat protein/TAR RNA complexes required for HIV-1 transcription. Bioorg Med. Chem. (1997) 5:1173–1184.
   Google Scholar
• MCKNIGHT KL, HEINZ BA: RNA as a target for developing antivirals. Anti vir. Chem. Chemother. (2003) 14:61–73.
   PubMedGoogle Scholar
• FROEYEN M, HERDEWIJN P: RNA as a target for drug design, the example of Tat-TAR interaction. Curr. Top. Med. Chem. (2002) 2:1123–1145.
   PubMedGoogle Scholar
• BABA M: Inhibitors of HIV-1 gene expression and transcription. Curr. Top. Med. Chem. (2004) 4:871–882.
   PubMed Web of Science ®Google Scholar
• LUEDTKE NW, TORY: Fluorescence-based methods for evaluating the RNA affinity and specificity of HIV-1 Rev-RRE inhibitors. Biopo/ymers (2003) 70:103–119.
   PubMed Web of Science ®Google Scholar
• •Comprehensive outline of fluorescence-based techniques for the discovery and systematic evaluation of several Rev-RRE inhibitor classes. Emphasis is given to assess both the affinity and specificity of the RNA ligands.
   Google Scholar
• LUEDTKE NW, LIU Q, TORY: RNA-ligand interactions: affinity and specificity of aminoglycoside dimers and acridine conjugates to the HIV-1 Rev response element. Biochemistry (2003) 42:11391–11403.
   PubMed Web of Science ®Google Scholar
• ••Systematic study of the relationshipbetween target binding affinity and specificity of RNA-directed ligands, using the HIV Rev-RRE complex as a model system.
   Google Scholar
• LUEDTKE NW, LIU Q, TORY: Synthesis, photophysical properties, and nucleic acid binding of phenanthridinium derivatives based on ethidium. Chembiochem (2003) 11:5235–5247.
   Google Scholar
• LUEDTKE NW, BAKER TJ, GOODMAN M, TORY: Guanidinoglycosides: a novel family of RNA ligands. J. Am. Chem. Soc. (2000) 122:12035–12036.
   Web of Science ®Google Scholar
• LUEDTKE NW, CARMICHAEL P, TORY: Cellular uptake of aminoglycosides, guanidinoglycosides, and poly-arginine. J. Am. Chem. Soc. (2003) 125:12374–12375.
   PubMed Web of Science ®Google Scholar
• BAKER TJ, LUEDTKE NW, TORY, GOODMAN M: Synthesis and anti-HIV activity of guanidinoglycosides. J. Org. Chem. (2000) 65:9054–9058.
   PubMed Web of Science ®Google Scholar
• LACOURCIERE KA, STIVERS JT, MARINO JP: Mechanism of neomycin and Rev peptide binding to the Rev responsive element of HIV-1 as determined by fluorescence and NMR spectroscopy. Biochemistry (2000) 39:5630–5641.
   PubMed Web of Science ®Google Scholar
• DEJONG ES, CHANG C, GILSON MK, MARINO JP: Proflavine as a Rev inhibitor by targeting the high-affinity Reb binding site of the Rev responsive element of HIV-1. Biochemistry (2003) 42:8035–8046.
   PubMed Web of Science ®Google Scholar
• CHAPMAN RL, STANLEY TB, HAZEN R, GARVEY EP: Small molecule modulators of HIV Rev/Rev response element interaction identified by random screening Antiviral Res. (2002) 54:149–162.
   Google Scholar
• TAO J, FRANKEL AD: Specific binding of arginine to TAR RNA. Proc. Natl Acad. Sci. USA (1992) 89:2723–2726.
   PubMed Web of Science ®Google Scholar
• BLOUNT KF, TORY: Using pyrene-labeled HIV-1 TAR to measure RNA-small molecule binding. Nucleic Acids Res. (2003) 31:5490–5500.
   PubMed Web of Science ®Google Scholar
• BRADICK TD, MARINO JP: Ligand-induced changes in 2-aminopurine fluorescence as a probe for small molecule binding to HIV-1 TAR RNA. RNA (2004) 10:1459–1468.
   PubMed Web of Science ®Google Scholar
• HAMY F, FELDER E, LIPSON K, KLIMKAIT T: Merged screening for human immunodeficiency virus Tat and Rev inhibitors. J. Biomol Screen. (2001) 6:179–187.
   PubMedGoogle Scholar
• WANG M, XU Z, TU P, YU X, XIA S, YANG M: a,a-Trehalose derivatives bearing guanidino groups as inhibitors to HIV-1 Tat-TAR RNA interaction in human cells. Bioorg Med. Chem. Lett. (2004) 14:2585–2588.
   PubMed Web of Science ®Google Scholar
• YU X, LIN W, LI J, YANG M: Synthesisand biological evaluation of novel a-carboline derivatives as Tat-TAR interaction inhibitors. Bioorg. Med. Chem. Lett. (2004) 14:3127–3130.
   PubMed Web of Science ®Google Scholar
• HERMANN T, WESTHOF E: Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations. Structure (1998) 6:1303–1314.
   PubMed Web of Science ®Google Scholar
• HERMANN T, WESTHOF E: Docking of cationic antibiotics to negatively charged pockets in RNA folds./ Med. Chem. (1999) 42:1250–1261.
   PubMed Web of Science ®Google Scholar
• DAVIS B, AFSHAR M, VARANI G et al.:Rational design of inhibitors of HIV-1 TAR RNA through the stabilisation of electrostatic 'hot spots'. J. MoL Biol. (2004) 336:343–356.
   PubMed Web of Science ®Google Scholar
• MURCHIE AIH, DAVIS B, ISEL C et al: Structure -based drug design targeting an inactive RNA conformation: exploiting the flexibility of HIV-1 TAR RNA. J. Md. Biol. (2004) 336:625–638.
   PubMed Web of Science ®Google Scholar
• •This paper and [78] describe comprehensively a structure-based medicinal chemistry programme focusing on the TAR RNA target. The stepwise procedure from the initial compound design to iterative rounds of ligand improvement is outlined along with NMR structural studies on the ligand-RNA complexes.
   Google Scholar
• HERMANN T: Rational ligand design for RNA: the role of static structure and conformational flexibility in target recognition. Biochimie (2002) 84:869–875.
   PubMed Web of Science ®Google Scholar
• LIND KE, DU Z, FUJINAGA K, PETERLIN BM, JAMES TL: Structure-based computational database screening, in vitro assay, and NMR assessment of compounds that target TAR RNA. Chem. Biol. (2002) 9:185–193.
   PubMed Web of Science ®Google Scholar
• DU Z, LIND KE, JAMES TL: Structure of TAR RNA complexed with a Tat-TAR interaction nanomolar inhibitor that was identified by computational screening. Chem. Biol. (2002) 9:707–712.
   PubMedGoogle Scholar
• MAYER M, JAMES TL: NMR-based characterization of phenothiazines as a RNA binding scaffold. J. Am. Chem. Soc. (2004) 126:4453–4460.
   Google Scholar
• HAMY F, BRONDANI V, FLORSHEIMER A, STARK W, BLOMMERS MJ, KLIMKAIT T: A new class of HIV-1 Tat antagonist acting through Tat-TAR inhibition. Biochemistry (1998) 37:5086–5095.
   PubMed Web of Science ®Google Scholar
• GAYLE AY, BARANGER AM: Inhibition of the U1A-RNA complex by an aminoacridine derivative. Bioorg. Med. Chem. Lett. (2002) 12:2839–2842.
   PubMed Web of Science ®Google Scholar
• CECCHETTI V PAROLIN C, MORO S et al.: 6-Aminoquinolones as new potential anti-HIV agents. J. Med. Chem. (2000) 43:3799–3802.
   PubMed Web of Science ®Google Scholar
• PAROLIN C, GATTO B, DEL VECCHIO C et al: New anti-HIV Type 1 6-aminoquinolones: mechanism of action. Antimicrob. Agents Chemother. (2003) 47:889–896.
   PubMed Web of Science ®Google Scholar
• RICHTER S, PAROLIN C, GATTO B et al:Inhibition of human immunodeficiency virus Type 1 Tat-trans-activation-responsive region interaction by an antiviral quinolone derivative. Anti microb. Agents Chemother (2004) 48:1895-1899. This paper and [87] describe a novel class of Tat-TAR inhibitors based on 6-aminoquinolones, which were originally discovered by compound screening against infected cell lines. Investigation of the mechanism of action and molecular target of the novel inhibitors is outlined. The publications describe an approach that is exemplary and unique in the field of targeting viral RNA as they outline an inverse discovery route, that is, tracing a path from an empirically observed in vivo activity to a molecular RNA target-ligand interaction.
   Google Scholar
• RICHTER S, PAROLIN C, PALUMBO M, PALU G: Antiviral properties of quinolone-based drugs. Curr. Drug Targets Infect. Disord. (2004) 4:111–116.
   PubMedGoogle Scholar
• ENNIFAR E, PAILLART JC, MARQUET R et al: HIV-1 RNA dimerization initiation site is structurally similar to the ribosomal A site and binds aminoglycoside antibiotics. J. Biol. Chem. (2003) 278:2723–2730.
   PubMed Web of Science ®Google Scholar
• MCPIKE MP, GOODISMAN J, DABROWIAK JC: Footprinting and circular dichroism studies on paromomycin binding to the packaging region of human immunodeficiency virus type-1. Bioorg Med. Chem. (2002) 10:3663–3672.
   PubMed Web of Science ®Google Scholar
• MCPIKE MP, GOODISMAN J, DABROWIAK JC: Specificity of neomycin analogues bound to the packaging region of human immunodficiency virus type 1 RNA. Bioorg Med. Chem. (2004) 12:1835–1843.
   PubMed Web of Science ®Google Scholar
• COHEN J: Chiron stakes out its teritory. Science (1999) 285:28.
   Google Scholar
• GALLEGO J, VARANI G: The hepatitis C virus internal ribosome-entry site: a new target for antiviral research. Biochem. Soc. Trans. (2002) 30:140–145.
   PubMed Web of Science ®Google Scholar
• JUBIN R: Targeting hepatitis C virus translation: stopping HCV where its starts. Cun: Opin. Investig. Drugs (2003) 4:162–167.
   PubMedGoogle Scholar
• SPAHN CM, KIEFT JS, GRASSUCI RAet al: Hepatitis C virus IRES RNA-induced changes in the conformation of the 40S ribosomal subunit. Science (2001) 291: 1959-1962.
   Google Scholar
• KLINCK R. WESTHOF E, WALKERS, AFSHAR M, COLLIER A. ABOUL-ELA F: A potential RNA drug target in the hepatitis C virus internal ribosome entry site. RNA (2000) 6:1423–1431.
   PubMed Web of Science ®Google Scholar
• LUKAVSKY PJ, OTTO GA, LANCASTER AM, SARNOW P, PUGLISI JD: Structures of two RNA domains essential for hepatitis C virus internal ribosome entry site function. Nat. Struct. Biol. (2000) 7:1105–1110.
   PubMedGoogle Scholar
• KIEFT JS, ZHOU K, GRECH A, JUBIN R, DOUDNA JA: Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation. Nat. Struct. Biol. (2002) 9:370–374.
   PubMedGoogle Scholar
• KIM I, LUKAVSKY PJ, PUGLISI JD: NMR study of 100 lcDa HCV IRES RNA using segmental isotope labeling. J. Am. Chem. Soc. (2002) 124:9338–9339.
   PubMed Web of Science ®Google Scholar
• LUKAVSKY PJ, KIM I, OTTO GA, PUGLISI JD: Structure of HCV IRES domain II determined by NMR. Nat. Struct. Biol. (2003) 10:1033–1038.
   PubMedGoogle Scholar
• GOODING KB, HIGGS R, HODGE B et al.: High throughput screening of library compounds against an oligonucleotide substructure of an RNA target. J. Am. Soc. Mass Spectrom. (2004) 15:884–892.
   PubMed Web of Science ®Google Scholar
• JEFFERSON EA, SETH PP, ROBINSON DE et al.: Biaryl guanidine inhibitors of in vitro HCV-IRES activity. Bioorg. Med. Chem. Lett. (2004), 14:5139–5143.
   PubMed Web of Science ®Google Scholar
• SCHMID MB: Seeing is believing: the impact of structural genomics on antimicrobial drug discovery. Nat. Rev. Microbiol (2004) 2:739–746.
   PubMed Web of Science ®Google Scholar