HIV-1 integrase and RNase H activities as therapeutic targets

Bibliography

• ASANTE-APPIAH E, SKALKA AM: HIV-1 integrase: structural organization, conformational changes, and catalysis. Adv. Virus. Res. (1999) 52:351–369.
   PubMed Web of Science ®Google Scholar
• FOUCHIER RA, MALIM MH: Nuclear import of human immunodeficiency virus type-1 preintegration complexes. Adv. Virus. Res. (1999) 52:275–299.
   PubMed Web of Science ®Google Scholar
• BUKRINSKY MI, HAFFAE OK: HIV-1 nuclear import: in search of a leader. Front. BioscL (1999) 4:772–781.
   PubMedGoogle Scholar
• WHITTAKER GR, KAHN M,HELENIUS A: Viral entry into the nucleus. Ann. Rev Cell. Dev. Biol. (2000) 16:627.
   PubMed Web of Science ®Google Scholar
• •Short review on the mechanism of PIC entry into the nucleus.
   Google Scholar
• MILLER MD, FARNET CM, BUSHMAN FD: Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Vim/.(1997) 71:5382–5390.
   Google Scholar
• FARNET CM, BUSHMAN FD: HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes M vitro. Cell (1997) 88:483–492.
   PubMed Web of Science ®Google Scholar
• CHEN H, ENGELMAN A: The barrier-to-autointegration protein is a host factor for HIV Type 1 integration. Proc. Nati Acad. Sri USA (1998) 95:15270–15274.
   PubMed Web of Science ®Google Scholar
• VOGT P: Historical introduction to the general properties of retroviruses. In: Retroviruses. Coffin JM, Hughes SH, Varmus HE (Eds), Cold Spring Harbor Press (1997).
   Google Scholar
• KOHLSTAEDT LA, WANG J, FRIEDMAN JM, RICE PA, STEITZ TA: Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science (1992) 256:1783–1790.
   Google Scholar
• ••Describes clearly the structure of RT incomplex with an inhibitor.
   Google Scholar
• HOSTOMSKY Z, HOSTOMSKA Z, HUDSON GO, MOOMAW EW, NODES BR: Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus Type 1 reverse transcriptase. Proc. Nati Acad. Sci USA (1991) 88:1148–1152.
   PubMed Web of Science ®Google Scholar
• DAVIES IF, HOSTOMSKA Z, HOSTOMSKY Z, JORDAN SR, MATTHEWS DA: Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science (1991) 252:88–95.
   PubMed Web of Science ®Google Scholar
• GOPALAKRISHNAN V, PELISKA IA, BENKOVIC SJ: Human immunodeficiency virus Type 1 reverse transcriptase: spatial and temporal relationship between the polymerase andRNase H activities. Proc. Nati Acad. Sci USA (1992) 89:10763–10767.
   PubMed Web of Science ®Google Scholar
• JACOBO-MOLINA A, DING J, NANNI RG et al.: Crystal structure of human immunodeficiency virus Type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA. Proc. Nati Acad. Sri USA (1993) 90:6320–6324.
   Google Scholar
• DESTEFANO II, BUISER RG,MALLABER LM, FAY PJ, BAMBARA RA: Parameters that influence processive synthesis and site-specific termination by human immunodeficiency virus reverse transcriptase on RNA and DNA templates. Biochim. Biophys. Acta (1992) 1131:270–280.
   PubMedGoogle Scholar
• PELISKA JA, BENKOVIC SJ: Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. Science (1992) 258:1112–1118.
   PubMed Web of Science ®Google Scholar
• BLAIN SW, GOFF SP: Effects on DNA synthesis and translocation caused by mutations in the RNase H domain of Moloney murine leukemia virus reversetranscriptase.Virol. (1995) 69:4440–4452.
   Web of Science ®Google Scholar
• BURKE CJ, SANYAL G, BRUNER MW et al.: Structuralimplications of spectroscopiccharacterization of a putative zinc fingerpeptide from HIV-1 integrase. I Biol. Chem. (1992) 267:9639–9644.
   Google Scholar
• BUSHMAN FD, ENGELMAN A, PALMER I, WINGFIELD P, CRAIGIE R Domains of the integrase protein of human immunodeficiency virus Type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Nati Acad. Sci USA (1993) 90:3428–3432.
   PubMed Web of Science ®Google Scholar
• ZHENG R, JENKINS TM, CRAIGIE R Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Nati Acad. Sri USA (1996) 93:13659–13664.
   PubMed Web of Science ®Google Scholar
• CHEN IC, KRUCINSKI I,MIERCKE LJ et al.: Crystal structure of theHIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proc. Nati Acad. Sci. USA (2000) 97:8233–8238.
   Google Scholar
• CHEN Z, YAN Y, MUNSHI S et al: X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293) - an initial glance of the viral DNA binding platform. J. Ma. Biol. (2000) 296:521–533.
   Google Scholar
• YANG ZN, MUESER TC, BUSHMAN FD, HYDE CC: Crystalstructure of an active two-domain derivative of Rous sarcoma virus integrase. Ma Biol. (2000) 296:535–548.
   Google Scholar
• YANG W, STEITZ TA: Recombining the structures of HIV integrase, RuvC and RNase H. Structure (1995) 3:131–134.
   PubMed Web of Science ®Google Scholar
• •Comparison of the structures of these enzymes.
   Google Scholar
• FESEN MR, KOHN KW, LETEURTRE F, POMMIER Y: Inhibitors of human immunodeficiency virus integrase. Proc. Nati Acad. Sri USA (1993) 90:2399–2403.
   PubMed Web of Science ®Google Scholar
• MOUSCADET JF, CARTEAU S, GOULAOUIC H, SUBRA F,AUCLAIR C: Triplex-mediated inhibition of HIV DNA integration M vitro. I Biol. Chem. (1994) 269:21635–21638.
   Web of Science ®Google Scholar
• BOUZIANE M, CHERNY DI,MOUSCADET IF, AUCLAIR C: Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration M vitro. I Biol. Chem. (1996) 271:10359–10364.
   Web of Science ®Google Scholar
• BRODIN P, PINSKAYA M,VOLKOV E et al: Branched oligonucleotide-intercalator conjugate forming a parallel stranded structure inhibits HIV-1 integrase. FEBS Lett. (1999) 460:270–274.
   PubMed Web of Science ®Google Scholar
• NEAMATI N, MAZUMDER A, SUNDER S et al.: Highly potent synthetic polyamides, bisdistamycins, and lexitropsins as inhibitors of human immunodeficiency virus Type 1 integrase. Mol. Pharmacol (1998) 54:280–290.
   PubMed Web of Science ®Google Scholar
• RYABININ VA, ZAKHAROVA OD, YURCHENKO EY et al.: Synthesis and evaluation of oligo-1,3-thiazolecarboxamide derivatives as HIV-1 reverse transcriptase inhibitors. Bioorg. Med. Chem. (2000) 8:985–993.
   PubMed Web of Science ®Google Scholar
• RYABININ VA, SINYAKOV AN, RICHARD DE et al: Inhibition of HIV-1 integrase-catalysed reaction by new DNA minor groove ligands: the oligo-1,3–
   Google Scholar
• ••thiazolecarboxamide derivatives. Eur. Med. Chem. (2000) 35:989–1000.
   Google Scholar
• CUSHMAN M, SHERMAN P: Inhibitionof HIV-1 integration protein by aurintricarboxylic acid monomers, monomer analogs, and polymer fractions.Biochem. Biophys. Res. Commun. (1992) 185:85–90.
   PubMed Web of Science ®Google Scholar
• MAZUMDER A, LEVITZKI A, NICKLAUS M, YUNG J,KOHLAGEN G, POMMIER Y: Effects of tyrphostins, protein kinase inhibitors, on human immunodeficiency virus Type 1 integrase. Biochemistry (1995) 34:15111–15122.
   PubMed Web of Science ®Google Scholar
• FARNET CM, BUSHMAN FD: HIV cDNA integration: molecular biology and inhibitor development. AIDS (1996) 10:3–11.
   Web of Science ®Google Scholar
• ETCH E, PERTZ H, KALOGA M et al.:(-)-Arctigenin as a lead structure for inhibitors of human immunodeficiency virus Type-1 integrase. J. Med. Chem. (1996) 39:86–95.
   PubMed Web of Science ®Google Scholar
• LAFEMINA RL, GRAHAM PL, LEGROW K et al.: Inhibition of human immunodeficiency virus integrase by bis-catechols. Antimicrob. Agents Chemother.(1995) 39:320–324.
   PubMed Web of Science ®Google Scholar
• DUPONT R, JEANSON L,MOUSCADETJF, COTELLE P: Synthesis and HIV-1 integrase inhibitory activities of catechol and bis-catechol derivatives. Biorg. Med Chem. Lett. (2001) 11:3175–3178.
   PubMed Web of Science ®Google Scholar
• ZOUHIRI F, MOUSCADET JF, MEKOUAR K et al.: Structure-activity relationships and binding mode of styrylquinolines as potent inhibitors of HIV-1 integrase and replication of HIV-1 in cell culture. / Med. Chem. (2000) 43:1533–1540.
   PubMed Web of Science ®Google Scholar
• FESEN MR, POMMIER Y,LETEURTRE F, HIROGUCHI S,YUNG J, KOHN KW: Inhibition of HIV-1 integrase by flavones, caffeic acid phenethylester (CAPE) and related compounds. Biochem. Pharmacol (1994) 48:595–608.
   PubMed Web of Science ®Google Scholar
• MAZUMDER A, RAGHA VAN K, WEINSTEIN J, KOHN KW,POMMIER Y: Inhibition of human immunodeficiency virus type-1 integrase by curcumin. Biochem. Pharmacol. (1995) 49:1165–1170.
   PubMed Web of Science ®Google Scholar
• MAZUMDER A, NEAMATI N, SUNDER S et al.: Curcumin analogs with altered potencies against HIV-1 integrase as probes for biochemical mechanisms of drugaction. J. Med. Chem. (1997) 40:3057–3063.
   PubMed Web of Science ®Google Scholar
• ROBINSON WE JR, REINECKE MG, ABDEL-MALEK S, JIA Q, CHOW SA: Inhibitors of HIV-1 replication inhibit HIV integrase. Proc. Natl Acad. Sci. USA (1996) 93:6326–6331.
   PubMed Web of Science ®Google Scholar
• PLUYMERS W, NEAMATI N, PANNECOUQUE C et al.: Viral entry as the primary target for the anti-HIV activity of chicoric acid and its tetra-acetyl esters.MM. Pharmacol (2000) 58:641–648.
   PubMed Web of Science ®Google Scholar
• HAZUDA D J, FELOCK P,WITMER M et al.: Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells. Science (2000) 287:646–650.
   Google Scholar
• ••Discusses one of the most potent INinhibitors.
   Google Scholar
• ESPESETH AS, FELOCK P,WOLFE A et al.: HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. Proc. Natl. Acad. Sci. USA (2000) 97:11244–11249.
   Google Scholar
• •Discusses one of the most potent IN inhibitors.
   Google Scholar
• KIMPTON J, EMERMAN M: Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. /Virol (1992) 66:2232–2239.
   PubMed Web of Science ®Google Scholar
• WAI JS, EGBERTSON MS,PAYNE LS et al.: 4-Aryl-2,4-dioxobutanoic acid inhibitors of HIV-1 integrase and viral replication in cells. J. Med. Chem. (2000) 43:4923–4926.
   Google Scholar
• MARCHAND C, ZHANG X,PATS CG et al.: Structural determinants for HIV-1 integrase inhibition by P-diketo acids. J. Bio/. Chem. (2002) 277:12596–12603.
   Google Scholar
• •Very recent work where the authors report a novel bifunctional DKA derivative.
   Google Scholar
• GOLD GUR Y, CRAIGIE R,COHEN GH et al.: Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design. Proc. Natl Acad. Sci. USA (1999) 96:13040–13043.
   Google Scholar
• NI H, SOTRIFFER CA,MCCAMMON JA: Ordered water and ligand mobility in the HIV-1 integrase-5CITEP complex: a molecular dynamics study. J. Med. Chem. (2001) 44:3043–3047.
   PubMed Web of Science ®Google Scholar
• KESERU GM, KOLOSSVARY I: Fullyflexible low-mode docking: application to induced fit in HIV integrase. I Am. Chem. Soc. (2001) 123:12708–12709.
   PubMed Web of Science ®Google Scholar
• KOLONIN MG, FINLEY RL JR: Targeting cyclin-dependent kinases in Drosophila with peptide aptamers. Proc. Natl Acad. Sci. USA (1998) 95:14266–14271.
   PubMed Web of Science ®Google Scholar
• PURAS-LUTZKE RA, EPPENS NA, WEBER PA, HOUGHTEN RA, PLASTERK RH: Identification of a hexapeptide inhibitor of the human immunodeficiency virus integrase protein by using a combinatorial chemical library.Proc. Natl Acad. Sci USA (1995) 92:11456–11460.
   PubMed Web of Science ®Google Scholar
• SOURGEN F, MAROUN RG,FRERE V et al.: A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vitro integration activity of the enzyme. Correlated biochemical and spectroscopic results. Ear. J. Biochem. (1996) 240:765–773.
   Google Scholar
• MAROUN RG, GAYET S,BENLEULMI MS et al.: Peptide inhibitors of HIV-1 integrase dissociate the enzyme oligomers. Biochemistry (2001) 40:13840–13848.
   Google Scholar
• DIVITA G, RESTLE T, GOODY RS, CHERMANN JC, BAILLON JG:Inhibition of human immunodeficiency virus Type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. J. Bio/. Chem. (1994) 269:13080–13083.
   PubMed Web of Science ®Google Scholar
• MORRIS MC, BERDUCOU C, MERY J, HEITZ F, DIVITA G: The thumb domain of the P51-subunit is essential for activation of HIV reverse transcriptase. Biochemistry (1999) 38:15097–15103.
   PubMed Web of Science ®Google Scholar
• RICHARD DE, RICHARD DE SOULTRAIT V, CAUMONT A et al.: A novel short peptide is a specific inhibitor of the human immunodeficiency virus Type 1integrase. Ma Biol. (2002) In press.
   Google Scholar
• LOWMAN HB: Bacteriophage display and discovery of peptide leads for drug development. Ann. Rev Biophys. Biomol. Struct. (1997) 26:401–424.
   PubMedGoogle Scholar
• RODI DJ, MAKOWSKI L: Phage-display technology-finding a needle in a vast molecular haystack. Carr: Opin. Biotechnol(1999) 10:87–93.
   PubMed Web of Science ®Google Scholar
• LI M: Applications of display technology inprotein analysis. Nat. Biotechnol (2000) 18:1251–1256.
   PubMed Web of Science ®Google Scholar
• DRAKE RR, NEAMATI N,HONG H et al.: Identification of a nucleotide binding site in HIV-1 integrase. Proc. Nati Acad. Sri USA (1998) 95:4170–4175.
   Google Scholar
• TAKTAKISHVILI M, NEAMATI N, POMMIER Y, NAIR V: Discovery of a nuclease-resistant, non-natural dinucleotide that inhibits HIV-1 integrase. Bioorg. Med. Chem. Lett. (2001) 11:1433–1435.
   PubMed Web of Science ®Google Scholar
• JING N: Developing G-quartet oligonucleotides as novel anti-HIV agents: focus on anti-HIV drug design. Expert Opin. Investig. Drugs (2000) 9:1777–1785.
   PubMed Web of Science ®Google Scholar
• •Review on G-quartet oligonucleotides as anti-HIV agents.
   Google Scholar
• ESTE JA, CABRERA C, SCHOLS D et al.:Human immunodeficiency virus glycoprotein gp120 as the primary target for the antiviral action of AR177 (Zintevir). Mol Pharmacol (1998) 53:340–345.
   PubMed Web of Science ®Google Scholar
• JING N, XIONG W, GUAN Y, PALLANSCH L, WANG S: Potassium-dependant folding: a key to intracellular delivery of G-quartet oligonucleotides as HIV inhibitors. Biochemistry (2002) 41:5397–5403.
   PubMed Web of Science ®Google Scholar
• FIELD AK: Oligonucleotides as antiretroviral agents. In: Antiretroviral Therapy Clercq DE (Ed), ASM Press, Washington DC, USA (2001) 129–145.
   Google Scholar
• ALLEN P, WORLAND S, GOLD L: Isolation of high-affinity RNA ligands to HIV-1 integrase from a random pool. Virology (1995) 209:327–336.
   PubMed Web of Science ®Google Scholar
• TRAMONTANO E, COLLA PL, CHENG YC: Biochemical characterization of the HIV-1 integrase 3'-processing activity and its inhibition by phosphorothioate oligonucleotides. Biochemistry (1998) 37:7237–7243.
   PubMed Web of Science ®Google Scholar
• SNASEL J, REJMAN D,LIBOSKA R et al.: Inhibition of HIV-1 integrase by modified oligonucleotides derived from U5' LTR. Eur. j Biochem. (2001) 268:980–986.
   Google Scholar
• BRODIN P, GOTTIKH M, AUCLAIR C, MOUS CADET JF: Inhibition of HIV-1 integration by mono- & bi-functionalized triple helix forming oligonucleotides. Nucleosides Nucleotides (1999) 18: 1717-1718.
   Google Scholar
• CAUMONT AB, JAMIESON GA, RICHARD DE SOULTRAIT V et al:High affinity interaction of HIV-1 integrase with specific and non- specific single-stranded short oligonucleotides. FEBS Lett. (1999) 455:154–158.
   PubMed Web of Science ®Google Scholar
• CARTEAU S, GORELICK RJ, BUSHMAN FD: Coupled integration of human immunodeficiency virus Type 1 cDNA ends by purified integrase in vitro: stimulation by the viral nucleocapsid protein. Virol. (1999) 73:6670–6679.
   Web of Science ®Google Scholar
• CAUMONT AB, JAMIESON GA, PICHUANTES S et al.: Expression of functional HIV-1 integrase in the yeast Saccharomyces cerevisiae leads to the emergence of a lethal phenotype: potential use for inhibitor screening. Curr. Genet. (1996) 29:503–510.
   PubMed Web of Science ®Google Scholar
• SCHATZ 0, CROMME F, NAAS T et al:Inactivation of the RNase H domain of HIV-1 reverse transcriptase blocks viral infectivity. In: Oncogenesis and AIDS. Papas TS (Ed), Portfolio Publishing Company, Texas, USA (1990) 293–303.
   Google Scholar
• •Shows the importance of RNase H activity in the viral cycle.
   Google Scholar
• MOELLING K, SCHULZE T, DIRINGER H: Inhibition of human immunodeficiency virus Type 1 RNase H by sulfated polyanions. Virol (1989) 63:5489–5491.
   Web of Science ®Google Scholar
• ANDREOLA ML, THARAUD D, LITVAK S, TARRAGO-LITVAK L: The ribonuclease H activity of HIV-1 reverse transcriptase: further biochemical characterization and search of inhibitors. Biochimie (1993) 75:127–134.
   PubMed Web of Science ®Google Scholar
• TAN CK, CIVIL R, MIAN AM, SO AG, DOWNEY KM: Inhibition of the RNase H activity of HIV reverse transcriptase by azidothymidylate. Biochemistry (1991) 30:4831–4835.
   PubMed Web of Science ®Google Scholar
• ALLEN P, COLLINS B, BROWN D, HOSTOMSKY Z, GOLD L: A specific RNA structural motif mediates high affinity binding by the HIV-1 nucleocapsid protein (NCp7). Virology (1996) 225:306–315.
   PubMed Web of Science ®Google Scholar
• LOYA S, HIZI A: The interaction of illimaquinone, a selective inhibitor of the RNase H activity, with the reverse transcriptases of human immunodeficiency and murine leukemia retroviruses. I Biol. Chem. (1993) 268:9323–9328.
   Web of Science ®Google Scholar
• MIN BS, NAKAMURA N,MIYASHIRO H, KIM YH, HATTORI M: Inhibition of human immunodeficiency virus Type 1 reverse transcriptase and ribonuclease H activities by constituents ofJuglans mandshurica. Chem. Pharm. Bull. (2000) 48:194–200.
   PubMed Web of Science ®Google Scholar
• BORKOW G, FLETCHER RS, BARNARD J et al.: Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoy1)-2-hydroxy-l-naphthaldehyde hydrazone. Biochemistry (1997) 36:3179–3185.
   PubMed Web of Science ®Google Scholar
• •Discusses one of the most potent IN inhibitors.
   Google Scholar
• ARION D, SLUIS-CREMER N, MIN KL et al.: Mutational analysis of Y501 of HIV-1 reverse transcriptase: Effects on ribonuclease H activity and inhibition of this activity by N-acyl hydrazones. J. Biol. Chem. (2001) 277:1370–1374.
   PubMed Web of Science ®Google Scholar
• TANESE N, GOFF SP: Domain structure of the Moloney murine leukemia virus reverse transcriptase: mutational analysis and separate expression of the DNA polymerase and RNase H activities. Proc. Nati Acad. Sri USA (1988) 85:1777–1781.
   PubMed Web of Science ®Google Scholar
• PALANIAPPAN C, FAY PJ,BAMBARA RA: Nevirapine alters the cleavage specificity of ribonuclease H of human immunodeficiency virus 1 reverse transcriptase. J. Biol. Chem. (1995) 270:4861–4869.
   PubMed Web of Science ®Google Scholar
• GERONDELIS P, ARCHER RH, PALANIAPPAN C et al: The P236L delavirdine-resistant human immunodeficiency virus Type 1 mutant is replication defective and demonstrates alterations in both RNA 5'-end- and DNA 3'-end-directed RNase H activities.' Virol (1999) 73:5803–5813.
   PubMed Web of Science ®Google Scholar
• ARCHER RH, DYKES C,GERONDELIS P et al.: Mutants of human immunodeficiency virus Type 1 (HIV-1) reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors demonstrate altered rates of RNase H cleavage that correlate with HIV-1 replication fitness in cell culture. " Viral (2000) 74:8390–8401.
   Google Scholar
• GABBARA S, DAVIS WR, HUPE L, HUPE D, PELISKA JA: Inhibitors of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. Biochemistry (1999) 38:13070–13076.
   PubMed Web of Science ®Google Scholar
• ••Refers to an inhibitor, which acts on theRNase H activity of RT without affecting the DNA polymerase one.
   Google Scholar
• DAVIS WR, TOMSHO J, NIKAM S, COOK EM, SOMAND D, PELISKA JA: Inhibition of HIV-1 reverse transcriptase-catalyzed DNA strand transfer reactions by4-chlorophenylhydrazone of mesoxalic acid.Biochemistry (2000) 39:14279–14291.
   PubMed Web of Science ®Google Scholar
• TUERK C, MACDOUGAL-WAUGH S: In vitro evolution of functional nucleic acids: high-affinity RNA ligands of HIV-1 proteins. Gene (1993) 137:33–39.
   PubMed Web of Science ®Google Scholar
• BURKE DH, SCATES L, ANDREWS K, GOLD L: Bent pseudoknots and novel RNA inhibitors of Type 1 human immunodeficiency virus (HIV-1) reverse transcriptase. Mo/. Bid (1996) 264:650–666.
   PubMed Web of Science ®Google Scholar
• SCHNEIDER DJ, FEIGON J,HOSTOMSKY Z, GOLD L: High-affinity ssDNA inhibitors of the reverse transcriptase of Type 1 human immunodeficiency virus. Biochemistry(1995) 34:9599–9610.
   PubMed Web of Science ®Google Scholar
• ELLINGTON AD, SZOSTAK JVV: In vitro selection of RNA molecules that bind specific ligands. Nature (1990) 346:818–822.
   PubMed Web of Science ®Google Scholar
• TUERK C, GOLD L: Systematic evolutionof ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science (1990) 249:505–510.
   PubMed Web of Science ®Google Scholar
• GOLD L, BROWN D, HEY, SHTATLAND T, SINGER BS, VVU From oligonucleotide shapes to genomic SELEX: novel biological regulatory loops. Proc. Nati Acad. Sci USA (1997) 94:59-64.Carr. Top. Microbial. Immunol (1999) 243:123.
   Google Scholar
• JAYASENA SD: Aptamers: an emerging class of molecules that rival antibodies in diagnostics. Clin. Chem. (1999) 45:1628–1650.
   PubMed Web of Science ®Google Scholar
• •Review that compares aptamers and antibodies and describes the interest of in vitro selection for diagnostic purposes.
   Google Scholar
• TOULME JJ: Aptamers: selected oligonucleotides for therapy. Can: Opin. Ther. (2000) 2:318–324.
   PubMedGoogle Scholar
• TUCKER CE, CHEN LS, JUDKINS MB, FARMER JA, GILL SC, DROLET DW:Detection and plasma pharmacokinetics of an anti-vascular endothelial growth factor oligonucleotide-aptamer (NX1838) in rhesus monkeys. I Chromatogr. B. Biomed. Sci. Appl. (1999) 732:203–212.
   PubMed Web of Science ®Google Scholar
• •A nice example of an aptamer in therapeutical use.
   Google Scholar
• TUERK C, MACDOUGAL S, GOLD L: RNA pseudoknots that inhibit human immunodeficiency virus Type 1 reverse transcriptase. Proc. Nati Acad. Sci. USA(1992) 89:6988.
   PubMed Web of Science ®Google Scholar
• •Describes the first potent RNA inhibitor against HIV-1 RT obtained by in vitro selection.
   Google Scholar
• CHEN H, GOLD L: Selection of high-affinity RNA ligands to reverse transcriptase: inhibition of cDNA synthesis and RNase H activity. Biochemistry (1994) 33:8746–8756.
   PubMed Web of Science ®Google Scholar
• ANDREOLA ML, PILEUR F,CALMELS C et al: DNA aptamers selected against the HIV-1 RNase H display in vitro antiviral activity. Biochemistry (2001)40:10087–10094.
   PubMed Web of Science ®Google Scholar
• CASAUBON RL, SNAPPER ML: ..Cadenosylmethionine reverses ilimaquinone's vesiculation of the Golgi apparatus. A fluorescence study on the cellular interactions of ilimaquinone Biorg. Med. Chem. Letters (2001) 11:133–136.
   PubMed Web of Science ®Google Scholar