Inhibitors of HIV cellular fusion

Bibliography

• CAMMACK N: Human immunodeficiency virus Type 1 entry and chemokine receptors: a new therapeutic target. Antivir. Chem. Chemother. (1999) 10:53–62.
   PubMed Web of Science ®Google Scholar
• ••Review of the role of the chemokine coreceptor in HIV andcurrent therapeutic approaches to modulating this target.
   Google Scholar
• FRANKEL AD, YOUNG JA: HIV-1: fifteen proteins and an RNA. Ann. Rev. Biochem. (1998) 67:1–25.
   PubMed Web of Science ®Google Scholar
• •Review of HIV replication.
   Google Scholar
• ROSSI D, ZLOTNIK A: The biology of chemokines and their receptors. Ann. Rev. Immunol (2000) 18:217–242.
   PubMed Web of Science ®Google Scholar
• •Generalised review.
   Google Scholar
• CHAN DC, KIM PS: HIV entry and its inhibition. Cell (1998) 93:681–684.
   PubMed Web of Science ®Google Scholar
• RABUT GE, KONNER JA, KAJUMO F, MOORE JP, DRAGIC T: Alanine substitutions of polar and nonpolar residues in the amino-terminal domain of CCR5 differently impair entry of macrophage- and dualtropic isolates of human immunodeficiency virus Type 1.1 Virol (1998) 72:3464–3468.
   PubMedGoogle Scholar
• HOWARD OM, SHIRAKAWA AK, TURPIN JA et al: Naturally occurring CCR5 ex tr acellular and tr an smembr an e domain variants affect HIV-1 co-receptor and ligand binding function." Biol. Chem. (1999) 274:16228–16234.
   PubMed Web of Science ®Google Scholar
• SICILIANO SJ, KUHMANN SE, WENG Y et al.: A critical site in the core of the CCR5 chemokine receptor required for binding and infectivity of human immunodefi-ciency virus Type 1. J. Biol. Chem. (1999) 274:1905–1913.
   PubMed Web of Science ®Google Scholar
• CHADWICK DR, LEVER AML: Gene therapy for HIV. Exp. Opin. Ther. Patents (1998) 8:983–990.
   Google Scholar
• •Current review.
   Google Scholar
• AMADO RG, MITSUYASU RT, ZACK JA: Gene therapy for the treatment of AIDS: animal models and human clinical experience. Front. Biosci. (1999) 4:D468–475.
   Google Scholar
• NAGASAWA T, TACHIBANA K, KISHIMOTO T: A novelCXC chemokine PBSF/SDF-1 and its receptor CXCR4: their functions in development, hematopoiesis and HIV infection. Semin. Immunol. (1998) 10:179–185.
   PubMed Web of Science ®Google Scholar
• MACPHERSON JL, ELY JA, SUN LQ, SYMONDS GP: Ribozymes in gene therapy of HIV-i. Front. Biosci. (1999) 4:D497–505.
   Google Scholar
• •Current review.
   Google Scholar
• SU SB, GONG WH, GAO JL et al.: T20/DP178, an ectodo-main peptide of human immunodeficiency virus Type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor. Blood (1999) 93:3885–3892.
   PubMed Web of Science ®Google Scholar
• ECKERT DM, MALASHKEVICH VN, HONG LH, CARR PA, KIM PS: Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell (1999) 99:103–115.
   PubMed Web of Science ®Google Scholar
• ••Identification of a specific binding domain in the coreceptorand design of potential peptide inhibitors.
   Google Scholar
• MISSE D, CERUTTI M, NORAZ N et al.: A CD4 -independent interaction of human immunodeficiency virus-1 gp120 with CXCR4 induces their cointernaliza-tion, cell signaling and T-cell chemotaxis. Blood (1999) 93:2454–2462.
   PubMedGoogle Scholar
• DOLEI A, BIOLCHINI A, SERRA C, CURRELI S, GOMES E, DIANZANI F: Increased replication of T-cell-tropic HIV strains and CXC-chemokine receptor-4 induction in T cells treated with macrophage inflammatory protein (MIP) -I alpha,MIP-1 betaandRANTESbeta-chemokines. AIDS (1998) 12:183–190.
   PubMed Web of Science ®Google Scholar
• •Potential negative effects of antichemokine therapy.
   Google Scholar
• ABBATE I, DIANZANI F, BIANCHI F et al.: RANTESstimulates cell-mediated transmission of HIV-1 infection. J. Interferon Cytokine Res. (1999) 19:345–350.
   PubMedGoogle Scholar
• YANG OO, SWANBERG SL, LU Z et al.: Enhanced inhibi-tion of human immunodeficiency virus Type 1 by Met-stromal-derived factor 1beta correlates with down-modulation of CXCR4. J. Viroi. (1999) 73:4582–4589.
   PubMed Web of Science ®Google Scholar
• SCHWARZ MK, WELLS TN: Interfering with chemokinenetworks - the hope for new therapeutics. CUIT. Opin. Chem. Biol. (1999) 3:407–417.
   PubMedGoogle Scholar
• •Review of modified chemokines as HIV-1 inhibitors.
   Google Scholar
• SIMMONS G, CLAPHAM PR, PICARD L et al.: Potent inhibi- tion of HIV-1 infectivity in macrophages and lympho-cytes by a novel CCR5 antagonist. Science (1997) 276:276–279.
   PubMed Web of Science ®Google Scholar
• PROUDFOOT AE, POWER CA, HOOGEWERF et al.: Extension of recombinant human RANTES by the retention of the initiating methionine produces a potent antagonist. J. Biol. Chem. (1996) 271:2599–2603.
   PubMed Web of Science ®Google Scholar
• MOSIER DE, PICCHIO GR, GULIZIA RJ et al.: Highlypotent RANTES analogues either prevent CCR5-using human immunodeficiency virus Type 1 infection in vivo or rapidly select for CXCR4-using variants. J. Virol (1999) 73:3544–3550.
   PubMed Web of Science ®Google Scholar
• YLISASTIGUI L, VIZZAVONA J, DRAKOPOULOU E et al.:Synthetic full-length and truncated RANTES inhibit HIV-1 infection of primary macrophages. AIDS (1998) 12:977–984.
   PubMed Web of Science ®Google Scholar
• SCHOLS D, PROOST P, STRUYF S et al.: CD26-processedRANTES (3-68), but not intact RANTES, has potent anti-HIV-1 activity [published erratum appears in Antiviral Res 1999 Jan;40(3):189-90]. Antiviral Res. (1998) 39:175–187.
   PubMed Web of Science ®Google Scholar
• MURAKAMI T, NAKAJIMA T, KOYANAGI Y et al.: A smallmolecule CXCR4 inhibitor that blocks Tcell line-tropic HIV-1 infection. J. Exp. Med. (1997) 186:1389–1393.
   PubMed Web of Science ®Google Scholar
• •T22 small peptide inhibitor.
   Google Scholar
• TAMAMURA H, XU Y, HATTORI T et al.: A low-molecular-weight inhibitor against the chemokine receptor CXCR4: a strong anti-H1Vpeptide T1 40. Biochem. Biophys. Res. Commun. (1 9 9 8) 253:877–882.
   Google Scholar
• TAMAMURA H, IMAI M, ISHIHARA T et al.: Pharma-cophore identification of a chemokine receptor (CXCR4) antagonist, T22 ([Tyr(5,12),Lys7]-polyph-emusin II), which specifically blocks T cell-line-tropic HIV-1 infection. Bioorg. Med. Chem. (1998) 6:1033–1041.
   PubMed Web of Science ®Google Scholar
• ARAKAKI R, TAMAMURA H, PREMANATHAN M et al.: 1134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure. J. Virol (1999) 73:1719–1723.
   PubMed Web of Science ®Google Scholar
• HALLIDAY SM, LACKMAN-SMITH C, BADER JP et al.:Inhibition of human immunodeficiency virus replica-tion by the sulfonated stilbene dye resobene. Antiviral Res. (1996) 33:41–53.
   PubMed Web of Science ®Google Scholar
• CLANTON DJ, MORAN RA, MCMAHON JB et al.: Sulfonicacid dyes: inhibition of the human immunodeficiency virus and mechanism of action. J. Acquir. Immune Defk. Syndr. (1992) 5:771–781.
   PubMed Web of Science ®Google Scholar
• JAGODZINSKI PP, WIADERKIEWICZ R, KURZAWSKI G etal.: Mechanism of the inhibitory effect of curdlan sulfate on HIV-1 infection in vitro. Virology (1994) 202:735–745.
   Google Scholar
• DE CLERCQ E: Novel compound in preclinical/early clinical development for the treatment of HIV infections. Rev. Med. Vim]. (2000) 10:255–277.
   PubMed Web of Science ®Google Scholar
• ••AMD 3100 review.
   Google Scholar
• EGBERINK HF, DE CLERCQ E, VAN VLIET AL et al:Bicyclams, selective antagonists of the human chemokine receptor CXCR4, potently inhibit feline immunodeficiency virus replication. J Vim/ (1999) 73:6346–6352.
   Google Scholar
• DE CLERCQ E: Inhibition of H1Vinfection by bicyclams, highly potent and specific CXCR4 antagonists. Mol. Pharmacol. (2000) 57:833–839.
   PubMed Web of Science ®Google Scholar
• ••Comprehensive review of AMD 3100 antiviral activity.
   Google Scholar
• SCHOLS D, ESTE JA, CABRERA C, DE CLERCQ E: T-cell-line-tropic human immunodeficiency virus Type 1 that is made resistant to stromal cell-derived factor 1 alpha contains mutations in the envelope gp120 but does not show a switch in coreceptor use. J. Virol. (1998) 72:4032–4037.
   PubMed Web of Science ®Google Scholar
• BRIDGER GJ, SKERLJ RT, PADMANABHAN S et al.: Synthesis and structure-activity relationships of phenylenebis(methylene)-linked bis-azamacrocycles that inhibit HIV-1 and HIV-2 replication by antagonism of the chemokine receptor CXCR4. JMed. Chem. (1999) 42:3971–3981.
   PubMed Web of Science ®Google Scholar
• ESTE JA, CABRERA C, BLANCO J et al: Shift of clinicalhuman immunodeficiency virus Type 1 isolates from X4 to R5 and prevention of emergence of the syncytium-inducing phenotype by blockade of CXCR4.j Virol. (1999) 73:5577–5585.
   PubMed Web of Science ®Google Scholar
• •Suggests AMD 3100 may slow HIV disease progression by selection of R5 virus.
   Google Scholar
• SCHRAMM B, PENN ML, SPECK RF et at: Viral entrythrough CXCR4 is a pathogenic factor and therapeutic target in human immunodeficiency virus Type 1 disease. J. Vim/ (2000) 74:184–192.
   Google Scholar
• DE VREESE K, KOFLER-MONGOLD V, LEUTGEB C et al:The molecular target of bicyclams, potent inhibitors of human immunodeficiency virus replication. J Vim/ (1996) 70:689–696.
   Google Scholar
• HENDRIX CW, FLEXNER C, MACFARLAND RT et al: Pharmacokinetics and safety of AMD-3100, a novel antagonist of the CXCR- 4 chemokine receptor, in human volunteers. Antimicrob. Agents Chemother. (2000) 44:1667–1673.
   PubMed Web of Science ®Google Scholar
• •Phase I clinical trial summary of AMD 3100.
   Google Scholar
• DATEMA R, RABIN L, HINCENBERGS M et al: Antiviral efficacy in vivo of the anti-human immunodeficiency virus bicyclam SDZ SID 791 (JM 3100), an inhibitor of infectious cell entry. Antimicrob. Agents Chemother. (1996) 40:750–754.
   PubMed Web of Science ®Google Scholar
• CLANTON DJ, BUCKHEIT RW, JR., TERPENING SJ et al.: Novel sulfonated and phosphonated analogs of distamycin which inhibit the replication of HIV. Antiviral Res. (1995) 27:335–354.
   Google Scholar
• HOWARD OM, OPPENHEIM JJ, HOLLINGSHEAD MG et al: Inhibition of in vitro and in vivo HIV replication by a distamycin analogue that interferes with chemokine receptor function: a candidate for chemotherapeutic and microbicidal application. J. Med. Chem. (1998) 41:2184–2193.
   PubMed Web of Science ®Google Scholar
• ••First identified inhibitor of CXCR4 and CCR5 in a singlechemically defined structure.
   Google Scholar
• HOLLINGSHEAD M, ROBERSON J, DECKER W et al: In vivo drug screening applications of HIV-infected cells cultivated within hollow fibers in two physiologic compartments of mice. Antiviral Res. (1995) 28:265–279.
   PubMedGoogle Scholar
• CLAPHAM PR, REEVES JD, SIMMONS G, DEJUCQ N, HIBBITTS S, MCKNIGHT A: niv coreceptors, cell tropism and inhibition by chemokine receptor ligands. Mol. Membr. Biol. (1999) 16:49–55.
   PubMed Web of Science ®Google Scholar
• BERSON JF, DOMS RW: Structure-function studies of the Hill-1 coreceptors. Semin. Immunol. (1998) 10:237–248.
   PubMed Web of Science ®Google Scholar
• BABA M, NISHIMURA O, KANZAKI N et al: A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-H1V-1 activity. Proc. Natl. Acad. ScL USA (1999) 96:5698–5703.
   PubMed Web of Science ®Google Scholar
• •First publication of the antiviral effects of TAK 799.
   Google Scholar
• RUCKER J, SAMSON M, DORANZ BJ et al.: Regions in beta-chemokine receptors CCR5 and CCR2b that determine H1V-1 cofactor specificity. Cell (1996) 87:437–446.
   PubMed Web of Science ®Google Scholar
• SHIRAISHI M, ARAMAKI Y, SETO M et al.: Discovery ofnovel, potent and selective small-molecule CCR5 antagonists as anti-HIV-1 agents: synthesis and biological evaluation of anilide derivatives with a quaternary ammonium moiety. J. Med. Chem. (2000) 43:2049–2063.
   PubMed Web of Science ®Google Scholar
• DRAGIC T, TRKOLA A, THOMPSON DA et al.: A bindingpocket for a small molecule inhibitor of Hill-1 entry within the transmembrane helices of CCR5. Proc. Natl. Acad. ScL USA (2000) 97:5639–5644.
   PubMed Web of Science ®Google Scholar
• •Identification of a binding pocket on the receptor for CCR5 inhibitor TAK 799
   Google Scholar