Potential therapies for coronaviruses

Bibliography

• WU Y-S, LIN W-H, HSU J, HSIEH HP: Antiviral drug discovery against SARS-CoV. Curr. Med. Chem. (2006) (In Press).
   Google Scholar
• DE CLERCQ E: Potential antivirals and antiviral strategies against SARS coronavirus infections. Expert Rev. Anti-Infect. Ther. (2006) 4(2):291-302.
   PubMedGoogle Scholar
• WU CJ, CHAN YL: Antiviral applications of RNAi for coronavirus. Expert Opin. Investig. Drugs (2006) 15(2):89-97.
   PubMed Web of Science ®Google Scholar
• LI W, MOORE MJ, VASILIEVA N et al.: Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature (2003) 426(6965):450-454.
   PubMed Web of Science ®Google Scholar
• HOFMANN H, PYRC K, VAN DER HOEK L, GEIER M, BERKHOUT B, PÖHLMANN S: Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry. Proc. Natl. Acad. Sci. USA (2005) 102(22):7988-7993.
   PubMed Web of Science ®Google Scholar
• TOWLER P, STAKER B, PRASAD SG et al.: ACE2 X-Ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J. Biol. Chem. (2004) 279(17):17996-18007.
   PubMed Web of Science ®Google Scholar
• BARTLAM M, YANG H, RAO Z: Structural insights into SARS coronavirus proteins. Curr. Opin. Struct. Biol. (2005) 15(6):664-672
   PubMed Web of Science ®Google Scholar
• XIAO X, CHAKRABORTI S, DIMITROV AS, GRAMATIKOFF K, DIMITROV DS: The SARS-CoV S glycoprotein: expression and functional characterization. Biochem. Biophys. Res. Commun. (2003) 312(4):1159-1164.
   PubMed Web of Science ®Google Scholar
• LI W, ZHANG C, SUI J et al.: Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. (2005) 4(8):1634-1643.
   Google Scholar
• HAN DP, PENN-NICHOLSON A, CHO MW: Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. Virology (2006) 350(1):15-25.
   PubMed Web of Science ®Google Scholar
• SMITH DH, BYRN RA, MARSTERS SA et al.: Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen. Science (1987) 238(4834):1704-1707.
   PubMed Web of Science ®Google Scholar
• KILBY JM, HOPKINS S, VENETTA TM et al.: Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat. Med. (1998) 4(11):1302-1307.
   PubMed Web of Science ®Google Scholar
• BLAU DM, HOLMES K: Human Coronavirus hCoV-229E enters susceptible cells via the endocytic pathway. Adv. Exp. Med. Biol. (2001) 494:193-198.
   PubMed Web of Science ®Google Scholar
• SAVARINO A, BOELAERT JR, CASSONE A et al.: Effects of chloroquine on viral infections: an old drug against today's diseases? Lancet Infect. Dis. (2003) 3(11):722-727.
   PubMed Web of Science ®Google Scholar
• PEIRIS JS, CHU CM, CHENG VC: Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: a prospective study. Lancet (2003) 361(9371):1767-1772.
   Google Scholar
• KEYAERTSE, VIJGEN L, MAES P: In vitro inhibition of severe acute respiratory syndrome coronavirus by chloroquine. Biochem. Biophys. Res. Commun. (2004) 323(1):264-268.
   PubMed Web of Science ®Google Scholar
• VINCENT MJ, BERGERON E, BENJANNET S: Chloroquine is a potent inhibitor of SARS coronavirus infection and spread. Virol. J. (2005) 2(69).
   PubMedGoogle Scholar
• LI BJ, TANG Q, CHENG D et al.: Using siRNA in prophylactic and therapeutic regimens against SARS coronavirus in Rhesus macaque. Nat. Med. (2005) 11(9):944-951.
   Google Scholar
• ZIEBUHR J: The coronavirus replicase. Curr. Top Microbiol. Immunol. (2005) 287:57-94.
   PubMedGoogle Scholar
• SULEA T, LINDNER HA, PURISIMA EO, MENARD R: Binding site-based classification of coronaviral papain-like proteases. Proteins (2006) 62(3):760-775.
   PubMed Web of Science ®Google Scholar
• ZIEBUHR J, SNIJDER EJ, GORBALENYA AE: Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. (2000) 81(4):853-879.
   PubMedGoogle Scholar
• BROCKWAY SM, LU XT, PETERS TR, DERMODY TS, DENISON MR: Intracellular localization and protein interactions of the gene 1 protein p28 during mouse hepatitis virus replication. J. Virol. (2004) 78(21):11551-11562.
   Google Scholar
• PRENTICE E, MCAULIFFE J, LU X, SUBBARAO K, DENISON MR: Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins. J. Virol. (2004) 78(18):9977-9986.
   PubMedGoogle Scholar
• SALONEN A, AHOLA T, KAARIAINEN L: Viral RNA replication in association with cellular membranes. Curr. Top. Microbiol. Immunol. (2005) 285:139-173.
   PubMed Web of Science ®Google Scholar
• ANAND K, ZIEBUHR J, WADHWANI P, MESTERS JR, HILGENFELD R: Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science (2003) 300(5626):1763-1767.
   PubMed Web of Science ®Google Scholar
• SHI J, WEI Z, SONG J: Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors. J. Biol.Chem. (2004) 279(23):24765-24773.
   Google Scholar
• SHAN YF, LI SF, XU GJ: A novel auto-cleavage assay for studying mutational effects of the active site of severe acute respiratory syndrome coronavirus 3C-like protease. Biochem. Biophys. Res. Commun. (2004) 324(2):579-583.
   PubMedGoogle Scholar
• CHENG VC, TONG BS, WU AK, CHU CM, YUEN KY: Medical treatment of viral pneumonia including SARS in immunocompetent adult. J. Infect. (2004) 49(4):262-273.
   PubMed Web of Science ®Google Scholar
• CHAN KS, LAI ST, CHU CM: Treatment of severe acute respiratory syndrome with lopinavir/ritonavir: a multicentre retrospective matched cohort study. Med. J. (2003) 9(6):399-406.
   Web of Science ®Google Scholar
• CHU CM, CHENG V, HUNG IF et al.: Role of lopinavir/ritonavir in the treatment of SARS: initial virological and clinical findings. Thorax (2004) 59(3):252-256.
   Google Scholar
• YAMAMOTO N, YANG R, YOSHINAKA Y, AMARI S, NAKANO T, CINATL J: HIV protease inhibitor nelfinavir inhibits replication of SARS-associated coronavirus. Biochem. biophys. res. commun. (2004) 318(3):719-725.
   PubMed Web of Science ®Google Scholar
• CHEN F, CHAN K H, JIANG Y, KAO R, LU H, FAN K: In vitro susceptibility of 10 clinical isolates of SARS coronavirus to selected antiviral compounds. J. Clin. Virol. (2004) 31(1):69-75.
   PubMed Web of Science ®Google Scholar
• STROHER SU, DICARO A, LI Y, STRONG J, AOKI F, PLUMMER F: Severe acute respiratory syndrome-related coronavirus is inhibited by IFN-α. J. Infect. Dis. (2004) 189(7):1164-1167.
   PubMed Web of Science ®Google Scholar
• SAVARINO A: Expanding the frontiers of existing antiviral drugs: possible effects of HIV-1 protease inhibitors against SARS and avian influenza. J. Clin. Virol. (2005) 34(3):170-178.
   PubMed Web of Science ®Google Scholar
• JENWITHEESUK E, SAMUDRALA R: Identifying inhibitors of the SARS coronavirus proteinase. Bioorg. Med. Chem. Lett. (2003) 13(22):3989-3992.
   PubMedGoogle Scholar
• ZHANG XW, YAP YL: Old drugs as lead compounds for a new disease? Binding analysis of SARS coronavirus main proteinase with HIV, psychotic and parasite drugs. Bioorg. Med. Chem. (2004) 12(10):2517-2521.
   PubMed Web of Science ®Google Scholar
• CIGLER P, KOZISEK M, REZACOVA P: From nonpeptide toward noncarbon protease inhibitors: metallacarboranes as specific and potent inhibitors of HIV protease. Proc. Natl. Acad. Sci. USA (2005) 102(43):15394-15399.
   PubMed Web of Science ®Google Scholar
• RAWLINGS ND, TOLLE DP, BARRETT AJ, MEROP S: The peptidase database. Nucleic Acids Res. (2004) 32(Database issue):D160-D164.
   PubMed Web of Science ®Google Scholar
• THIEL V, IVANOV KA, PUTICS A et al.: Mechanisms and enzymes involved in SARS coronavirus genome expression. J. Gen. Virol. (2003) 84(9):2305-2315.
   PubMed Web of Science ®Google Scholar
• RATIA K, SAIKATENDU KS, SANTARSIERO BD et al.: Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme. Proc. Natl. Acad. Sci. USA (2006) 103(15):5717-5722.
   PubMed Web of Science ®Google Scholar
• SNIJDER EJ, BREDENBEEK PJ, DOBBE JC: Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. (2003) 331(5):991-1004.
   PubMed Web of Science ®Google Scholar
• LINDNER HA, FOTOUHI-ARDAKANI N, LYTVYN V, LACHANCE P, SULEA T, MENARD R: The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J. Virol. (2005) 79(24):15199-15208.
   PubMed Web of Science ®Google Scholar
• HAN YS, CHANG GG, JUOCJ et al.: Papain-like protease(s) (PLpro) – Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition. Biochemistry. (2005) 44:10349-10359.
   PubMed Web of Science ®Google Scholar
• ZIEBUHR J: Molecular biology of severe acute respiratory syndrome coronavirus. Curr. Opin. Microbiol. (2004) 7(4):412-419.
   PubMed Web of Science ®Google Scholar
• XU X, LIU Y, WEISS S, ARNOLD E, SARAFIANOS SG, DING J: Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design. Nucleic Acids Res. (2003) 31(24):7117-7130.
   PubMed Web of Science ®Google Scholar
• TANNER JA, WATT RM, CHAI YB: The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases. J. Biol. Chem. (2003) 278(41):39578-39582.
   PubMed Web of Science ®Google Scholar
• TANNER JA, ZHENG BJ, ZHOU J et al.: The adamantane-derived bananins are potent inhibitors of the helicase activities and replication of SARS coronavirus. Chem. Biol. (2005) 12(3):303-311.
   PubMedGoogle Scholar
• CHANG W, JIA J, CHI C et al.: Inhibition of severe acute respiratory syndrome coronavirus replication by niclosamide. Antimicrob. Agents Chemother. (2004) 48(7):2693-2696.
   PubMed Web of Science ®Google Scholar