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Volumn 59, Issue 9, 2015, Pages 5814-5818

The enterovirus 3C protease inhibitor SG85 efficiently blocks rhinovirus replication and is not cross-resistant with rupintrivir

Author keywords

[No Author keywords available]

Indexed keywords

3C PROTEASE; AMINO ACID; ANTIVIRUS AGENT; CYTOPROTECTIVE AGENT; PEPTIDOMIMETIC AGENT; PLECONARIL; PROTEINASE; PROTEINASE INHIBITOR; RUPINTRIVIR; SG 85; UNCLASSIFIED DRUG; VIRUS ENZYME; 2 PYRROLIDONE DERIVATIVE; ISOXAZOLE DERIVATIVE; VIRAL PROTEIN;

EID: 84940944425     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00534-15     Document Type: Article
Times cited : (19)

References (22)
  • 2
    • 84919708057 scopus 로고    scopus 로고
    • Classification and evolution of human rhinoviruses
    • Palmenberg A, Gern J. 2015. Classification and evolution of human rhinoviruses. Methods Mol Biol 1221:1-10. http://dx.doi.org/10.1007/978-1-4939-1571-2-1.
    • (2015) Methods Mol Biol , vol.1221 , pp. 1-10
    • Palmenberg, A.1    Gern, J.2
  • 3
    • 0031001399 scopus 로고    scopus 로고
    • Detection of rhinovirus RNA in lower airway cells during experimentally induced infection
    • Gern JE, Galagan DM, Jarjour NN, Dick EC, Busse WW 1997. Detection of rhinovirus RNA in lower airway cells during experimentally induced infection. Am J Respir Crit Care Med 155:1159-1161. http://dx.doi.org/10.1164/ajrccm.155.3.9117003.
    • (1997) Am J Respir Crit Care Med , vol.155 , pp. 1159-1161
    • Gern, J.E.1    Galagan, D.M.2    Jarjour, N.N.3    Dick, E.C.4    Busse, W.W.5
  • 4
    • 84919772736 scopus 로고    scopus 로고
    • How rhinovirus infections cause exacerbations of asthma
    • Gern JE. 2015. How rhinovirus infections cause exacerbations of asthma. Clin Exp Allergy 45:32-42. http://dx.doi.org/10.1111/cea.12428.
    • (2015) Clin Exp Allergy , vol.45 , pp. 32-42
    • Gern, J.E.1
  • 6
    • 83955164248 scopus 로고    scopus 로고
    • Combating enterovirus replication: State-of-The-art on antiviral research
    • Thibaut HJ, De Palma AM, Neyts J. 2012. Combating enterovirus replication: state-of-the-art on antiviral research. Biochem Pharmacol 83: 185-192. http://dx.doi.org/10.1016/j.bcp.2011.08.016.
    • (2012) Biochem Pharmacol , vol.83 , pp. 185-192
    • Thibaut, H.J.1    De Palma, A.M.2    Neyts, J.3
  • 7
    • 12944268369 scopus 로고    scopus 로고
    • Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor
    • Binford SL, Maldonado F, Brothers MA, Weady PT, Zalman LS, Meador JW, III, Matthews DA, Patick AK. 2005. Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor. Antimicrob Agents Chemother 49:619-626. http://dx.doi.org/10.1128/AAC.49.2.619-626.2005.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 619-626
    • Binford, S.L.1    Maldonado, F.2    Brothers, M.A.3    Weady, P.T.4    Zalman, L.S.5    Meador, J.W.6    Matthews, D.A.7    Patick, A.K.8
  • 9
    • 0027500787 scopus 로고
    • Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5'-noncoding region of the viral RNA. Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities
    • Leong LE, Walker PA, Porter AG 1993. Human rhinovirus-14 protease 3C (3Cpro) binds specifically to the 5'-noncoding region of the viral RNA. Evidence that 3Cpro has different domains for the RNA binding and proteolytic activities. J Biol Chem 268:25735-25739.
    • (1993) J Biol Chem , vol.268 , pp. 25735-25739
    • Leong, L.E.1    Walker, P.A.2    Porter, A.G.3
  • 10
    • 84881340606 scopus 로고    scopus 로고
    • Rhinovirus 3C protease facilitates specific nucleoporin cleavage and mislocalisation of nuclear proteins in infected host cells
    • Walker EJ, Younessi P, Fulcher AJ, McCuaig R, Thomas BJ, Bardin PG, Jans DA, Ghildyal R. 2013. Rhinovirus 3C protease facilitates specific nucleoporin cleavage and mislocalisation of nuclear proteins in infected host cells. PLoS One 8:e71316. http://dx.doi.org/10.1371/journal.pone.0071316.
    • (2013) PLoS One , vol.8
    • Walker, E.J.1    Younessi, P.2    Fulcher, A.J.3    McCuaig, R.4    Thomas, B.J.5    Bardin, P.G.6    Jans, D.A.7    Ghildyal, R.8
  • 11
    • 0029086385 scopus 로고
    • The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
    • Malcolm BA. 1995. The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds. Protein Sci 4:1439-1445. http://dx.doi.org/10.1002/pro.5560040801.
    • (1995) Protein Sci , vol.4 , pp. 1439-1445
    • Malcolm, B.A.1
  • 13
    • 0033535579 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics
    • Dragovich PS, Prins TJ, Zhou R, Fuhrman SA, Patick AK, Matthews DA, Ford CE, Meador JW, III, Ferre RA, Worland ST. 1999. Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics. J Med Chem 42:1203-1212.
    • (1999) J Med Chem , vol.42 , pp. 1203-1212
    • Dragovich, P.S.1    Prins, T.J.2    Zhou, R.3    Fuhrman, S.A.4    Patick, A.K.5    Matthews, D.A.6    Ford, C.E.7    Meador, J.W.8    Ferre, R.A.9    Worland, S.T.10
  • 16
    • 0344012008 scopus 로고    scopus 로고
    • Phase II, randomized, double-blind, placebo-controlled studies of ruprintrivir nasal spray 2-percent suspension for prevention and treatment of experimentally induced rhinovirus colds in healthy volunteers
    • Hayden FG, Turner RB, Gwaltney JM, Chi-Burris K, Gersten M, Hsyu P, Patick AK, Smith GJ, III, Zalman LS. 2003. Phase II, randomized, double-blind, placebo-controlled studies of ruprintrivir nasal spray 2-percent suspension for prevention and treatment of experimentally induced rhinovirus colds in healthy volunteers. Antimicrob Agents Chemother 47:3907-3916. http://dx.doi.org/10.1128/AAC.47.12.3907-3916.2003.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3907-3916
    • Hayden, F.G.1    Turner, R.B.2    Gwaltney, J.M.3    Chi-Burris, K.4    Gersten, M.5    Hsyu, P.6    Patick, A.K.7    Smith, G.J.8    Zalman, L.S.9
  • 18
    • 84875769296 scopus 로고    scopus 로고
    • 3C protease of enterovirus 68: Structure-based design of michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses
    • Tan J, George S, Kusov Y, Perbandt M, Anemuller S, Mesters JR, Norder H, Coutard B, Lacroix C, Leyssen P, Neyts J, Hilgenfeld R. 2013. 3C protease of enterovirus 68: structure-based design of Michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses. J Virol 87:4339-4351. http://dx.doi.org/10.1128/JVI.01123-12.
    • (2013) J Virol , vol.87 , pp. 4339-4351
    • Tan, J.1    George, S.2    Kusov, Y.3    Perbandt, M.4    Anemuller, S.5    Mesters, J.R.6    Norder, H.7    Coutard, B.8    Lacroix, C.9    Leyssen, P.10    Neyts, J.11    Hilgenfeld, R.12
  • 19
    • 84908628085 scopus 로고    scopus 로고
    • The capsid binder vapendavir and novel protease inhibitor SG85 inhibit enterovirus 71 replication
    • Tijsma A, Franco D, Tucker S, Hilgenfeld R, Froeyen M, Leyssen P, Neyts J. 2014. The capsid binder vapendavir and novel protease inhibitor SG85 inhibit enterovirus 71 replication. Antimicrob Agents Chemother 58:6990-6992. http://dx.doi.org/10.1128/AAC.03328-14.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 6990-6992
    • Tijsma, A.1    Franco, D.2    Tucker, S.3    Hilgenfeld, R.4    Froeyen, M.5    Leyssen, P.6    Neyts, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.