Chalcones isolated from Angelica keiskei inhibit cysteine proteases of SARS-CoV

References

• Peiris JS, Guan Y, Yuen KY. Severe acute respiratory syndrome. Nat Med 2004;10:S88–97
   PubMed Web of Science ®Google Scholar
• Stadler K, Masignani V, Eickmann M, et al. SARS – beginning to understand a new virus. Nat Rev Microbiol 2003;1:209–18
   PubMed Web of Science ®Google Scholar
• Chou K-C, Wei D-Q, Zhong W-Z. Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS. Biochem Biophys Res Commun 2003;308:148–51
   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;84:2305–15
   PubMed Web of Science ®Google Scholar
• Ghosh AK, Xi K, Johnson ME, et al. Progress in anti-SARS coronavirus chemistry, biology and chemotherapy. Annu Rep Med Chem 2006;41:183–96
   Web of Science ®Google Scholar
• Harcourt BH, Jukneliene D, Kanjanahaluethai A, et al. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J Virol 2004;78:13600–12
   PubMed Web of Science ®Google Scholar
• Anand K, Ziebuhr J, Wadhwani P, et al. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 2003;300:1763–7
   PubMed Web of Science ®Google Scholar
• Fear G, Komarnytsky S, Raskin I. Protease inhibitors and their peptidomimetic derivatives as potential drugs. Pharmacol Ther 2007;113:354–68
   PubMed Web of Science ®Google Scholar
• Park J-Y, Jeong HJ, Kim JH, et al. Diarylheptanoids from Alnus japonica inhibit papain-like protease of severe acute respiratory syndrome coronavirus. Biol Pharm Bull 2012;35:2036–42
   PubMed Web of Science ®Google Scholar
• Park J-Y, Kim JH, Kim YM, et al. Tanshinones as selective and slow-binding inhibitors for SARS-CoV cysteine proteases. Bioorg Med Chem 2012;20:5928–35
   PubMed Web of Science ®Google Scholar
• Kim DW, Seo KH, Curtis-Long MJ, et al. Phenolic phytochemical displaying SARS-CoV papain-like protease inhibition from the seeds of Psoralea corylifolia. J Enzyme Inhib Med Chem 2014;29:59–63
   PubMed Web of Science ®Google Scholar
• Song SH, Kim DW, Curtis-Long MJ, et al. Papain-like protease (PLpro) inhibitory effects of cinnamic amides from Tribulus terrestris fruits. Biol Pharm Bull 2014;37:1021–8
   PubMed Web of Science ®Google Scholar
• Baba K, Nakata K, Taniguchi M, et al. Chalcones from Angelica keiskei. Phytochemistry 1990;29:3907–10
   Web of Science ®Google Scholar
• Akihisa T, Tokuda H, Ukiya M, et al. Chalcones, coumarins, and flavanones from the exudate of Angelica keiskei and their chemopreventive effects. Cancer Lett 2003;201:133–7
   PubMed Web of Science ®Google Scholar
• Akihisa T, Tokuda H, Hasegawa D, et al. Chalcones and other compounds from the exudates of Angelica keiskei and their cancer chemopreventive effects. J Nat Prod 2006;69:38–42
   PubMed Web of Science ®Google Scholar
• Nishimura R, Tabata K, Arakawa M, et al. Isobavachalcone, a chalcone constituent of Angelica keiskei, induces apoptosis in neuroblastoma. Biol Pharm Bull 2007;30:1878–83
   PubMed Web of Science ®Google Scholar
• Enoki T, Ohnogi H, Nagamine K, et al. Antidiabetic activities of chalcones isolated from a Japanese herb, Angelica keieskei. J Agric Food Chem 2007;55:6013–17
   PubMed Web of Science ®Google Scholar
• Shimizu E, Hayashi A, Takahashi R, et al. Effects of angiotensin I-converting enzyme inhibitor from Ashitaba (Angelica keiskei) on blood pressure of spontaneously hypertensive rats. J Nutr Sci Vitaminol 1999;45:375–83
   PubMed Web of Science ®Google Scholar
• Park J-Y, Jeong HJ, Kim YM, et al. Characteristic of alkylated chalcones from Angelica keiskei on influenza virus neuraminidase inhibition. Bioorg Med Chem Lett 2011;21:5602–4
   PubMed Web of Science ®Google Scholar
• Sun H, Luo H, Yu C, et al. Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus. Protein Expr Purif 2003;32:302–8
   PubMed Web of Science ®Google Scholar
• Han YS, Chang GG, Juo CG, et al. Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV)-expression, purification, characterization, and inhibition. Biochemistry 2005;44:349–59
   Google Scholar
• Park J-Y, Kim JH, Kwon JM, et al. Dieckol, SARS-CoV 3CLpro inhibitor, isolated from the edible brown algae Ecklonia cava. Bioorg Med Chem 2013;21:3730–7
   PubMed Web of Science ®Google Scholar
• Lin CW, Tsai CH, Tsai FJ, et al. Characterization of trans- and cis-cleavage activity of the SARS coronavirus 3CLpro protease: basis for the in vitro screening of anti-SARS drugs. FEBS Lett 2004;574:131–7
   PubMed Web of Science ®Google Scholar
• Lin CW, Tsai FJ, Tsai CH, et al. Anti-SARS coronavirus 3C-like protease effects of Isatis indigotica root and plant-derived phenolic compounds. Antiviral Res 2005;68:36–42
   PubMed Web of Science ®Google Scholar
• Ratia K, Pegan S, Takayama J, et al. A noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication. Proc Natl Acad Sci USA 2008;105:16119–24
   PubMed Web of Science ®Google Scholar
• Chou CY, Chien CH, Han YS, et al. Thiopurine analogues inhibit papain-like protease of severe acute respiratory syndrome coronavirus. Biochem Pharmacol 2008;75:1601–9
   PubMed Web of Science ®Google Scholar
• Castillo-Yáñez FJ, Pacheco-Aguilar R, García-Carreño FL, et al. Purification and biochemical characterization of chymotrypsin from the viscera of Monterey sardine (Sardinops sagax caeruleus). Food Chem 2006;99:252–9
   Web of Science ®Google Scholar
• Guisan JM, Blanco RM. Stabilization of trypsin by multiple-point attachment to aldehyde-agarose gels. Ann N Y Acad Sci 1987;501:67–72
   PubMed Web of Science ®Google Scholar
• Morris GM, Goodsell DS, Halliday RS, et al. Automated docking using a Lamarckian genetic algorithm and and empirical binding free energy function. Comput Chem 1998;19:1639–62
   Google Scholar
• Lee CC, Kuo CJ, Ko TP, et al. Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds. J Biol Chem 2009;284:7646–55
   PubMed Web of Science ®Google Scholar
• Ghosh AK, Takayama J, Rao KV, et al. Severe acute respiratory syndrome coronavirus papain-like novel protease inhibitors: design, synthesis, protein-ligand X-ray structure and biological evaluation. J Med Chem 2010;53:4968–79
   PubMed Web of Science ®Google Scholar
• Sanner MF, Olson AJ, Spehner JC. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 1996;38:305–20
   PubMed Web of Science ®Google Scholar
• Barretto N, Jukneliene D, Ratia K, et al. The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J Virol 2005;79:15189–98
   PubMed Web of Science ®Google Scholar
• Lindner HA, Fotouhi-Ardakani N, Lytvyn V, et al. The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J Virol 2005;79:15199–208
   PubMed Web of Science ®Google Scholar