參考文獻 |
1. Wu, Y. C., et al. (2020). “The outbreak of COVID-19: An overview.” Journal of the Chinese Medical Association, 83(3): 217-220.
2. Tyrrell, D. A. and M. L. Bynoe (1961). “Some further virus isolations from common colds.” British Medical Journal, 1(5223): 393-397.
3. Kahn, J. S., & McIntosh, K. (2005). “History and recent advances in coronavirus discovery.” The Pediatric infectious disease journal, 24(11 Suppl): S223–S226.
4. Peiris, J. S., et al. (2003). “Coronavirus as a possible cause of severe acute respiratory syndrome.” The Lancet, 361(9366): 1319-1325.
5. Drosten, C., et al. (2003). “Identification of a novel coronavirus in patients with severe acute respiratory syndrome.” The New England Journal of Medicine, 348(20): 1967-1976.
6. Lang, J., et al. (2011). “Inhibition of SARS Pseudovirus Cell Entry by Lactoferrin Binding to Heparan Sulfate Proteoglycans.” Public Library of Science, 6(8): e23710.
7. Irving, A. T., et al. (2021). “Lessons from the host defences of bats, a unique viral reservoir.” Nature, 589(7842): 363-370.
8. van den Brand, J. M., et al. (2015). “Pathogenesis of Middle East respiratory syndrome coronavirus.” The Journal of Pathology, 235(2): 175-184.
9. Li, Y., et al. (2020). “The MERS-CoV Receptor DPP4 as a Candidate Binding Target of the SARS-CoV-2 Spike.” iScience: Cell Press, 23(6): 101160.
10. Sheahan, T., et al. (2008). “Mechanisms of zoonotic severe acute respiratory syndrome coronavirus host range expansion in human airway epithelium.” Journal of Virology, 82(5): 2274-2285.
11. Rossi, G. A., et al. (2020). “Differences and similarities between SARS-CoV and SARS-CoV-2: spike receptor-binding domain recognition and host cell infection with support of cellular serine proteases.” Infection 48(5): 665-669.
12. Kavsan, V. M., et al. (2011). “Immortalized cells and one oncogene in malignant transformation: old insights on new explanation.” BMC Molecular and Cell Biology, 12: 23.
13. Gorbalenya, A. E., et al. (2006). “Nidovirales: evolving the largest RNA virus genome.” Virus Research 117(1): 17-37.
14. Payne S. (2017). “Family Coronaviridae.” Viruses, 149–158.
15. Seah, I., et al. (2020). “Revisiting the dangers of the coronavirus in the ophthalmology practice.” Eye, 34(7): 1155-1157.
16. Mousavizadeh, L. and S. Ghasemi (2021). “Genotype and phenotype of COVID-19: Their roles in pathogenesis.” Journal of Microbiology, Immunology and Infection, 54(2): 159-163.
17. Bassendine, M. F., et al. (2020). “COVID-19 and comorbidities: A role for dipeptidyl peptidase 4 (DPP4) in disease severity?.” Journal of diabetes, 12(9), 649–658.
18. Scheen, A. J. (2021). “DPP-4 inhibition and COVID-19: From initial concerns to recent expectations.” Diabetes & Metabolism Journal, 47(2): 101213.
19. Hikmet, F., et al. (2020). “The protein expression profile of ACE2 in human tissues.” Molecular systems biology, 16(7): e9610.
20. Tikellis, C., and Thomas, M. C. (2012). “Angiotensin-Converting Enzyme 2 (ACE2) Is a Key Modulator of the Renin Angiotensin System in Health and Disease.” International journal of peptides, 2012: 256-294.
21. Samavati, L. and Uhal B.D. (2020). “ACE2, Much More Than Just a Receptor for SARS-COV-2.” Frontiers in Cellular and Infection Microbiology, 10: 317.
22. Hoffmann, M., et al. (2020). “A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells.” Molecular Cell: Cell Press, 78(4): 779-784.e5.
23. Wrapp, D., et al. (2020). “Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation.” Science (New York, N.Y.): 367(6483), 1260–1263.
24. Peacock, T. P., et al. (2021). “The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets.” Nature Microbiology, 6(7): 899-909.
25. Wrobel, A. G., et al. (2020). “SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.” Nature Structural and Molecular Biology, 27(8): 763-767.
26. Johnson, B. A., et al. (2021). “Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis.” Nature, 591(7849): 293–299.
27. Chan, Y. A., and Zhan, S. H. (2022). “The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2.” Molecular Biology and Evolution, 39(1): msab327.
28. Lan, J., et al. (2020). “Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.” Nature, 581(7807): 215–220.
29. Wang, Q., et al. (2020). “Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2.” Cell, 181(4): 894–904.e9.
30. Berger, I. and Schaffitzel, C. (2020). “The SARS-CoV-2 spike protein: balancing stability and infectivity.” Cell Research, 30(12): 1059-1060.
31. Shang, J., et al. (2020). “Cell entry mechanisms of SARS-CoV-2.” Proceedings of the National Academy of Sciences of the United States of America, 117(21): 11727–11734.
32. Rossi, Á. D., et al. (2021). “Association between ACE2 and TMPRSS2 nasopharyngeal expression and COVID-19 respiratory distress.” Scientific reports, 11(1): 9658.
33. Hoffmann, M., et al. (2020). “A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells.” Molecular cell, 78(4): 779–784.e5.
34. Mollica, V., et al. (2020). “The pivotal role of TMPRSS2 in coronavirus disease 2019 and prostate cancer.” Future oncology (London, England), 16(27): 2029–2033.
35. Heurich, A., et al. (2014). “TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein.” Journal of virology, 88(2): 1293–1307.
36. Brest, P., et al. (2020). “Host Polymorphisms May Impact SARS-CoV-2 Infectivity.” Trends in genetics : TIG, 36(11): 813–815.
37. Makowski, L., et al. (2021). “Biological and Clinical Consequences of Integrin Binding via a Rogue RGD Motif in the SARS CoV-2 Spike Protein.” Viruses, 13(2): 146.
38. Yan, S., et al. (2020). “New Strategy for COVID-19: An Evolutionary Role for RGD Motif in SARS-CoV-2 and Potential Inhibitors for Virus Infection.” Frontiers in pharmacology, 11: 912.
39. Carvacho, I., and Piesche, M. (2021). “RGD-binding integrins and TGF-β in SARS-CoV-2 infections - novel targets to treat COVID-19 patients?.” Clinical & Translational Immunology, 10(3): e1240.
40. Stupack, D. G. (2005). “Integrins as a distinct subtype of dependence receptors.” Cell death and Differentiation, 12(8): 1021–1030.
41. Hussein, H. A., et al. (2015). “Beyond RGD: virus interactions with integrins.” Archives of virology, 160(11): 2669–2681.
42. Shi, G., et al. (2021). “Opposing activities of IFITM proteins in SARS-CoV-2 infection.” The European Molecular Biology Organization journal, 40(3): e106501.
43. Krishnamoorthy, S., et al. (2020). “SARS-CoV, MERS-CoV, and 2019-nCoV viruses: an overview of origin, evolution, and genetic variations.” Indian Journal of Virology: Virusdisease, 31(4): 411–423.
44. Harrison, A. G., Lin, T., and Wang, P. (2020). “Mechanisms of SARS-CoV-2 Transmission and Pathogenesis.” Trends in immunology, 41(12), 1100–1115.
45. Wu, A., et al. (2020). “Genome Composition and Divergence of the Novel Coronavirus (2019-nCoV) Originating in China.” Cell host and microbe, 27(3): 325-328.
46. Huang, Y., et al. (2020). “Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19.” Acta Pharmacologica Sinica, 41(9): 1141–1149.
47. Rahbar Saadat, Y., et al. (2021). “Host Serine Proteases: A Potential Targeted Therapy for COVID-19 and Influenza.” Frontiers in molecular biosciences, 8: 725528.
48. 楊美珠. (2018). 茶葉兒茶素之代謝機制與生物活性. 國立臺灣大學園藝暨景觀學系博士論文. 台北市. 取自https://hdl.handle.net/11296/t6jx5p.
49. Cho, J.Y., et al. (2007). “Chemical Profiling and Gene Expression Profiling during the Manufacturing Process of Taiwan Oolong Tea Oriental Beauty.” Bioscience, Biotechnology, and Biochemistry, 71(6):1476-1486.
50. Mori, H., et al. (1995). “Potent Aroma Components of Rhizomes from Alpinia galanga Willd. L.” Journal of the Japanese Society for Food Science and Technology (Nippon Shokuhin Kagaku Kogaku Kaishi), 42(12): 989-995.
51. 津志田, 藤., et al. (1987). “γ‐アミノ酪酸を畜積させた茶の製造とその特徴.” 日本農芸化学会誌 61(7): 817-822.
52. Chacko, S. M., et al. (2010). “Beneficial effects of green tea: a literature review.”Chinese medicine, 5:13.
53. Harbowy, M. and D. Balentine (1997). “Tea Chemistry.” Critical Reviews in Plant Sciences, 16: 415-480.
54. 物部美 (2017). “Control of functional ingredients in tea (Camellia sinensis)” 第四屆茶業科技研討會. 桃園市. 取自https :// www. tres.gov.tw/theme_data. php?theme= news&sub_theme= hot&id= 2678.
55. Pohanka M. (2015). “The perspective of caffeine and caffeine derived compounds in therapy.” Bratislava Medical Journal (Bratislavske lekarske listy): AEPress, 116(9): 520-530.
56. Takemoto, M., and Takemoto, H. (2018). “Synthesis of Theaflavins and Their Functions.” Molecules (Basel, Switzerland), 23(4): 918.
57. Kuhnert, N. (2010). “Unraveling the structure of the black tea thearubigins.” Archives of Biochemistry and Biophysics, 501(1): 37-51.
58. Menet M. C., et al. (2004). “Analysis of Theaflavins and Thearubigins from Black Tea Extract by MALDI-TOF Mass Spectrometry.” Journal of Agricultural and Food Chemistry 52(9): 2455-2461.
59. RiceEvans C. (1999). “Implications of the mechanisms of action of tea polyphenols as antioxidants in vitro for chemoprevention in humans.” Proceedings of the Society for Experimental Biology and Medicine, 220(4):262-6.
60. .Legeay, S., et al. (2015). “Epigallocatechin Gallate: A Review of Its Beneficial Properties to Prevent Metabolic Syndrome.” Nutrients, 7(7):5443-68.
61. Liu L., et al. (2017) “Epigallocatechin-3-gallate suppresses cell proliferation and promotes apoptosis in Ec9706 and Eca109 esophageal carcinoma cells.” Oncology Letters, 14(4):4391-4395.
62. Wang R.L., et al. (2022) “Skin reactions to mRNA-1273 SARS-CoV-2 vaccine.” Quarterly Journal of Medicine, hcac008.
63. Shih L.J., et al. (2016) “Green tea (-)-epigallocatechin gallate inhibits the growth of human villous trophoblasts via the ERK, p38, AMP-activated protein kinase, and protein kinase B pathways.” American Journal of Physiology-Cell Physiology, 311(2):C308-21.
64. 陳雯婷. (2021). 綠茶表沒食子兒茶素沒食子酸酯經由MicroRNA-let-7a/HMGA2訊息路徑抑制米色前脂肪細胞的生長. 國立中央大學生命科學系碩士論文. 桃園市. 取自https://hdl.handle.net/11296/hu26hs.
65. Ortsäter H., et al. (2012). “Diet supplementation with green tea extract epigallocatechin gallate prevents progression to glucose intolerance in db/db mice.” Nutrition and Metabolism, 9:11.
66. Ahmad R.S., et al. (2015). “Preventive role of green tea catechins from obesity and related disorders especially hypercholesterolemia and hyperglycemia.” Journal of Translational Medicine, 13:79.
67. Potenza M.A., et al. (2007). “EGCG, a green tea polyphenol, improves endothelial function and insulin sensitivity, reduces blood pressure, and protects against myocardial I/R injury in SHR.” American Journal of Physiology-Endocrinology and Metabolism, 292(5):E1378-E1387.
68. Williamson G., et al. (2011). “Flavanols from green tea and phenolic acids from coffee: critical quantitative evaluation of the pharmacokinetic data in humans after consumption of single doses of beverages.” Molecular Nutrition and Food Research, 55(6):864-873.
69. Manach C., et al. (2005). “Bioavailability and bioefficacy of polyphenols in humans. I. Review of 97 bioavailability studies.” The American Journal of Clinical Nutrition, 81(1 Suppl):230S-242S.
70. Chu K.O., et al. (2006). “Pharmacokinetic studies of green tea catechins in maternal plasma and fetuses in rats.” Journal of Pharmaceutical Sciences, 95(6):1372-1381.
71. Lin L.C., et al. (2007). “Pharmacokinetics of (-)-epigallocatechin-3-gallate in conscious and freely moving rats and its brain regional distribution.” Journal of Agricultural and Food Chemistry,55(4):1517-1524.
72. Scholey A., et al. (2012). “Acute neurocognitive effects of epigallocatechin gallate (EGCG)” Appetite, 58(2):767-70.
73. Gonçalves P.B., et al. (2012) “Green Tea Epigallocatechin-3-gallate (EGCG) Targeting Protein Misfolding in Drug Discovery for Neurodegenerative Diseases.” Biomolecules,11(5):767.
74. Docea, A. O., et al. (2020). “A new threat from an old enemy: Re‑emergence of coronavirus.” International journal of molecular medicine, 45(6): 1631-1643.
75. Harapan, H., et al. (2020). “Coronavirus disease 2019 (COVID-19): A literature review.” Journal of infection and public health, 13(5): 667-673.
76. Elezkurtaj, S., et al. (2021). “Causes of death and comorbidities in hospitalized patients with COVID-19.” Scientific reports, 11(1): 4263.
77. Jafarzadeh, A., et al. (2021). “Therapeutic potential of ginger against COVID-19: Is there enough evidence?.” Journal of Traditional Chinese Medical Sciences, 8(4): 267-279.
78. Tay, M. Z., et al. (2020). “The trinity of COVID-19: immunity, inflammation and intervention.” Nature reviews Immunology, 20(6): 363-374.
79. Del Valle, D. M., et al. (2020). “An inflammatory cytokine signature predicts COVID-19 severity and survival.” Nature medicine, 26(10): 1636-1643.
80. Liu, J., Cao, et al. (2020). “Hydroxychloroquine, a less toxic derivative of chloroquine, is effective in inhibiting SARS-CoV-2 infection in vitro.” Nature cell discovery, 6, 16.
81. Trivedi, A., et al. (2021). “Prophylactic and therapeutic potential of selected immunomodulatory agents from Ayurveda against coronaviruses amidst the current formidable scenario: an in silico analysis.” Journal of biomolecular structure and dynamics: Advance online publication, 1-53.
82. Dai, W., et al. (2020). “Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease.” Science, 368(6497): 1331-1335.
83. Soni, U., et al. (2022). “Lichen planus drugs re-purposing as potential anti COVID-19 therapeutics through molecular docking and molecular dynamics simulation approach.” Journal of clinical and translational research, 8(2): 127-146.
84. Das, G., et al. (2020). “An overview of key potential therapeutic strategies for combat in the COVID-19 battle.” Royal Society of Chemistry Advances, 10(47): 28243-28266.
85. Pillaiyar, T., et al. (2020). “Recent discovery and development of inhibitors targeting coronaviruses.” Drug discovery today, 25(4): 668-688.
86. Asselah, T., et al. (2021). “COVID-19: Discovery, diagnostics and drug development.” Journal of hepatology, 74(1): 168-184.
87. Zhou, Y. W., et al. (2021). “Therapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies.” Signal transduction and targeted therapy, 6(1): 317.
88. Li, Y., et al. (2021). “A Comprehensive Review of the Global Efforts on COVID-19 Vaccine Development.” American Chemical Society: central science, 7(4), 512-533.
89. Verma, J., and Subbarao, N. (2021). “A comparative study of human betacoronavirus spike proteins: structure, function and therapeutics.” Archives of virology, 166(3): 697-714.
90. Forni, G., et al (2021). COVID-19 vaccines: where we stand and challenges ahead. Cell death and differentiation, 28(2), 626–639.
91. Matheson, N. J. and P. J. Lehner (2020). “How does SARS-CoV-2 cause COVID-19?” Science (New York, N.Y.), 369(6503): 510-511.
92. Junqueira, C., et al. (2022). “FcγR-mediated SARS-CoV-2 infection of monocytes activates inflammation.” Nature, 606(7914): 576-584.
93. Le Bert, N., et al. (2020). “SARS-CoV-2-specific T cell immunity in cases of COVID-19 and SARS, and uninfected controls.” Nature, 584(7821): 457-462.
94. Reyes, A. Z., et al. (2021). “Anti-inflammatory therapy for COVID-19 infection: the case for colchicine.” Annals of the rheumatic diseases, 80(5): 550-557.
95. Gautret P., et al. (2020). “Natural history of COVID-19 and therapeutic options.” Expert Review of Clinical Immunology, 16(12):1159-1184.
96. Mhatre, S., Srivastava, T., Naik, S., and Patravale, V. (2021). “Antiviral activity of green tea and black tea polyphenols in prophylaxis and treatment of COVID-19: A review.” Phytomedicine : international journal of phytotherapy and phytopharmacology, 85: 153286.
97. Rout, J., Swain, B. C., and Tripathy, U. (2022). “In silico investigation of spice molecules as potent inhibitor of SARS-CoV-2.” Journal of biomolecular structure and dynamics, 40(2): 860-874.
98. Mhatre, S., Naik, S., and Patravale, V. (2021). “A molecular docking study of EGCG and theaflavin digallate with the druggable targets of SARS-CoV-2.” Computers in biology and medicine, 129: 104137.
99. Khan, M.F., et al. (2020). Identification of Dietary Molecules as Therapeutic Agents to Combat COVID-19 Using Molecular Docking Studies.
100. Zhou, P., et al. (2020). “Discovery of a novel coronavirus associated with the recent pneumonia outbreak in humans and its potential bat origin.” bioRxiv, 914952.
101. Wu, C.-Y., et al. (2020). “Potential Simultaneous Inhibitors of Angiotensin-Converting Enzyme 2 and Transmembrane Protease, Serine 2.” Frontiers in Pharmacology, 11.
102. Maiti, S., and Banerjee, A. (2021). “Epigallocatechin gallate and theaflavin gallate interaction in SARS-CoV-2 spike-protein central channel with reference to the hydroxychloroquine interaction: Bioinformatics and molecular docking study.” Drug development research, 82(1): 86-96.
103. Abubakar, M. B., et al. (2021). “Natural Products Modulating Angiotensin Converting Enzyme 2 (ACE2) as Potential COVID-19 Therapies.” Frontiers in Pharmacology, 12.
104. Ngwa, W., et al. (2020). “Potential of Flavonoid-Inspired Phytomedicines against COVID-19.” Molecules (Basel, Switzerland), 25(11): 2707.
105. Vidoni, C., et al. (2022). “Targeting autophagy with natural products to prevent SARS-CoV-2 infection.” Journal of traditional and complementary medicine, 12(1), 55-68.
106. Maiti, S., Banerjee, A., and Kanwar, M. (2022). “Effects of theaflavin-gallate in-silico binding with different proteins of SARS-CoV-2 and host inflammation and vasoregulations referring an experimental rat-lung injury.” Phytomedicine Plus : International journal of phytotherapy and phytopharmacology, 2(2): 100237.
107. Zhang, D., et al. (2021). “Identification of natural compounds as SARS-CoV-2 entry inhibitors by molecular docking-based virtual screening with bio-layer interferometry.” Pharmacological research, 172: 105820.
108. Zhang, Z., et al. (2021). “Potential protective mechanisms of green tea polyphenol EGCG against COVID-19.” Trends in food science and technology, 114: 11-24.
109. Joseph, J., et al. (2021). “Epigallocatechin-3-gallate (EGCG): a potential molecule for the development of therapeutics against emerging SARS-CoV-1, MERS-CoV and SARS-CoV-2 coronaviruses.” Journal of global antimicrobial resistance, 26: 26-28.
110. Park, J., et al. (2021). “Therapeutic Potential of EGCG, a Green Tea Polyphenol, for Treatment of Coronavirus Diseases.” Life (Basel, Switzerland), 11(3): 197.
111. Henss, L., et al. (2021). “The green tea catechin epigallocatechin gallate inhibits SARS-CoV-2 infection.” The Journal of general virology, 102(4): 1574.
112. Ohgitani, E., et al. (2021). “Significant Inactivation of SARS-CoV-2 In Vitro by a Green Tea Catechin, a Catechin-Derivative, and Black Tea Galloylated Theaflavins.” Molecules (Basel, Switzerland), 26(12): 3572.
113. Ohgitani, E., et al. (2021). “Rapid Inactivation In Vitro of SARS-CoV-2 in Saliva by Black Tea and Green Tea.” Pathogens (Basel, Switzerland), 10(6): 721.
114. Wang, X., et al. (2022). “Polygoni multiflori radix extracts inhibit SARS-CoV-2 pseudovirus entry in HEK293T cells and zebrafish larvae.” Phytomedicine : international journal of phytotherapy and phytopharmacology, 102: 154154.
115. Xu, Z., Liu, K., & Gao, G. F. (2022). “Omicron variant of SARS-CoV-2 imposes a new challenge for the global public health.” Biosafety and health, 4(3): 147-149.
116. Yang, T. J., et al. (2021). “D614G mutation in the SARS-CoV-2 spike protein enhances viral fitness by desensitizing it to temperature-dependent denaturation.” The Journal of biological chemistry, 297(4): 101238.
117. Gobeil, S. M., et al. (2021). “D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction.” Cell reports, 34(2): 108630.
118. Zhang, J., et al. (2021). “Structural impact on SARS-CoV-2 spike protein by D614G substitution.” Science (New York, N.Y.), 372(6541): 525-530.
119. Komurcu SZM, et al. (2022). “The evaluation of potential global impact of the N501Y mutation in SARS-COV-2 positive patients.” Journal of Medical Virology, 94(3):1009-1019.
120. Cai, Y., et al. (2021). “Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.” Science (New York, N.Y.), 373(6555): 642-648.
121. Chen, C., et al. (2021). “Computational prediction of the effect of amino acid changes on the binding affinity between SARS-CoV-2 spike RBD and human ACE2.” Proceedings of the National Academy of Sciences of the United States of America, 118(42): e2106480118.
122. Negi, S. S., Schein, C. H., and Braun, W. (2022). “Regional and temporal coordinated mutation patterns in SARS-CoV-2 spike protein revealed by a clustering and network analysis.” Scientific reports, 12(1): 1128.
123. Turoňová, B., et al. (2020). “In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges.” Science (New York, N.Y.), 370(6513), 203-208.
124. Toovey, O., et al. (2021). “Introduction of Brazilian SARS-CoV-2 484K.V2 related variants into the UK.” The Journal of infection, 82(5), e23-e24.
125. Yang, Y., and Du, L. (2021). “SARS-CoV-2 spike protein: a key target for eliciting persistent neutralizing antibodies.” Signal transduction and targeted therapy, 6(1): 95.
126. Tai, W., Zhang, et al. (2020). “Identification of SARS-CoV RBD-targeting monoclonal antibodies with cross-reactive or neutralizing activity against SARS-CoV-2.” Antiviral research, 179: 104820.
127. Vega-Magaña N, et al. (2021). “RT-qPCR Assays for Rapid Detection of the N501Y, 69-70del, K417N, and E484K SARS-CoV-2 Mutations: A Screening Strategy to Identify Variants With Clinical Impact.” Frontiers in Cellular and Infection Microbiology, 11:672562.
128. Mittal, A., Khattri, A., and Verma, V. (2022). “Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants.” PLoS pathogens, 18(2): e1010260.
129. Kannan, S. R., et al. (2021). “Evolutionary analysis of the Delta and Delta Plus variants of the SARS-CoV-2 viruses.” Journal of autoimmunity, 124: 102715.
130. Focosi D, et al. (2021). “Emergence of SARS-COV-2 Spike Protein Escape Mutation Q493R after Treatment for COVID-19.” Emerging Infectious Diseases, 27(10):2728-2731.
131. Hodcroft EB, et al. (2020). “Emergence and spread of a SARS-CoV-2 variant through Europe in the summer of 2020.” MedRxiv preprint, 2020.10.25.20219063.
132. Han, P., et al. (2022). “Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.” Cell, 185(4): 630–640.e10.
133. Heggestad, J. T., et al. (2021). “Rapid test to assess the escape of SARS-CoV-2 variants of concern.” Science advances, 7(49): eabl7682.
134. Wu, L., et al. (2022).”SARS-CoV-2 Omicron RBD shows weaker binding affinity than the currently dominant Delta variant to human ACE2.” Signal transduction and targeted therapy, 7(1): 8.
135. Hu, J., et al. (2022). “Increased immune escape of the new SARS-CoV-2 variant of concern Omicron.” Cellular and molecular immunology, 19(2), 293-295.
136. VanBlargan, L., et al. (2021). “An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies.” Research square, rs.3: rs-1175516.
137. Ye, G., Liu, B., and Li, F. (2022). “Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain.” Nature communications, 13(1): 1214.
138. Mannar, D., et al. (2022). “SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex.” Science (New York, N.Y.), 375(6582): 760–764.
139. Su, S. C., et al. (2021). “Structure-guided antibody cocktail for prevention and treatment of COVID-19.” PLoS pathogens, 17(10), e1009704.
140. Zhou, T., et al. (2022). “Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.” Science (New York, N.Y.), 376(6591): eabn8897.
141. Tai, W., et al. (2020). “Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.” Cellular and molecular immunology, 17(6): 613-620.
142. Walls, A. C., et al. (2020). “Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.” Cell, 181(2), 281-292.e6.
143. McCallum, M., et al. (2022). “Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement.” Science (New York, N.Y.), 375(6583): 864-868.
144. Tsai, R.T. and Steven R.J. (2010). Chinese-English Tea Studies Terminology. Lu-Yu Tea Culture Institute Publications Department; Taiwan.
145. Skoog, D.A., et al. (2016). Principles of Instrumental Analysis. Cengage learning seventh edition; United States.
146. Quinn, H. M. (2014). “A Reconciliation of Packed Column Permeability Data: Column Permeability as a Function of Particle Porosity.” Journal of Materials, 2014: 636507.
147. Zhu B.Y., Mant C.T., and Hodges R.S. (1991). “Hydrophilic-interaction chromatography of peptides on hydrophilic and strong cation-exchange columns.” Journal of Chromatography A, 548(1-2):13-24.
148. 林瑋德:胺機酸分析經驗.(2011).取自https:// cmurdc. cmu. edu. tw / epaper/detail.php?epaperno=16&class=C&id=121
149. Horie H., and Kohata K. (2000). “Analysis of tea components by high-performance liquid chromatography and high-performance capillary electrophoresis.” Journal of Chromatography A, 881(1-2): 425-438.
150. Singleton, V. L., et al. (1999). “[14] Analysis of total phenols and other oxidation substrates and antioxidants by means of folin-ciocalteu reagent.” Methods in Enzymology, Academic Press, 299: 152-178.
151. Everette JD, et al. (2010). “Thorough study of reactivity of various compound classes toward the Folin-Ciocalteu reagent.” Journal of Agricultural and Food Chemistry, 58(14):8139-8144.
152. Obuchowicz, J., et al. (2011). “Flavanol database for green and black teas utilising ISO 14502-1 and ISO 14502-2 as analytical tools.” Journal of Food Composition and Analysis 24(3): 411-417.
153. Nguyen, T. H. and A. L. Waterhouse (2021). “Redox Cycling of Iron: Effects of Chemical Composition on Reaction Rates with Phenols and Oxygen in Model Wine.” American Journal of Enology and Viticulture: ajev, 2021.20024.
154. Wilson, H. (2007). “Analysis of the current research into the chemistry of Iron Gall Ink and its implications for Paper Conservation.” Master of Chemistry, doi:10.13140/2.1.4803.2000
155. Hynes, M. J., and Coinceanainn, M. O. (2001). “The kinetics and mechanisms of the reaction of iron(III) with gallic acid, gallic acid methyl ester and catechin.” Journal of inorganic biochemistry, 85(2-3): 131-142.
156. Gary, L.M., et al. (2013). Inorganic Chemistry; Person fifth edition; International edition.
157. Tajbakhsh, M., et al. (2017). “Reusable and efficient polyvinylpolypyrrolidone-supported triflic acid catalyst for acylation of alcohols, phenols, amines, and thiols under solvent-free conditions.” Monatshefte für Chemie - Chemical Monthly , 148(6): 1117-1122.
158. Robinson, A., et al. (2016). “Polyvinylpolypyrrolidone reduces cross-reactions between antibodies and phenolic compounds in an enzyme-linked immunosorbent assay for the detection of ochratoxin A.” Food Chemistry, 214.
159. Mitchell, A. E., et al. (2005). “A Comparison of Polyvinylpolypyrrolidone (PVPP), Silica Xerogel and a Polyvinylpyrrolidone (PVP)-Silica Co-Product for Their Ability to Remove Polyphenols from Beer.” Journal of the Institute of Brewing, 111(1): 20-25.
160. Folch-Cano, C., et al. (2013). “Structural and thermodynamic factors on the adsorption process of phenolic compounds onto polyvinylpolypyrrolidone.” Colloids and Surfaces A: Physicochemical and Engineering Aspects, 418: 105-111.
161. Pitts, L. J., et al. (2014). “A novel ninhydrin reagent for analysing nitrogen-containing compounds.” European patent application; 13193944.9.
162. Takahashi S. (1978). “Sodium borohydride as a reducing agent for preparing ninhydrin reagent for amino acid analysis.” The Journal of Biochemistry, 83(1): 57-60.
163. Lennard, C. (2013). “Forensic sciences: fingerprint techniques.” Encyclopedia of Analytical Science: 414-423.
164. Keeling, C. I., et al. (1999). “ Stable carbon isotope measurements of the carboxyl carbons in bone collagen*.” Archaeometry, 41(1): 151-164.
165. Navarrete D. T., M. A. and F. L. García-Carreño (2003). “Evaluation of the Progress of Protein Hydrolysis.” Current Protocols in Food Analytical Chemistry, 10(1): B2.2.1-B2.2.14.
166. Standara, S., et al. (1999). “Amino acid analysis: Reduction of ninhydrin by sodium borohydride.” Food Nahrung, 43(6): 410-413.
167. Najafpour, G. D., (2007). “CHAPTER 10: Application of Fermentation Processes.” Biochemical Engineering and Biotechnology; p. 252-262.
168. Singh, P., et al. (2021). “Stimulation of Pithecellobium dulce (jungle jalebi) seed with electromagnetic exposure and its impact on biochemical parameter and growth.” Materials Today: Proceedings, 42: 1513-1518.
169. Deshavath, N. N., et al. (2020). “Pitfalls in the 3, 5-dinitrosalicylic acid (DNS) assay for the reducing sugars: Interference of furfural and 5-hydroxymethylfurfural.” International journal of biological macromolecules, 156, 180-185.
170. Miller, G. L. (1959). “Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar.” Analytical Chemistry, 31(3): 426-428.
171. Atomssa, T. and A. Gholap (2011). “Characterization of caffeine and determination of caffeine in tea leaves using UV-visible spectrometer.” African Journal of Pure and Applied Chemistry, 5.
172. Aydin S. (2015). “A short history, principles, and types of ELISA, and our laboratory experience with peptide/protein analyses using ELISA.” Peptides, 72, 4-15.
173. Hendrickson, W. A., et al. (1989). “Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation.” Proceedings of the National Academy of Sciences of the United States of America, 86(7): 2190-2194.
174. Grubmüller, H., et al. (1996). “Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force.” Science (New York, N.Y.), 271(5251): 997-999.
175. Wong, J., et al. (1999). “Direct force measurements of the streptavidin–biotin interaction.” Biomolecular Engineering 16(1): 45-55.
176. Gajhede, M., et al. (1997). “Crystal structure of horseradish peroxidase C at 2.15 Å resolution.” Nature Structural Biology 4(12): 1032-1038.
177. Keller, G., (2008). Managerial Statistics: Chapter 11 Introduction to Hypothesis Testing; Cengage Learning; United States.
178. Narai-Kanayama, A., et al. (2016). “Specificity of tyrosinase-catalyzed synthesis of theaflavins.” Journal of Molecular Catalysis B: Enzymatic, 133: S452-S458.
179. Engelhardt, U. H. (2010). “Chemistry of Tea. Comprehensive Natural Products II.” Oxford, Elsevier: 999-1032.
180. Ghosh, A., et al. (2016). “Chapter 24 - Electronic Tongue for the Estimation of Important Quality Compounds in Finished Tea.” Electronic Noses and Tongues in Food Science, San Diego, Academic Press: 245-253.
181. Ribaudo, G., et al. (2021). “Computational and experimental insights on the interaction of artemisinin, dihydroartemisinin and chloroquine with SARS-CoV-2 spike protein receptor-binding domain (RBD).” Natural product research, 1-6. Advance online publication.
182. Maurya, V. K., et al. (2020). “Therapeutic Development and Drugs for the Treatment of COVID-19.” Coronavirus Disease 2019 (COVID-19): Epidemiology, Pathogenesis, Diagnosis, and Therapeutics, S. K. Saxena. Singapore, Springer Singapore: 109-126.
183. Tateyama-Makino, R., et al. (2021). “The inhibitory effects of toothpaste and mouthwash ingredients on the interaction between the SARS-CoV-2 spike protein and ACE2, and the protease activity of TMPRSS2 in vitro.” PloS one, 16(9): e0257705.
184. Hati, S., and Bhattacharyya, S. (2020). “Impact of Thiol-Disulfide Balance on the Binding of Covid-19 Spike Protein with Angiotensin-Converting Enzyme 2 Receptor.” American Chemical Society Omega, 5(26): 16292–16298.
185. Khanna, K., et al. (2021). “Thiol drugs decrease SARS-CoV-2 lung injury in vivo and disrupt SARS-CoV-2 spike complex binding to ACE2 in vitro.” bioRxiv : the preprint server for biology, 2020.12.08.415505.
186. Fazary, A. E., et al. (2020). “Protonation Equilibria of N-Acetylcysteine.” American Chemical Society Omega, 5(31): 19598-19605.
187. Choudhary, S., et al. (2020). “Identification of SARS-CoV-2 Cell Entry Inhibitors by Drug Repurposing Using in silico Structure-Based Virtual Screening Approach.” Frontiers in immunology, 11: 1664.
188. González, R. G., et al. (1980). “Mechanism of action of polymeric aurintricarboxylic acid, a potent inhibitor of protein--nucleic acid interactions.” Biochemistry, 19(18): 4299-4303.
189. Zhou, P., et al.(2013). “Therapeutic potential of EGCG on acute renal damage in a rat model of obstructive nephropathy.” Molecular Medicine Reports, 7: 1096-1102.
190. Mhatre, S., et al. (2021). “Entry-inhibitory role of catechins against SARS-CoV-2 and its UK variant.” Computers in biology and medicine, 135: 104560.
191. Liu, J., et al. (2021). “Epigallocatechin gallate from green tea effectively blocks infection of SARS-CoV-2 and new variants by inhibiting spike binding to ACE2 receptor.” Cell and bioscience, 11(1): 168.
192. Tsvetkov, V., et al. (2021). “EGCG as an anti-SARS-CoV-2 agent: Preventive versus therapeutic potential against original and mutant virus.” Biochimie, 191, 27-32.
193. Hu, J., et al. (2018). “The safety of green tea and green tea extract consumption in adults - Results of a systematic review.” Regulatory toxicology and pharmacology : RTP, 95: 412-433.
194. Lambert, J., et al. (2009). “Hepatotoxicity of High Oral Dose (-)-Epigallocatechin-3-Gallate in Mice.” Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association, 48: 409-416.
195. Ramachandran, B., et al. (2016). “Repeated dose studies with pure Epigallocatechin-3-gallate demonstrated dose and route dependant hepatotoxicity with associated dyslipidemia.” Toxicology reports, 3: 336-345.
196. Kicker, E., et al. (2022). “SARS-CoV-2 neutralizing activity of polyphenols in a special green tea extract preparation.” Phytomedicine : international journal of phytotherapy and phytopharmacology, advance online publication :98, 153970.
197. LeBlanc, E. V., and Colpitts, C. C. (2022). “The green tea catechin EGCG provides proof-of-concept for a pan-coronavirus attachment inhibitor.” Scientific reports, 12(1): 12899.
198. Yang, C., Huang, Y., and Liu, S. (2021). “Therapeutic Development in COVID-19.” Advances in experimental medicine and biology, 1318, 435-448.
199. Cao, Y., et al. (2022). “BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection.” Nature, 608(7923):593-602.
200. Mercer, T. R., & Salit, M. (2021). “Testing at scale during the COVID-19 pandemic.” Nature reviews: Genetics, 22(7): 415-426.
201. Zhao, J., et al. (2020). “The Potential Intermediate Hosts for SARS-CoV-2.” Frontiers in microbiology, 11: 580137.
202. Xie, Y., et al. (2021). “The pH Effects on SARS-CoV and SARS-CoV-2 Spike Proteins in the Process of Binding to hACE2.” Research square, rs.3.rs-871118.
203. Warwicker J. (2021). “A model for pH coupling of the SARS-CoV-2 spike protein open/closed equilibrium.” Briefings in bioinformatics, 22(2): 1499-1507.
204. Zhou, T., et al. (2020). “A pH-dependent switch mediates conformational masking of SARS-CoV-2 spike.” bioRxiv : the preprint server for biology, 2020.07.04.187989.
205. Petrović, T., et al. (2021). “The Importance of Glycosylation in COVID-19 Infection.” Advances in experimental medicine and biology, 1325: 239-264.
206. Zhu, Q.Y., et al. (1997). “Stability of Green Tea Catechins.” Journal of Agricultural and Food Chemistry, 45: 4624-4628.
207. Su, Y., et al. (2003). “Stability of tea theaflavins and catechins.” Food Chemistry, 83: 189-195.
208. Krupkova, O.,et al. (2016). “Stability of (-)-epigallocatechin gallate and its activity in liquid formulations and delivery systems.” The Journal of nutritional biochemistry, 37:1-12.
209. Friedman, M., & Jürgens, H. S. (2000). “Effect of pH on the stability of plant phenolic compounds.” Journal of agricultural and food chemistry, 48(6): 2101-2110.
210. O′Brien, E. P., et al. (2012). “Effects of pH on proteins: predictions for ensemble and single-molecule pulling experiments.” Journal of the American Chemical Society, 134(2): 979-987.
211. Deshpande, S., et al. (2016). “Synthesis, Structure, and Tandem Mass Spectrometric Characterization of the Diastereomers of Quinic Acid.” Journal of Agricultural and Food Chemistry, 64(38): 7298-7306.
212. Chen, T.-Y., et al. (2018). “Pancreatic lipase inhibition of strictinin isolated from Pu’er tea (Cammelia sinensis) and its anti-obesity effects in C57BL6 mice.” Journal of Functional Foods, 48: 1-8.
213. Sánchez-Zuno, G. A., et al. (2021). “A review: Antibody-dependent enhancement in COVID-19: The not so friendly side of antibodies.” International Journal of Immunopathology and Pharmacology, 35:20587384211050199.
214. Brann, D. H., et al. (2020). “Non-neuronal expression of SARS-CoV-2 entry genes in the olfactory system suggests mechanisms underlying COVID-19-associated anosmia.” Science advances, 6(31): eabc5801.
215. Shelton, J. F., et al. (2022). “The UGT2A1/UGT2A2 locus is associated with COVID-19-related loss of smell or taste.” Nature genetics, 54(2), 121-124.
216. Douaud, G., et al. (2022). “SARS-CoV-2 is associated with changes in brain structure in UK Biobank.” Nature, 604(7907): 697-707.
217. Pepe, A., et al. (2022). “Tunneling nanotubes provide a route for SARS-CoV-2 spreading.” Science advances, 8(29): eabo0171.
218. Currey, J. M., et al. (2022). “C57BL/6J Mice Are Not Suitable for Modeling Severe SARS-CoV-2 Beta and Gamma Variant Infection.” Viruses, 14(5): 966.
219. Wu, T.-J., et al. (2013). “Tracking the engraftment and regenerative capabilities of transplanted lung stem cells using fluorescent nanodiamonds.” Nature Nanotechnology, 8(9): 682-689.
220. Pham, M. D., et al. (2017). “Glycosaminoglycans-Specific Cell Targeting and Imaging Using Fluorescent Nanodiamonds Coated with Viral Envelope Proteins.” Analytical Chemistry, 89(12): 6527-6534.
221. Tuan, P., et al. (2014). “Enhancement of Chlorogenic Acid Production in Hairy Roots of Platycodon grandiflorum by Over-Expression of An Arabidopsis thaliana Transcription Factor AtPAP1.” International journal of molecular sciences, 15(8): 14743-14752.
222. Xu, Y.-Q., et al. (2019). “Combined effect of pH and temperature on the stability and antioxidant capacity of epigallocatechin gallate (EGCG) in aqueous system.” Journal of Food Engineering, 250: 46-54.
223. Walls, A.C., et al. (2020) “PDB ID: 6VYB”; National Institute of General Medical Sciences (NIGMS), Severe acute respiratory syndrome coronavirus 2; doi: 10.2210/pdb6VYB/pdb.
224. Cong, Y., Liu, C.X. (2021) “PDB ID: 7W92”; Chinese Academy of Sciences, Severe acute respiratory syndrome coronavirus 2; doi: 10.2210/pdb7W92/pdb.
225. Jen-Hao Hsieh, Tsung-Chen Su, Mei-Chu Yang, Chih-Chun Kuo, Li-Jane Shih, and Yung-Hsi Kao. “Green tea extracts and catechins inhibited the binding of COVID-19 spike protein to angiotensin-converting enzyme 2.” NCU-NHRI Conference, Nov 5, 2021, Chungli, Taoyuan.
226. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yen-Yue Lin, Li-Jane Shih, and Yung-Hsi Kao. “Taiwan teas inhibited the binding of COVID-19 to the ACE2 receptor.” The 28th Symposium on Recent Advances in Cellular and Molecular Biology. Kaohsiung, Jan 14th-16th, 2022.
227. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yen-Yue Lin, Li-Jane Shih, and Yung-Hsi Kao. “Research of the function of tea on the effect of a variety of Taiwanese teas and tea polyphenols on COVID-19 receptor.” 2022 The 36th Joint Annual Conference of Biomedical Science. Taipei, Mar 25th-27th, 2022.
228. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yi-Wei Tsuei, Li-Jane Shih, and Yung-Hsi Kao. “Taiwan teas inhibited the binding of COVID-19 spike protein to the ACE2 receptor and thereby elevating the value of Taiwan tea.” 2022年第十三屆桃園四校生命科技領域聯合學術研討會. Microsoft Teams, May 27th, 2022.
229. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yen-Yue Lin, Li-Jane Shih, and Yung-Hsi Kao. “臺灣茶和多元酚抑制新冠病毒對血管收縮素轉化酶2接受器接合的能力” 2022 多元健康茶飲與智能產製銷研討會. Taoyuan, Jul 26th-27th, 2022.
230. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yi-Wei Tsuei, Li-Jane Shih, and Yung-Hsi Kao. “臺灣茶對於抑制新冠病毒對血管收縮素轉化酶2接受器接合的能力.” 2022多元健康茶飲與智能產製銷研討會(口頭發表). Taoyuan, Jul 26th-27th, 2022.
231. Jen-Hao Hsieh, Tsung-Chen Su, Meei-Ju Yang, Chih-Chun Kuo, Yi-Wei Tsuei, Li-Jane Shih, Li-Hua Zhang and Yung-Hsi Kao “Taiwan teas inhibited the binding of coronavirus disease 2019 spike protein variants to the angiotensin-converting enzyme 2 receptor” 2022 ICCB & APOCB Joint Meeting (14th International Congress of Cell Biology & 9th Asian Pacific Organization for Cell Biology). Taipei, Academia Sinica, Nov 7th-11th, 2022. |