[1] E. I. Azhar et al., “Evidence for camel-to-human transmission of MERS coronavirus.,” The New England journal of medicine, vol. 370, no. 26, pp. 2499–505, Jun. 2014, doi: 10.1056/NEJMoa1401505.
[2] A. Assiri et al., “Multifacility Outbreak of Middle East Respiratory Syndrome in Taif, Saudi Arabia,” Emerging infectious diseases, vol. 22, no. 1, pp. 32–40, Jan. 2016, doi: 10.3201/eid2201.151370.
[3] A. A. Rabaan et al., “MERS-CoV: epidemiology, molecular dynamics, therapeutics, and future challenges,” Annals of Clinical Microbiology and Antimicrobials, vol. 20, no. 1, p. 8, 2021, doi: 10.1186/s12941-020-00414-7.
[4] “WHO 2021.” www.emro.who.int/health-topics/mers-cov/mers-outbreaks.html%0D (accessed Jan. 28, 2021).
[5] B. Alosaimi et al., “MERS-CoV infection is associated with downregulation of genes encoding Th1 and Th2 cytokines/chemokines and elevated inflammatory innate immune response in the lower respiratory tract,” Cytokine, vol. 126, Feb. 2020, doi: 10.1016/j.cyto.2019.154895.
[6] J. Tynell et al., “Middle east respiratory syndrome coronavirus shows poor replication but significant induction of antiviral responses in human monocyte-derived macrophages and dendritic cells,” Journal of General Virology, vol. 97, no. 2, pp. 344–355, 2016, doi: 10.1099/jgv.0.000351.
[7] W. H. Mahallawi, O. F. Khabour, Q. Zhang, H. M. Makhdoum, and B. A. Suliman, “Cytokine MERS-CoV infection in humans is associated with a pro-in fl ammatory Th1 and Th17 cytokine pro fi le,” vol. 104, no. November 2017, pp. 8–13, 2018, doi: 10.1016/j.cyto.2018.01.025.
[8] H.-S. Shin et al., “Immune Responses to Middle East Respiratory Syndrome Coronavirus During the Acute and Convalescent Phases of Human Infection.,” Clinical infectious diseases : an official publication of the Infectious Diseases Society of America, vol. 68, no. 6, pp. 984–992, Mar. 2019, doi: 10.1093/cid/ciy595.
[9] R. Reghunathan et al., “Expression profile of immune response genes in patients with severe acute respiratory syndrome,” BMC Immunology, vol. 6, 2005, doi: 10.1186/1471-2172-6-2.
[10] R. Channappanavar and S. Perlman, “Pathogenic human coronavirus infections: causes and consequences of cytokine storm and immunopathology,” Seminars in Immunopathology, vol. 39, no. 5, pp. 529–539, 2017, doi: 10.1007/s00281-017-0629-x.
[11] M. Marchetti, “COVID-19-driven endothelial damage: complement, HIF-1, and ABL2 are potential pathways of damage and targets for cure,” Annals of Hematology, vol. 99, no. 8, pp. 1701–1707, 2020, doi: 10.1007/s00277-020-04138-8.
[12] M. Noris and G. Remuzzi, “Overview of complement activation and regulation,” Seminars in nephrology, vol. 33, no. 6, pp. 479–492, Nov. 2013, doi: 10.1016/j.semnephrol.2013.08.001.
[13] N. S. Merle, R. Noe, L. Halbwachs-Mecarelli, V. Fremeaux-Bacchi, and L. T. Roumenina, “Complement system part II: Role in immunity,” Frontiers in Immunology, vol. 6, no. MAY, pp. 1–26, 2015, doi: 10.3389/fimmu.2015.00257.
[14] M. Riedl et al., “Spectrum of complement-mediated thrombotic microangiopathies: pathogenetic insights identifying novel treatment approaches.,” Seminars in thrombosis and hemostasis, vol. 40, no. 4, pp. 444–464, Jun. 2014, doi: 10.1055/s-0034-1376153.
[15] R. Wang, H. Xiao, R. Guo, Y. Li, and B. Shen, “The role of C5a in acute lung injury induced by highly pathogenic viral infections,” Emerging Microbes and Infections, vol. 4, no. January, pp. 1–7, 2015, doi: 10.1038/emi.2015.28.
[16] R. Ohta, Y. Torii, M. Imai, H. Kimura, N. Okada, and Y. Ito, “Serum concentrations of complement anaphylatoxins and proinflammatory mediators in patients with 2009 H1N1 influenza.,” Microbiology and immunology, vol. 55, no. 3, pp. 191–198, Mar. 2011, doi: 10.1111/j.1348-0421.2011.00309.x.
[17] C. Magro et al., “Complement associated microvascular injury and thrombosis in the pathogenesis of severe COVID-19 infection: A report of five cases,” Translational research : the journal of laboratory and clinical medicine, vol. 220, pp. 1–13, Jun. 2020, doi: 10.1016/j.trsl.2020.04.007.
[18] R. Wang, H. Xiao, R. Guo, Y. Li, and B. Shen, “The role of C5a in acute lung injury induced by highly pathogenic viral infections,” Emerging microbes & infections, vol. 4, no. 5, pp. e28–e28, May 2015, doi: 10.1038/emi.2015.28.
[19] K. V Argyropoulos et al., “Association of Initial Viral Load in Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Patients with Outcome and Symptoms,” The American Journal of Pathology, vol. 190, no. 9, pp. 1881–1887, 2020, doi: https://doi.org/10.1016/j.ajpath.2020.07.001.
[20] M. Cevik, M. Tate, O. Lloyd, A. E. Maraolo, J. Schafers, and A. Ho, “SARS-CoV-2, SARS-CoV-1 and MERS-CoV viral load dynamics, duration of viral shedding and infectiousness: a living systematic review and meta-analysis.” medRxiv, 2020, doi: 10.1101/2020.07.25.20162107.
[21] J. A. Al-Tawfiq, “Viral loads of SARS-CoV, MERS-CoV and SARS-CoV-2 in respiratory specimens: What have we learned?,” Travel medicine and infectious disease, vol. 34, p. 101629, 2020, doi: 10.1016/j.tmaid.2020.101629.
[22] I. F. N. Hung et al., “Viral loads in clinical specimens and SARS manifestations,” Emerging infectious diseases, vol. 10, no. 9, pp. 1550–1557, Sep. 2004, doi: 10.3201/eid1009.040058.
[23] M.-D. Oh et al., “Viral Load Kinetics of MERS Coronavirus Infection.,” The New England journal of medicine, vol. 375, no. 13. United States, pp. 1303–1305, Sep. 2016, doi: 10.1056/NEJMc1511695.
[24] H. M. Al-Abdely et al., “Middle East Respiratory Syndrome Coronavirus Infection Dynamics and Antibody Responses among Clinically Diverse Patients, Saudi Arabia.,” Emerging infectious diseases, vol. 25, no. 4, pp. 753–766, Apr. 2019, doi: 10.3201/eid2504.181595.
[25] J. Zhou et al., “Active replication of Middle East respiratory syndrome coronavirus and aberrant induction of inflammatory cytokines and chemokines in human macrophages: implications for pathogenesis.,” The Journal of infectious diseases, vol. 209, no. 9, pp. 1331–1342, May 2014, doi: 10.1093/infdis/jit504.
[26] M. W. Lo, C. Kemper, and T. M. Woodruff, “COVID-19: Complement, Coagulation, and Collateral Damage,” The Journal of Immunology, vol. 205, no. 6, pp. 1488 LP – 1495, Sep. 2020, doi: 10.4049/jimmunol.2000644.
[27] A. A. Ansari, “Clinical features and pathobiology of Ebolavirus infection.,” Journal of autoimmunity, vol. 55, pp. 1–9, Dec. 2014, doi: 10.1016/j.jaut.2014.09.001.
[28] A. Allegra, M. Di Gioacchino, A. Tonacci, C. Musolino, and S. Gangemi, “Immunopathology of SARS-CoV-2 Infection: Immune Cells and Mediators, Prognostic Factors, and Immune-Therapeutic Implications,” International journal of molecular sciences, vol. 21, no. 13, p. 4782, Jul. 2020, doi: 10.3390/ijms21134782.
[29] A. Haque, D. Hober, and L. H. Kasper, “Confronting potential influenza A (H5N1) pandemic with better vaccines.,” Emerging infectious diseases, vol. 13, no. 10. pp. 1512–1518, Oct. 2007, doi: 10.3201/eid1310.061262.
[30] K.-J. Huang et al., “An interferon-γ-related cytokine storm in SARS patients,” Journal of Medical Virology, vol. 75, no. 2, pp. 185–194, Feb. 2005, doi: 10.1002/jmv.20255.
[31] C. C. Garcia et al., “Complement C5 Activation during Influenza A Infection in Mice Contributes to Neutrophil Recruitment and Lung Injury,” PLOS ONE, vol. 8, no. 5, p. e64443, May 2013, [Online]. Available: https://doi.org/10.1371/journal.pone.0064443.
[32] S. Sun et al., “Treatment With Anti-C5a Antibody Improves the Outcome of H7N9 Virus Infection in African Green Monkeys,” Clinical Infectious Diseases, vol. 60, no. 4, pp. 586–595, Feb. 2015, doi: 10.1093/cid/ciu887.
[33] D. M. Eldewi et al., “Expression levels of complement regulatory proteins (CD35, CD55 and CD59) on peripheral blood cells of patients with chronic kidney disease,” International Journal of General Medicine, vol. 12, pp. 343–351, Sep. 2019, doi: 10.2147/IJGM.S216989.
[34] R.-F. Guo and P. A. Ward, “ROLE OF C5A IN INFLAMMATORY RESPONSES,” Annual Review of Immunology, vol. 23, no. 1, pp. 821–852, Sep. 2004, doi: 10.1146/annurev.immunol.23.021704.115835.
[35] R. Wang, H. Xiao, R. Guo, Y. Li, and B. Shen, “The role of C5a in acute lung injury induced by highly pathogenic viral infections,” Emerging Microbes and Infections, vol. 4, 2015, doi: 10.1038/emi.2015.28.
[36] L. E. Gralinski et al., “Complement Activation Contributes to Severe Acute Respiratory Syndrome Coronavirus Pathogenesis.,” mBio, vol. 9, no. 5, Oct. 2018, doi: 10.1128/mBio.01753-18.
[37] Y. Jiang et al., “Blockade of the C5a–C5aR axis alleviates lung damage in hDPP4 -transgenic mice infected with MERS-CoV,” Emerging Microbes & Infections, vol. 7, no. 1, pp. 1–12, Dec. 2018, doi: 10.1038/s41426-018-0063-8.
[38] S. Sun et al., “Inhibition of complement activation alleviates acute lung injury induced by highly pathogenic avian influenza H5N1 virus infection,” American Journal of Respiratory Cell and Molecular Biology, vol. 49, no. 2, pp. 221–230, 2013, doi: 10.1165/rcmb.2012-0428OC.
[39] J. L. Huang et al., “Th2 predominance and CD8+ memory T cell depletion in patients with severe acute respiratory syndrome,” Microbes and Infection, vol. 7, no. 3, pp. 427–436, 2005, doi: 10.1016/j.micinf.2004.11.017.
[40] J.-H. Chen et al., “Plasma proteome of severe acute respiratory syndrome analyzed by two-dimensional gel electrophoresis and mass spectrometry,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 49, pp. 17039 LP – 17044, Dec. 2004, doi: 10.1073/pnas.0407992101.
[41] D. van Riel et al., “H5N1 Virus Attachment to Lower Respiratory Tract,” Science, vol. 312, no. 5772, pp. 399 LP – 399, Apr. 2006, doi: 10.1126/science.1125548.
[42] K. B. O’Brien, T. E. Morrison, D. Y. Dundore, M. T. Heise, and S. Schultz-Cherry, “A Protective Role for Complement C3 Protein during Pandemic 2009 H1N1 and H5N1 Influenza A Virus Infection,” PLOS ONE, vol. 6, no. 3, p. e17377, Mar. 2011, [Online]. Available: https://doi.org/10.1371/journal.pone.0017377.
[43] T. Gao et al., “Highly pathogenic coronavirus N protein aggravates lung injury by MASP-2-mediated complement over-activation,” medRxiv, p. 2020.03.29.20041962, Jan. 2020, doi: 10.1101/2020.03.29.20041962.
[44] M. M. Bera et al., “Th17 Cytokines Are Critical for Respiratory Syncytial Virus-Associated Airway Hyperreponsiveness through Regulation by Complement C3a and Tachykinins,” The Journal of Immunology, vol. 187, no. 8, pp. 4245 LP – 4255, Oct. 2011, doi: 10.4049/jimmunol.1101789.
[45] D. Rittirsch, H. Redl, and M. Huber-Lang, “Role of Complement in Multiorgan Failure,” Clinical and Developmental Immunology, vol. 2012, p. 962927, 2012, doi: 10.1155/2012/962927.
[46] K. J. Szretter et al., “Role of Host Cytokine Responses in the Pathogenesis of Avian H5N1 Influenza Viruses in Mice,” Journal of Virology, vol. 81, no. 6, pp. 2736 LP – 2744, Mar. 2007, doi: 10.1128/JVI.02336-06.
[47] T. Chotpitayasunondh et al., “Human disease from influenza A (H5N1), Thailand, 2004,” Emerging infectious diseases, vol. 11, no. 2, pp. 201–209, Feb. 2005, doi: 10.3201/eid1102.041061.
[48] L. Yu et al., “Clinical, Virological, and Histopathological Manifestations of Fatal Human Infections by Avian Influenza A(H7N9) Virus,” Clinical Infectious Diseases, vol. 57, no. 10, pp. 1449–1457, Nov. 2013, doi: 10.1093/cid/cit541.
[49] K. K. W. To, J. F. W. Chan, H. Chen, L. Li, and K.-Y. Yuen, “The emergence of influenza A H7N9 in human beings 16 years after influenza A H5N1: a tale of two cities,” The Lancet Infectious Diseases, vol. 13, no. 9, pp. 809–821, 2013, doi: https://doi.org/10.1016/S1473-3099(13)70167-1.
[50] W.-F. Ng, K.-F. To, W. W. L. Lam, T.-K. Ng, and K.-C. Lee, “The comparative pathology of severe acute respiratory syndrome and avian influenza A subtype H5N1—a review,” Human Pathology, vol. 37, no. 4, pp. 381–390, 2006, doi: https://doi.org/10.1016/j.humpath.2006.01.015.
[51] V. A. Meliopoulos et al., “Human H7N9 and H5N1 Influenza Viruses Differ in Induction of Cytokines and Tissue Tropism,” Journal of Virology, vol. 88, no. 22, pp. 12982 LP – 12991, Nov. 2014, doi: 10.1128/JVI.01571-14.
[52] L. E. Gralinski et al., “Mechanisms of severe acute respiratory syndrome coronavirus-induced acute lung injury.,” mBio, vol. 4, no. 4, Aug. 2013, doi: 10.1128/mBio.00271-13.
[53] R. Channappanavar and S. Perlman, “Pathogenic human coronavirus infections: causes and consequences of cytokine storm and immunopathology,” Seminars in Immunopathology, vol. 39, no. 5, pp. 529–539, 2017, doi: 10.1007/s00281-017-0629-x.
[54] T. Narasaraju et al., “Excessive neutrophils and neutrophil extracellular traps contribute to acute lung injury of influenza pneumonitis,” American Journal of Pathology, vol. 179, no. 1, pp. 199–210, 2011, doi: 10.1016/j.ajpath.2011.03.013.
[55] O. Z. Cheng and N. Palaniyar, “NET balancing: A problem in inflammatory lung diseases,” Frontiers in Immunology, vol. 4, no. JAN, pp. 1–13, 2013, doi: 10.3389/fimmu.2013.00001.
[56] H. H. Ng, T. Narasaraju, M. C. Phoon, M. K. Sim, J. E. Seet, and V. T. Chow, “Doxycycline treatment attenuates acute lung injury in mice infected with virulent influenza H3N2 virus: Involvement of matrix metalloproteinases,” Experimental and Molecular Pathology, vol. 92, no. 3, pp. 287–295, 2012, doi: https://doi.org/10.1016/j.yexmp.2012.03.003.
[57] S. Yousefi, C. Mihalache, E. Kozlowski, I. Schmid, and H. U. Simon, “Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps,” Cell Death & Differentiation, vol. 16, no. 11, pp. 1438–1444, 2009, doi: 10.1038/cdd.2009.96.
[58] S. L. Smits et al., “Distinct severe acute respiratory syndrome coronavirus-induced acute lung injury pathways in two different nonhuman primate species.,” Journal of virology, vol. 85, no. 9, pp. 4234–4245, May 2011, doi: 10.1128/JVI.02395-10.
[59] L. Wang et al., “Regulation of IL-8 production by complement-activated product, C5a, in vitro and in vivo during sepsis,” Clinical Immunology, vol. 137, no. 1, pp. 157–165, 2010, doi: https://doi.org/10.1016/j.clim.2010.05.012.
[60] M. M. Marc et al., “Complement Factors C3a, C4a, and C5a in Chronic Obstructive Pulmonary Disease and Asthma,” American Journal of Respiratory Cell and Molecular Biology, vol. 31, no. 2, pp. 216–219, Aug. 2004, doi: 10.1165/rcmb.2003-0394OC.
[61] D. P. Rosanna and C. Salvatore, “Reactive oxygen species, inflammation, and lung diseases.,” Current pharmaceutical design, vol. 18, no. 26, pp. 3889–3900, 2012, doi: 10.2174/138161212802083716.
[62] I.-T. Lee and C.-M. Yang, “Role of NADPH oxidase/ROS in pro-inflammatory mediators-induced airway and pulmonary diseases.,” Biochemical pharmacology, vol. 84, no. 5, pp. 581–590, Sep. 2012, doi: 10.1016/j.bcp.2012.05.005.
[63] J. F.-W. Chan, K. K.-W. To, H. Tse, D.-Y. Jin, and K.-Y. Yuen, “Interspecies transmission and emergence of novel viruses: lessons from bats and birds.,” Trends in microbiology, vol. 21, no. 10, pp. 544–555, Oct. 2013, doi: 10.1016/j.tim.2013.05.005.
[64] W. Domej, K. Oettl, and W. Renner, “Oxidative stress and free radicals in COPD--implications and relevance for treatment.,” International journal of chronic obstructive pulmonary disease, vol. 9, pp. 1207–1224, 2014, doi: 10.2147/COPD.S51226.
[65] T. Akaike et al., “Dependence on O2- generation by xanthine oxidase of pathogenesis of influenza virus infection in mice.,” The Journal of clinical investigation, vol. 85, no. 3, pp. 739–745, Mar. 1990, doi: 10.1172/JCI114499.
[66] T. Sprong et al., “Inhibition of C5a-induced inflammation with preserved C5b-9-mediated bactericidal activity in a human whole blood model of meningococcal sepsis.,” Blood, vol. 102, no. 10, pp. 3702–3710, Nov. 2003, doi: 10.1182/blood-2003-03-0703.
[67] T. E. Mollnes et al., “Essential role of the C5a receptor in E coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation.,” Blood, vol. 100, no. 5, pp. 1869–1877, Sep. 2002.
[68] M. Bosmann and P. A. Ward, “Protein-based therapies for acute lung injury: targeting neutrophil extracellular traps.,” Expert opinion on therapeutic targets, vol. 18, no. 6, pp. 703–714, Jun. 2014, doi: 10.1517/14728222.2014.902938.
[69] L. Sun, R.-F. Guo, H. Gao, J. V. Sarma, F. S. Zetoune, and P. A. Ward, “Attenuation of IgG immune complex-induced acute lung injury by silencing C5aR in lung epithelial cells.,” FASEB journal : official publication of the Federation of American Societies for Experimental Biology, vol. 23, no. 11, pp. 3808–3818, Nov. 2009, doi: 10.1096/fj.09-133694.
[70] Y. Li et al., “Complement 3 mediates periodontal destruction in patients with type 2 diabetes by regulating macrophage polarization in periodontal tissues.,” Cell proliferation, vol. 53, no. 10, p. e12886, Oct. 2020, doi: 10.1111/cpr.12886.
[71] S. Sun et al., “Inhibition of complement activation alleviates acute lung injury induced by highly pathogenic avian influenza H5N1 virus infection.,” American journal of respiratory cell and molecular biology, vol. 49, no. 2, pp. 221–230, Aug. 2013, doi: 10.1165/rcmb.2012-0428OC.
[72] A. Rattan et al., “Synergy between the classical and alternative pathways of complement is essential for conferring effective protection against the pandemic influenza A(H1N1) 2009 virus infection,” PLOS Pathogens, vol. 13, no. 3, p. e1006248, Mar. 2017, [Online]. Available: https://doi.org/10.1371/journal.ppat.1006248.
[73] M. Cugno et al., “Complement activation in patients with COVID-19: A novel therapeutic target.,” The Journal of allergy and clinical immunology, vol. 146, no. 1. pp. 215–217, Jul. 2020, doi: 10.1016/j.jaci.2020.05.006.
[74] J. Yu, X. Yuan, H. Chen, S. Chaturvedi, E. M. Braunstein, and R. A. Brodsky, “Direct activation of the alternative complement pathway by SARS-CoV-2 spike proteins is blocked by factor D inhibition,” Blood, vol. 136, no. 18, pp. 2080–2089, Oct. 2020, doi: 10.1182/blood.2020008248.
[75] P. F. Stahel and S. R. Barnum, “Complement Inhibition in Coronavirus Disease (COVID)-19: A Neglected Therapeutic Option ,” Frontiers in Immunology , vol. 11. p. 1661, 2020, [Online]. Available: https://www.frontiersin.org/article/10.3389/fimmu.2020.01661.
[76] J. Carvelli et al., “Association of COVID-19 inflammation with activation of the C5a–C5aR1 axis,” Nature, vol. 588, no. 7836, pp. 146–150, 2020, doi: 10.1038/s41586-020-2600-6.
[77] F. Diurno et al., “Eculizumab treatment in patients with COVID-19: preliminary results from real life ASL Napoli 2 Nord experience.,” European review for medical and pharmacological sciences, vol. 24, no. 7, pp. 4040–4047, Apr. 2020, doi: 10.26355/eurrev_202004_20875.
[78] S. Meri and H. Jarva, “Complement Regulatory Proteins and Related Diseases,” eLS. Jun. 13, 2013, doi: https://doi.org/10.1002/9780470015902.a0001434.pub3.
[79] P. Ghosh, R. Sahoo, A. Vaidya, M. Chorev, and J. A. Halperin, “Role of Complement and Complement Regulatory Proteins in the Complications of Diabetes,” Endocrine Reviews, vol. 36, no. 3, pp. 272–288, Jun. 2015, doi: 10.1210/er.2014-1099.
[80] J. M. Thurman and B. Renner, “Dynamic control of the complement system by modulated expression of regulatory proteins,” Laboratory Investigation, vol. 91, no. 1, pp. 4–11, 2011, doi: 10.1038/labinvest.2010.173.
[81] P. Agrawal, R. Nawadkar, H. Ojha, J. Kumar, and A. Sahu, “Complement Evasion Strategies of Viruses: An Overview,” Frontiers in microbiology, vol. 8, p. 1117, Jun. 2017, doi: 10.3389/fmicb.2017.01117.
[82] A. Fletcher-Sandersjöö and B.-M. Bellander, “Is COVID-19 associated thrombosis caused by overactivation of the complement cascade? A literature review,” Thrombosis research, vol. 194, pp. 36–41, Oct. 2020, doi: 10.1016/j.thromres.2020.06.027.
[83] V. Afshar-Kharghan, “The role of the complement system in cancer,” The Journal of clinical investigation, vol. 127, no. 3, pp. 780–789, Mar. 2017, doi: 10.1172/JCI90962.
[84] F. Corvillo et al., “Serum properdin consumption as a biomarker of C5 convertase dysregulation in C3 glomerulopathy.,” Clinical and experimental immunology, vol. 184, no. 1, pp. 118–125, Apr. 2016, doi: 10.1111/cei.12754.
[85] P. Dimitrova, N. Ivanovska, W. Schwaeble, V. Gyurkovska, and C. Stover, “The role of properdin in murine zymosan-induced arthritis.,” Molecular immunology, vol. 47, no. 7–8, pp. 1458–1466, Apr. 2010, doi: 10.1016/j.molimm.2010.02.007.
[86] Y. Wang et al., “Properdin Contributes to Allergic Airway Inflammation through Local C3a Generation.,” Journal of immunology (Baltimore, Md. : 1950), vol. 195, no. 3, pp. 1171–1181, Aug. 2015, doi: 10.4049/jimmunol.1401819.
[87] D. Pauly et al., “A novel antibody against human properdin inhibits the alternative complement system and specifically detects properdin from blood samples.,” PloS one, vol. 9, no. 5, p. e96371, 2014, doi: 10.1371/journal.pone.0096371.
[88] Y. Ueda et al., “Blocking Properdin Prevents Complement-Mediated Hemolytic Uremic Syndrome and Systemic Thrombophilia.,” Journal of the American Society of Nephrology : JASN, vol. 29, no. 7, pp. 1928–1937, Jul. 2018, doi: 10.1681/ASN.2017121244.
[89] M. Noris and G. Remuzzi, “Glomerular Diseases Dependent on Complement Activation, Including Atypical Hemolytic Uremic Syndrome, Membranoproliferative Glomerulonephritis, and C3 Glomerulopathy: Core Curriculum 2015.,” American journal of kidney diseases : the official journal of the National Kidney Foundation, vol. 66, no. 2, pp. 359–375, Aug. 2015, doi: 10.1053/j.ajkd.2015.03.040.
[90] P. F. Zipfel et al., “The role of complement in C3 glomerulopathy.,” Molecular immunology, vol. 67, no. 1, pp. 21–30, Sep. 2015, doi: 10.1016/j.molimm.2015.03.012.
[91] M. A. H. M. Michels, E. B. Volokhina, N. C. A. J. van de Kar, and L. P. W. J. van den Heuvel, “The role of properdin in complement-mediated renal diseases: a new player in complement-inhibiting therapy?,” Pediatric Nephrology, vol. 34, no. 8, pp. 1349–1367, 2019, doi: 10.1007/s00467-018-4042-z.
[92] J. C. Holter et al., “Systemic complement activation is associated with respiratory failure in COVID-19 hospitalized patients,” Proceedings of the National Academy of Sciences, vol. 117, no. 40, pp. 25018 LP – 25025, Oct. 2020, doi: 10.1073/pnas.2010540117.
[93] C. M. Wilk, “Coronaviruses hijack the complement system,” Nature Reviews Immunology, vol. 20, no. 6, p. 350, 2020, doi: 10.1038/s41577-020-0314-5.
[94] M. Nangaku, “Complement Regulatory Proteins: Are They Important in Disease?,” Journal of the American Society of Nephrology, vol. 14, no. 9, pp. 2411 LP – 2413, Sep. 2003, doi: 10.1097/01.ASN.0000088010.15313.A1.
[95] M. Kawano, “Complement Regulatory Proteins and Autoimmunity BT - Autoimmunity,” A. Górski, H. Krotkiewski, and M. Zimecki, Eds. Dordrecht: Springer Netherlands, 2001, pp. 73–82.
[96] K. R. Machlus et al., “CCL5 derived from platelets increases megakaryocyte proplatelet formation,” Blood, vol. 127, no. 7, pp. 921–926, Feb. 2016, doi: 10.1182/blood-2015-05-644583.
[97] Y. Cong et al., “MERS-CoV pathogenesis and antiviral efficacy of licensed drugs in human monocyte-derived antigen-presenting cells,” PloS one, vol. 13, no. 3, pp. e0194868–e0194868, Mar. 2018, doi: 10.1371/journal.pone.0194868.
[98] S. Li et al., “Clinical and pathological investigation of patients with severe COVID-19,” JCI insight, vol. 5, no. 12, p. e138070, Jun. 2020, doi: 10.1172/jci.insight.138070.
[99] Y. Zhao et al., “Longitudinal COVID-19 profiling associates IL-1RA and IL-10 with disease severity and RANTES with mild disease,” JCI insight, vol. 5, no. 13, p. e139834, Jul. 2020, doi: 10.1172/jci.insight.139834.
[100] R. L. Chua et al., “COVID-19 severity correlates with airway epithelium–immune cell interactions identified by single-cell analysis,” Nature Biotechnology, vol. 38, no. 8, pp. 970–979, 2020, doi: 10.1038/s41587-020-0602-4.
[101] B. K. Patterson et al., “CCR5 inhibition in critical COVID-19 patients decreases inflammatory cytokines, increases CD8 T-cells, and decreases SARS-CoV2 RNA in plasma by day 14,” International Journal of Infectious Diseases, vol. 103, pp. 25–32, 2021, doi: https://doi.org/10.1016/j.ijid.2020.10.101.
[102] F. J. Culley et al., “Role of CCL5 (RANTES) in Viral Lung Disease,” Journal of Virology, vol. 80, no. 16, pp. 8151 LP – 8157, Aug. 2006, doi: 10.1128/JVI.00496-06.
[103] M. Schaller, C. M. Hogaboam, N. Lukacs, and S. L. Kunkel, “Respiratory viral infections drive chemokine expression and exacerbate the asthmatic response,” Journal of Allergy and Clinical Immunology, vol. 118, no. 2, pp. 295–302, Aug. 2006, doi: 10.1016/j.jaci.2006.05.025.
[104] A. E. John, A. A. Berlin, and N. W. Lukacs, “Respiratory syncytial virus-induced CCL5/RANTES contributes to exacerbation of allergic airway inflammation.,” European journal of immunology, vol. 33, no. 6, pp. 1677–1685, Jun. 2003, doi: 10.1002/eji.200323930.
[105] N. Bostanci et al., “Targeted Proteomics Guided by Label-free Quantitative Proteome Analysis in Saliva Reveal Transition Signatures from Health to Periodontal Disease*,” Molecular & Cellular Proteomics, vol. 17, no. 7, pp. 1392–1409, 2018, doi: https://doi.org/10.1074/mcp.RA118.000718.
[106] V. Taraslia et al., “A High-Resolution Proteomic Landscaping of Primary Human Dental Stem Cells: Identification of SHED- and PDLSC-Specific Biomarkers,” International Journal of Molecular Sciences , vol. 19, no. 1. 2018, doi: 10.3390/ijms19010158.
[107] X. Xiao et al., “Characterization of Odontogenic Differentiation from Human Dental Pulp Stem Cells Using TMT-Based Proteomic Analysis,” BioMed Research International, vol. 2020, p. 3871496, 2020, doi: 10.1155/2020/3871496.