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Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Review Article

Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy

Author(s): Patrick Müller, Hannah Maus, Stefan Josef Hammerschmidt, Philip Maximilian Knaff, Volker Mailänder, Tanja Schirmeister and Christian Kersten*

Volume 29, Issue 4, 2022

Published on: 03 August, 2021

Page: [635 - 665] Pages: 31

DOI: 10.2174/0929867328666210526111318

Price: $65

Abstract

Due to its fast international spread and substantial mortality, the coronavirus disease COVID-19 evolved to a global threat. Since there is currently no causative drug against this viral infection available, science is striving for new drugs and other approaches to treat the new disease. Studies have shown that the cell entry of coronaviruses into host cells takes place through the binding of the viral spike (S) protein to cell receptors. Priming of the S protein occurs via hydrolysis by different host proteases. The inhibition of these proteases could impair the processing of the S protein, thereby affecting the interaction with the host-cell receptors and preventing virus cell entry. Hence, inhibition of these proteases could be a promising strategy for treatment against SARSCoV- 2. In this review, we discuss the current state of the art of developing inhibitors against the entry proteases furin, the transmembrane serine protease type-II (TMPRSS2), trypsin, and cathepsin L.

Keywords: SARS-CoV-2, COVID-19, host proteases, protease inhibitors, furin, cathepsin L, TMPRSS2, trypsin.

[1]
Wu, F.; Zhao, S.; Yu, B.; Chen, Y-M.; Wang, W.; Song, Z-G.; Hu, Y.; Tao, Z-W.; Tian, J-H.; Pei, Y-Y.; Yuan, M-L.; Zhang, Y-L.; Dai, F-H.; Liu, Y.; Wang, Q-M.; Zheng, J-J.; Xu, L.; Holmes, E.C.; Zhang, Y-Z. A new coronavirus associated with human respiratory disease in China. Nature, 2020, 579(7798), 265-269.
[http://dx.doi.org/10.1038/s41586-020-2008-3] [PMID: 32015508]
[2]
Zhu, N.; Zhang, D.; Wang, W.; Li, X.; Yang, B.; Song, J.; Zhao, X.; Huang, B.; Shi, W.; Lu, R.; Niu, P.; Zhan, F.; Ma, X.; Wang, D.; Xu, W.; Wu, G.; Gao, G.F.; Tan, W. A novel coronavirus from patients with pneumonia in China, 2019. N. Engl. J. Med., 2020, 382(8), 727-733.
[http://dx.doi.org/10.1056/NEJMoa2001017] [PMID: 31978945]
[3]
Lu, R.; Zhao, X.; Li, J.; Niu, P.; Yang, B.; Wu, H.; Wang, W.; Song, H.; Huang, B.; Zhu, N.; Bi, Y.; Ma, X.; Zhan, F.; Wang, L.; Hu, T.; Zhou, H.; Hu, Z.; Zhou, W.; Zhao, L.; Chen, J.; Meng, Y.; Wang, J.; Lin, Y.; Yuan, J.; Xie, Z.; Ma, J.; Liu, W.J.; Wang, D.; Xu, W.; Holmes, E.C.; Gao, G.F.; Wu, G.; Chen, W.; Shi, W.; Tan, W. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet, 2020, 395(10224), 565-574.
[http://dx.doi.org/10.1016/S0140-6736(20)30251-8] [PMID: 32007145]
[4]
Coronaviridae Study Group of the International Committee on Taxonomy of Viruses. The species severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2. Nat. Microbiol., 2020, 5(4), 536-544.
[http://dx.doi.org/10.1038/s41564-020-0695-z] [PMID: 32123347]
[5]
WHO. WHO Coronavirus Disease (COVID-19) Dashboard. Available from: https://covid19.who.int/(Accessed date: February 05, 2020)
[6]
Walsh, E.E.; Frenck, R.W., Jr; Falsey, A.R.; Kitchin, N.; Absalon, J.; Gurtman, A.; Lockhart, S.; Neuzil, K.; Mulligan, M.J.; Bailey, R.; Swanson, K.A.; Li, P.; Koury, K.; Kalina, W.; Cooper, D.; Fontes-Garfias, C.; Shi, P-Y.; Türeci, Ö.; Tompkins, K.R.; Lyke, K.E.; Raabe, V.; Dormitzer, P.R.; Jansen, K.U.; Şahin, U.; Gruber, W.C. Safety and immunogenicity of two RNA-based COVID-19 vaccine candidates. N. Engl. J. Med., 2020, 383(25), 2439-2450.
[http://dx.doi.org/10.1056/NEJMoa2027906] [PMID: 33053279]
[7]
Corbett, K.S.; Flynn, B.; Foulds, K.E.; Francica, J.R.; Boyoglu-Barnum, S.; Werner, A.P.; Flach, B.; O’Connell, S.; Bock, K.W.; Minai, M.; Nagata, B.M.; Andersen, H.; Martinez, D.R.; Noe, A.T.; Douek, N.; Donaldson, M.M.; Nji, N.N.; Alvarado, G.S.; Edwards, D.K.; Flebbe, D.R.; Lamb, E.; Doria-Rose, N.A.; Lin, B.C.; Louder, M.K.; O’Dell, S.; Schmidt, S.D.; Phung, E.; Chang, L.A.; Yap, C.; Todd, J.M.; Pessaint, L.; Van Ry, A.; Browne, S.; Greenhouse, J.; Putman-Taylor, T.; Strasbaugh, A.; Campbell, T-A.; Cook, A.; Dodson, A.; Steingrebe, K.; Shi, W.; Zhang, Y.; Abiona, O.M.; Wang, L.; Pegu, A.; Yang, E.S.; Leung, K.; Zhou, T.; Teng, I-T.; Widge, A.; Gordon, I.; Novik, L.; Gillespie, R.A.; Loomis, R.J.; Moliva, J.I.; Stewart-Jones, G.; Himansu, S.; Kong, W-P.; Nason, M.C.; Morabito, K.M.; Ruckwardt, T.J.; Ledgerwood, J.E.; Gaudinski, M.R.; Kwong, P.D.; Mascola, J.R.; Carfi, A.; Lewis, M.G.; Baric, R.S.; McDermott, A.; Moore, I.N.; Sullivan, N.J.; Roederer, M.; Seder, R.A.; Graham, B.S. Evaluation of the mRNA-1273 vaccine against SARS-CoV-2 in nonhuman primates. N. Engl. J. Med., 2020, 383(16), 1544-1555.
[http://dx.doi.org/10.1056/NEJMoa2024671] [PMID: 32722908]
[8]
Baden, L.R.; El Sahly, H.M.; Essink, B.; Kotloff, K.; Frey, S.; Novak, R.; Diemert, D.; Spector, S.A.; Rouphael, N.; Creech, C.B.; McGettigan, J.; Khetan, S.; Segall, N.; Solis, J.; Brosz, A.; Fierro, C.; Schwartz, H.; Neuzil, K.; Corey, L.; Gilbert, P.; Janes, H.; Follmann, D.; Marovich, M.; Mascola, J.; Polakowski, L.; Ledgerwood, J.; Graham, B.S.; Bennett, H.; Pajon, R.; Knightly, C.; Leav, B.; Deng, W.; Zhou, H.; Han, S.; Ivarsson, M.; Miller, J.; Zaks, T. Efficacy and safety of the mRNA-1273 SARS-CoV-2 vaccine. N. Engl. J. Med., 2021, 384(5), 403-416.
[http://dx.doi.org/10.1056/NEJMoa2035389] [PMID: 33378609]
[9]
Voysey, M.; Clemens, S.A.C.; Madhi, S.A.; Weckx, L.Y.; Folegatti, P.M.; Aley, P.K.; Angus, B.; Baillie, V.L.; Barnabas, S.L.; Bhorat, Q.E.; Bibi, S.; Briner, C.; Cicconi, P.; Collins, A.M.; Colin-Jones, R.; Cutland, C.L.; Darton, T.C.; Dheda, K.; Duncan, C.J.A.; Emary, K.R.W.; Ewer, K.J.; Fairlie, L.; Faust, S.N.; Feng, S.; Ferreira, D.M.; Finn, A.; Goodman, A.L.; Green, C.M.; Green, C.A.; Heath, P.T.; Hill, C.; Hill, H.; Hirsch, I.; Hodgson, S.H.C.; Izu, A.; Jackson, S.; Jenkin, D.; Joe, C.C.D.; Kerridge, S.; Koen, A.; Kwatra, G.; Lazarus, R.; Lawrie, A.M.; Lelliott, A.; Libri, V.; Lillie, P.J.; Mallory, R.; Mendes, A.V.A.; Milan, E.P.; Minassian, A.M.; McGregor, A.; Morrison, H.; Mujadidi, Y.F.; Nana, A.; O’Reilly, P.J.; Padayachee, S.D.; Pittella, A.; Plested, E.; Pollock, K.M.; Ramasamy, M.N.; Rhead, S.; Schwarzbold, A.V.; Singh, N.; Smith, A.; Song, R.; Snape, M.D.; Sprinz, E.; Sutherland, R.K.; Tarrant, R.; Thomson, E.C.; Török, M.E.; Toshner, M.; Turner, D.P.J.; Vekemans, J.; Villafana, T.L.; Watson, M.E.E.; Williams, C.J.; Douglas, A.D.; Hill, A.V.S.; Lambe, T.; Gilbert, S.C.; Pollard, A.J.; Aban, M.; Abayomi, F.; Abeyskera, K.; Aboagye, J.; Adam, M.; Adams, K.; Adamson, J.; Adelaja, Y.A.; Adewetan, G.; Adlou, S.; Ahmed, K.; Akhalwaya, Y.; Akhalwaya, S.; Alcock, A.; Ali, A.; Allen, E.R.; Allen, L.; Almeida, T.C.D.S.C.; Alves, M.P.S.; Amorim, F.; Andritsou, F.; Anslow, R.; Appleby, M.; Arbe-Barnes, E.H.; Ariaans, M.P.; Arns, B.; Arruda, L.; Azi, P.; Azi, L.; Babbage, G.; Bailey, C.; Baker, K.F.; Baker, M.; Baker, N.; Baker, P.; Baldwin, L.; Baleanu, I.; Bandeira, D.; Bara, A.; Barbosa, M.A.S.; Barker, D.; Barlow, G.D.; Barnes, E.; Barr, A.S.; Barrett, J.R.; Barrett, J.; Bates, L.; Batten, A.; Beadon, K.; Beales, E.; Beckley, R.; Belij-Rammerstorfer, S.; Bell, J.; Bellamy, D.; Bellei, N.; Belton, S.; Berg, A.; Bermejo, L.; Berrie, E.; Berry, L.; Berzenyi, D.; Beveridge, A.; Bewley, K.R.; Bexhell, H.; Bhikha, S.; Bhorat, A.E.; Bhorat, Z.E.; Bijker, E.; Birch, G.; Birch, S.; Bird, A.; Bird, O.; Bisnauthsing, K.; Bittaye, M.; Blackstone, K.; Blackwell, L.; Bletchly, H.; Blundell, C.L.; Blundell, S.R.; Bodalia, P.; Boettger, B.C.; Bolam, E.; Boland, E.; Bormans, D.; Borthwick, N.; Bowring, F.; Boyd, A.; Bradley, P.; Brenner, T.; Brown, P.; Brown, C.; Brown-O’Sullivan, C.; Bruce, S.; Brunt, E.; Buchan, R.; Budd, W.; Bulbulia, Y.A.; Bull, M.; Burbage, J.; Burhan, H.; Burn, A.; Buttigieg, K.R.; Byard, N.; Cabera Puig, I.; Calderon, G.; Calvert, A.; Camara, S.; Cao, M.; Cappuccini, F.; Cardoso, J.R.; Carr, M.; Carroll, M.W.; Carson-Stevens, A.; Carvalho, Y. Safety and efficacy of the ChAdOx1 nCoV-19 vaccine (AZD1222) against SARS-CoV-2: an interim analysis of four randomised controlled trials in Brazil, South Africa, and the UK. Lancet, 2021, 397(10269), 99-111.
[http://dx.doi.org/10.1016/S0140-6736(20)32661-1] [PMID: 33306989]
[10]
WHO Draft landscape and tracker of COVID-19 candidate vaccines., Available from: https://www.who.int/publications/m/item/draft-landscape-of-covid-19-candidate-vaccines(Accessed date: October 01, 2020)
[11]
Zhang, Y.; Zeng, G.; Pan, H.; Li, C.; Hu, Y.; Chu, K.; Han, W.; Chen, Z.; Tang, R.; Yin, W.; Chen, X. Articles safety, tolerability, and immunogenicity of an inactivated SARS-CoV-2 vaccine in healthy adults aged 18 – 59 years. Lancet Infect. Dis., 21(2), 181-192.
[http://dx.doi.org/10.1016/S1473-3099(20)30843-4] [PMID: 33217362]
[12]
U.S. National Library of Medicine. Clinical trial of efficacy, safety, and immunogenicity of gam-COVID-vac vaccine against COVID-19 (RESIST). Available from: https://clinicaltrials.gov/ct2/show/NCT04530396?term=Gam-COVID-Vac&draw=2(Accessed date: October 01, 2020)
[13]
Muik, A.; Wallisch, A-K.; Sänger, B.; Swanson, K.A.; Mühl, J.; Chen, W.; Cai, H.; Maurus, D.; Sarkar, R.; Türeci, Ö.; Dormitzer, P.R.; Şahin, U. Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine-elicited human sera. Science, 2021, 371(6534), 1152-1153.
[http://dx.doi.org/10.1126/science.abg6105] [PMID: 33514629]
[14]
Remuzzi, A.; Remuzzi, G. COVID-19 and Italy: what next? Lancet, 2020, 395(10231), 1225-1228.
[http://dx.doi.org/10.1016/S0140-6736(20)30627-9] [PMID: 32178769]
[15]
Saglietto, A.; D’Ascenzo, F.; Zoccai, G.B.; De Ferrari, G.M. COVID-19 in Europe: the Italian lesson. Lancet, 2020, 395(10230), 1110-1111.
[http://dx.doi.org/10.1016/S0140-6736(20)30690-5] [PMID: 32220279]
[16]
Dhama, K.; Sharun, K.; Tiwari, R.; Dadar, M.; Malik, Y.S.; Singh, K.P.; Chaicumpa, W. COVID-19, an emerging coronavirus infection: advances and prospects in designing and developing vaccines, immunotherapeutics, and therapeutics. Hum. Vaccin. Immunother., 2020, 16(6), 1232-1238.
[http://dx.doi.org/10.1080/21645515.2020.1735227] [PMID: 32186952]
[17]
Shah, B.; Modi, P.; Sagar, S.R. In silico studies on therapeutic agents for COVID-19: drug repurposing approach. Life Sci., 2020, 252(March)117652
[http://dx.doi.org/10.1016/j.lfs.2020.117652] [PMID: 32278693]
[18]
Warren, T.K.; Jordan, R.; Lo, M.K.; Ray, A.S.; Mackman, R.L.; Soloveva, V.; Siegel, D.; Perron, M.; Bannister, R.; Hui, H.C.; Larson, N.; Strickley, R.; Wells, J.; Stuthman, K.S.; Van Tongeren, S.A.; Garza, N.L.; Donnelly, G.; Shurtleff, A.C.; Retterer, C.J.; Gharaibeh, D.; Zamani, R.; Kenny, T.; Eaton, B.P.; Grimes, E.; Welch, L.S.; Gomba, L.; Wilhelmsen, C.L.; Nichols, D.K.; Nuss, J.E.; Nagle, E.R.; Kugelman, J.R.; Palacios, G.; Doerffler, E.; Neville, S.; Carra, E.; Clarke, M.O.; Zhang, L.; Lew, W.; Ross, B.; Wang, Q.; Chun, K.; Wolfe, L.; Babusis, D.; Park, Y.; Stray, K.M.; Trancheva, I.; Feng, J.Y.; Barauskas, O.; Xu, Y.; Wong, P.; Braun, M.R.; Flint, M.; McMullan, L.K.; Chen, S-S.; Fearns, R.; Swaminathan, S.; Mayers, D.L.; Spiropoulou, C.F.; Lee, W.A.; Nichol, S.T.; Cihlar, T.; Bavari, S. Therapeutic efficacy of the small molecule GS-5734 against Ebola virus in rhesus monkeys. Nature, 2016, 531(7594), 381-385.
[http://dx.doi.org/10.1038/nature17180] [PMID: 26934220]
[19]
Tchesnokov, E.P.; Feng, J.Y.; Porter, D.P.; Götte, M. Mechanism of inhibition of Ebola virus RNA-dependent RNA polymerase by remdesivir. Viruses, 2019, 11(4), 326.
[http://dx.doi.org/10.3390/v11040326] [PMID: 30987343]
[20]
Goldman, J.D.; Lye, D.C.B.; Hui, D.S.; Marks, K.M.; Bruno, R.; Montejano, R.; Spinner, C.D.; Galli, M.; Ahn, M-Y.; Nahass, R.G.; Chen, Y-S.; SenGupta, D.; Hyland, R.H.; Osinusi, A.O.; Cao, H.; Blair, C.; Wei, X.; Gaggar, A.; Brainard, D.M.; Towner, W.J.; Muñoz, J.; Mullane, K.M.; Marty, F.M.; Tashima, K.T.; Diaz, G.; Subramanian, A. Remdesivir for 5 or 10 days in patients with severe COVID-19. N. Engl. J. Med., 2020, 383(19), 1827-1837.
[http://dx.doi.org/10.1056/NEJMoa2015301] [PMID: 32459919]
[21]
Beigel, J.H.; Tomashek, K.M.; Dodd, L.E.; Mehta, A.K.; Zingman, B.S.; Kalil, A.C.; Hohmann, E.; Chu, H.Y.; Luetkemeyer, A.; Kline, S.; Lopez de Castilla, D.; Finberg, R.W.; Dierberg, K.; Tapson, V.; Hsieh, L.; Patterson, T.F.; Paredes, R.; Sweeney, D.A.; Short, W.R.; Touloumi, G.; Lye, D.C.; Ohmagari, N.; Oh, M.; Ruiz-Palacios, G.M.; Benfield, T.; Fätkenheuer, G.; Kortepeter, M.G.; Atmar, R.L.; Creech, C.B.; Lundgren, J.; Babiker, A.G.; Pett, S.; Neaton, J.D.; Burgess, T.H.; Bonnett, T.; Green, M.; Makowski, M.; Osinusi, A.; Nayak, S.; Lane, H.C. Remdesivir for the treatment of COVID-19 — preliminary report. N. Engl. J. Med., 2020, 383(19), 1813-1826.
[http://dx.doi.org/10.1056/NEJMoa2007764] [PMID: 32445440 ]
[22]
WHO Solidarity Trial Consortium Pan, H.; Peto, R.; Henao-Restrepo, A.M.; Preziosi, M.P.; Sathiyamoorthy, V.; Abdool Karim, Q.; Alejandria, M.M.; Hernández García, C.; Kieny, M.P.; Malekzadeh, R.; Murthy, S.; Reddy, K.S.; Roses Periago, M.; Abi Hanna, P.; Ader, F.; Al-Bader, A.M.; Alhasawi, A.; Allum, E.; Alotaibi, A., Swaminathan, S. Repurposed antiviral drugs for COVID-19 –interim WHO SOLIDARITY trial results. N. Engl. J. Med., 2020, 384(6), 497-511.
[http://dx.doi.org/10.1056/NEJMoa2023184] [PMID: 33264556]
[23]
Edwards, A. What are the odds of finding a COVID-19 drug from a lab repurposing screen? J. Chem. Inf. Model., 2020, 60(12), 5727-5729.
[http://dx.doi.org/10.1021/acs.jcim.0c00861] [PMID: 32914973]
[24]
Din, O.S.; Woll, P.J. Treatment of gastrointestinal stromal tumor: focus on imatinib mesylate. Ther. Clin. Risk Manag., 2008, 4(1), 149-162.
[http://dx.doi.org/10.2147/TCRM.S1526] [PMID: 18728705]
[25]
Majid, M.; Fatemeh, M.; Shahrokh, S. An overview on coronaviruses family from past to COVID-19: introduce some inhibitors as antiviruses from Gillan’s plants. Biointerface Res. Appl. Chem., 2020, 10(3), 5575-5585.
[http://dx.doi.org/10.33263/BRIAC103.575585]
[26]
Chan, J.F-W.; Kok, K-H.; Zhu, Z.; Chu, H.; To, K.K-W.; Yuan, S.; Yuen, K-Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect., 2020, 9(1), 221-236.
[http://dx.doi.org/10.1080/22221751.2020.1719902] [PMID: 31987001]
[27]
Zhou, P.; Yang, X-L.; Wang, X-G.; Hu, B.; Zhang, L.; Zhang, W.; Si, H-R.; Zhu, Y.; Li, B.; Huang, C-L.; Chen, H-D.; Chen, J.; Luo, Y.; Guo, H.; Jiang, R-D.; Liu, M-Q.; Chen, Y.; Shen, X-R.; Wang, X.; Zheng, X-S.; Zhao, K.; Chen, Q-J.; Deng, F.; Liu, L-L.; Yan, B.; Zhan, F-X.; Wang, Y-Y.; Xiao, G-F.; Shi, Z-L. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature, 2020, 579(7798), 270-273.
[http://dx.doi.org/10.1038/s41586-020-2012-7] [PMID: 32015507]
[28]
Yao, H.; Song, Y.; Chen, Y.; Wu, N.; Xu, J.; Sun, C.; Zhang, J.; Weng, T.; Zhang, Z.; Wu, Z.; Cheng, L.; Shi, D.; Lu, X.; Lei, J.; Crispin, M.; Shi, Y.; Li, L.; Li, S. Molecular architecture of the SARS-CoV-2 virus. Cell, 2020, 183(3), 730-738.e13.
[http://dx.doi.org/10.1016/j.cell.2020.09.018] [PMID: 32979942]
[29]
Fehr, A.R.; Perlman, S. Coronaviruses: An Overview of Their Replication and Pathogenesis; Springer Protocolls, 2015, pp. 1-23.
[30]
Kim, D.; Lee, J.Y.; Yang, J.S.; Kim, J.W.; Kim, V.N.; Chang, H. The architecture of SARS-CoV-2 transcriptome. Cell, 2020, 181(4), 914-921.e10.
[http://dx.doi.org/10.1016/j.cell.2020.04.011] [PMID: 32330414]
[31]
Astuti, I. Ysrafil. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2): an overview of viral structure and host response. Diabetes Metab. Syndr., 2020, 14(4), 407-412.
[http://dx.doi.org/10.1016/j.dsx.2020.04.020] [PMID: 32335367]
[32]
Bárcena, M.; Oostergetel, G.T.; Bartelink, W.; Faas, F.G.A.; Verkleij, A.; Rottier, P.J.M.; Koster, A.J.; Bosch, B.J. Cryo-electron tomography of mouse hepatitis virus: insights into the structure of the coronavirion. Proc. Natl. Acad. Sci. USA, 2009, 106(2), 582-587.
[http://dx.doi.org/10.1073/pnas.0805270106] [PMID: 19124777]
[33]
Neuman, B.W.; Adair, B.D.; Yoshioka, C.; Quispe, J.D.; Orca, G.; Kuhn, P.; Milligan, R.A.; Yeager, M.; Buchmeier, M.J. Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy. J. Virol., 2006, 80(16), 7918-7928.
[http://dx.doi.org/10.1128/JVI.00645-06] [PMID: 16873249]
[34]
Berman, H.M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T.N.; Weissig, H.; Shindyalov, I.N.; Bourne, P.E. The protein data bank. Nucleic Acids Res., 2000, 28(1), 235-242.
[http://dx.doi.org/10.1093/nar/28.1.235] [PMID: 10592235]
[35]
Lukassen, S.; Chua, R.L.; Trefzer, T.; Kahn, N.C.; Schneider, M.A.; Muley, T.; Winter, H.; Meister, M.; Veith, C.; Boots, A.W.; Hennig, B.P.; Kreuter, M.; Conrad, C.; Eils, R. SARS-CoV-2 receptor ACE2 and TMPRSS2 are primarily expressed in bronchial transient secretory cells. EMBO J., 2020, 39(10)e105114
[http://dx.doi.org/10.15252/embj.2020105114] [PMID: 32246845]
[36]
Lan, J.; Ge, J.; Yu, J.; Shan, S.; Zhou, H.; Fan, S.; Zhang, Q.; Shi, X.; Wang, Q.; Zhang, L.; Wang, X. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature, 2020, 581(7807), 215-220.
[http://dx.doi.org/10.1038/s41586-020-2180-5] [PMID: 32225176]
[37]
Shang, J.; Ye, G.; Shi, K.; Wan, Y.; Luo, C.; Aihara, H.; Geng, Q.; Auerbach, A.; Li, F. Structural basis of receptor recognition by SARS-CoV-2. Nature, 2020, 581(7807), 221-224.
[http://dx.doi.org/10.1038/s41586-020-2179-y] [PMID: 32225175]
[38]
Shin, D.; Mukherjee, R.; Grewe, D.; Bojkova, D.; Baek, K.; Bhattacharya, A.; Schulz, L.; Widera, M.; Mehdipour, A.R.; Tascher, G.; Geurink, P.P.; Wilhelm, A.; van der Heden van Noort, G.J.; Ovaa, H.; Müller, S.; Knobeloch, K-P.; Rajalingam, K.; Schulman, B.A.; Cinatl, J.; Hummer, G.; Ciesek, S.; Dikic, I. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature, 2020, 587(7835), 657-662.
[http://dx.doi.org/10.1038/s41586-020-2601-5] [PMID: 32726803]
[39]
Harcourt, B.H.; Jukneliene, D.; Kanjanahaluethai, A.; Bechill, J.; Severson, K.M.; Smith, C.M.; Rota, P.A.; Baker, S.C. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J. Virol., 2004, 78(24), 13600-13612.
[http://dx.doi.org/10.1128/JVI.78.24.13600-13612.2004] [PMID: 15564471]
[40]
Chen, S.; Jonas, F.; Shen, C.; Hilgenfeld, R. Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode. Protein Cell, 2010, 1(1), 59-74.
[http://dx.doi.org/10.1007/s13238-010-0011-4] [PMID: 21203998]
[41]
Ziebuhr, J. Molecular biology of severe acute respiratory syndrome coronavirus. Curr. Opin. Microbiol., 2004, 7(4), 412-419.
[http://dx.doi.org/10.1016/j.mib.2004.06.007] [PMID: 15358261]
[42]
Toelzer, C.; Gupta, K.; Yadav, S.K.N.; Borucu, U.; Davidson, A.D.; Kavanagh Williamson, M.; Shoemark, D.K.; Garzoni, F.; Staufer, O.; Milligan, R.; Capin, J.; Mulholland, A.J.; Spatz, J.; Fitzgerald, D.; Berger, I.; Schaffitzel, C. Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein. Science, 2020, 370(6517), 725-730.
[http://dx.doi.org/10.1126/science.abd3255] [PMID: 32958580]
[43]
Jin, Z.; Du, X.; Xu, Y.; Deng, Y.; Liu, M.; Zhao, Y.; Zhang, B.; Li, X.; Zhang, L.; Peng, C.; Duan, Y.; Yu, J.; Wang, L.; Yang, K.; Liu, F.; Jiang, R.; Yang, X.; You, T.; Liu, X.; Yang, X.; Bai, F.; Liu, H.; Liu, X.; Guddat, L.W.; Xu, W.; Xiao, G.; Qin, C.; Shi, Z.; Jiang, H.; Rao, Z.; Yang, H. Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors. Nature, 2020, 582(7811), 289-293.
[http://dx.doi.org/10.1038/s41586-020-2223-y] [PMID: 32272481]
[44]
Klemm, T.; Ebert, G.; Calleja, D.J.; Allison, C.C.; Richardson, L.W.; Bernardini, J.P.; Lu, B.G.; Kuchel, N.W.; Grohmann, C.; Shibata, Y.; Gan, Z.Y.; Cooney, J.P.; Doerflinger, M.; Au, A.E.; Blackmore, T.R.; van der Heden van Noort, G.J.; Geurink, P.P.; Ovaa, H.; Newman, J.; Riboldi-Tunnicliffe, A.; Czabotar, P.E.; Mitchell, J.P.; Feltham, R.; Lechtenberg, B.C.; Lowes, K.N.; Dewson, G.; Pellegrini, M.; Lessene, G.; Komander, D. Mechanism and inhibition of the papain-like protease, PLpro, of SARS-CoV-2. EMBO J., 2020, 39(18)e106275
[http://dx.doi.org/10.15252/embj.2020106275] [PMID: 32845033]
[45]
Barile, E.; Baggio, C.; Gambini, L.; Shiryaev, S.A.; Strongin, A.Y.; Pellecchia, M. Potential therapeutic targeting of coronavirus spike glycoprotein priming. Molecules, 2020, 25(10), 2424.
[http://dx.doi.org/10.3390/molecules25102424] [PMID: 32455942]
[46]
Rahman, N.; Basharat, Z.; Yousuf, M.; Castaldo, G.; Rastrelli, L.; Khan, H. Virtual screening of natural products against type II transmembrane serine protease (TMPRSS2), the priming agent of coronavirus 2 (SARS-CoV-2). Molecules, 2020, 25(10), 2271.
[http://dx.doi.org/10.3390/molecules25102271] [PMID: 32408547]
[47]
Xia, S.; Lan, Q.; Su, S.; Wang, X.; Xu, W.; Liu, Z.; Zhu, Y.; Wang, Q.; Lu, L.; Jiang, S. The role of furin cleavage site in SARS-CoV-2 spike protein-mediated membrane fusion in the presence or absence of trypsin. Signal Transduct. Target. Ther., 2020, 5(1), 92.
[http://dx.doi.org/10.1038/s41392-020-0184-0] [PMID: 32532959]
[48]
Jaimes, J. A.; Millet, J. K.; Whittaker, G. R. Proteolytic cleavage of the SARS-CoV-2 spike protein and the role of the novel S1/S2 Site. iScience, 2020, 23(6) 101212
[49]
Wrapp, D.; Wang, N.; Corbett, K.S.; Goldsmith, J.A.; Hsieh, C-L.; Abiona, O.; Graham, B.S.; McLellan, J.S. Cryo-EM structure of the 2019-NCoV spike in the prefusion conformation. Science, 2020, 367(6483), 1260-1263.
[http://dx.doi.org/10.1126/science.abb2507] [PMID: 32075877]
[50]
Watanabe, Y.; Allen, J.D.; Wrapp, D.; McLellan, J.S.; Crispin, M. Site-specific glycan analysis of the SARS-CoV-2 spike. Science, 2020, 369(6501), 330-333.
[http://dx.doi.org/10.1126/science.abb9983] [PMID: 32366695]
[51]
Tan, L.; Wang, Q.; Zhang, D.; Ding, J.; Huang, Q.; Tang, Y.Q.; Wang, Q.; Miao, H. Lymphopenia predicts disease severity of COVID-19: a descriptive and predictive study. Signal Transduct. Target. Ther., 2020, 5(1), 16-18.
[http://dx.doi.org/10.1038/s41392-020-0148-4] [PMID: 32296041]
[52]
White, J.M.; Delos, S.E.; Brecher, M.; Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol., 2008, 43(3), 189-219.
[http://dx.doi.org/10.1080/10409230802058320] [PMID: 18568847]
[53]
Tortorici, M.A.; Walls, A.C.; Lang, Y.; Wang, C.; Li, Z.; Koerhuis, D.; Boons, G.J.; Bosch, B.J.; Rey, F.A.; de Groot, R.J.; Veesler, D. Structural basis for human coronavirus attachment to sialic acid receptors. Nat. Struct. Mol. Biol., 2019, 26(6), 481-489.
[http://dx.doi.org/10.1038/s41594-019-0233-y] [PMID: 31160783]
[54]
Yang, J.; Petitjean, S.J.L.; Koehler, M.; Zhang, Q.; Dumitru, A.C.; Chen, W.; Derclaye, S.; Vincent, S.P.; Soumillion, P.; Alsteens, D. Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor. Nat. Commun., 2020, 11(1), 4541.
[http://dx.doi.org/10.1038/s41467-020-18319-6] [PMID: 32917884]
[55]
Hoffmann, M.; Kleine-Weber, H.; Schroeder, S.; Krüger, N.; Herrler, T.; Erichsen, S.; Schiergens, T.S.; Herrler, G.; Wu, N.H.; Nitsche, A.; Müller, M.A.; Drosten, C.; Pöhlmann, S. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell, 2020, 181(2), 271-280.e8.
[http://dx.doi.org/10.1016/j.cell.2020.02.052] [PMID: 32142651]
[56]
Hamming, I.; Timens, W.; Bulthuis, M.L.; Lely, A.T.; Navis, G.; van Goor, H. Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis. J. Pathol., 2004, 203(2), 631-637.
[http://dx.doi.org/10.1002/path.1570] [PMID: 15141377]
[57]
Becerra-Flores, M.; Cardozo, T. SARS-CoV-2 viral spike G614 mutation exhibits higher case fatality rate. Int. J. Clin. Pract., 2020, 74(8)e13525
[http://dx.doi.org/10.1111/ijcp.13525] [PMID: 32374903]
[58]
Wang, C.; Liu, Z.; Chen, Z.; Huang, X.; Xu, M.; He, T.; Zhang, Z. The establishment of reference sequence for SARS-CoV-2 and variation analysis. J. Med. Virol., 2020, 92(6), 667-674.
[http://dx.doi.org/10.1002/jmv.25762] [PMID: 32167180]
[59]
Jaimes, J.A; Millet, J.K.; Whittaker, GR. Proteolytic cleavage of the SARS-CoV-2 spike protein and the role of the novel S1/S2 site. iScience 2020, 23(6) 101212
[http://dx.doi.org/10.1016/j.isci.2020.101212] [PMID: 32512386]
[60]
Barrett, C.T.; Dutch, R.E. Viral membrane fusion and the transmembrane domain. Viruses, 2020, 12(7), 693.
[http://dx.doi.org/10.3390/v12070693] [PMID: 32604992]
[61]
Jaimes, J.A.; Whittaker, G.R. Feline coronavirus: insights into viral pathogenesis based on the spike protein structure and function. Virology, 2018, 517, 108-121.
[http://dx.doi.org/10.1016/j.virol.2017.12.027] [PMID: 29329682]
[62]
Seidah, N.G.; Day, R.; Marcinkiewicz, M.; Chretien, M. Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins. Ann. N. Y. Acad. Sci., 1998, 839(1), 9-24.
[http://dx.doi.org/10.1111/j.1749-6632.1998.tb10727.x] [PMID: 9629127]
[63]
Seidah, N.G.; Prat, A. The biology and therapeutic targeting of the proprotein convertases. Nat. Rev. Drug Discov., 2012, 11(5), 367-383.
[http://dx.doi.org/10.1038/nrd3699] [PMID: 22679642]
[64]
Jaaks, P.; Bernasconi, M. The proprotein convertase furin in tumour progression. Int. J. Cancer, 2017, 141(4), 654-663.
[http://dx.doi.org/10.1002/ijc.30714] [PMID: 28369813]
[65]
Steiner, D.F. The proprotein convertases. Curr. Opin. Chem. Biol., 1998, 2(1), 31-39.https://doi.org/https://doi.org/10.1016/S1367-5931(98)80033-1
[PMID: 9667917]
[66]
Zhou, A.; Martin, S.; Lipkind, G.; LaMendola, J.; Steiner, D.F. Regulatory roles of the P domain of the subtilisin-like prohormone convertases. J. Biol. Chem., 1998, 273(18), 11107-11114.
[http://dx.doi.org/10.1074/jbc.273.18.11107] [PMID: 9556596]
[67]
Thacker, C.; Rose, A.M. A look at the caenorhabditis elegans Kex2/subtilisin-like proprotein convertase family. BioEssays, 2000, 22(6), 545-553.
[http://dx.doi.org/10.1002/(SICI)1521-1878(200006)22:6< 545:AID-BIES7>3.0.CO;2-F] [PMID: 10842308]
[68]
Thomas, G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol., 2002, 3(10), 753-766.
[http://dx.doi.org/10.1038/nrm934] [PMID: 12360192]
[69]
Dahms, S.O.; Hardes, K.; Steinmetzer, T.; Than, M.E. X-ray Structures of the proprotein convertase furin bound with substrate analogue inhibitors reveal substrate specificity determinants beyond the S4 Pocket. Biochemistry, 2018, 57(6), 925-934.
[http://dx.doi.org/10.1021/acs.biochem.7b01124] [PMID: 29314830]
[70]
Roebroek, A.J.M.; Schalken, J.A.; Bussemakers, M.J.G.; van Heerikhuizen, H.; Onnekink, C.; Debruyne, F.M.J.; Bloemers, H.P.J.; Van de Ven, W.J.M. Characterization of human c-fes/fps reveals a new transcription unit (fur) in the immediately upstream region of the proto-oncogene. Mol. Biol. Rep., 1986, 11(2), 117-125.
[http://dx.doi.org/10.1007/BF00364823] [PMID: 3488499]
[71]
Rehemtulla, A.; Dorner, A.J.; Kaufman, R.J. Regulation of PACE propeptide-processing activity: requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation. Proc. Natl. Acad. Sci. USA, 1992, 89(17), 8235-8239.
[http://dx.doi.org/10.1073/pnas.89.17.8235] [PMID: 1325651]
[72]
Anderson, E.D.; Molloy, S.S.; Jean, F.; Fei, H.; Shimamura, S.; Thomas, G. The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation. J. Biol. Chem., 2002, 277(15), 12879-12890.
[http://dx.doi.org/10.1074/jbc.M108740200] [PMID: 11799113]
[73]
Davey, J.; Davis, K.; Imai, Y.; Yamamoto, M.; Matthews, G. Isolation and characterization of krp, a dibasic endopeptidase required for cell viability in the fission yeast schizosaccharomyces pombe. EMBO J., 1994, 13(24), 5910-5921.
[http://dx.doi.org/10.1002/j.1460-2075.1994.tb06936.x] [PMID: 7813430]
[74]
Molloy, S.S.; Thomas, L.; VanSlyke, J.K.; Stenberg, P.E.; Thomas, G. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO J., 1994, 13(1), 18-33.
[http://dx.doi.org/10.1002/j.1460-2075.1994.tb06231.x] [PMID: 7508380]
[75]
Bresnahan, P.A.; Leduc, R.; Thomas, L.; Thorner, J.; Gibson, H.L.; Brake, A.J.; Barr, P.J.; Thomas, G. Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo. J. Cell Biol., 1990, 111(6 Pt 2), 2851-2859.
[http://dx.doi.org/10.1083/jcb.111.6.2851] [PMID: 2269657]
[76]
Takahashi, S.; Nakagawa, T.; Kasai, K.; Banno, T.; Duguay, S.J. Van de Ven, Wim J.M.; Murakami, K.; Nakayama, K. A Second mutant allele of furin in the processing-incompetent cell line, LoVo evidence for involvement of the homo B domain in autocatalytic activation. J. Biol. Chem., 1995, 270(44), 26565-26569.
[http://dx.doi.org/10.1074/jbc.270.44.26565] [PMID: 7592877]
[77]
Creemers, J.W.; Siezen, R.J.; Roebroek, A.J.; Ayoubi, T.A.; Huylebroeck, D.; Van de Ven, W.J. Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis. J. Biol. Chem., 1993, 268(29), 21826-21834.
[http://dx.doi.org/10.1016/S0021-9258(20)80616-4] [PMID: 8408037]
[78]
Leduc, R.; Molloy, S.S.; Thorne, B.A.; Thomas, G. Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. J. Biol. Chem., 1992, 267(20), 14304-14308.
[http://dx.doi.org/10.1016/S0021-9258(19)49712-3] [PMID: 1629222]
[79]
Than, M.E.; Henrich, S.; Bourenkov, G.P.; Bartunik, H.D.; Huber, R.; Bode, W. The endoproteinase furin contains two essential Ca2+ ions stabilizing its N-terminus and the unique S1 specificity pocket. Acta Crystallogr. D Biol. Crystallogr., 2005, 61(Pt 5), 505-512.
[http://dx.doi.org/10.1107/S0907444905002556] [PMID: 15858259]
[80]
Dahms, S.O.; Arciniega, M.; Steinmetzer, T.; Huber, R.; Than, M.E. Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism. Proc. Natl. Acad. Sci. USA, 2016, 113(40), 11196-11201.
[http://dx.doi.org/10.1073/pnas.1613630113] [PMID: 27647913]
[81]
Seidah, N.G.; Chrétien, M. Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res., 1999, 848(1-2), 45-62.
[http://dx.doi.org/10.1016/S0006-8993(99)01909-5] [PMID: 10701998]
[82]
Molloy, S.S.; Bresnahan, P.A.; Leppla, S.H.; Klimpel, K.R.; Thomas, G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem., 1992, 267(23), 16396-16402.
[http://dx.doi.org/10.1016/S0021-9258(18)42016-9] [PMID: 1644824]
[83]
Walker, J.A.; Molloy, S.S.; Thomas, G.; Sakaguchi, T.; Yoshida, T.; Chambers, T.M.; Kawaoka, Y. Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus. J. Virol., 1994, 68(2), 1213-1218.
[http://dx.doi.org/10.1128/jvi.68.2.1213-1218.1994] [PMID: 8289354]
[84]
Molloy, S.S.; Anderson, E.D.; Jean, F.; Thomas, G. Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. Trends Cell Biol., 1999, 9(1), 28-35.
[http://dx.doi.org/10.1016/S0962-8924(98)01382-8] [PMID: 10087614]
[85]
Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem., 2003, 72(1), 137-174.
[http://dx.doi.org/10.1146/annurev.biochem.72.121801.161712] [PMID: 12543708]
[86]
Wu, Y.; Yakar, S.; Zhao, L.; Hennighausen, L.; LeRoith, D. Circulating insulin-like growth factor-I levels regulate colon cancer growth and metastasis. Cancer Res., 2002, 62(4), 1030-1035.
[PMID: 11861378]
[87]
Klimpel, K.R.; Molloy, S.S.; Thomas, G.; Leppla, S.H. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc. Natl. Acad. Sci. USA, 1992, 89(21), 10277-10281.
[http://dx.doi.org/10.1073/pnas.89.21.10277] [PMID: 1438214]
[88]
Gordon, V.M.; Benz, R.; Fujii, K.; Leppla, S.H.; Tweten, R.K. Clostridium septicum alpha-toxin is proteolytically activated by furin. Infect. Immun., 1997, 65(10), 4130-4134.
[http://dx.doi.org/10.1128/iai.65.10.4130-4134.1997] [PMID: 9317018]
[89]
Jin, W.; Fuki, I.V.; Seidah, N.G.; Benjannet, S.; Glick, J.M.; Rader, D.J. Proprotein convertases [corrected] are responsible for proteolysis and inactivation of endothelial lipase. J. Biol. Chem., 2005, 280(44), 36551-36559.
[http://dx.doi.org/10.1074/jbc.M502264200] [PMID: 16109723]
[90]
Essalmani, R.; Susan-Resiga, D.; Chamberland, A.; Abifadel, M.; Creemers, J.W.; Boileau, C.; Seidah, N.G.; Prat, A. In vivo evidence that furin from hepatocytes inactivates PCSK9. J. Biol. Chem., 2011, 286(6), 4257-4263.
[http://dx.doi.org/10.1074/jbc.M110.192104] [PMID: 21147780]
[91]
Roebroek, A.J.M.; Umans, L.; Pauli, I.G.L.; Robertson, E.J.; van Leuven, F.; Van de Ven, W.J.M.; Constam, D.B. Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin. Development, 1998, 125(24), 4863-4876.
[http://dx.doi.org/10.1242/dev.125.24.4863] [PMID: 9811571]
[92]
Lee, R. Regulation of cell survival by secreted proneurotrophins. Science, 2001, 294(5548), 1945-1948.
[http://dx.doi.org/10.1126/science.1065057] [PMID: 11729324]
[93]
Bassi, D.E.; Mahloogi, H.; Al-Saleem, L.; Lopez De Cicco, R.; Ridge, J.A.; Klein-Szanto, A.J.P. Elevated furin expression in aggressive human head and neck tumors and tumor cell lines. Mol. Carcinog., 2001, 31(4), 224-232.
[http://dx.doi.org/10.1002/mc.1057] [PMID: 11536372]
[94]
Mbikay, M.; Sirois, F.; Yao, J.; Seidah, N.G.; Chrétien, M. Comparative analysis of expression of the proprotein convertases furin, PACE4, PC1 and PC2 in human lung tumours. Br. J. Cancer, 1997, 75(10), 1509-1514.
[http://dx.doi.org/10.1038/bjc.1997.258] [PMID: 9166946]
[95]
Braun, E.; Sauter, D. Furin-mediated protein processing in infectious diseases and cancer. Clin. Transl. Immunology, 2019, 8(8)e1073
[http://dx.doi.org/10.1002/cti2.1073] [PMID: 31406574]
[96]
Hallenberger, S.; Bosch, V.; Angliker, H.; Shaw, E.; Klenk, H-D.; Garten, W. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature, 1992, 360(6402), 358-361.
[http://dx.doi.org/10.1038/360358a0] [PMID: 1360148]
[97]
Rabaan, A.A.; Al-Ahmed, S.H.; Haque, S.; Sah, R.; Tiwari, R.; Malik, Y.S.; Dhama, K.; Yatoo, M.I.; Bonilla-Aldana, D.K.; Rodriguez-Morales, A.J. SARS-CoV-2, SARS-CoV, and MERS-COV: a comparative overview. Infez. Med., 2020, 28(2), 174-184.
[PMID: 32275259]
[98]
Rossi, G.A.; Sacco, O.; Mancino, E.; Cristiani, L.; Midulla, F. 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, 2020, 48(5), 665-669.
[http://dx.doi.org/10.1007/s15010-020-01486-5] [PMID: 32737833]
[99]
Chen, Y.; Liu, Q.; Guo, D. Emerging coronaviruses: genome structure, replication, and pathogenesis. J. Med. Virol., 2020, 92(4), 418-423.
[http://dx.doi.org/10.1002/jmv.25681] [PMID: 31967327]
[100]
Tortorici, M.A.; Veesler, D. Structural insights into coronavirus entry. Adv. Virus Res., 2019, 105, 93-116.
[http://dx.doi.org/10.1016/bs.aivir.2019.08.002] [PMID: 31522710]
[101]
Izaguirre, G. The proteolytic regulation of virus cell entry by furin and other proprotein convertases. Viruses, 2019, 11(9), 837.
[http://dx.doi.org/10.3390/v11090837] [PMID: 31505793]
[102]
Shang, J.; Wan, Y.; Luo, C.; Ye, G.; Geng, Q.; Auerbach, A.; Li, F. Cell entry mechanisms of SARS-CoV-2. Proc. Natl. Acad. Sci. USA, 2020, 117(21), 11727-11734.
[http://dx.doi.org/10.1073/pnas.2003138117] [PMID: 32376634]
[103]
Coutard, B.; Valle, C.; de Lamballerie, X.; Canard, B.; Seidah, N.G.; Decroly, E. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. Antiviral Res., 2020, 176104742
[http://dx.doi.org/10.1016/j.antiviral.2020.104742] [PMID: 32057769]
[104]
Hoffmann, M.; Kleine-Weber, H.; Pöhlmann, S. A Multibasic cleavage site in the spike protein of SARS-CoV-2 is essential for infection of human lung cells. Mol. Cell, 2020, 78(4), 779-784.e5.
[http://dx.doi.org/10.1016/j.molcel.2020.04.022] [PMID: 32362314]
[105]
Millet, J.K.; Whittaker, G.R. Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein. Proc. Natl. Acad. Sci. USA, 2014, 111(42), 15214-15219.
[http://dx.doi.org/10.1073/pnas.1407087111] [PMID: 25288733]
[106]
Henrich, S.; Cameron, A.; Bourenkov, G.P.; Kiefersauer, R.; Huber, R.; Lindberg, I.; Bode, W.; Than, M.E. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat. Struct. Biol., 2003, 10(7), 520-526.
[http://dx.doi.org/10.1038/nsb941] [PMID: 12794637]
[107]
Cheng, Y-W.; Chao, T-L.; Li, C-L.; Chiu, M-F.; Kao, H-C.; Wang, S-H.; Pang, Y-H.; Lin, C-H.; Tsai, Y-M.; Lee, W.-H.; Tao, M-H.; Ho, T-C.; Wu, P-Y.; Jang, L-T.; Chen, P-J.; Chang, S-Y.; Yeh, S-H. Furin inhibitors block SARS-CoV-2 spike protein cleavage to suppress virus production and cytopathic effects. Cell Rep., 2020, 33(2)108254
[http://dx.doi.org/10.1016/j.celrep.2020.108254] [PMID: 33007239]
[108]
Remacle, A.G.; Shiryaev, S.A.; Oh, E.S.; Cieplak, P.; Srinivasan, A.; Wei, G.; Liddington, R.C.; Ratnikov, B.I.; Parent, A.; Desjardins, R.; Day, R.; Smith, J.W.; Lebl, M.; Strongin, A.Y. Substrate cleavage analysis of furin and related proprotein convertases. A comparative study. J. Biol. Chem., 2008, 283(30), 20897-20906.
[http://dx.doi.org/10.1074/jbc.M803762200] [PMID: 18505722]
[109]
Shieh, W.J.; Hsiao, C.H.; Paddock, C.D.; Guarner, J.; Goldsmith, C.S.; Tatti, K.; Packard, M.; Mueller, L.; Wu, M.Z.; Rollin, P.; Su, I.J.; Zaki, S.R. Immunohistochemical, in situ hybridization, and ultrastructural localization of SARS-associated coronavirus in lung of a fatal case of severe acute respiratory syndrome in Taiwan. Hum. Pathol., 2005, 36(3), 303-309.
[http://dx.doi.org/10.1016/j.humpath.2004.11.006] [PMID: 15791576]
[110]
Komiyama, T.; Swanson, J.A.; Fuller, R.S. Protection from anthrax toxin-mediated killing of macrophages by the combined effects of furin inhibitors and chloroquine. Antimicrob. Agents Chemother., 2005, 49(9), 3875-3882.
[http://dx.doi.org/10.1128/AAC.49.9.3875-3882.2005] [PMID: 16127065]
[111]
Willstätter, R.; Bemann, E. Über die proteasen der magenschleimhaut. Physiol. Chem., 1929, 180, 127-143.
[http://dx.doi.org/10.1515/bchm2.1929.180.1-3.127]
[112]
Otto, H.H.; Schirmeister, T. Cysteine proteases and their inhibitors. Chem. Rev., 1997, 97(1), 133-172.
[http://dx.doi.org/10.1021/cr950025u] [PMID: 11848867]
[113]
McGrath, M.E. The lysosomal cysteine proteases. Annu. Rev. Biophys. Biomol. Struct., 1999, 28, 181-204.
[http://dx.doi.org/10.1146/annurev.biophys.28.1.181] [PMID: 10410800]
[114]
Rawlings, N.D.; Barrett, A.J. Families of cysteine peptidases. Methods Enzymol., 1994, 244, 461-486.
[http://dx.doi.org/10.1016/0076-6879(94)44034-4] [PMID: 7845226]
[115]
Simmons, G.; Bertram, S.; Glowacka, I.; Steffen, I.; Chaipan, C.; Agudelo, J.; Lu, K.; Rennekamp, A.J.; Hofmann, H.; Bates, P.; Pöhlmann, S. Different host cell proteases activate the SARS-coronavirus spike-protein for cell-cell and virus-cell fusion. Virology, 2011, 413(2), 265-274.
[http://dx.doi.org/10.1016/j.virol.2011.02.020] [PMID: 21435673]
[116]
Simmons, G.; Gosalia, D.N.; Rennekamp, A.J.; Reeves, J.D.; Diamond, S.L.; Bates, P. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl. Acad. Sci. USA, 2005, 102(33), 11876-11881.
[http://dx.doi.org/10.1073/pnas.0505577102] [PMID: 16081529]
[117]
Simmons, G.; Zmora, P.; Gierer, S.; Heurich, A.; Pöhlmann, S. Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research. Antiviral Res., 2013, 100(3), 605-614.
[http://dx.doi.org/10.1016/j.antiviral.2013.09.028] [PMID: 24121034]
[118]
Huang, I-C.; Bosch, B.J.; Li, F.; Li, W.; Lee, K.H.; Ghiran, S.; Vasilieva, N.; Dermody, T.S.; Harrison, S.C.; Dormitzer, P.R.; Farzan, M.; Rottier, P.J.M.; Choe, H. SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells. J. Biol. Chem., 2006, 281(6), 3198-3203.
[http://dx.doi.org/10.1074/jbc.M508381200] [PMID: 16339146]
[119]
Millet, J.K.; Whittaker, G.R. Host cell proteases: critical determinants of coronavirus tropism and pathogenesis. Virus Res., 2015, 202, 120-134.
[http://dx.doi.org/10.1016/j.virusres.2014.11.021] [PMID: 25445340]
[120]
Mason, R.W.; Green, G.D.J.; Barrett, A.J. Human liver cathepsin L. Biochem. J., 1985, 226(1), 233-241.
[http://dx.doi.org/10.1042/bj2260233] [PMID: 3977867]
[121]
Chauhan, S.S.; Popescu, N.C.; Ray, D.; Fleischmann, R.; Gottesman, M.M.; Troen, B.R. Cloning, genomic organization, and chromosomal localization of human cathepsin L. J. Biol. Chem., 1993, 268(2), 1039-1045.
[http://dx.doi.org/10.1016/S0021-9258(18)54038-2] [PMID: 8419312]
[122]
Kirschke, H. Cathepsin L. Handb. Proteolytic Enzym., 2013, 2, pp. 1808-1817.
[http://dx.doi.org/10.1016/B978-0-12-382219-2.00410-5]
[123]
Dana, D.; Pathak, S.K. A review of small molecule inhibitors and functional probes of human cathepsin L. Molecules, 2020, 25(3), 698.
[http://dx.doi.org/10.3390/molecules25030698] [PMID: 32041276]
[124]
Saito, S.; Takahashi-Sasaki, N.; Araki, W. Identification and characterization of a novel human APH-1b splice variant lacking exon 4. Biochem. Biophys. Res. Commun., 2005, 330(4), 1068-1072.
[http://dx.doi.org/10.1016/j.bbrc.2005.03.096] [PMID: 15823552]
[125]
Caserman, S.; Kenig, S.; Sloane, B.F.; Lah, T.T.; Cathepsin, L. Cathepsin L splice variants in human breast cell lines. Biol. Chem., 2006, 387(5), 629-634.
[http://dx.doi.org/10.1515/BC.2006.080] [PMID: 16740135]
[126]
Jean, D.; Guillaume, N.; Frade, R.; Inserm, U.; Inserm, C.; Saint-antoine, H.; Saint-antoine, F. Characterization of human cathepsin L promoter and identification of binding sites for NF-Y, Sp1 and Sp3 that are essential for its activity. Biochem. J., 2002, 361(Pt 1), 173-184.
[http://dx.doi.org/10.1042/bj3610173] [PMID: 11742542]
[127]
Sansanwal, P.; Shukla, A.A.; Das, T.K.; Chauhan, S.S. Truncated human cathepsin L, encoded by a novel splice variant, exhibits altered subcellular localization and cytotoxicity. Protein Pept. Lett., 2010, 17(2), 238-245.
[http://dx.doi.org/10.2174/092986610790225932] [PMID: 19663777]
[128]
Seth, P.; Mahajan, V.S.; Chauhan, S.S. Transcription of human cathepsin L mRNA species hCATL B from a novel alternative promoter in the first intron of its gene. Gene, 2003, 321(1–2), 83-91.
[http://dx.doi.org/10.1016/S0378-1119(03)00838-2] [PMID: 14636995]
[129]
Rescheleit, D.K.; Rommerskirch, W.J.; Wiederanders, B. Sequence analysis and distribution of two new human cathepsin L splice variants. FEBS Lett., 1996, 394(3), 345-348.
[http://dx.doi.org/10.1016/0014-5793(96)00986-6] [PMID: 8830671]
[130]
Lang, L.; Reitman, M.; Tang, J.; Roberts, R.M.; Kornfeld, S. Lysosomal enzyme phosphorylation. Recognition of a protein-dependent determinant allows specific phosphorylation of oligosaccharides present on lysosomal enzymes. J. Biol. Chem., 1984, 259(23), 14663-14671.
[http://dx.doi.org/10.1016/S0021-9258(17)42654-8] [PMID: 6094568]
[131]
Carmona, E.; Dufour, E.; Plouffe, C.; Takebe, S.; Mason, P.; Mort, J.S.; Ménard, R. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry, 1996, 35(25), 8149-8157.
[http://dx.doi.org/10.1021/bi952736s] [PMID: 8679567]
[132]
Salminen, A.; Gottesman, M.M. Inhibitor studies indicate that active cathepsin L is probably essential to its own processing in cultured fibroblasts. Biochem. J., 1990, 272(1), 39-44.
[http://dx.doi.org/10.1042/bj2720039] [PMID: 2264836]
[133]
Jerala, R.; Zerovnik, E.; Kidric, J.; Turk, V. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. J. Biol. Chem., 1998, 273(19), 11498-11504.
[http://dx.doi.org/10.1074/jbc.273.19.11498] [PMID: 9565563]
[134]
Mason, R.W.; Gal, S.; Gottesman, M.M. The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J., 1987, 248(2), 449-454.
[http://dx.doi.org/10.1042/bj2480449] [PMID: 3435459]
[135]
McDonald, J.K.; Kadkhodayan, S.; Cathepsin, L. Cathepsin L--a latent proteinase in guinea pig sperm. Biochem. Biophys. Res. Commun., 1988, 151(2), 827-835.
[http://dx.doi.org/10.1016/S0006-291X(88)80356-5] [PMID: 3348813]
[136]
McDonald, J.K.; Emerick, J.M.C. Purification and characterization of procathepsin L, a self-processing zymogen of guinea pig spermatozoa that acts on a cathepsin D assay substrate. Arch. Biochem. Biophys., 1995, 323(2), 409-422.
[http://dx.doi.org/10.1006/abbi.1995.0062] [PMID: 7487106]
[137]
Fairhead, M.; Kelly, S.M.; van der Walle, C.F. A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation. Biochem. Biophys. Res. Commun., 2008, 366(3), 862-867.
[http://dx.doi.org/10.1016/j.bbrc.2007.12.062] [PMID: 18086562]
[138]
Kihara, M.; Kakegawa, H.; Matano, Y.; Murata, E.; Tsuge, H.; Kido, H.; Katunuma, N. Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L. Biol. Chem., 2002, 383(12), 1925-1929.
[http://dx.doi.org/10.1515/BC.2002.216] [PMID: 12553729]
[139]
Mason, R.W.; Massey, S.D. Surface activation of pro-cathepsin L. Biochem. Biophys. Res. Commun., 1992, 189(3), 1659-1666.
[http://dx.doi.org/10.1016/0006-291X(92)90268-P] [PMID: 1482371]
[140]
Nishimura, Y.; Kawabata, T.; Furuno, K.; Kato, K. Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosomes. Arch. Biochem. Biophys., 1989, 271(2), 400-406.
[http://dx.doi.org/10.1016/0003-9861(89)90289-0] [PMID: 2658811]
[141]
Wiederanders, B.; Kirschke, H. The processing of a cathepsin L precursor in vitro. Arch. Biochem. Biophys., 1989, 272(2), 516-521.
[http://dx.doi.org/10.1016/0003-9861(89)90247-6] [PMID: 2751313]
[142]
Hara, K.; Kominami, E.; Katunuma, N. Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages. FEBS Lett., 1988, 231(1), 229-231.
[http://dx.doi.org/10.1016/0014-5793(88)80737-3] [PMID: 3360127]
[143]
Ritonja, A.; Popović, T.; Kotnik, M.; Machleidt, W.; Turk, V. Amino acid sequences of the human kidney cathepsins H and L. FEBS Lett., 1988, 228(2), 341-345.
[http://dx.doi.org/10.1016/0014-5793(88)80028-0] [PMID: 3342889]
[144]
Ishidoh, K.; Kominami, E. Multi-step processing of procathepsin L in vitro. FEBS Lett., 1994, 352(3), 281-284.
[http://dx.doi.org/10.1016/0014-5793(94)00924-4] [PMID: 7925987]
[145]
Nishimura, Y.; Furuno, K.; Kato, K. Biosynthesis and processing of lysosomal cathepsin L in primary cultures of rat hepatocytes. Arch. Biochem. Biophys., 1988, 263(1), 107-116.
[http://dx.doi.org/10.1016/0003-9861(88)90618-2] [PMID: 3369855]
[146]
Coulombe, R.; Grochulski, P.; Sivaraman, J.; Ménard, R.; Mort, J.S.; Cygler, M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J., 1996, 15(20), 5492-5503.
[http://dx.doi.org/10.1002/j.1460-2075.1996.tb00934.x] [PMID: 8896443]
[147]
Brömme, D.; Bonneau, P.R.; Lachance, P.; Storer, A.C. Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity. J. Biol. Chem., 1994, 269(48), 30238-30242.
[http://dx.doi.org/10.1016/S0021-9258(18)43803-3] [PMID: 7982933]
[148]
Gal, S.; Gottesman, M.M. The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificity. Biochem. Biophys. Res. Commun., 1986, 139(1), 156-162.
[http://dx.doi.org/10.1016/S0006-291X(86)80093-6] [PMID: 3533059]
[149]
Kärgel, H-J.; Dettmer, R.; Etzold, G.; Kirschke, H.; Bohley, P.; Langner, J. Action of cathepsin L on the oxidized B-chain of bovine insulin. FEBS Lett., 1980, 114(2), 257-260.
[http://dx.doi.org/10.1016/0014-5793(80)81128-8] [PMID: 6993230]
[150]
Kirschke, H.; Kembhavi, A.A.; Bohley, P.; Barrett, A.J. Action of rat liver cathepsin L on collagen and other substrates. Biochem. J., 1982, 201(2), 367-372.
[http://dx.doi.org/10.1042/bj2010367] [PMID: 7082295]
[151]
Portaro, F.C.V.; Santos, A.B.F.; Cezari, M.H.S.; Juliano, M.A.; Juliano, L.; Carmona, E. Probing the specificity of cysteine proteinases at subsites remote from the active site: analysis of P4, P3, P2′ and P3′ variations in extended substrates. Biochem. J., 2000, 347(Pt 1), 123-129.
[http://dx.doi.org/10.1042/bj3470123] [PMID: 10727410]
[152]
Rawlings, N.D.; Barrett, A.J.; Bateman, A. MEROPS: the peptidase database. Nucleic Acids Res., 2010, 38(Database issue)(Suppl. 1), D227-D233.
[http://dx.doi.org/10.1093/nar/gkp971] [PMID: 19892822]
[153]
Choe, Y.; Leonetti, F.; Greenbaum, D.C.; Lecaille, F.; Bogyo, M.; Brömme, D.; Ellman, J.A.; Craik, C.S. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem., 2006, 281(18), 12824-12832.
[http://dx.doi.org/10.1074/jbc.M513331200] [PMID: 16520377]
[154]
Bohley, P.; Seglen, P.O. Proteases and proteolysis in the lysosome. Experientia, 1992, 48(2), 151-157.
[http://dx.doi.org/10.1007/BF01923508] [PMID: 1740187]
[155]
Petermann, I.; Mayer, C.; Stypmann, J.; Biniossek, M.L.; Tobin, D.J.; Engelen, M.A.; Dandekar, T.; Grune, T.; Schild, L.; Peters, C.; Reinheckel, T. Lysosomal, cytoskeletal, and metabolic alterations in cardiomyopathy of cathepsin L knockout mice. FASEB J., 2006, 20(8), 1266-1268.
[http://dx.doi.org/10.1096/fj.05-5517fje] [PMID: 16636100]
[156]
Spira, D.; Stypmann, J.; Tobin, D.J.; Petermann, I.; Mayer, C.; Hagemann, S.; Vasiljeva, O.; Günther, T.; Schüle, R.; Peters, C.; Reinheckel, T. Cell type-specific functions of the lysosomal protease cathepsin L in the heart. J. Biol. Chem., 2007, 282(51), 37045-37052.
[http://dx.doi.org/10.1074/jbc.M703447200] [PMID: 17942402]
[157]
Tang, Q.; Cai, J.; Shen, D.; Bian, Z.; Yan, L.; Wang, Y.X.; Lan, J.; Zhuang, G.Q.; Ma, W.Z.; Wang, W. Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3β signaling. J. Mol. Med. (Berl.), 2009, 87(3), 249-260.
[http://dx.doi.org/10.1007/s00109-008-0423-2] [PMID: 19096818]
[158]
Stypmann, J.; Gläser, K.; Roth, W.; Tobin, D.J.; Petermann, I.; Matthias, R.; Mönnig, G.; Haverkamp, W.; Breithardt, G.; Schmahl, W.; Peters, C.; Reinheckel, T. Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L. Proc. Natl. Acad. Sci. USA, 2002, 99(9), 6234-6239.
[http://dx.doi.org/10.1073/pnas.092637699] [PMID: 11972068]
[159]
Nakagawa, T.; Roth, W.; Wong, P.; Nelson, A.; Farr, A.; Deussing, J.; Villadangos, J.A.; Ploegh, H.; Peters, C.; Rudensky, A.Y.; Cathepsin, L. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science, 1998, 280(5362), 450-453.
[http://dx.doi.org/10.1126/science.280.5362.450] [PMID: 9545226]
[160]
Hsieh, C.S.; deRoos, P.; Honey, K.; Beers, C.; Rudensky, A.Y. A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J. Immunol., 2002, 168(6), 2618-2625.
[http://dx.doi.org/10.4049/jimmunol.168.6.2618] [PMID: 11884425]
[161]
Lombardi, G.; Burzyn, D.; Mundin, J.; Berguer, P.; Bekinschtein, P.; Costa, H.; Castillo, L.F.; Goldman, A.; Meiss, R.; Piazzon, I.; Nepomnaschy, I. Thymic output and of peripheral T cell number 1. J. Immunol., 2005, 17, 7022-7032.
[http://dx.doi.org/10.4049/jimmunol.174.11.7022] [PMID: 15905545]
[162]
Sevenich, L.; Hagemann, S.; Stoeckle, C.; Tolosa, E.; Peters, C.; Reinheckel, T. Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice. Biochimie, 2010, 92(11), 1674-1680.
[http://dx.doi.org/10.1016/j.biochi.2010.03.014] [PMID: 20347002]
[163]
Hsing, L.C.; Kirk, E.A.; McMillen, T.S.; Hsiao, S.H.; Caldwell, M.; Houston, B.; Rudensky, A.Y.; LeBoeuf, R.C. Roles for cathepsins S, L, and B in insulitis and diabetes in the NOD mouse. J. Autoimmun., 2010, 34(2), 96-104.
[http://dx.doi.org/10.1016/j.jaut.2009.07.003] [PMID: 19664906]
[164]
Maehr, R.; Mintern, J.D.; Herman, A.E.; Lennon-Duménil, A.M.; Mathis, D.; Benoist, C.; Ploegh, H.L. Cathepsin L is essential for onset of autoimmune diabetes in NOD mice. J. Clin. Invest., 2005, 115(10), 2934-2943.
[http://dx.doi.org/10.1172/JCI25485] [PMID: 16184198]
[165]
Yamada, A.; Ishimaru, N.; Arakaki, R.; Katunuma, N.; Hayashi, Y.; Cathepsin, L. Cathepsin L inhibition prevents murine autoimmune diabetes via suppression of CD8(+) T cell activity. PLoS One, 2010, 5(9)e12894
[http://dx.doi.org/10.1371/journal.pone.0012894] [PMID: 20877570]
[166]
Delaissé, J.M.; Ledent, P.; Vaes, G. Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase. Biochem. J., 1991, 279(Pt 1), 167-174.
[http://dx.doi.org/10.1042/bj2790167] [PMID: 1930136]
[167]
Delaissé, J-M.; Eeckhout, Y.; Vaes, G. In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption. Biochem. Biophys. Res. Commun., 1984, 125(2), 441-447.
[http://dx.doi.org/10.1016/0006-291X(84)90560-6] [PMID: 6393977]
[168]
Debari, K.; Sasaki, T.; Udagawa, N.; Rifkin, B.R. An ultrastructural evaluation of the effects of cysteine-proteinase inhibitors on osteoclastic resorptive functions. Calcif. Tissue Int., 1995, 56(6), 566-570.
[http://dx.doi.org/10.1007/BF00298591] [PMID: 7648488]
[169]
Reinheckel, T.; Hagemann, S.; Dollwet-Mack, S.; Martinez, E.; Lohmüller, T.; Zlatkovic, G.; Tobin, D.J.; Maas-Szabowski, N.; Peters, C. The lysosomal cysteine protease cathepsin L regulates keratinocyte proliferation by control of growth factor recycling. J. Cell Sci., 2005, 118(Pt 15), 3387-3395.
[http://dx.doi.org/10.1242/jcs.02469] [PMID: 16079282]
[170]
Hagemann, S.; Günther, T.; Dennemärker, J.; Lohmüller, T.; Brömme, D.; Schüle, R.; Peters, C.; Reinheckel, T. The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles. Eur. J. Cell Biol., 2004, 83(11-12), 775-780.
[http://dx.doi.org/10.1078/0171-9335-00404] [PMID: 15679121]
[171]
Luft, F.C. From furless to heartless-unraveling the diverse functions of cathepsin L. J. Mol. Med. (Berl.), 2009, 87(3), 225-227.
[http://dx.doi.org/10.1007/s00109-009-0438-3] [PMID: 19169657]
[172]
Roth, W.; Deussing, J.; Botchkarev, V.A.; Pauly-Evers, M.; Saftig, P.; Hafner, A.; Schmidt, P.; Schmahl, W.; Scherer, J.; Anton-Lamprecht, I.; Von Figura, K.; Paus, R.; Peters, C. Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling. FASEB J., 2000, 14(13), 2075-2086.
[http://dx.doi.org/10.1096/fj.99-0970com] [PMID: 11023992]
[173]
Tobin, D.J.; Foitzik, K.; Reinheckel, T.; Mecklenburg, L.; Botchkarev, V.A.; Peters, C.; Paus, R. The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling. Am. J. Pathol., 2002, 160(5), 1807-1821.
[http://dx.doi.org/10.1016/S0002-9440(10)61127-3] [PMID: 12000732]
[174]
Zeeuwen, P.L.J.M.; van Vlijmen-Willems, I.M.J.J.; Cheng, T.; Rodijk-Olthuis, D.; Hitomi, K.; Hara-Nishimura, I.; John, S.; Smyth, N.; Reinheckel, T.; Hendriks, W.J.A.J.; Schalkwijk, J.; Cst, C.M.E. The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea. FASEB J., 2010, 24(10), 3744-3755.
[http://dx.doi.org/10.1096/fj.10-155879] [PMID: 20495178]
[175]
Kawase, M.; Shirato, K.; van der Hoek, L.; Taguchi, F.; Matsuyama, S. Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry. J. Virol., 2012, 86(12), 6537-6545.
[http://dx.doi.org/10.1128/JVI.00094-12] [PMID: 22496216]
[176]
Shirato, K.; Kawase, M.; Matsuyama, S. Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2. J. Virol., 2013, 87(23), 12552-12561.
[http://dx.doi.org/10.1128/JVI.01890-13] [PMID: 24027332]
[177]
Guo, X.Q.; Qiu, K.Y.; De Feng, X. Studies on the Kinetics and Initiation Mechanism of acrylamide polymerization using persulfatehliphatic diamine systems as initiator. Makromol. Chem., 1990, 587, 577-587.
[http://dx.doi.org/10.1002/macp.1990.021910313]
[178]
Ou, X.; Liu, Y.; Lei, X.; Li, P.; Mi, D.; Ren, L.; Guo, L.; Guo, R.; Chen, T.; Hu, J.; Xiang, Z.; Mu, Z.; Chen, X.; Chen, J.; Hu, K.; Jin, Q.; Wang, J.; Qian, Z. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat. Commun., 2020, 11(1), 1620.
[http://dx.doi.org/10.1038/s41467-020-15562-9] [PMID: 32221306]
[179]
Elshabrawy, H.A.; Fan, J.; Haddad, C.S.; Ratia, K.; Broder, C.C.; Caffrey, M.; Prabhakar, B.S. Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assay. J. Virol., 2014, 88(8), 4353-4365.
[http://dx.doi.org/10.1128/JVI.03050-13] [PMID: 24501399]
[180]
Vargas-Alarcón, G.; Posadas-Sánchez, R.; Ramírez-Bello, J. Variability in genes related to SARS-CoV-2 entry into host cells (ACE2, TMPRSS2, TMPRSS11A, ELANE, and CTSL) and its potential use in association studies. Life Sci., 2020, 260118313
[http://dx.doi.org/10.1016/j.lfs.2020.118313] [PMID: 32835700]
[181]
Bertram, S.; Glowacka, I.; Müller, M.A.; Lavender, H.; Gnirss, K.; Nehlmeier, I.; Niemeyer, D.; He, Y.; Simmons, G.; Drosten, C.; Soilleux, E.J.; Jahn, O.; Steffen, I.; Pöhlmann, S. Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease. J. Virol., 2011, 85(24), 13363-13372.
[http://dx.doi.org/10.1128/JVI.05300-11] [PMID: 21994442]
[182]
Mingo, R.M.; Simmons, J.A.; Shoemaker, C.J.; Nelson, E.A.; Schornberg, K.L.; D’Souza, R.S.; Casanova, J.E.; White, J.M. Ebola virus and severe acute respiratory syndrome coronavirus display late cell entry kinetics: evidence that transport to NPC1+ endolysosomes is a rate-defining step. J. Virol., 2015, 89(5), 2931-2943.
[http://dx.doi.org/10.1128/JVI.03398-14] [PMID: 25552710]
[183]
Blaess, M.; Kaiser, L.; Sauer, M.; Csuk, R.; Deigner, H.P. COVID-19/SARS-CoV-2 infection: lysosomes and lysosomotropism implicate new treatment strategies and personal risks. Int. J. Mol. Sci., 2020, 21(14), 4953.
[http://dx.doi.org/10.3390/ijms21144953] [PMID: 32668803]
[184]
Liu, T.; Luo, S.; Libby, P.; Shi, G.P. Cathepsin L-selective inhibitors: a potentially promising treatment for COVID-19 patients. Pharmacol. Ther., 2020, 213107587
[http://dx.doi.org/10.1016/j.pharmthera.2020.107587] [PMID: 32470470]
[185]
Shenoy, R.T.; Sivaraman, J. Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors. J. Struct. Biol., 2011, 173(1), 14-19.
[http://dx.doi.org/10.1016/j.jsb.2010.09.007] [PMID: 20850545]
[186]
Gupta, A.; Pradhan, A.; Maurya, V.K.; Kumar, S.; Theengh, A.; Puri, B.; Saxena, S.K. Therapeutic approaches for SARS-CoV-2 infection. Methods, 2021, 195, 29-43.
[http://dx.doi.org/10.1016/j.ymeth.2021.04.026] [PMID: 33962011]
[187]
Zhou, Y.; Vedantham, P.; Lu, K.; Agudelo, J.; Carrion, R., Jr; Nunneley, J.W.; Barnard, D.; Pöhlmann, S.; McKerrow, J.H.; Renslo, A.R.; Simmons, G. Protease inhibitors targeting coronavirus and filovirus entry. Antiviral Res., 2015, 116, 76-84.
[http://dx.doi.org/10.1016/j.antiviral.2015.01.011] [PMID: 25666761]
[188]
Adedeji, A.O.; Severson, W.; Jonsson, C.; Singh, K.; Weiss, S.R.; Sarafianos, S.G. Novel inhibitors of severe acute respiratory syndrome coronavirus entry that act by three distinct mechanisms. J. Virol., 2013, 87(14), 8017-8028.
[http://dx.doi.org/10.1128/JVI.00998-13] [PMID: 23678171]
[189]
Shah, P.P.; Wang, T.; Kaletsky, R.L.; Myers, M.C.; Purvis, J.E.; Jing, H.; Huryn, D.M.; Greenbaum, D.C.; Smith, A.B., III; Bates, P.; Diamond, S.L. A small-molecule oxocarbazate inhibitor of human cathepsin L blocks severe acute respiratory syndrome and Ebola pseudotype virus infection into human embryonic kidney 293T cells. Mol. Pharmacol., 2010, 78(2), 319-324.
[http://dx.doi.org/10.1124/mol.110.064261] [PMID: 20466822]
[190]
Chen, Z.; Du, R.; Galvan Achi, J.M.; Rong, L.; Cui, Q. SARS-CoV-2 cell entry and targeted antiviral development. Acta Pharm. Sin. B, 2021, 11(12), 3879-3888.
[http://dx.doi.org/10.1016/j.apsb.2021.05.007] [PMID: 34002130]
[191]
Kamboj, R.C.; Raghav, N.; Mittal, A.; Khurana, S.; Sadana, R.; Singh, H. Effects of some antituberculous and anti-leprotic drugs on cathepsins B, H and L. Indian J. Clin. Biochem., 2003, 18(2), 39-47.
[http://dx.doi.org/10.1007/BF02867366] [PMID: 23105391]
[192]
Cai, J.; Zhong, H.; Wu, J.; Chen, R.F.; Yang, H.; Al-Abed, Y.; Li, Y.; Li, X.; Jiang, W.; Montenegro, M.F.; Yuan, H.; Billiar, T.; Chen, A.F.; Cathepsin, L. Cathepsin L promotes vascular intimal hyperplasia after arterial injury. Mol. Med., 2017, 23, 92-100.
[http://dx.doi.org/10.2119/molmed.2016.00222] [PMID: 28332696]
[193]
Ting, P.; F, H.; Jun, L.; Weiwei, L.; Yingtong, L.; Yaochang, Y.; Tao, Y.; Rong, L.; Xu, Z.; Fan, Z.; Bingfeng, L.; Kai, D.; Xin, H.; Hui, Z.; Yiwen, Z. Teicoplanin potently blocks the cell entry of 2019-NCoV. PREPRINT-bioRxiv, 2020. ID: ppbiorxiv-935387.
[194]
Zhou, N.; Pan, T.; Zhang, J.; Li, Q.; Zhang, X.; Bai, C.; Huang, F.; Peng, T.; Zhang, J.; Liu, C.; Tao, L.; Zhang, H. Glycopeptide antibiotics potently inhibit cathepsin L in the late endosome/lysosome and block the entry of Ebola virus, Middle East respiratory syndrome coronavirus (MERS-CoV), and severe acute respiratory syndrome coronavirus (SARS-CoV). J. Biol. Chem., 2016, 291(17), 9218-9232.
[http://dx.doi.org/10.1074/jbc.M116.716100] [PMID: 26953343]
[195]
Wang, M.; Cao, R.; Zhang, L.; Yang, X.; Liu, J.; Xu, M.; Shi, Z.; Hu, Z.; Zhong, W.; Xiao, G. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res., 2020, 30(3), 269-271.
[http://dx.doi.org/10.1038/s41422-020-0282-0] [PMID: 32020029]
[196]
Tang, T.T.; Lv, L.L.; Pan, M.M.; Wen, Y.; Wang, B.; Li, Z.L.; Wu, M.; Wang, F.M.; Crowley, S.D.; Liu, B.C. Hydroxychloroquine attenuates renal ischemia/reperfusion injury by inhibiting cathepsin mediated NLRP3 inflammasome activation. Cell Death Dis., 2018, 9(3), 351.
[http://dx.doi.org/10.1038/s41419-018-0378-3] [PMID: 29500339]
[197]
Shivanna, V.; Kim, Y.; Chang, K.O.S. Endosomal acidification and cathepsin L activity is required for calicivirus replication. Virology, 2014, 464-465, 287-295.
[http://dx.doi.org/10.1016/j.virol.2014.07.025] [PMID: 25108379]
[198]
Porotto, M.; Orefice, G.; Yokoyama, C.C.; Mungall, B.A.; Realubit, R.; Sganga, M.L.; Aljofan, M.; Whitt, M.; Glickman, F.; Moscona, A. Simulating henipavirus multicycle replication in a screening assay leads to identification of a promising candidate for therapy. J. Virol., 2009, 83(10), 5148-5155.
[http://dx.doi.org/10.1128/JVI.00164-09] [PMID: 19264786]
[199]
Tönnesmann, E.; Kandolf, R.; Lewalter, T. Chloroquine cardiomyopathy - a review of the literature. Immunopharmacol. Immunotoxicol., 2013, 35(3), 434-442.
[http://dx.doi.org/10.3109/08923973.2013.780078] [PMID: 23635029]
[200]
Craik, C.S.; Largman, C.; Fletcher, T.; Roczniak, S.; Barr, P.J.; Fletterick, R.; Rutter, W.J. Redesigning trypsin: alteration of substrate specificity. Science, 1985, 228, 291-297.
[http://dx.doi.org/10.1126/science.3838593] [PMID: 3838593]
[201]
Schellenberger, V.; Turck, C.W.; Rutter, W.J. Role of the S′ subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, α-lytic protease, and cercarial protease from Schistosoma mansoni. Biochemistry, 1994, 33(14), 4251-4257.
[http://dx.doi.org/10.1021/bi00180a020] [PMID: 8155642]
[202]
Corey, D.R.; McGrath, M.E.; Vásquez, J.R.; Fletterick, R.J.; Craik, C.S. An alternate geometry for the catalytic triad of serine proteases. J. Am. Chem. Soc., 1992, 114(12), 4905-4907.
[http://dx.doi.org/10.1021/ja00038a067 ]
[203]
Baird, T.T.; Craik, C.S. Trypsin. Handb. Proteolytic Enzym., 1983, 2013(3), 2594-2600.
[http://dx.doi.org/10.1016/B978-0-12-382219-2.00575-5]
[204]
Harris, J.L.; Backes, B.J.; Leonetti, F.; Mahrus, S.; Ellman, J.A.; Craik, C.S. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc. Natl. Acad. Sci. USA, 2000, 97(14), 7754-7759.
[http://dx.doi.org/10.1073/pnas.140132697] [PMID: 10869434]
[205]
Huber, R.; Kukla, D.; Bode, W.; Schwager, P.; Bartels, K.; Deisenhofer, J.; Steigemann, W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 a resolution. J. Mol. Biol., 1974, 89(1), 73-101.
[http://dx.doi.org/10.1016/0022-2836(74)90163-6] [PMID: 4475115]
[206]
Stroud, R.M.; Kay, L.M.; Dickerson, R.E. The structure of bovine trypsin: electron density maps of the inhibited enzyme at 5 angstrom and at 2-7 angstron resolution. J. Mol. Biol., 1974, 83(2), 185-208.
[http://dx.doi.org/10.1016/0022-2836(74)90387-8] [PMID: 4821870]
[207]
Delbaere, L.T.J.; Hutcheon, W.L.B.; James, M.N.G.; Thiessen, W.E. Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes. Nature, 1975, 257(5529), 758-763.
[http://dx.doi.org/10.1038/257758a0] [PMID: 1186854]
[208]
Bode, W.; Schwager, P.; Huber, R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 a resolution. J. Mol. Biol., 1978, 118(1), 99-112.
[http://dx.doi.org/10.1016/0022-2836(78)90246-2] [PMID: 625059]
[209]
Matsuyama, S.; Ujike, M.; Morikawa, S.; Tashiro, M.; Taguchi, F. Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection. Proc. Natl. Acad. Sci. USA, 2005, 102(35), 12543-12547.
[http://dx.doi.org/10.1073/pnas.0503203102] [PMID: 16116101]
[210]
Kaur, U.; Chakrabarti, S.S.; Ojha, B.; Pathak, B.K.; Singh, A.; Saso, L.; Chakrabarti, S. Targeting host cell proteases to prevent SARS-CoV-2 invasion. Curr. Drug Targets, 2021, 22(2), 192-201.
[http://dx.doi.org/10.2174/1389450121666200924113243] [PMID: 32972339]
[211]
Bojkova, D.; McGreig, J.E.; McLaughlin, K-M.; Masterson, S.; Widera, M.; Krähling, V.; Ciesek, S.; Wass, M.; Michaelis, M.; Cinatl, J. SARS-CoV-2 and SARS-CoV differ in their cell tropism and drug sensitivity profiles. bioRxiv, 2020. preprint
[http://dx.doi.org/10.1101/2020.04.03.024257]
[212]
Böttcher, E.; Matrosovich, T.; Beyerle, M.; Klenk, H-D.; Garten, W.; Matrosovich, M. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J. Virol., 2006, 80(19), 9896-9898.
[http://dx.doi.org/10.1128/JVI.01118-06] [PMID: 16973594]
[213]
Shulla, A.; Heald-Sargent, T.; Subramanya, G.; Zhao, J.; Perlman, S.; Gallagher, T. A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry. J. Virol., 2011, 85(2), 873-882.
[http://dx.doi.org/10.1128/JVI.02062-10] [PMID: 21068237]
[214]
Bestle, D.; Heindl, M.R.; Limburg, H.; Van, T.V.L.; Pilgram, O.; Moulton, H.; Stein, D.; Hardes, K.; Eickmann, M.; Dolnik, O.; Rohde, C.; Becker, S.; Klenk, H-D.; Garten, W.; Steinmetzer, T.; Böttcher-Friebertshäuser, E. TMPRSS2 and furin are both essential for proteolytic activation and spread of SARS-CoV-2 in human airway epithelial cells and provide promising drug targets. Life Sci Alliance, 2020, 3(9)e202000786
[http://dx.doi.org/10.26508/lsa.202000786] [PMID: 32703818]
[215]
Konttinen, Y.T.; Porola, P.; Konttinen, L.; Laine, M.; Poduval, P. Immunohistopathology of Sjögren’s syndrome. Autoimmun. Rev., 2006, 6(1), 16-20.
[http://dx.doi.org/10.1016/j.autrev.2006.03.003] [PMID: 17110311]
[216]
Paoloni-Giacobino, A.; Chen, H.; Peitsch, M.C.; Rossier, C.; Antonarakis, S.E. Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3. Genomics, 1997, 44(3), 309-320.
[http://dx.doi.org/10.1006/geno.1997.4845] [PMID: 9325052]
[217]
Yamaoka, K.; Masuda, K.; Ogawa, H.; Takagi, K.; Umemoto, N.; Yasuoka, S. Cloning and characterization of the cDNA for human airway trypsin-like protease. J. Biol. Chem., 1998, 273(19), 11895-11901.
[http://dx.doi.org/10.1074/jbc.273.19.11895] [PMID: 9565616]
[218]
Hattori, M.; Fujiyama, A.; Taylor, T.D.; Watanabe, H.; Yada, T.; Park, H.S.; Toyoda, A.; Ishii, K.; Totoki, Y.; Choi, D.K.; Groner, Y.; Soeda, E.; Ohki, M.; Takagi, T.; Sakaki, Y.; Taudien, S.; Blechschmidt, K.; Polley, A.; Menzel, U.; Delabar, J.; Kumpf, K.; Lehmann, R.; Patterson, D.; Reichwald, K.; Rump, A.; Schillhabel, M.; Schudy, A.; Zimmermann, W.; Rosenthal, A.; Kudoh, J.; Schibuya, K.; Kawasaki, K.; Asakawa, S.; Shintani, A.; Sasaki, T.; Nagamine, K.; Mitsuyama, S.; Antonarakis, S.E.; Minoshima, S.; Shimizu, N.; Nordsiek, G.; Hornischer, K.; Brant, P.; Scharfe, M.; Schon, O.; Desario, A.; Reichelt, J.; Kauer, G.; Blocker, H.; Ramser, J.; Beck, A.; Klages, S.; Hennig, S.; Riesselmann, L.; Dagand, E.; Haaf, T.; Wehrmeyer, S.; Borzym, K.; Gardiner, K.; Nizetic, D.; Francis, F.; Lehrach, H.; Reinhardt, R.; Yaspo, M.L. The DNA sequence of human chromosome 21. Nature, 2000, 405(6784), 311-319.
[http://dx.doi.org/10.1038/35012518] [PMID: 10830953]
[219]
Hooper, J.D.; Clements, J.A.; Quigley, J.P.; Antalis, T.M. Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes. J. Biol. Chem., 2001, 276(2), 857-860.
[http://dx.doi.org/10.1074/jbc.R000020200] [PMID: 11060317]
[220]
Rawlings, N.D.; Barrett, A.J.; Finn, R. Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res., 2016, 44(D1), D343-D350.
[http://dx.doi.org/10.1093/nar/gkv1118] [PMID: 26527717]
[221]
Netzel-Arnett, S.; Hooper, J.D.; Szabo, R.; Madison, E.L.; Quigley, J.P.; Bugge, T.H.; Antalis, T.M. Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer Metastasis Rev., 2003, 22(2-3), 237-258.
[http://dx.doi.org/10.1023/A:1023003616848] [PMID: 12784999]
[222]
Jacquinet, E.; Rao, N.V.; Rao, G.V.; Zhengming, W.; Albertine, K.H.; Hoidal, J.R. Cloning and characterization of the cDNA and gene for human epitheliasin. Eur. J. Biochem., 2001, 268(9), 2687-2699.
[http://dx.doi.org/10.1046/j.1432-1327.2001.02165.x] [PMID: 11322890]
[223]
Jacquinet, E.; Rao, N.V.; Rao, G.V.; Hoidal, J.R. Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase: epitheliasin. FEBS Lett., 2000, 468(1), 93-100.
[http://dx.doi.org/10.1016/S0014-5793(00)01196-0] [PMID: 10683448]
[224]
Krieger, M.; Herz, J. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu. Rev. Biochem., 1994, 63, 601-637.
[http://dx.doi.org/10.1146/annurev.bi.63.070194.003125] [PMID: 7979249]
[225]
Resnick, D.; Chatterton, J.E.; Schwartz, K.; Slayter, H.; Krieger, M. Structures of class A macrophage scavenger receptors. Electron microscopic study of flexible, multidomain, fibrous proteins and determination of the disulfide bond pattern of the scavenger receptor cysteine-rich domain. J. Biol. Chem., 1996, 271(43), 26924-26930.
[http://dx.doi.org/10.1074/jbc.271.43.26924] [PMID: 8900177]
[226]
Hohenester, E.; Sasaki, T.; Timpl, R. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nat. Struct. Biol., 1999, 6(3), 228-232.
[http://dx.doi.org/10.1038/6669] [PMID: 10074941]
[227]
Liu, L.; Yang, J.; Qiu, L.; Wang, L.; Zhang, H.; Wang, M.; Vinu, S.S.; Song, L. A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding. Dev. Comp. Immunol., 2011, 35(2), 227-239.
[http://dx.doi.org/10.1016/j.dci.2010.09.010] [PMID: 20888856]
[228]
Afar, D.E.H.; Vivanco, I.; Hubert, R.S.; Kuo, J.; Chen, E.; Saffran, D.C.; Raitano, A.B.; Jakobovits, A. Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia. Cancer Res., 2001, 61(4), 1686-1692.
[PMID: 11245484]
[229]
Zhirnov, O.P.; Ikizler, M.R.; Wright, P.F. Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases. J. Virol., 2002, 76(17), 8682-8689.
[http://dx.doi.org/10.1128/JVI.76.17.8682-8689.2002] [PMID: 12163588]
[230]
Chi, M.; Shi, X.; Huo, X.; Wu, X.; Zhang, P.; Wang, G. Dexmedetomidine promotes breast cancer cell migration through Rab11-mediated secretion of exosomal TMPRSS2. Ann. Transl. Med., 2020, 8(8), 531-531.
[http://dx.doi.org/10.21037/atm.2020.04.28] [PMID: 32411754]
[231]
Lu, D.; Fütterer, K.; Korolev, S.; Zheng, X.; Tan, K.; Waksman, G.; Sadler, J.E. Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide. J. Mol. Biol., 1999, 292(2), 361-373.
[http://dx.doi.org/10.1006/jmbi.1999.3089] [PMID: 10493881]
[232]
Friedrich, R.; Fuentes-Prior, P.; Ong, E.; Coombs, G.; Hunter, M.; Oehler, R.; Pierson, D.; Gonzalez, R.; Huber, R.; Bode, W.; Madison, E.L. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J. Biol. Chem., 2002, 277(3), 2160-2168.
[http://dx.doi.org/10.1074/jbc.M109830200] [PMID: 11696548]
[233]
Schechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun., 1967, 27(2), 157-162.
[http://dx.doi.org/10.1016/S0006-291X(67)80055-X] [PMID: 6035483]
[234]
Perona, J.J.; Craik, C.S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem., 1997, 272(48), 29987-29990.
[http://dx.doi.org/10.1074/jbc.272.48.29987] [PMID: 9374470]
[235]
Meyer, D.; Sielaff, F.; Hammami, M.; Böttcher-Friebertshäuser, E.; Garten, W.; Steinmetzer, T. Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation. Biochem. J., 2013, 452(2), 331-343.
[http://dx.doi.org/10.1042/BJ20130101] [PMID: 23527573]
[236]
Lin, B.; Ferguson, C.; White, J.T.; Wang, S.; Vessella, R.; True, L.D.; Hood, L.; Nelson, P.S. Prostate-localized and androgen-regulated expression of the membrane-bound serine protease TMPRSS2. Cancer Res., 1999, 59(17), 4180-4184.
[PMID: 10485450]
[237]
Donaldson, S.H.; Hirsh, A.; Li, D.C.; Holloway, G.; Chao, J.; Boucher, R.C.; Gabriel, S.E. Regulation of the epithelial sodium channel by serine proteases in human airways. J. Biol. Chem., 2002, 277(10), 8338-8345.
[http://dx.doi.org/10.1074/jbc.M105044200] [PMID: 11756432]
[238]
Kim, T.S.; Heinlein, C.; Hackman, R.C.; Nelson, P.S. Phenotypic analysis of mice lacking the Tmprss2-encoded protease. Mol. Cell. Biol., 2006, 26(3), 965-975.
[http://dx.doi.org/10.1128/MCB.26.3.965-975.2006] [PMID: 16428450]
[239]
Garty, H.; Palmer, L.G. Epithelial sodium channels: function, structure, and regulation. Physiol. Rev., 1997, 77(2), 359-396.
[http://dx.doi.org/10.1152/physrev.1997.77.2.359] [PMID: 9114818]
[240]
Wu, Q.; Type, I.I. Type II transmembrane serine proteases. Curr. Top. Dev. Biol., 2003, 54, 167-206.
[http://dx.doi.org/10.1016/S0070-2153(03)54009-1] [PMID: 12696750]
[241]
Brown, M.S.; Herz, J.; Goldstein, J.L. LDL-receptor structure. Calcium cages, acid baths and recycling receptors. Nature, 1997, 388(6643), 629-630.
[http://dx.doi.org/10.1038/41672] [PMID: 9262394]
[242]
Nykjaer, A.; Conese, M.; Christensen, E.I.; Olson, D.; Cremona, O.; Gliemann, J.; Blasi, F. Recycling of the urokinase receptor upon internalization of the uPA:serpin complexes. EMBO J., 1997, 16(10), 2610-2620.
[http://dx.doi.org/10.1093/emboj/16.10.2610] [PMID: 9184208]
[243]
Kounnas, M.Z.; Church, F.C.; Argraves, W.S.; Strickland, D.K. Cellular internalization and degradation of antithrombin III-thrombin, heparin cofactor II-thrombin, and alpha 1-antitrypsin-trypsin complexes is mediated by the low density lipoprotein receptor-related protein. J. Biol. Chem., 1996, 271(11), 6523-6529.
[http://dx.doi.org/10.1074/jbc.271.11.6523] [PMID: 8626456]
[244]
Lam, D.K.; Dang, D.; Flynn, A.N.; Hardt, M.; Schmidt, B.L. TMPRSS2, a novel membrane-anchored mediator in cancer pain. Pain, 2015, 156(5), 923-930.
[http://dx.doi.org/10.1097/j.pain.0000000000000130] [PMID: 25734995]
[245]
Vaarala, M.H.; Porvari, K.; Kyllönen, A.; Lukkarinen, O.; Vihko, P. The TMPRSS2 gene encoding transmembrane serine protease is overexpressed in a majority of prostate cancer patients: detection of mutated TMPRSS2 form in a case of aggressive disease. Int. J. Cancer, 2001, 94(5), 705-710.
[http://dx.doi.org/10.1002/ijc.1526] [PMID: 11745466]
[246]
Lubieniecka, J.M.; Cheteri, M.K.; Stanford, J.L.; Ostrander, E.A. Met160Val polymorphism in the TRMPSS2 gene and risk of prostate cancer in a population-based case-control study. Prostate, 2004, 59(4), 357-359.
[http://dx.doi.org/10.1002/pros.20005] [PMID: 15065083]
[247]
Wilson, S.; Greer, B.; Hooper, J.; Zijlstra, A.; Walker, B.; Quigley, J.; Hawthorne, S. The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells. Biochem. J., 2005, 388(Pt 3), 967-972.
[http://dx.doi.org/10.1042/BJ20041066] [PMID: 15537383]
[248]
Bahou, W.F. Protease-activated receptors. Curr. Top. Dev. Biol., 2003, 54, 343-369.
[http://dx.doi.org/10.1016/S0070-2153(03)54014-5] [PMID: 12696755]
[249]
Lazarowitz, S.G.; Choppin, P.W. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology, 1975, 68(2), 440-454.
[http://dx.doi.org/10.1016/0042-6822(75)90285-8] [PMID: 128196]
[250]
Klenk, H.D.; Rott, R.; Orlich, M.; Blödorn, J. Activation of influenza A viruses by trypsin treatment. Virology, 1975, 68(2), 426-439.
[http://dx.doi.org/10.1016/0042-6822(75)90284-6] [PMID: 173078]
[251]
Shirogane, Y.; Takeda, M.; Iwasaki, M.; Ishiguro, N.; Takeuchi, H.; Nakatsu, Y.; Tahara, M.; Kikuta, H.; Yanagi, Y. Efficient multiplication of human metapneumovirus in vero cells expressing the transmembrane serine protease TMPRSS2. J. Virol., 2008, 82(17), 8942-8946.
[http://dx.doi.org/10.1128/JVI.00676-08] [PMID: 18562527]
[252]
van den Hoogen, B.G.; Bestebroer, T.M.; Osterhaus, A.D.M.E.; Fouchier, R.A.M. Analysis of the genomic sequence of a human metapneumovirus. Virology, 2002, 295(1), 119-132.
[http://dx.doi.org/10.1006/viro.2001.1355] [PMID: 12033771]
[253]
Shirato, K.; Matsuyama, S.; Ujike, M.; Taguchi, F. Role of proteases in the release of porcine epidemic diarrhea virus from infected cells. J. Virol., 2011, 85(15), 7872-7880.
[http://dx.doi.org/10.1128/JVI.00464-11] [PMID: 21613395]
[254]
Li, F.; Berardi, M.; Li, W.; Farzan, M.; Dormitzer, P.R.; Harrison, S.C. Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain. J. Virol., 2006, 80(14), 6794-6800.
[http://dx.doi.org/10.1128/JVI.02744-05] [PMID: 16809285]
[255]
Belouzard, S.; Chu, V.C.; Whittaker, G.R. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc. Natl. Acad. Sci. USA, 2009, 106(14), 5871-5876.
[http://dx.doi.org/10.1073/pnas.0809524106] [PMID: 19321428]
[256]
Bosch, B.J.; van der Zee, R.; de Haan, C.A.M.; Rottier, P.J.M. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol., 2003, 77(16), 8801-8811.
[http://dx.doi.org/10.1128/JVI.77.16.8801-8811.2003] [PMID: 12885899]
[257]
Kam, Y.W.; Okumura, Y.; Kido, H.; Ng, L.F.P.; Bruzzone, R.; Altmeyer, R. Cleavage of the SARS coronavirus spike glycoprotein by airway proteases enhances virus entry into human bronchial epithelial cells in vitro. PLoS One, 2009, 4(11)e7870
[http://dx.doi.org/10.1371/journal.pone.0007870] [PMID: 19924243]
[258]
Glowacka, I.; Bertram, S.; Müller, M.A.; Allen, P.; Soilleux, E.; Pfefferle, S.; Steffen, I.; Tsegaye, T.S.; He, Y.; Gnirss, K.; Niemeyer, D.; Schneider, H.; Drosten, C.; Pöhlmann, S. Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J. Virol., 2011, 85(9), 4122-4134.
[http://dx.doi.org/10.1128/JVI.02232-10] [PMID: 21325420]
[259]
Perdue, M.L.; García, M.; Senne, D.; Fraire, M. Virulence-associated sequence duplication at the hemagglutinin cleavage site of avian influenza viruses. Virus Res., 1997, 49(2), 173-186.
[http://dx.doi.org/10.1016/S0168-1702(97)01468-8] [PMID: 9213392]
[260]
Tian, X.; Li, C.; Huang, A.; Xia, S.; Lu, S.; Shi, Z.; Lu, L.; Jiang, S.; Yang, Z.; Wu, Y.; Ying, T. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg. Microbes Infect., 2020, 9(1), 382-385.
[http://dx.doi.org/10.1080/22221751.2020.1729069] [PMID: 32065055]
[261]
Moore, M.J.; Dorfman, T.; Li, W.; Wong, S.K.; Li, Y.; Kuhn, J.H.; Coderre, J.; Vasilieva, N.; Han, Z.; Greenough, T.C.; Farzan, M.; Choe, H. Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2. J. Virol., 2004, 78(19), 10628-10635.
[http://dx.doi.org/10.1128/JVI.78.19.10628-10635.2004] [PMID: 15367630]
[262]
Li, F.; Li, W.; Farzan, M.; Harrison, S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science, 2005, 309(5472), 1864-1868.
[http://dx.doi.org/10.1126/science.1116480] [PMID: 16166518]
[263]
Beniac, D.R.; deVarennes, S.L.; Andonov, A.; He, R.; Booth, T.F. Conformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusion. PLoS One, 2007, 2(10)e1082
[http://dx.doi.org/10.1371/journal.pone.0001082] [PMID: 17957264]
[264]
Sui, J.; Li, W.; Murakami, A.; Tamin, A.; Matthews, L.J.; Wong, S.K.; Moore, M.J.; Tallarico, A.S.C.; Olurinde, M.; Choe, H.; Anderson, L.J.; Bellini, W.J.; Farzan, M.; Marasco, W.A. Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association. Proc. Natl. Acad. Sci. USA, 2004, 101(8), 2536-2541.
[http://dx.doi.org/10.1073/pnas.0307140101] [PMID: 14983044]
[265]
Li, W.; Moore, M.J.; Vasilieva, N.; Sui, J.; Wong, S.K.; Berne, M.A.; Somasundaran, M.; Sullivan, J.L.; Luzuriaga, K.; Greenough, T.C.; Choe, H.; Farzan, M. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature, 2003, 426(6965), 450-454.
[http://dx.doi.org/10.1038/nature02145] [PMID: 14647384]
[266]
Nicholls, J.M.; Bourne, A.J.; Chen, H.; Guan, Y.; Peiris, J.S. Sialic acid receptor detection in the human respiratory tract: evidence for widespread distribution of potential binding sites for human and avian influenza viruses. Respir. Res., 2007, 8, 73.
[http://dx.doi.org/10.1186/1465-9921-8-73] [PMID: 17961210]
[267]
Bertram, S.; Heurich, A.; Lavender, H.; Gierer, S.; Danisch, S.; Perin, P.; Lucas, J.M.; Nelson, P.S.; Pöhlmann, S.; Soilleux, E.J. Influenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tracts. PLoS One, 2012, 7(4)e35876
[http://dx.doi.org/10.1371/journal.pone.0035876] [PMID: 22558251]
[268]
Iwata-Yoshikawa, N.; Okamura, T.; Shimizu, Y.; Hasegawa, H.; Takeda, M.; Nagata, N. TMPRSS2 Contributes to virus spread and immunopathology in the airways of murine models after coronavirus infection. J. Virol., 2019, 93(6), 1-15.
[http://dx.doi.org/10.1128/JVI.01815-18] [PMID: 30626688]
[269]
Montopoli, M.; Zumerle, S.; Vettor, R.; Rugge, M.; Zorzi, M.; Catapano, C.V.; Carbone, G.M.; Cavalli, A.; Pagano, F.; Ragazzi, E.; Prayer-Galetti, T.; Alimonti, A. Androgen-deprivation therapies for prostate cancer and risk of infection by SARS-CoV-2: a population-based study (N = 4532). Ann. Oncol., 2020, 31(8), 1040-1045.
[http://dx.doi.org/10.1016/j.annonc.2020.04.479] [PMID: 32387456]
[270]
Hawthorne, S.; Hamilton, R.; Walker, B.J.; Walker, B. Utilization of biotinylated diphenyl phosphonates for disclosure of serine proteases. Anal. Biochem., 2004, 326(2), 273-275.
[http://dx.doi.org/10.1016/j.ab.2003.12.002] [PMID: 15003568]
[271]
Böttcher, E.; Freuer, C.; Steinmetzer, T.; Klenk, H.D.; Garten, W. MDCK cells that express proteases TMPRSS2 and HAT provide a cell system to propagate influenza viruses in the absence of trypsin and to study cleavage of HA and its inhibition. Vaccine, 2009, 27(45), 6324-6329.
[http://dx.doi.org/10.1016/j.vaccine.2009.03.029] [PMID: 19840668]
[272]
Zhirnov, O.P.; Klenk, H.D.; Wright, P.F. Aprotinin and similar protease inhibitors as drugs against influenza. Antiviral Res., 2011, 92(1), 27-36.
[http://dx.doi.org/10.1016/j.antiviral.2011.07.014] [PMID: 21802447]
[273]
Dittmann, M.; Hoffmann, H-H.; Scull, M.A.; Gilmore, R.H.; Bell, K.L.; Ciancanelli, M.; Wilson, S.J.; Crotta, S.; Yu, Y.; Flatley, B.; Xiao, J.W.; Casanova, J.L.; Wack, A.; Bieniasz, P.D.; Rice, C.M. A serpin shapes the extracellular environment to prevent influenza A virus maturation. Cell, 2015, 160(4), 631-643.
[http://dx.doi.org/10.1016/j.cell.2015.01.040] [PMID: 25679759]
[274]
Faller, N.; Gautschi, I.; Schild, L. Functional analysis of a missense mutation in the serine protease inhibitor SPINT2 associated with congenital sodium diarrhea. PLoS One, 2014, 9(4)e94267
[http://dx.doi.org/10.1371/journal.pone.0094267] [PMID: 24722141]
[275]
Szabo, R.; Hobson, J.P.; List, K.; Molinolo, A.; Lin, C.Y.; Bugge, T.H. Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity. J. Biol. Chem., 2008, 283(43), 29495-29504.
[http://dx.doi.org/10.1074/jbc.M801970200] [PMID: 18713750]
[276]
Sielaff, F.; Böttcher-Friebertshäuser, E.; Meyer, D.; Saupe, S.M.; Volk, I.M.; Garten, W.; Steinmetzer, T. Development of substrate analogue inhibitors for the human airway trypsin-like protease HAT. Bioorg. Med. Chem. Lett., 2011, 21(16), 4860-4864.
[http://dx.doi.org/10.1016/j.bmcl.2011.06.033] [PMID: 21741839]
[277]
Sisay, M.T.; Steinmetzer, T.; Stirnberg, M.; Maurer, E.; Hammami, M.; Bajorath, J.; Gütschow, M. Identification of the first low-molecular-weight inhibitors of matriptase-2. J. Med. Chem., 2010, 53(15), 5523-5535.
[http://dx.doi.org/10.1021/jm100183e] [PMID: 20684597]
[278]
Biela, A.; Sielaff, F.; Terwesten, F.; Heine, A.; Steinmetzer, T.; Klebe, G. Ligand binding stepwise disrupts water network in thrombin: enthalpic and entropic changes reveal classical hydrophobic effect. J. Med. Chem., 2012, 55(13), 6094-6110.
[http://dx.doi.org/10.1021/jm300337q] [PMID: 22612268]
[279]
Steinmetzer, T.; Schweinitz, A.; Stürzebecher, A.; Dönnecke, D.; Uhland, K.; Schuster, O.; Steinmetzer, P.; Müller, F.; Friedrich, R.; Than, M.E.; Bode, W.; Stürzebecher, J. Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase. J. Med. Chem., 2006, 49(14), 4116-4126.
[http://dx.doi.org/10.1021/jm051272l] [PMID: 16821772]
[280]
Hammami, M.; Rühmann, E.; Maurer, E.; Heine, A.; Gütschow, M.; Klebe, G.; Steinmetzer, T. New 3-amidinophenylalanine-derived inhibitors of matriptase. MedChemComm, 2012, 3(7), 807-813.
[http://dx.doi.org/10.1039/c2md20074k]
[281]
Steinmetzer, T.; Dönnecke, D.; Korsonewski, M.; Neuwirth, C.; Steinmetzer, P.; Schulze, A.; Saupe, S.M.; Schweinitz, A. Modification of the N-terminal sulfonyl residue in 3-amidinophenylalanine-based matriptase inhibitors. Bioorg. Med. Chem. Lett., 2009, 19(1), 67-73.
[http://dx.doi.org/10.1016/j.bmcl.2008.11.019] [PMID: 19036586]
[282]
Lucas, J.M.; Heinlein, C.; Kim, T.; Hernandez, S.A.; Malik, M.S.; True, L.D.; Morrissey, C.; Corey, E.; Montgomery, B.; Mostaghel, E.; Clegg, N.; Coleman, I.; Brown, C.M.; Schneider, E.L.; Craik, C.; Simon, J.A.; Bedalov, A.; Nelson, P.S. The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis. Cancer Discov., 2014, 4(11), 1310-1325.
[http://dx.doi.org/10.1158/2159-8290.CD-13-1010] [PMID: 25122198]
[283]
Shrimp, J.H.; Kales, S.C.; Sanderson, P.E.; Simeonov, A.; Shen, M.; Hall, M.D. An enzymatic TMPRSS2 assay for assessment of clinical candidates and discovery of inhibitors as potential treatment of COVID-19. bioRxiv, 2020. preprint
[http://dx.doi.org/10.1101/2020.06.23.167544] [PMID: 32596694]
[284]
NIH Clinical Trials of Bromhexine for COVID19. Available from: https://833 19&term=bromhexine&cntry=&state=&city=&dist=&Se(Accessed date: October 01, 2020)
[285]
Böttcher-Friebertshäuser, E.; Stein, D.A.; Klenk, H-D.; Garten, W. Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2. J. Virol., 2011, 85(4), 1554-1562.
[http://dx.doi.org/10.1128/JVI.01294-10] [PMID: 21123387]
[286]
Matsuyama, S.; Nagata, N.; Shirato, K.; Kawase, M.; Takeda, M.; Taguchi, F. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J. Virol., 2010, 84(24), 12658-12664.
[http://dx.doi.org/10.1128/JVI.01542-10] [PMID: 20926566]
[287]
Simmons, G.; Reeves, J.D.; Rennekamp, A.J.; Amberg, S.M.; Piefer, A.J.; Bates, P. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl. Acad. Sci. USA, 2004, 101(12), 4240-4245.
[http://dx.doi.org/10.1073/pnas.0306446101] [PMID: 15010527]
[288]
Talukdar, R.; Tandon, R.K. Pancreatic stellate cells: new target in the treatment of chronic pancreatitis. J. Gastroenterol. Hepatol., 2008, 23(1), 34-41.
[http://dx.doi.org/10.1111/j.1440-1746.2007.05206.x] [PMID: 17995943]
[289]
Sai, J.K.; Suyama, M.; Kubokawa, Y.; Matsumura, Y.; Inami, K.; Watanabe, S. Efficacy of camostat mesilate against dyspepsia associated with non-alcoholic mild pancreatic disease. J. Gastroenterol., 2010, 45(3), 335-341.
[http://dx.doi.org/10.1007/s00535-009-0148-1] [PMID: 19876587]
[290]
Okuno, M.; Kojima, S.; Akita, K.; Matsushima-Nishiwaki, R.; Adachi, S.; Sano, T.; Takano, Y.; Takai, K.; Obora, A.; Yasuda, I.; Shiratori, Y.; Okano, Y.; Shimada, J.; Suzuki, Y.; Muto, Y.; Moriwaki, Y. Retinoids in liver fibrosis and cancer. Front. Biosci., 2002, 7, d204-d218.
[http://dx.doi.org/10.2741/okuno] [PMID: 11779708]
[291]
Shirato, K.; Kawase, M.; Matsuyama, S. Wild-type human coronaviruses prefer cell-surface TMPRSS2 to endosomal cathepsins for cell entry. Virology, 2018, 517(517), 9-15.
[http://dx.doi.org/10.1016/j.virol.2017.11.012] [PMID: 29217279]
[292]
Lee, M.G.; Kim, K.H.; Park, K.Y.; Kim, J.S. Evaluation of anti-influenza effects of camostat in mice infected with non-adapted human influenza viruses. Arch. Virol., 1996, 141(10), 1979-1989.
[http://dx.doi.org/10.1007/BF01718208] [PMID: 8920829]
[293]
Yamaya, M.; Shimotai, Y.; Hatachi, Y.; Lusamba Kalonji, N.; Tando, Y.; Kitajima, Y.; Matsuo, K.; Kubo, H.; Nagatomi, R.; Hongo, S.; Homma, M.; Nishimura, H. The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells. Pulm. Pharmacol. Ther., 2015, 33, 66-74.
[http://dx.doi.org/10.1016/j.pupt.2015.07.001] [PMID: 26166259]
[294]
NIH Clinical Trials of Camostat for COVID-19. Available from: https://clinicaltrials.gov/ct2/results?cond= Covid19&term=camostat&cntry=&state=&city=&dist=(Accessed date: October 01, 2020)
[295]
Midgley, I.; Hood, A.J.; Proctor, P.; Chasseaud, L.F.; Irons, S.R.; Cheng, K.N.; Brindley, C.J.; Bonn, R. Metabolic fate of 14C-camostat mesylate in man, rat and dog after intravenous administration. Xenobiotica, 1994, 24(1), 79-92.
[http://dx.doi.org/10.3109/00498259409043223] [PMID: 8165824]
[296]
Yamamoto, M.; Matsuyama, S.; Li, X.; Takeda, M.; Kawaguchi, Y.; Inoue, J.I.; Matsuda, Z. Identification of nafamostat as a potent inhibitor of middle east respiratory syndrome coronavirus S protein-mediated membrane fusion using the split-protein-based cell-cell fusion assay. Antimicrob. Agents Chemother., 2016, 60(11), 6532-6539.
[http://dx.doi.org/10.1128/AAC.01043-16] [PMID: 27550352]
[297]
Chen, X.; Xu, Z.; Zeng, S.; Wang, X.; Liu, W.; Qian, L.; Wei, J.; Yang, X.; Shen, Q.; Gong, Z.; Yan, Y. The molecular aspect of antitumor effects of protease inhibitor nafamostat mesylate and its role in potential clinical applications. Front. Oncol., 2019, 9, 852.
[http://dx.doi.org/10.3389/fonc.2019.00852] [PMID: 31552177]
[298]
Sadahiro, T.; Yuzawa, H.; Kimura, T.; Oguchi, M.; Morito, T.; Mizushima, S.; Hirose, Y. Current practices in acute blood purification therapy in japan and topics for further study. Contrib. Nephrol., 2018, 196, 209-214.
[http://dx.doi.org/10.1159/000485724] [PMID: 30041229]
[299]
NIH Clinical Trials for Nafamostat for COVID-19 Available at: https://clinicaltrials.gov/ct2/results?cond= Clinical+Trials+for+Nafamostat+for+COVID-19.&term=&cntry=&state=&city=&dist=(Accessed date: October 01, 2020)
[300]
Spraggon, G.; Hornsby, M.; Shipway, A.; Tully, D.C.; Bursulaya, B.; Danahay, H.; Harris, J.L.; Lesley, S.A. Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Protein Sci., 2009, 18(5), 1081-1094.
[http://dx.doi.org/10.1002/pro.118] [PMID: 19388054]
[301]
Millies, B.; von Hammerstein, F.; Gellert, A.; Hammerschmidt, S.; Barthels, F.; Göppel, U.; Immerheiser, M.; Elgner, F.; Jung, N.; Basic, M.; Kersten, C.; Kiefer, W.; Bodem, J.; Hildt, E.; Windbergs, M.; Hellmich, U.A.; Schirmeister, T. Proline-based allosteric inhibitors of zika and dengue virus NS2B/NS3 proteases. J. Med. Chem., 2019, 62(24), 11359-11382.
[http://dx.doi.org/10.1021/acs.jmedchem.9b01697] [PMID: 31769670]
[302]
Matthews, D.A.; Dragovich, P.S.; Webber, S.E.; Fuhrman, S.A.; Patick, A.K.; Zalman, L.S.; Hendrickson, T.F.; Love, R.A.; Prins, T.J.; Marakovits, J.T.; Zhou, R.; Tikhe, J.; Ford, C.E.; Meador, J.W.; Ferre, R.A.; Brown, E.L.; Binford, S.L.; Brothers, M.A.; DeLisle, D.M.; Worland, S.T. Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc. Natl. Acad. Sci. USA, 1999, 96(20), 11000-11007.
[http://dx.doi.org/10.1073/pnas.96.20.11000] [PMID: 10500114]
[303]
Deeks, S.G.; Smith, M.; Holodniy, M.; Kahn, J.O. HIV-1 protease inhibitors. A review for clinicians. JAMA, 1997, 277(2), 145-153.
[http://dx.doi.org/10.1001/jama.1997.03540260059037] [PMID: 8990341]
[304]
de Leuw, P.; Stephan, C. Protease inhibitors for the treatment of hepatitis C virus infection. GMS Infect. Dis., 2017, 5, Doc08.
[http://dx.doi.org/10.3205/id000034] [PMID: 30671330]
[305]
Welker, A.; Kersten, C.; Müller, C.; Madhugiri, R.; Zimmer, C.; Müller, P.; Zimmermann, R.; Hammerschmidt, S.; Maus, H.; Ziebuhr, J.; Sotriffer, C.; Schirmeister, T. Structure-activity relationships of benzamides and isoindolines designed as SARS-CoV protease inhibitors effective against SARS-CoV-2. ChemMedChem, 2020.
[http://dx.doi.org/10.1002/cmdc.202000548] [PMID: 32930481]
[306]
Báez-Santos, Y.M.; St John, S.E.; Mesecar, A.D. The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds. Antiviral Res., 2015, 115, 21-38.
[http://dx.doi.org/10.1016/j.antiviral.2014.12.015] [PMID: 25554382]
[307]
McKee, D.L.; Sternberg, A.; Stange, U.; Laufer, S.; Naujokat, C. Candidate drugs against SARS-CoV-2 and COVID-19. Pharmacol. Res., 2020, 157104859
[http://dx.doi.org/10.1016/j.phrs.2020.104859] [PMID: 32360480]
[308]
Declercq, J.; Creemers, J.W.M. Therapeutic potential of furin inhibition: an evaluation using a conditional furin knockout mouse model. Colloq. Ser. Protein Act. Cancer, 2012, 1(4), 1-30.
[http://dx.doi.org/10.4199/C00068ED1V01Y201211PAC004]

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