메뉴 건너뛰기




Volumn 8, Issue 8, 2019, Pages

Furin-mediated protein processing in infectious diseases and cancer

Author keywords

bacterial toxins; cancer; furin; guanylate binding proteins; proprotein convertases; viral glycoproteins

Indexed keywords

BACTERIAL TOXIN; EXOTOXIN; FURIN; GBP2 PROTEIN; GBP5 PROTEIN; PAR1 PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG; VIRAL PROTEIN; VIRUS GLYCOPROTEIN;

EID: 85079563205     PISSN: None     EISSN: 20500068     Source Type: Journal    
DOI: 10.1002/cti2.1073     Document Type: Review
Times cited : (234)

References (144)
  • 2
    • 79952257801 scopus 로고    scopus 로고
    • FurinDB: a database of 20-residue furin cleavage site motifs, substrates and their associated drugs
    • Tian S, Huang Q, Fang Y et al. FurinDB: a database of 20-residue furin cleavage site motifs, substrates and their associated drugs. Int J Mol Sci 2011; 12: 1060–1065.
    • (2011) Int J Mol Sci , vol.12 , pp. 1060-1065
    • Tian, S.1    Huang, Q.2    Fang, Y.3
  • 3
    • 0014200189 scopus 로고
    • Insulin biosynthesis: evidence for a precursor
    • Steiner DF, Cunningham D, Spigelman L et al. Insulin biosynthesis: evidence for a precursor. Science 1967; 157: 697–700.
    • (1967) Science , vol.157 , pp. 697-700
    • Steiner, D.F.1    Cunningham, D.2    Spigelman, L.3
  • 4
    • 0022779175 scopus 로고
    • Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein
    • Roebroek AJ, Schalken JA, Leunissen JA et al. Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein. EMBO J 1986; 5: 2197–2202.
    • (1986) EMBO J , vol.5 , pp. 2197-2202
    • Roebroek, A.J.1    Schalken, J.A.2    Leunissen, J.A.3
  • 5
    • 0025522624 scopus 로고
    • Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes
    • van de Ven WJ, Voorberg J, Fontijn R et al. Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes. Mol Biol Rep 1990; 14: 265–275.
    • (1990) Mol Biol Rep , vol.14 , pp. 265-275
    • van de Ven, W.J.1    Voorberg, J.2    Fontijn, R.3
  • 6
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah NG, Prat A. The biology and therapeutic targeting of the proprotein convertases. Nat Rev Drug Discov 2012; 11: 367–383.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 7
    • 0033529545 scopus 로고    scopus 로고
    • Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins
    • Cheng D, Espenshade PJ, Slaughter CA et al. Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins. J Biol Chem 1999; 274: 22805–22812.
    • (1999) J Biol Chem , vol.274 , pp. 22805-22812
    • Cheng, D.1    Espenshade, P.J.2    Slaughter, C.A.3
  • 8
    • 34547137377 scopus 로고    scopus 로고
    • Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells
    • McNutt MC, Lagace TA, Horton JD. Catalytic activity is not required for secreted PCSK9 to reduce low density lipoprotein receptors in HepG2 cells. J Biol Chem 2007; 282: 20799–20803.
    • (2007) J Biol Chem , vol.282 , pp. 20799-20803
    • McNutt, M.C.1    Lagace, T.A.2    Horton, J.D.3
  • 9
    • 84920269464 scopus 로고    scopus 로고
    • Tissue-based map of the human proteome
    • Uhlén M, Fagerberg L, Hallström BM et al. Tissue-based map of the human proteome. Science 2015; 347: 1260419.
    • (2015) Science , vol.347 , pp. 1260419
    • Uhlén, M.1    Fagerberg, L.2    Hallström, B.M.3
  • 10
    • 0028292383 scopus 로고
    • Expression of the dibasic proprotein processing enzyme furin is directed by multiple promoters
    • Ayoubi TA, Creemers JW, Roebroek AJ et al. Expression of the dibasic proprotein processing enzyme furin is directed by multiple promoters. J Biol Chem 1994; 269: 9298–9303.
    • (1994) J Biol Chem , vol.269 , pp. 9298-9303
    • Ayoubi, T.A.1    Creemers, J.W.2    Roebroek, A.J.3
  • 11
    • 33746600246 scopus 로고    scopus 로고
    • Proprotein convertase furin is preferentially expressed in T helper 1 cells and regulates interferon γ
    • Pesu M, Muul L, Kanno Y et al. Proprotein convertase furin is preferentially expressed in T helper 1 cells and regulates interferon γ. Blood 2006; 108: 983–985.
    • (2006) Blood , vol.108 , pp. 983-985
    • Pesu, M.1    Muul, L.2    Kanno, Y.3
  • 12
    • 0030612684 scopus 로고    scopus 로고
    • TGFβ1 regulates gene expression of its own converting enzyme furin
    • Blanchette F, Day R, Dong W et al. TGFβ1 regulates gene expression of its own converting enzyme furin. J Clin Invest 1997; 99: 1974–1983.
    • (1997) J Clin Invest , vol.99 , pp. 1974-1983
    • Blanchette, F.1    Day, R.2    Dong, W.3
  • 13
    • 0028362008 scopus 로고
    • The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM)
    • Decroly E, Vandenbranden M, Ruysschaert JM et al. The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). J Biol Chem 1994; 269: 12240–12247.
    • (1994) J Biol Chem , vol.269 , pp. 12240-12247
    • Decroly, E.1    Vandenbranden, M.2    Ruysschaert, J.M.3
  • 14
    • 84885766791 scopus 로고    scopus 로고
    • Processing of human toll-like receptor 7 by furin-like proprotein convertases is required for its accumulation and activity in endosomes
    • Hipp MM, Shepherd D, Gileadi U et al. Processing of human toll-like receptor 7 by furin-like proprotein convertases is required for its accumulation and activity in endosomes. Immunity 2013; 39: 711–721.
    • (2013) Immunity , vol.39 , pp. 711-721
    • Hipp, M.M.1    Shepherd, D.2    Gileadi, U.3
  • 15
    • 0027421103 scopus 로고
    • Intramolecular chaperones and protein folding
    • Shinde U, Inouye M. Intramolecular chaperones and protein folding. Trends Biochem Sci 1993; 18: 442–446.
    • (1993) Trends Biochem Sci , vol.18 , pp. 442-446
    • Shinde, U.1    Inouye, M.2
  • 16
    • 0031001304 scopus 로고    scopus 로고
    • Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage
    • Anderson ED, VanSlyke JK, Thulin CD et al. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO J 1997; 16: 1508–1518.
    • (1997) EMBO J , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    VanSlyke, J.K.2    Thulin, C.D.3
  • 17
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: from protein traffic to embryogenesis and disease
    • Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol 2002; 3: 753–766.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 18
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface
    • Molloy SS, Thomas L, VanSlyke JK et al. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO J 1994; 13: 18–33.
    • (1994) EMBO J , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3
  • 19
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey M, Schäfer W, Berghöfer S et al. Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J Cell Biol 1994; 127: 1829–1842.
    • (1994) J Cell Biol , vol.127 , pp. 1829-1842
    • Vey, M.1    Schäfer, W.2    Berghöfer, S.3
  • 20
    • 0035868365 scopus 로고    scopus 로고
    • “Shed” furin: mapping of the cleavage determinants and identification of its C-terminus
    • Plaimauer B, Mohr G, Wernhart W et al. “Shed” furin: mapping of the cleavage determinants and identification of its C-terminus. Biochem J 2001; 354: 689–695.
    • (2001) Biochem J , vol.354 , pp. 689-695
    • Plaimauer, B.1    Mohr, G.2    Wernhart, W.3
  • 21
    • 77649161633 scopus 로고    scopus 로고
    • A 20 Residues motif delineates the furin cleavage site and its physical properties may influence viral fusion
    • Tian S. A 20 Residues motif delineates the furin cleavage site and its physical properties may influence viral fusion. Biochem Insights 2009; 2: BCI.S2049.
    • (2009) Biochem Insights , vol.2 , pp. BCI.S2049
    • Tian, S.1
  • 22
    • 27644578453 scopus 로고    scopus 로고
    • Proprotein convertases [corrected] are responsible for proteolysis and inactivation of endothelial lipase
    • Jin W, Fuki IV, Seidah NG et al. Proprotein convertases [corrected] are responsible for proteolysis and inactivation of endothelial lipase. J Biol Chem 2005; 280: 36551–36559.
    • (2005) J Biol Chem , vol.280 , pp. 36551-36559
    • Jin, W.1    Fuki, I.V.2    Seidah, N.G.3
  • 23
    • 79953022875 scopus 로고    scopus 로고
    • In vivo evidence that furin from hepatocytes inactivates PCSK9
    • Essalmani R, Susan-Resiga D, Chamberland A et al. In vivo evidence that furin from hepatocytes inactivates PCSK9. J Biol Chem 2011; 286: 4257–4263.
    • (2011) J Biol Chem , vol.286 , pp. 4257-4263
    • Essalmani, R.1    Susan-Resiga, D.2    Chamberland, A.3
  • 24
    • 0032443652 scopus 로고    scopus 로고
    • Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin
    • Roebroek AJ, Umans L, Pauli IG et al. Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase Furin. Development 1998; 125: 4863–4876.
    • (1998) Development , vol.125 , pp. 4863-4876
    • Roebroek, A.J.1    Umans, L.2    Pauli, I.G.3
  • 25
    • 84866280245 scopus 로고    scopus 로고
    • Loss of endothelial furin leads to cardiac malformation and early postnatal death
    • Kim W, Essalmani R, Szumska D et al. Loss of endothelial furin leads to cardiac malformation and early postnatal death. Mol Cell Biol 2012; 32: 3382–3391.
    • (2012) Mol Cell Biol , vol.32 , pp. 3382-3391
    • Kim, W.1    Essalmani, R.2    Szumska, D.3
  • 26
    • 0035912849 scopus 로고    scopus 로고
    • Mutations within a furin consensus sequence block proteolytic release of ectodysplasin-A and cause X-linked hypohidrotic ectodermal dysplasia
    • Chen Y, Molloy SS, Thomas L et al. Mutations within a furin consensus sequence block proteolytic release of ectodysplasin-A and cause X-linked hypohidrotic ectodermal dysplasia. Proc Natl Acad Sci USA 2001; 98: 7218–7223.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7218-7223
    • Chen, Y.1    Molloy, S.S.2    Thomas, L.3
  • 27
    • 0025292828 scopus 로고
    • Haemophilia B: database of point mutations and short additions and deletions
    • Giannelli F, Green PM, High KA et al. Haemophilia B: database of point mutations and short additions and deletions. Nucleic Acids Res 1990; 18: 4053–4059.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4053-4059
    • Giannelli, F.1    Green, P.M.2    High, K.A.3
  • 28
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: “master switches” in the regulation of tumor growth and progression
    • Bassi DE, Fu J, Lopez de Cicco R et al. Proprotein convertases: “master switches” in the regulation of tumor growth and progression. Mol Carcinog 2005; 44: 151–161.
    • (2005) Mol Carcinog , vol.44 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de Cicco, R.3
  • 29
    • 85020131888 scopus 로고    scopus 로고
    • Proprotein convertase inhibition: paralyzing the cell's master switches
    • Klein-Szanto AJ, Bassi DE. Proprotein convertase inhibition: paralyzing the cell's master switches. Biochem Pharmacol 2017; 140: 8–15.
    • (2017) Biochem Pharmacol , vol.140 , pp. 8-15
    • Klein-Szanto, A.J.1    Bassi, D.E.2
  • 30
    • 85020943811 scopus 로고    scopus 로고
    • The proprotein convertase furin in tumour progression: the PC furin in tumour progression
    • Jaaks P, Bernasconi M. The proprotein convertase furin in tumour progression: the PC furin in tumour progression. Int J Cancer 2017; 141: 654–663.
    • (2017) Int J Cancer , vol.141 , pp. 654-663
    • Jaaks, P.1    Bernasconi, M.2
  • 31
    • 14844299760 scopus 로고    scopus 로고
    • Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1: impact on the bioactivation of proproteins
    • McMahon S, Grondin F, McDonald PP et al. Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1: impact on the bioactivation of proproteins. J Biol Chem 2005; 280: 6561–6569.
    • (2005) J Biol Chem , vol.280 , pp. 6561-6569
    • McMahon, S.1    Grondin, F.2    McDonald, P.P.3
  • 32
    • 82155192278 scopus 로고    scopus 로고
    • Hypoxia enhances cancer cell invasion through relocalization of the proprotein convertase furin from the trans-Golgi network to the cell surface
    • Arsenault D, Lucien F, Dubois CM. Hypoxia enhances cancer cell invasion through relocalization of the proprotein convertase furin from the trans-Golgi network to the cell surface. J Cell Physiol 2012; 227: 789–800.
    • (2012) J Cell Physiol , vol.227 , pp. 789-800
    • Arsenault, D.1    Lucien, F.2    Dubois, C.M.3
  • 33
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: integrins, signaling and cell survival
    • Stupack DG, Cheresh DA. Get a ligand, get a life: integrins, signaling and cell survival. J Cell Sci 2002; 115: 3729–3738.
    • (2002) J Cell Sci , vol.115 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 34
    • 85048476255 scopus 로고    scopus 로고
    • TGF-β in T cell biology: implications for cancer immunotherapy
    • Dahmani A, Delisle J-S. TGF-β in T cell biology: implications for cancer immunotherapy. Cancers 2018; 10: 194.
    • (2018) Cancers , vol.10 , pp. 194
    • Dahmani, A.1    Delisle, J.-S.2
  • 35
    • 51649112340 scopus 로고    scopus 로고
    • T cell-expressed proprotein convertase furin is essential for maintenance of peripheral tolerance
    • Pesu M, Watford WT, Wei L et al. T cell-expressed proprotein convertase furin is essential for maintenance of peripheral tolerance. Nature 2008; 455: 246–250.
    • (2008) Nature , vol.455 , pp. 246-250
    • Pesu, M.1    Watford, W.T.2    Wei, L.3
  • 36
    • 78650827011 scopus 로고    scopus 로고
    • Development and characterisation of an assay for furin activity
    • Bourne GL, Grainger DJ. Development and characterisation of an assay for furin activity. J Immunol Methods 2011; 364: 101–108.
    • (2011) J Immunol Methods , vol.364 , pp. 101-108
    • Bourne, G.L.1    Grainger, D.J.2
  • 37
    • 85039860563 scopus 로고    scopus 로고
    • The dark side of IFN-γ: its role in promoting cancer immunoevasion
    • Mojic M, Takeda K, Hayakawa Y. The dark side of IFN-γ: its role in promoting cancer immunoevasion. Int J Mol Sci 2017; 19: 89.
    • (2017) Int J Mol Sci , vol.19 , pp. 89
    • Mojic, M.1    Takeda, K.2    Hayakawa, Y.3
  • 38
    • 84991781106 scopus 로고    scopus 로고
    • Radiotherapy-associated furin expression and tumor invasiveness in recurrent laryngeal cancer
    • Lee M, Ryu CH, Chang HW et al. Radiotherapy-associated furin expression and tumor invasiveness in recurrent laryngeal cancer. Anticancer Res 2016; 36: 5117–5125.
    • (2016) Anticancer Res , vol.36 , pp. 5117-5125
    • Lee, M.1    Ryu, C.H.2    Chang, H.W.3
  • 39
    • 0028089159 scopus 로고
    • Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases
    • Gordon VM, Leppla SH. Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases. Infect Immun 1994; 62: 333–340.
    • (1994) Infect Immun , vol.62 , pp. 333-340
    • Gordon, V.M.1    Leppla, S.H.2
  • 40
    • 0027495717 scopus 로고
    • Evidence for involvement of furin in cleavage and activation of diphtheria toxin
    • Tsuneoka M, Nakayama K, Hatsuzawa K et al. Evidence for involvement of furin in cleavage and activation of diphtheria toxin. J Biol Chem 1993; 268: 26461–26465.
    • (1993) J Biol Chem , vol.268 , pp. 26461-26465
    • Tsuneoka, M.1    Nakayama, K.2    Hatsuzawa, K.3
  • 41
    • 0026455183 scopus 로고
    • Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol
    • Ogata M, Fryling CM, Pastan I et al. Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol. J Biol Chem 1992; 267: 25396–25401.
    • (1992) J Biol Chem , vol.267 , pp. 25396-25401
    • Ogata, M.1    Fryling, C.M.2    Pastan, I.3
  • 42
    • 0014202360 scopus 로고
    • Effect of diphtheria toxin on protein synthesis: inactivation of one of the transfer factors
    • Collier RJ. Effect of diphtheria toxin on protein synthesis: inactivation of one of the transfer factors. J Mol Biol 1967; 25: 83–98.
    • (1967) J Mol Biol , vol.25 , pp. 83-98
    • Collier, R.J.1
  • 43
    • 0025203984 scopus 로고
    • Cellular processing of the interleukin-2 fusion toxin DAB486-IL-2 and efficient delivery of diphtheria fragment A to the cytosol of target cells requires Arg194
    • Williams DP, Wen Z, Watson RS et al. Cellular processing of the interleukin-2 fusion toxin DAB486-IL-2 and efficient delivery of diphtheria fragment A to the cytosol of target cells requires Arg194. J Biol Chem 1990; 265: 20673–20677.
    • (1990) J Biol Chem , vol.265 , pp. 20673-20677
    • Williams, D.P.1    Wen, Z.2    Watson, R.S.3
  • 44
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy SS, Bresnahan PA, Leppla SH et al. 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: 16396–16402.
    • (1992) J Biol Chem , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3
  • 45
    • 0036070576 scopus 로고    scopus 로고
    • Bacteriophage control of bacterial virulence
    • Wagner PL, Waldor MK. Bacteriophage control of bacterial virulence. Infect Immun 2002; 70: 3985–3993.
    • (2002) Infect Immun , vol.70 , pp. 3985-3993
    • Wagner, P.L.1    Waldor, M.K.2
  • 46
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk HD, Garten W. Host cell proteases controlling virus pathogenicity. Trends Microbiol 1994; 2: 39–43.
    • (1994) Trends Microbiol , vol.2 , pp. 39-43
    • Klenk, H.D.1    Garten, W.2
  • 48
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk HD, Rott R. The molecular biology of influenza virus pathogenicity. Adv Virus Res 1988; 34: 247–281.
    • (1988) Adv Virus Res , vol.34 , pp. 247-281
    • Klenk, H.D.1    Rott, R.2
  • 49
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard M, Decroly E. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim Biophys Acta 2000; 1469: 121–132.
    • (2000) Biochim Biophys Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 50
    • 0026577244 scopus 로고
    • Immunological analysis of human immunodeficiency virus type 1 envelope glycoprotein proteolytic cleavage
    • Fenouillet E, Gluckman JC. Immunological analysis of human immunodeficiency virus type 1 envelope glycoprotein proteolytic cleavage. Virology 1992; 187: 825–828.
    • (1992) Virology , vol.187 , pp. 825-828
    • Fenouillet, E.1    Gluckman, J.C.2
  • 51
    • 0023678264 scopus 로고
    • Improved antigenicity of the HIV env protein by cleavage site removal
    • Kieny MP, Lathe R, Rivière Y et al. Improved antigenicity of the HIV env protein by cleavage site removal. Protein Eng 1988; 2: 219–225.
    • (1988) Protein Eng , vol.2 , pp. 219-225
    • Kieny, M.P.1    Lathe, R.2    Rivière, Y.3
  • 52
    • 0032924008 scopus 로고    scopus 로고
    • The extracellular processing of HIV-1 envelope glycoprotein gp160 by human plasmin
    • Okumura Y, Yano M, Murakami M et al. The extracellular processing of HIV-1 envelope glycoprotein gp160 by human plasmin. FEBS Lett 1999; 442: 39–42.
    • (1999) FEBS Lett , vol.442 , pp. 39-42
    • Okumura, Y.1    Yano, M.2    Murakami, M.3
  • 53
    • 0023136546 scopus 로고
    • Role of Staphylococcus protease in the development of influenza pneumonia
    • Tashiro M, Ciborowski P, Klenk H-D et al. Role of Staphylococcus protease in the development of influenza pneumonia. Nature 1987; 325: 536.
    • (1987) Nature , vol.325 , pp. 536
    • Tashiro, M.1    Ciborowski, P.2    Klenk, H.-D.3
  • 54
    • 84939654675 scopus 로고    scopus 로고
    • Influenza virus activating host proteases: identification, localization and inhibitors as potential therapeutics
    • Garten W, Braden C, Arendt A et al. Influenza virus activating host proteases: identification, localization and inhibitors as potential therapeutics. Eur J Cell Biol 2015; 94: 375–383.
    • (2015) Eur J Cell Biol , vol.94 , pp. 375-383
    • Garten, W.1    Braden, C.2    Arendt, A.3
  • 55
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Böttcher E, Matrosovich T, Beyerle M et al. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J Virol 2006; 80: 9896–9898.
    • (2006) J Virol , vol.80 , pp. 9896-9898
    • Böttcher, E.1    Matrosovich, T.2    Beyerle, M.3
  • 56
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Gröber A, Vey M, Angliker H et al. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J 1992; 11: 2407–2414.
    • (1992) EMBO J , vol.11 , pp. 2407-2414
    • Stieneke-Gröber, A.1    Vey, M.2    Angliker, H.3
  • 57
    • 0028095251 scopus 로고
    • Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses
    • Horimoto T, Nakayama K, Smeekens SP et al. Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses. J Virol 1994; 68: 6074–6078.
    • (1994) J Virol , vol.68 , pp. 6074-6078
    • Horimoto, T.1    Nakayama, K.2    Smeekens, S.P.3
  • 58
    • 0030905724 scopus 로고    scopus 로고
    • Virulence-associated sequence duplication at the hemagglutinin cleavage site of avian influenza viruses
    • Perdue ML, García M, Senne D et al. Virulence-associated sequence duplication at the hemagglutinin cleavage site of avian influenza viruses. Virus Res 1997; 49: 173–186.
    • (1997) Virus Res , vol.49 , pp. 173-186
    • Perdue, M.L.1    García, M.2    Senne, D.3
  • 59
    • 0343337638 scopus 로고    scopus 로고
    • Different hemagglutinin cleavage site variants of H7N7 in an influenza outbreak in chickens in Leipzig, Germany
    • Röhm C, Süss J, Pohle V et al. Different hemagglutinin cleavage site variants of H7N7 in an influenza outbreak in chickens in Leipzig, Germany. Virology 1996; 218: 253–257.
    • (1996) Virology , vol.218 , pp. 253-257
    • Röhm, C.1    Süss, J.2    Pohle, V.3
  • 60
    • 0024521692 scopus 로고
    • Mutations at the cleavage site of the hemagglutinin alter the pathogenicity of influenza virus a/chick/penn/83 (H5N2)
    • Ohuchi M, Orlich M, Ohuchi R et al. Mutations at the cleavage site of the hemagglutinin alter the pathogenicity of influenza virus a/chick/penn/83 (H5N2). Virology 1989; 168: 274–280.
    • (1989) Virology , vol.168 , pp. 274-280
    • Ohuchi, M.1    Orlich, M.2    Ohuchi, R.3
  • 61
    • 84873046900 scopus 로고    scopus 로고
    • Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses
    • Baron J, Tarnow C, Mayoli-Nüssle D et al. Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses. J Virol 2013; 87: 1811–1820.
    • (2013) J Virol , vol.87 , pp. 1811-1820
    • Baron, J.1    Tarnow, C.2    Mayoli-Nüssle, D.3
  • 62
    • 84892475040 scopus 로고    scopus 로고
    • A novel activation mechanism of avian influenza virus H9N2 by furin
    • Tse LV, Hamilton AM, Friling T et al. A novel activation mechanism of avian influenza virus H9N2 by furin. J Virol 2014; 88: 1673–1683.
    • (2014) J Virol , vol.88 , pp. 1673-1683
    • Tse, L.V.1    Hamilton, A.M.2    Friling, T.3
  • 63
    • 0032510732 scopus 로고    scopus 로고
    • Processing of the Ebola virus glycoprotein by the proprotein convertase furin
    • Volchkov VE, Feldmann H, Volchkova VA et al. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc Natl Acad Sci USA 1998; 95: 5762–5767.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5762-5767
    • Volchkov, V.E.1    Feldmann, H.2    Volchkova, V.A.3
  • 64
    • 0034101994 scopus 로고    scopus 로고
    • Proteolytic processing of Marburg virus glycoprotein
    • Volchkov VE, Volchkova VA, Ströher U et al. Proteolytic processing of Marburg virus glycoprotein. Virology 2000; 268: 1–6.
    • (2000) Virology , vol.268 , pp. 1-6
    • Volchkov, V.E.1    Volchkova, V.A.2    Ströher, U.3
  • 65
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the Ebola virus envelope glycoprotein: cleavage is not required for function
    • Wool-Lewis RJ, Bates P. Endoproteolytic processing of the Ebola virus envelope glycoprotein: cleavage is not required for function. J Virol 1999; 73: 1419–1426.
    • (1999) J Virol , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 66
    • 33947431606 scopus 로고    scopus 로고
    • Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates
    • Neumann G, Geisbert TW, Ebihara H et al. Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates. J Virol 2007; 81: 2995–2998.
    • (2007) J Virol , vol.81 , pp. 2995-2998
    • Neumann, G.1    Geisbert, T.W.2    Ebihara, H.3
  • 67
    • 0029589329 scopus 로고
    • GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases
    • Volchkov VE, Becker S, Volchkova VA et al. GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology 1995; 214: 421–430.
    • (1995) Virology , vol.214 , pp. 421-430
    • Volchkov, V.E.1    Becker, S.2    Volchkova, V.A.3
  • 68
    • 0033527892 scopus 로고    scopus 로고
    • ∆-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus
    • Volchkova VA, Klenk HD, Volchkov VE. ∆-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus. Virology 1999; 265: 164–171.
    • (1999) Virology , vol.265 , pp. 164-171
    • Volchkova, V.A.1    Klenk, H.D.2    Volchkov, V.E.3
  • 69
    • 84920815552 scopus 로고    scopus 로고
    • The multiple roles of sGP in Ebola pathogenesis
    • de la Vega M-A, Wong G, Kobinger GP et al. The multiple roles of sGP in Ebola pathogenesis. Viral Immunol 2015; 28: 3–9.
    • (2015) Viral Immunol , vol.28 , pp. 3-9
    • de la Vega, M.-A.1    Wong, G.2    Kobinger, G.P.3
  • 70
    • 84859500348 scopus 로고    scopus 로고
    • Degrees of maturity: the complex structure and biology of flaviviruses
    • Pierson TC, Diamond MS. Degrees of maturity: the complex structure and biology of flaviviruses. Curr Opin Virol 2012; 2: 168–175.
    • (2012) Curr Opin Virol , vol.2 , pp. 168-175
    • Pierson, T.C.1    Diamond, M.S.2
  • 71
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • Guirakhoo F, Heinz FX, Mandl CW et al. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J Gen Virol 1991; 72: 1323–1329.
    • (1991) J Gen Virol , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3
  • 72
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu I-M, Zhang W, Holdaway HA et al. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 2008; 319: 1834–1837.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.-M.1    Zhang, W.2    Holdaway, H.A.3
  • 73
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu I-M, Holdaway HA, Chipman PR et al. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J Virol 2009; 83: 12101–12107.
    • (2009) J Virol , vol.83 , pp. 12101-12107
    • Yu, I.-M.1    Holdaway, H.A.2    Chipman, P.R.3
  • 74
    • 0037236396 scopus 로고    scopus 로고
    • Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus
    • Elshuber S, Allison SL, Heinz FX et al. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. J Gen Virol 2003; 84: 183–191.
    • (2003) J Gen Virol , vol.84 , pp. 183-191
    • Elshuber, S.1    Allison, S.L.2    Heinz, F.X.3
  • 75
    • 58149388463 scopus 로고    scopus 로고
    • Functional importance of dengue virus maturation: infectious properties of immature virions
    • Zybert IA, van der Ende-Metselaar H, Wilschut J et al. Functional importance of dengue virus maturation: infectious properties of immature virions. J Gen Virol 2008; 89: 3047–3051.
    • (2008) J Gen Virol , vol.89 , pp. 3047-3051
    • Zybert, I.A.1    van der Ende-Metselaar, H.2    Wilschut, J.3
  • 76
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • Davis CW, Nguyen H-Y, Hanna SL et al. West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. J Virol 2006; 80: 1290–1301.
    • (2006) J Virol , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.-Y.2    Hanna, S.L.3
  • 78
    • 55249088356 scopus 로고    scopus 로고
    • Differential modulation of prM cleavage, extracellular particle distribution, and virus infectivity by conserved residues at nonfurin consensus positions of the dengue virus pr-M junction
    • Junjhon J, Lausumpao M, Supasa S et al. Differential modulation of prM cleavage, extracellular particle distribution, and virus infectivity by conserved residues at nonfurin consensus positions of the dengue virus pr-M junction. J Virol 2008; 82: 10776–10791.
    • (2008) J Virol , vol.82 , pp. 10776-10791
    • Junjhon, J.1    Lausumpao, M.2    Supasa, S.3
  • 79
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection
    • Richards RM, Lowy DR, Schiller JT et al. Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection. Proc Natl Acad Sci USA 2006; 103: 1522–1527.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1522-1527
    • Richards, R.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 80
    • 74749099125 scopus 로고    scopus 로고
    • The role of furin in papillomavirus infection
    • Day PM, Schiller JT. The role of furin in papillomavirus infection. Future Microbiol 2009; 4: 1255–1262.
    • (2009) Future Microbiol , vol.4 , pp. 1255-1262
    • Day, P.M.1    Schiller, J.T.2
  • 81
    • 42449153250 scopus 로고    scopus 로고
    • Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies
    • Day PM, Gambhira R, Roden RBS et al. Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies. J Virol 2008; 82: 4638–4646.
    • (2008) J Virol , vol.82 , pp. 4638-4646
    • Day, P.M.1    Gambhira, R.2    Roden, R.B.S.3
  • 82
    • 64049108517 scopus 로고    scopus 로고
    • Characterization of genotype-specific carboxyl-terminal cleavage sites of hepatitis B virus e antigen precursor and identification of furin as the candidate enzyme
    • Ito K, Kim K-H, Lok AS-F et al. Characterization of genotype-specific carboxyl-terminal cleavage sites of hepatitis B virus e antigen precursor and identification of furin as the candidate enzyme. J Virol 2009; 83: 3507–3517.
    • (2009) J Virol , vol.83 , pp. 3507-3517
    • Ito, K.1    Kim, K.-H.2    Lok, A.S.-F.3
  • 83
    • 0037428471 scopus 로고    scopus 로고
    • Proteolytic processing of the hepatitis B virus e antigen precursor. Cleavage at two furin consensus sequences
    • Messageot F, Salhi S, Eon P et al. Proteolytic processing of the hepatitis B virus e antigen precursor. Cleavage at two furin consensus sequences. J Biol Chem 2003; 278: 891–895.
    • (2003) J Biol Chem , vol.278 , pp. 891-895
    • Messageot, F.1    Salhi, S.2    Eon, P.3
  • 84
    • 0032519919 scopus 로고    scopus 로고
    • The secreted hepatitis B precore antigen can modulate the immune response to the nucleocapsid: a mechanism for persistence
    • Milich DR, Chen MK, Hughes JL et al. The secreted hepatitis B precore antigen can modulate the immune response to the nucleocapsid: a mechanism for persistence. J Immunol 1998; 160: 2013–2021.
    • (1998) J Immunol , vol.160 , pp. 2013-2021
    • Milich, D.R.1    Chen, M.K.2    Hughes, J.L.3
  • 85
    • 6944244922 scopus 로고    scopus 로고
    • A function of the hepatitis B virus precore protein is to regulate the immune response to the core antigen
    • Chen MT, Billaud J-N, Sällberg M et al. A function of the hepatitis B virus precore protein is to regulate the immune response to the core antigen. Proc Natl Acad Sci USA 2004; 101: 14913–14918.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14913-14918
    • Chen, M.T.1    Billaud, J.-N.2    Sällberg, M.3
  • 86
    • 0024469591 scopus 로고
    • The secretory core protein of human hepatitis B virus is expressed on the cell surface
    • Schlicht HJ, Schaller H. The secretory core protein of human hepatitis B virus is expressed on the cell surface. J Virol 1989; 63: 5399–5404.
    • (1989) J Virol , vol.63 , pp. 5399-5404
    • Schlicht, H.J.1    Schaller, H.2
  • 87
    • 70349229382 scopus 로고    scopus 로고
    • Influence of a single nucleotide polymorphism in the P1 promoter of the furin gene on transcription activity and hepatitis B virus infection
    • Lei RX, Shi H, Peng XM et al. Influence of a single nucleotide polymorphism in the P1 promoter of the furin gene on transcription activity and hepatitis B virus infection. Hepatology 2009; 50: 763–771.
    • (2009) Hepatology , vol.50 , pp. 763-771
    • Lei, R.X.1    Shi, H.2    Peng, X.M.3
  • 88
    • 84867647908 scopus 로고    scopus 로고
    • Rules of engagement: molecular insights from host-virus arms races
    • Daugherty MD, Malik HS. Rules of engagement: molecular insights from host-virus arms races. Annu Rev Genet 2012; 46: 677–700.
    • (2012) Annu Rev Genet , vol.46 , pp. 677-700
    • Daugherty, M.D.1    Malik, H.S.2
  • 89
    • 84862777555 scopus 로고    scopus 로고
    • SAMHD1 restricts HIV-1 by reducing the intracellular pool of deoxynucleotide triphosphates
    • Lahouassa H, Daddacha W, Hofmann H et al. SAMHD1 restricts HIV-1 by reducing the intracellular pool of deoxynucleotide triphosphates. Nat Immunol 2012; 13: 223–228.
    • (2012) Nat Immunol , vol.13 , pp. 223-228
    • Lahouassa, H.1    Daddacha, W.2    Hofmann, H.3
  • 90
    • 84857477766 scopus 로고    scopus 로고
    • The intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication
    • Gariano GR, Dell'Oste V, Bronzini M et al. The intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication. PLoS Pathog 2012; 8: e1002498.
    • (2012) PLoS Pathog , vol.8
    • Gariano, G.R.1    Dell'Oste, V.2    Bronzini, M.3
  • 91
    • 84883162740 scopus 로고    scopus 로고
    • Modulation of protease activated receptor 1 influences human metapneumovirus disease severity in a mouse model
    • Aerts L, Hamelin M-È, Rhéaume C et al. Modulation of protease activated receptor 1 influences human metapneumovirus disease severity in a mouse model. PLoS ONE 2013; 8: e72529.
    • (2013) PLoS ONE , vol.8
    • Aerts, L.1    Hamelin, M.-È.2    Rhéaume, C.3
  • 92
    • 84944629624 scopus 로고    scopus 로고
    • Neuroinflammation-induced interactions between protease-activated receptor 1 and proprotein convertases in HIV-associated neurocognitive disorder
    • Kim W, Zekas E, Lodge R et al. Neuroinflammation-induced interactions between protease-activated receptor 1 and proprotein convertases in HIV-associated neurocognitive disorder. Mol Cell Biol 2015; 35: 3684–3700.
    • (2015) Mol Cell Biol , vol.35 , pp. 3684-3700
    • Kim, W.1    Zekas, E.2    Lodge, R.3
  • 93
    • 85060640957 scopus 로고    scopus 로고
    • HIV-induced neuroinflammation: impact of PAR1 and PAR2 processing by Furin
    • Sachan V, Lodge R, Mihara K et al. HIV-induced neuroinflammation: impact of PAR1 and PAR2 processing by Furin. Cell Death Differ 2019.
    • (2019) Cell Death Differ
    • Sachan, V.1    Lodge, R.2    Mihara, K.3
  • 94
    • 84929324871 scopus 로고    scopus 로고
    • Identification of potential HIV restriction factors by combining evolutionary genomic signatures with functional analyses
    • McLaren PJ, Gawanbacht A, Pyndiah N et al. Identification of potential HIV restriction factors by combining evolutionary genomic signatures with functional analyses. Retrovirology 2015; 12: 41.
    • (2015) Retrovirology , vol.12 , pp. 41
    • McLaren, P.J.1    Gawanbacht, A.2    Pyndiah, N.3
  • 95
    • 84961221171 scopus 로고    scopus 로고
    • Guanylate Binding Protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity
    • Krapp C, Hotter D, Gawanbacht A et al. Guanylate Binding Protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity. Cell Host Microbe 2016; 19: 504–514.
    • (2016) Cell Host Microbe , vol.19 , pp. 504-514
    • Krapp, C.1    Hotter, D.2    Gawanbacht, A.3
  • 96
    • 85065235566 scopus 로고    scopus 로고
    • Guanylate-Binding Proteins 2 and 5 exert broad antiviral activity by inhibiting furin-mediated processing of viral envelope proteins
    • e10
    • Braun E, Hotter D, Koepke L et al. Guanylate-Binding Proteins 2 and 5 exert broad antiviral activity by inhibiting furin-mediated processing of viral envelope proteins. Cell Rep 2019; 27: 2092–2104. e10.
    • (2019) Cell Rep , vol.27 , pp. 2092-2104
    • Braun, E.1    Hotter, D.2    Koepke, L.3
  • 97
    • 85044653262 scopus 로고    scopus 로고
    • Distinct prognostic value of mRNA expression of guanylate-binding protein genes in skin cutaneous melanoma
    • Wang Q, Wang X, Liang Q et al. Distinct prognostic value of mRNA expression of guanylate-binding protein genes in skin cutaneous melanoma. Oncol Lett 2018; 15: 7914–7922.
    • (2018) Oncol Lett , vol.15 , pp. 7914-7922
    • Wang, Q.1    Wang, X.2    Liang, Q.3
  • 98
    • 84904723337 scopus 로고    scopus 로고
    • Interferon-inducible guanylate binding protein (GBP2) is associated with better prognosis in breast cancer and indicates an efficient T cell response
    • Godoy P, Cadenas C, Hellwig B et al. Interferon-inducible guanylate binding protein (GBP2) is associated with better prognosis in breast cancer and indicates an efficient T cell response. Breast Cancer 2014; 21: 491–499.
    • (2014) Breast Cancer , vol.21 , pp. 491-499
    • Godoy, P.1    Cadenas, C.2    Hellwig, B.3
  • 99
    • 0027429771 scopus 로고
    • Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed α 1-antitrypsin variant
    • Anderson ED, Thomas L, Hayflick JS et al. Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed α 1-antitrypsin variant. J Biol Chem 1993; 268: 24887–24891.
    • (1993) J Biol Chem , vol.268 , pp. 24887-24891
    • Anderson, E.D.1    Thomas, L.2    Hayflick, J.S.3
  • 100
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M, Hirano A, Stenglein S et al. Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J Virol 1995; 69: 3206–3210.
    • (1995) J Virol , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3
  • 102
    • 0034711298 scopus 로고    scopus 로고
    • Polyarginines are potent furin inhibitors
    • Cameron A, Appel J, Houghten RA et al. Polyarginines are potent furin inhibitors. J Biol Chem 2000; 275: 36741–36749.
    • (2000) J Biol Chem , vol.275 , pp. 36741-36749
    • Cameron, A.1    Appel, J.2    Houghten, R.A.3
  • 103
    • 0033607676 scopus 로고    scopus 로고
    • The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity
    • Zhong M, Munzer JS, Basak A et al. The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity. J Biol Chem 1999; 274: 33913–33920.
    • (1999) J Biol Chem , vol.274 , pp. 33913-33920
    • Zhong, M.1    Munzer, J.S.2    Basak, A.3
  • 104
    • 35148878210 scopus 로고    scopus 로고
    • Opposing function of the proprotein convertases furin and PACE4 on breast cancer cells’ malignant phenotypes: role of tissue inhibitors of metalloproteinase-1
    • Lapierre M, Siegfried G, Scamuffa N et al. Opposing function of the proprotein convertases furin and PACE4 on breast cancer cells’ malignant phenotypes: role of tissue inhibitors of metalloproteinase-1. Cancer Res 2007; 67: 9030–9034.
    • (2007) Cancer Res , vol.67 , pp. 9030-9034
    • Lapierre, M.1    Siegfried, G.2    Scamuffa, N.3
  • 105
    • 0036893450 scopus 로고    scopus 로고
    • The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo
    • Sarac MS, Cameron A, Lindberg I. The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo. Infect Immun 2002; 70: 7136–7139.
    • (2002) Infect Immun , vol.70 , pp. 7136-7139
    • Sarac, M.S.1    Cameron, A.2    Lindberg, I.3
  • 106
    • 58249087702 scopus 로고    scopus 로고
    • Nona-D-arginine therapy for Pseudomonas aeruginosa keratitis
    • Karicherla P, Hobden JA. Nona-D-arginine therapy for Pseudomonas aeruginosa keratitis. Invest Ophthalmol Vis Sci 2009; 50: 256–262.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 256-262
    • Karicherla, P.1    Hobden, J.A.2
  • 107
    • 77950838153 scopus 로고    scopus 로고
    • Nona-D-arginine amide for prophylaxis and treatment of experimental Pseudomonas aeruginosa keratitis
    • Karicherla P, Hobden JA. Nona-D-arginine amide for prophylaxis and treatment of experimental Pseudomonas aeruginosa keratitis. Curr Eye Res 2010; 35: 220–224.
    • (2010) Curr Eye Res , vol.35 , pp. 220-224
    • Karicherla, P.1    Hobden, J.A.2
  • 108
    • 77249117734 scopus 로고    scopus 로고
    • Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics
    • Becker GL, Sielaff F, Than ME et al. Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics. J Med Chem 2010; 53: 1067–1075.
    • (2010) J Med Chem , vol.53 , pp. 1067-1075
    • Becker, G.L.1    Sielaff, F.2    Than, M.E.3
  • 109
    • 0037743535 scopus 로고    scopus 로고
    • The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
    • Henrich S, Cameron A, Bourenkov GP et al. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat Struct Biol 2003; 10: 520–526.
    • (2003) Nat Struct Biol , vol.10 , pp. 520-526
    • Henrich, S.1    Cameron, A.2    Bourenkov, G.P.3
  • 110
    • 84924978499 scopus 로고    scopus 로고
    • Therapeutic uses of furin and its inhibitors: a patent review
    • Couture F, Kwiatkowska A, Dory YL et al. Therapeutic uses of furin and its inhibitors: a patent review. Expert Opin Ther Pat 2015; 25: 379–396.
    • (2015) Expert Opin Ther Pat , vol.25 , pp. 379-396
    • Couture, F.1    Kwiatkowska, A.2    Dory, Y.L.3
  • 111
    • 32044433491 scopus 로고    scopus 로고
    • Guanidinylated 2,5-dideoxystreptamine derivatives as anthrax lethal factor inhibitors
    • Jiao G-S, Cregar L, Goldman ME et al. Guanidinylated 2,5-dideoxystreptamine derivatives as anthrax lethal factor inhibitors. Bioorg Med Chem Lett 2006; 16: 1527–1531.
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 1527-1531
    • Jiao, G.-S.1    Cregar, L.2    Goldman, M.E.3
  • 112
    • 85019551170 scopus 로고    scopus 로고
    • Structural studies revealed active site distortions of human furin by a small molecule inhibitor
    • Dahms SO, Jiao G-S, Than ME. Structural studies revealed active site distortions of human furin by a small molecule inhibitor. ACS Chem Biol 2017; 12: 1211–1216.
    • (2017) ACS Chem Biol , vol.12 , pp. 1211-1216
    • Dahms, S.O.1    Jiao, G.-S.2    Than, M.E.3
  • 113
    • 0024424169 scopus 로고
    • Inhibition of proteolytic activation of influenza virus hemagglutinin by specific peptidyl chloroalkyl ketones
    • Garten W, Stieneke A, Shaw E et al. Inhibition of proteolytic activation of influenza virus hemagglutinin by specific peptidyl chloroalkyl ketones. Virology 1989; 172: 25–31.
    • (1989) Virology , vol.172 , pp. 25-31
    • Garten, W.1    Stieneke, A.2    Shaw, E.3
  • 114
    • 84867762574 scopus 로고    scopus 로고
    • Generation and characterization of non-competitive furin-inhibiting nanobodies
    • Zhu J, Declercq J, Roucourt B et al. Generation and characterization of non-competitive furin-inhibiting nanobodies. Biochem J 2012; 448: 73–82.
    • (2012) Biochem J , vol.448 , pp. 73-82
    • Zhu, J.1    Declercq, J.2    Roucourt, B.3
  • 115
    • 85038587128 scopus 로고    scopus 로고
    • Regnase-1 and roquin nonredundantly regulate th1 differentiation causing cardiac inflammation and fibrosis
    • Cui X, Mino T, Yoshinaga M et al. Regnase-1 and roquin nonredundantly regulate th1 differentiation causing cardiac inflammation and fibrosis. J Immunol 2017; 199: 4066–4077.
    • (2017) J Immunol , vol.199 , pp. 4066-4077
    • Cui, X.1    Mino, T.2    Yoshinaga, M.3
  • 117
    • 0026481133 scopus 로고
    • Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor
    • Inaba K, Inaba M, Romani N et al. Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor. J Exp Med 1992; 176: 1693–1702.
    • (1992) J Exp Med , vol.176 , pp. 1693-1702
    • Inaba, K.1    Inaba, M.2    Romani, N.3
  • 118
    • 0028906190 scopus 로고
    • Processing of transforming growth factor β 1 precursor by human furin convertase
    • Dubois CM, Laprise MH, Blanchette F et al. Processing of transforming growth factor β 1 precursor by human furin convertase. J Biol Chem 1995; 270: 10618–10624.
    • (1995) J Biol Chem , vol.270 , pp. 10618-10624
    • Dubois, C.M.1    Laprise, M.H.2    Blanchette, F.3
  • 119
    • 0030893704 scopus 로고    scopus 로고
    • Contrasting effects of TGF-β1 and TNF-α on the development of dendritic cells from progenitors in mouse bone marrow
    • Yamaguchi Y, Tsumura H, Miwa M et al. Contrasting effects of TGF-β1 and TNF-α on the development of dendritic cells from progenitors in mouse bone marrow. Stem Cells 1997; 15: 144–153.
    • (1997) Stem Cells , vol.15 , pp. 144-153
    • Yamaguchi, Y.1    Tsumura, H.2    Miwa, M.3
  • 120
    • 84996553234 scopus 로고    scopus 로고
    • ® DNA engineered immunotherapy as maintenance in advanced stage ovarian cancer
    • ® DNA engineered immunotherapy as maintenance in advanced stage ovarian cancer. Gynecol Oncol 2016; 143: 504–510.
    • (2016) Gynecol Oncol , vol.143 , pp. 504-510
    • Oh, J.1    Barve, M.2    Matthews, C.M.3
  • 121
    • 0023811819 scopus 로고
    • Human cytomegalovirus strain Towne glycoprotein B is processed by proteolytic cleavage
    • Spaete RR, Thayer RM, Probert WS et al. Human cytomegalovirus strain Towne glycoprotein B is processed by proteolytic cleavage. Virology 1988; 167: 207–225.
    • (1988) Virology , vol.167 , pp. 207-225
    • Spaete, R.R.1    Thayer, R.M.2    Probert, W.S.3
  • 122
    • 0022481278 scopus 로고
    • Identification and structure of the gene encoding gpII, a major glycoprotein of varicella-zoster virus
    • Keller PM, Davison AJ, Lowe RS et al. Identification and structure of the gene encoding gpII, a major glycoprotein of varicella-zoster virus. Virology 1986; 152: 181–191.
    • (1986) Virology , vol.152 , pp. 181-191
    • Keller, P.M.1    Davison, A.J.2    Lowe, R.S.3
  • 123
    • 0023115697 scopus 로고
    • Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB
    • Gong M, Ooka T, Matsuo T et al. Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. J Virol 1987; 61: 499–508.
    • (1987) J Virol , vol.61 , pp. 499-508
    • Gong, M.1    Ooka, T.2    Matsuo, T.3
  • 124
    • 0022626625 scopus 로고
    • Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41
    • Cavanagh D, Davis PJ, Pappin DJ et al. Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41. Virus Res 1986; 4: 133–143.
    • (1986) Virus Res , vol.4 , pp. 133-143
    • Cavanagh, D.1    Davis, P.J.2    Pappin, D.J.3
  • 125
    • 2442680275 scopus 로고    scopus 로고
    • Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion
    • de Haan CAM, Stadler K, Godeke G-J et al. Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion. J Virol 2004; 78: 6048–6054.
    • (2004) J Virol , vol.78 , pp. 6048-6054
    • de Haan, C.A.M.1    Stadler, K.2    Godeke, G.-J.3
  • 126
    • 0021863828 scopus 로고
    • Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution
    • Rice CM, Lenches EM, Eddy SR et al. Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution. Science 1985; 229: 726–733.
    • (1985) Science , vol.229 , pp. 726-733
    • Rice, C.M.1    Lenches, E.M.2    Eddy, S.R.3
  • 127
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler K, Allison SL, Schalich J et al. Proteolytic activation of tick-borne encephalitis virus by furin. J Virol 1997; 71: 8475–8481.
    • (1997) J Virol , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3
  • 128
    • 0038212351 scopus 로고
    • Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins
    • Rice CM, Strauss JH. Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins. Proc Natl Acad Sci USA 1981; 78: 2062–2066.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2062-2066
    • Rice, C.M.1    Strauss, J.H.2
  • 129
    • 0037369080 scopus 로고    scopus 로고
    • Furin processing and proteolytic activation of Semliki Forest virus
    • Zhang X, Fugère M, Day R et al. Furin processing and proteolytic activation of Semliki Forest virus. J Virol 2003; 77: 2981–2989.
    • (2003) J Virol , vol.77 , pp. 2981-2989
    • Zhang, X.1    Fugère, M.2    Day, R.3
  • 130
    • 0031965319 scopus 로고    scopus 로고
    • Mechanism of Borna disease virus entry into cells
    • Gonzalez-Dunia D, Cubitt B, de la Torre JC. Mechanism of Borna disease virus entry into cells. J Virol 1998; 72: 783–788.
    • (1998) J Virol , vol.72 , pp. 783-788
    • Gonzalez-Dunia, D.1    Cubitt, B.2    de la Torre, J.C.3
  • 131
    • 2642647847 scopus 로고    scopus 로고
    • Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin
    • Richt JA, Fürbringer T, Koch A et al. Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin. J Virol 1998; 72: 4528–4533.
    • (1998) J Virol , vol.72 , pp. 4528-4533
    • Richt, J.A.1    Fürbringer, T.2    Koch, A.3
  • 132
    • 33645967164 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus glycoprotein precursor is cleaved by Furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein
    • Sanchez AJ, Vincent MJ, Erickson BR et al. Crimean-Congo hemorrhagic fever virus glycoprotein precursor is cleaved by Furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein. J Virol 2006; 80: 514–525.
    • (2006) J Virol , vol.80 , pp. 514-525
    • Sanchez, A.J.1    Vincent, M.J.2    Erickson, B.R.3
  • 133
    • 0023212842 scopus 로고
    • Molecular analyses of the hemagglutinin genes of H5 influenza viruses: origin of a virulent turkey strain
    • Kawaoka Y, Nestorowicz A, Alexander DJ et al. Molecular analyses of the hemagglutinin genes of H5 influenza viruses: origin of a virulent turkey strain. Virology 1987; 158: 218–227.
    • (1987) Virology , vol.158 , pp. 218-227
    • Kawaoka, Y.1    Nestorowicz, A.2    Alexander, D.J.3
  • 134
    • 0018600608 scopus 로고
    • Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA
    • Porter AG, Barber C, Carey NH et al. Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA. Nature 1979; 282: 471–477.
    • (1979) Nature , vol.282 , pp. 471-477
    • Porter, A.G.1    Barber, C.2    Carey, N.H.3
  • 135
    • 0023235834 scopus 로고
    • Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus
    • Toyoda T, Sakaguchi T, Imai K et al. Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus. Virology 1987; 158: 242–247.
    • (1987) Virology , vol.158 , pp. 242-247
    • Toyoda, T.1    Sakaguchi, T.2    Imai, K.3
  • 136
    • 0022476649 scopus 로고
    • Fusion glycoprotein of human parainfluenza virus type 3: nucleotide sequence of the gene, direct identification of the cleavage-activation site, and comparison with other paramyxoviruses
    • Spriggs MK, Olmsted RA, Venkatesan S et al. Fusion glycoprotein of human parainfluenza virus type 3: nucleotide sequence of the gene, direct identification of the cleavage-activation site, and comparison with other paramyxoviruses. Virology 1986; 152: 241–251.
    • (1986) Virology , vol.152 , pp. 241-251
    • Spriggs, M.K.1    Olmsted, R.A.2    Venkatesan, S.3
  • 137
    • 0023226696 scopus 로고
    • Cloning and sequencing of the mumps virus fusion protein gene
    • Waxham MN, Server AC, Goodman HM et al. Cloning and sequencing of the mumps virus fusion protein gene. Virology 1987; 159: 381–388.
    • (1987) Virology , vol.159 , pp. 381-388
    • Waxham, M.N.1    Server, A.C.2    Goodman, H.M.3
  • 138
    • 0022864334 scopus 로고
    • The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston strain): a comparison of fusion proteins from several different paramyxoviruses
    • Richardson C, Hull D, Greer P et al. The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston strain): a comparison of fusion proteins from several different paramyxoviruses. Virology 1986; 155: 508–523.
    • (1986) Virology , vol.155 , pp. 508-523
    • Richardson, C.1    Hull, D.2    Greer, P.3
  • 139
    • 0344919162 scopus 로고
    • Fusion protein of the paramyxovirus simian virus 5: nucleotide sequence of mRNA predicts a highly hydrophobic glycoprotein
    • Paterson RG, Harris TJ, Lamb RA. Fusion protein of the paramyxovirus simian virus 5: nucleotide sequence of mRNA predicts a highly hydrophobic glycoprotein. Proc Natl Acad Sci USA 1984; 81: 6706–6710.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6706-6710
    • Paterson, R.G.1    Harris, T.J.2    Lamb, R.A.3
  • 140
    • 0021742698 scopus 로고
    • Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus
    • Collins PL, Huang YT, Wertz GW. Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus. Proc Natl Acad Sci USA 1984; 81: 7683–7687.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7683-7687
    • Collins, P.L.1    Huang, Y.T.2    Wertz, G.W.3
  • 141
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune JM, Rabin LB, Feinberg MB et al. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 1988; 53: 55–67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3
  • 142
    • 0022252943 scopus 로고
    • Structural characterization of the avian retrovirus reverse transcriptase and endonuclease domains
    • Grandgenett D, Quinn T, Hippenmeyer PJ et al. Structural characterization of the avian retrovirus reverse transcriptase and endonuclease domains. J Biol Chem 1985; 260: 8243–8249.
    • (1985) J Biol Chem , vol.260 , pp. 8243-8249
    • Grandgenett, D.1    Quinn, T.2    Hippenmeyer, P.J.3
  • 143
    • 0023199650 scopus 로고
    • The role of envelope glycoprotein processing in murine leukemia virus infection
    • Freed EO, Risser R. The role of envelope glycoprotein processing in murine leukemia virus infection. J Virol 1987; 61: 2852–2856.
    • (1987) J Virol , vol.61 , pp. 2852-2856
    • Freed, E.O.1    Risser, R.2
  • 144
    • 10044260072 scopus 로고    scopus 로고
    • Furin-mediated cleavage of the feline foamy virus Env leader protein
    • Geiselhart V, Bastone P, Kempf T et al. Furin-mediated cleavage of the feline foamy virus Env leader protein. J Virol 2004; 78: 13573–13581.
    • (2004) J Virol , vol.78 , pp. 13573-13581
    • Geiselhart, V.1    Bastone, P.2    Kempf, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.