메뉴 건너뛰기




Volumn 140, Issue , 2017, Pages 8-15

Proprotein convertase inhibition: Paralyzing the cell's master switches

Author keywords

Molecular therapy; Proprotein convertases; Tumor progression

Indexed keywords

ALPHA 1 ANTITRYPSIN; CHLOROMETHYLKETONE DERIVATIVE; FURIN; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; NANOBODY; PEPTIDOMIMETIC AGENT; POLYARGININE; PRODRUG; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SHORT HAIRPIN RNA; STREPTAMINE DERIVATIVE; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; ISOENZYME; NEW DRUG; TUMOR PROTEIN;

EID: 85020131888     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2017.04.027     Document Type: Review
Times cited : (37)

References (116)
  • 1
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: from protein traffic to embryogenesis and disease, Nature reviews
    • Thomas, G., Furin at the cutting edge: from protein traffic to embryogenesis and disease, Nature reviews. Mol. Cell Biol 3:10 (2002), 753–766.
    • (2002) Mol. Cell Biol , vol.3 , Issue.10 , pp. 753-766
    • Thomas, G.1
  • 2
    • 13044279492 scopus 로고    scopus 로고
    • Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization
    • Seidah, N.G., Mowla, S.J., Hamelin, J., Mamarbachi, A.M., Benjannet, S., Toure, B.B., et al. Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. PNAS 96:4 (1999), 1321–1326.
    • (1999) PNAS , vol.96 , Issue.4 , pp. 1321-1326
    • Seidah, N.G.1    Mowla, S.J.2    Hamelin, J.3    Mamarbachi, A.M.4    Benjannet, S.5    Toure, B.B.6
  • 3
    • 0037417807 scopus 로고    scopus 로고
    • The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation
    • Seidah, N.G., Benjannet, S., Wickham, L., Marcinkiewicz, J., Jasmin, S.B., Stifani, S., et al. The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation. PNAS 100:3 (2003), 928–933.
    • (2003) PNAS , vol.100 , Issue.3 , pp. 928-933
    • Seidah, N.G.1    Benjannet, S.2    Wickham, L.3    Marcinkiewicz, J.4    Jasmin, S.B.5    Stifani, S.6
  • 4
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah, N.G., Prat, A., The biology and therapeutic targeting of the proprotein convertases. Nat. Rev. Drug Discov. 11:5 (2012), 367–383.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , Issue.5 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 5
    • 84881238159 scopus 로고    scopus 로고
    • The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions
    • Seidah, N.G., Sadr, M.S., Chretien, M., Mbikay, M., The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions. J. Biol. Chem. 288:30 (2013), 21473–21481.
    • (2013) J. Biol. Chem. , vol.288 , Issue.30 , pp. 21473-21481
    • Seidah, N.G.1    Sadr, M.S.2    Chretien, M.3    Mbikay, M.4
  • 6
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: “master switches” in the regulation of tumor growth and progression
    • Bassi, D.E., Fu, J., Lopez de Cicco, R., Klein-Szanto, A.J., Proprotein convertases: “master switches” in the regulation of tumor growth and progression. Mol. Carcinog. 44:3 (2005), 151–161.
    • (2005) Mol. Carcinog. , vol.44 , Issue.3 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de Cicco, R.3    Klein-Szanto, A.J.4
  • 7
    • 0038461962 scopus 로고    scopus 로고
    • Curbing activation: proprotein convertases in homeostasis and pathology
    • Taylor, N.A., Van De Ven, W.J., Creemers, J.W., Curbing activation: proprotein convertases in homeostasis and pathology. FASEB J. 7:10 (2003), 1215–1227.
    • (2003) FASEB J. , vol.7 , Issue.10 , pp. 1215-1227
    • Taylor, N.A.1    Van De Ven, W.J.2    Creemers, J.W.3
  • 8
    • 27744541223 scopus 로고    scopus 로고
    • Inhibitors of proprotein convertases
    • Basak, A., Inhibitors of proprotein convertases. J. Mol. Med. (Berlin, Germany) 83:11 (2005), 844–855.
    • (2005) J. Mol. Med. (Berlin, Germany) , vol.83 , Issue.11 , pp. 844-855
    • Basak, A.1
  • 9
    • 84860380797 scopus 로고    scopus 로고
    • On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications
    • Couture, F., D'Anjou, F., Day, R., On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications. Biomol. Concepts 2:5 (2011), 421–438.
    • (2011) Biomol. Concepts , vol.2 , Issue.5 , pp. 421-438
    • Couture, F.1    D'Anjou, F.2    Day, R.3
  • 10
    • 42649086528 scopus 로고    scopus 로고
    • Knock-out mouse models of proprotein convertases: unique functions or redundancy?
    • Creemers, J.W., Khatib, A.M., Knock-out mouse models of proprotein convertases: unique functions or redundancy?. Front. Biosci. 13 (2008), 4960–4971.
    • (2008) Front. Biosci. , vol.13 , pp. 4960-4971
    • Creemers, J.W.1    Khatib, A.M.2
  • 11
  • 12
    • 0035141634 scopus 로고    scopus 로고
    • Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme
    • Dubois, C.M., Blanchette, F., Laprise, M.H., Leduc, R., Grondin, F., Seidah, N.G., Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme. Am. J. Pathol. 158:1 (2001), 305–316.
    • (2001) Am. J. Pathol. , vol.158 , Issue.1 , pp. 305-316
    • Dubois, C.M.1    Blanchette, F.2    Laprise, M.H.3    Leduc, R.4    Grondin, F.5    Seidah, N.G.6
  • 13
    • 0038792251 scopus 로고    scopus 로고
    • Epigenetic regulation of proprotein convertase PACE4 gene expression in human ovarian cancer cells
    • Fu, Y., Campbell, E.J., Shepherd, T.G., Nachtigal, M.W., Epigenetic regulation of proprotein convertase PACE4 gene expression in human ovarian cancer cells. Mol. Cancer Res.: MCR 1:8 (2003), 569–576.
    • (2003) Mol. Cancer Res.: MCR , vol.1 , Issue.8 , pp. 569-576
    • Fu, Y.1    Campbell, E.J.2    Shepherd, T.G.3    Nachtigal, M.W.4
  • 14
    • 34447118236 scopus 로고    scopus 로고
    • Increased expression of the pro-protein convertase furin predicts decreased survival in ovarian cancer
    • Page, R.E., Klein-Szanto, A.J., Litwin, S., Nicolas, E., Al-Jumaily, R., Alexander, P., et al. Increased expression of the pro-protein convertase furin predicts decreased survival in ovarian cancer. Cell. Oncol. 29:4 (2007), 289–299.
    • (2007) Cell. Oncol. , vol.29 , Issue.4 , pp. 289-299
    • Page, R.E.1    Klein-Szanto, A.J.2    Litwin, S.3    Nicolas, E.4    Al-Jumaily, R.5    Alexander, P.6
  • 17
    • 84941649635 scopus 로고    scopus 로고
    • Enhanced aggressiveness of benzopyrene-induced squamous carcinomas in transgenic mice overexpressing the proprotein convertase PACE4 (PCSK6)
    • Bassi, D.E., Cenna, J., Zhang, J., Cukierman, E., Klein-Szanto, A.J., Enhanced aggressiveness of benzopyrene-induced squamous carcinomas in transgenic mice overexpressing the proprotein convertase PACE4 (PCSK6). Mol. Carcinog. 54:10 (2015), 1122–1131.
    • (2015) Mol. Carcinog. , vol.54 , Issue.10 , pp. 1122-1131
    • Bassi, D.E.1    Cenna, J.2    Zhang, J.3    Cukierman, E.4    Klein-Szanto, A.J.5
  • 18
    • 77954964400 scopus 로고    scopus 로고
    • Proprotein convertase inhibition results in decreased skin cell proliferation, tumorigenesis, and metastasis
    • Bassi, D.E., Zhang, J., Cenna, J., Litwin, S., Cukierman, E., Klein-Szanto, A.J., Proprotein convertase inhibition results in decreased skin cell proliferation, tumorigenesis, and metastasis. Neoplasia (New York, N.Y.) 12:7 (2010), 516–526.
    • (2010) Neoplasia (New York, N.Y.) , vol.12 , Issue.7 , pp. 516-526
    • Bassi, D.E.1    Zhang, J.2    Cenna, J.3    Litwin, S.4    Cukierman, E.5    Klein-Szanto, A.J.6
  • 20
    • 84862812875 scopus 로고    scopus 로고
    • A role for PACE4 in osteoarthritis pain: evidence from human genetic association and null mutant phenotype
    • Malfait, A.M., Seymour, A.B., Gao, F., Tortorella, M.D., Le Graverand-Gastineau, M.P., Wood, L.S., A role for PACE4 in osteoarthritis pain: evidence from human genetic association and null mutant phenotype. Ann. Rheum. Dis. 71:6 (2012), 1042–1048.
    • (2012) Ann. Rheum. Dis. , vol.71 , Issue.6 , pp. 1042-1048
    • Malfait, A.M.1    Seymour, A.B.2    Gao, F.3    Tortorella, M.D.4    Le Graverand-Gastineau, M.P.5    Wood, L.S.6
  • 21
  • 22
    • 84886787514 scopus 로고    scopus 로고
    • Short-term TNFalpha shedding is independent of cytoplasmic phosphorylation or furin cleavage of ADAM17
    • Schwarz, J., Broder, C., Helmstetter, A., Schmidt, S., Yan, I., Muller, M., et al. Short-term TNFalpha shedding is independent of cytoplasmic phosphorylation or furin cleavage of ADAM17. BBA 1833:12 (2013), 3355–3367.
    • (2013) BBA , vol.1833 , Issue.12 , pp. 3355-3367
    • Schwarz, J.1    Broder, C.2    Helmstetter, A.3    Schmidt, S.4    Yan, I.5    Muller, M.6
  • 23
    • 84911863918 scopus 로고    scopus 로고
    • Post-transcriptional modification of pro-BNP in heart failure: is glycosylation and circulating furin key for cardiovascular homeostasis?
    • Ichiki, T., Burnett, J.C. Jr, Post-transcriptional modification of pro-BNP in heart failure: is glycosylation and circulating furin key for cardiovascular homeostasis?. Eur. Heart. J. 35:43 (2014), 3001–3003.
    • (2014) Eur. Heart. J. , vol.35 , Issue.43 , pp. 3001-3003
    • Ichiki, T.1    Burnett, J.C.2
  • 24
    • 84905819404 scopus 로고    scopus 로고
    • Hepatic overexpression of the prodomain of furin lessens progression of atherosclerosis and reduces vascular remodeling in response to injury
    • Lei, X., Basu, D., Li, Z., Zhang, M., Rudic, R.D., Jiang, X.C., et al. Hepatic overexpression of the prodomain of furin lessens progression of atherosclerosis and reduces vascular remodeling in response to injury. Atherosclerosis 236:1 (2014), 121–130.
    • (2014) Atherosclerosis , vol.236 , Issue.1 , pp. 121-130
    • Lei, X.1    Basu, D.2    Li, Z.3    Zhang, M.4    Rudic, R.D.5    Jiang, X.C.6
  • 25
    • 84936752765 scopus 로고    scopus 로고
    • A genome-wide expression quantitative trait loci analysis of proprotein convertase subtilisin/kexin enzymes identifies a novel regulatory gene variant for FURIN expression and blood pressure
    • Turpeinen, H., Seppala, I., Lyytikainen, L.P., Raitoharju, E., Hutri-Kahonen, N., Levula, M., et al. A genome-wide expression quantitative trait loci analysis of proprotein convertase subtilisin/kexin enzymes identifies a novel regulatory gene variant for FURIN expression and blood pressure. Hum. Genet. 134:6 (2015), 627–636.
    • (2015) Hum. Genet. , vol.134 , Issue.6 , pp. 627-636
    • Turpeinen, H.1    Seppala, I.2    Lyytikainen, L.P.3    Raitoharju, E.4    Hutri-Kahonen, N.5    Levula, M.6
  • 26
    • 74749099125 scopus 로고    scopus 로고
    • The role of furin in papillomavirus infection
    • Day, P.M., Schiller, J.T., The role of furin in papillomavirus infection. Fut. Microbiol. 4:10 (2009), 1255–1262.
    • (2009) Fut. Microbiol. , vol.4 , Issue.10 , pp. 1255-1262
    • Day, P.M.1    Schiller, J.T.2
  • 28
    • 28244470961 scopus 로고    scopus 로고
    • Tip of another iceberg: Drosophila serpins
    • Reichhart, J.M., Tip of another iceberg: Drosophila serpins. Trends Cell. Biol. 15:12 (2005), 659–665.
    • (2005) Trends Cell. Biol. , vol.15 , Issue.12 , pp. 659-665
    • Reichhart, J.M.1
  • 29
    • 79958141469 scopus 로고    scopus 로고
    • Proteolytic cleavage of Notch: “HIT and RUN”
    • van Tetering, G., Vooijs, M., Proteolytic cleavage of Notch: “HIT and RUN”. Curr. Mol. Med. 11:4 (2011), 255–269.
    • (2011) Curr. Mol. Med. , vol.11 , Issue.4 , pp. 255-269
    • van Tetering, G.1    Vooijs, M.2
  • 31
    • 3042852155 scopus 로고    scopus 로고
    • Simultaneous expression of furin and vascular endothelial growth factor in human oral tongue squamous cell carcinoma progression
    • Lopez de Cicco, R., Watson, J.C., Bassi, D.E., Litwin, S., Klein-Szanto, A.J., Simultaneous expression of furin and vascular endothelial growth factor in human oral tongue squamous cell carcinoma progression. Clin. Cancer Res. 10:13 (2004), 4480–4488.
    • (2004) Clin. Cancer Res. , vol.10 , Issue.13 , pp. 4480-4488
    • Lopez de Cicco, R.1    Watson, J.C.2    Bassi, D.E.3    Litwin, S.4    Klein-Szanto, A.J.5
  • 32
    • 85006021755 scopus 로고    scopus 로고
    • The proprotein convertases in hypercholesterolemia and cardiovascular diseases: emphasis on proprotein convertase subtilisin/kexin 9
    • Seidah, N.G., Abifadel, M., Prost, S., Boileau, C., Prat, A., The proprotein convertases in hypercholesterolemia and cardiovascular diseases: emphasis on proprotein convertase subtilisin/kexin 9. Pharmacol. Rev. 69:1 (2017), 33–52.
    • (2017) Pharmacol. Rev. , vol.69 , Issue.1 , pp. 33-52
    • Seidah, N.G.1    Abifadel, M.2    Prost, S.3    Boileau, C.4    Prat, A.5
  • 33
    • 84996538521 scopus 로고    scopus 로고
    • Proprotein convertase subtilisin / kexin 9 (PCSK9) inhibitors and the future of dyslipidemia therapy: an updated patent review (2011–2015)
    • Elbitar, S., Khoury, P.E., Ghaleb, Y., Rabes, J.P., Varret, M., Seidah, N.G., et al. Proprotein convertase subtilisin / kexin 9 (PCSK9) inhibitors and the future of dyslipidemia therapy: an updated patent review (2011–2015). Expert Opin. Ther. Pat. 26:12 (2016), 1377–1392.
    • (2016) Expert Opin. Ther. Pat. , vol.26 , Issue.12 , pp. 1377-1392
    • Elbitar, S.1    Khoury, P.E.2    Ghaleb, Y.3    Rabes, J.P.4    Varret, M.5    Seidah, N.G.6
  • 34
    • 85007605396 scopus 로고    scopus 로고
    • Proprotein convertase subtilisin/kexin type 9 enzyme inhibitors: an emerging new therapeutic option for the treatment of dyslipidemia
    • Mazhar, F., Haider, N., Proprotein convertase subtilisin/kexin type 9 enzyme inhibitors: an emerging new therapeutic option for the treatment of dyslipidemia. J. Pharmacol. Pharmacother. 7:4 (2016), 190–193.
    • (2016) J. Pharmacol. Pharmacother. , vol.7 , Issue.4 , pp. 190-193
    • Mazhar, F.1    Haider, N.2
  • 35
    • 84977078991 scopus 로고    scopus 로고
    • PCSK9 inhibition with monoclonal antibodies: modern management of hypercholesterolemia
    • Ito, M.K., Santos, R.D., PCSK9 inhibition with monoclonal antibodies: modern management of hypercholesterolemia. J. Clin. Pharmacol. 57:1 (2017), 7–32.
    • (2017) J. Clin. Pharmacol. , vol.57 , Issue.1 , pp. 7-32
    • Ito, M.K.1    Santos, R.D.2
  • 36
    • 85014244905 scopus 로고    scopus 로고
    • PCSK9 inhibitors
    • Natarajan, P., Kathiresan, S., PCSK9 inhibitors. Cell, 165(5), 2016, 1037.
    • (2016) Cell , vol.165 , Issue.5 , pp. 1037
    • Natarajan, P.1    Kathiresan, S.2
  • 37
    • 84981717409 scopus 로고    scopus 로고
    • Monoclonal antibodies for the treatment of hypercholesterolemia: targeting PCSK9
    • Alkindi, M., Siminovitch, K.A., Gupta, M., Genest, J., Monoclonal antibodies for the treatment of hypercholesterolemia: targeting PCSK9. Can. J. Cardiol. 32:12 (2016), 1552–1560.
    • (2016) Can. J. Cardiol. , vol.32 , Issue.12 , pp. 1552-1560
    • Alkindi, M.1    Siminovitch, K.A.2    Gupta, M.3    Genest, J.4
  • 38
    • 84966293831 scopus 로고    scopus 로고
    • PCSK9 inhibition in the management of hyperlipidemia: focus on evolocumab
    • Blom, D.J., Dent, R., Castro, R.C., Toth, P.P., PCSK9 inhibition in the management of hyperlipidemia: focus on evolocumab. Vasc. Health Risk Manag. 12 (2016), 185–197.
    • (2016) Vasc. Health Risk Manag. , vol.12 , pp. 185-197
    • Blom, D.J.1    Dent, R.2    Castro, R.C.3    Toth, P.P.4
  • 40
    • 85017484987 scopus 로고    scopus 로고
    • PCSK9 inhibitors - mechanisms of action
    • Page, M.M., Watts, G.F., PCSK9 inhibitors - mechanisms of action. Australian Prescriber 39:5 (2016), 164–167.
    • (2016) Australian Prescriber , vol.39 , Issue.5 , pp. 164-167
    • Page, M.M.1    Watts, G.F.2
  • 41
    • 84979942215 scopus 로고    scopus 로고
    • Therapeutic efficacy of PCSK9 monoclonal antibodies in statin-nonresponsive patients with hypercholesterolemia and dyslipidemia: A systematic review and meta-analysis
    • Peng, W., Qiang, F., Peng, W., Qian, Z., Ke, Z., Yi, L., et al. Therapeutic efficacy of PCSK9 monoclonal antibodies in statin-nonresponsive patients with hypercholesterolemia and dyslipidemia: A systematic review and meta-analysis. Int. J. Cardiol. 222 (2016), 119–129.
    • (2016) Int. J. Cardiol. , vol.222 , pp. 119-129
    • Peng, W.1    Qiang, F.2    Peng, W.3    Qian, Z.4    Ke, Z.5    Yi, L.6
  • 42
    • 84981341424 scopus 로고    scopus 로고
    • PCSK9 inhibition as an emerging lipid lowering therapy: unanswered questions
    • Rallidis, L.S., Lekakis, J., PCSK9 inhibition as an emerging lipid lowering therapy: unanswered questions. Hellenic J. Cardiol. 57:2 (2016), 86–91.
    • (2016) Hellenic J. Cardiol. , vol.57 , Issue.2 , pp. 86-91
    • Rallidis, L.S.1    Lekakis, J.2
  • 43
    • 84992694478 scopus 로고    scopus 로고
    • Nonstatins and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors: role in non-familial hypercholesterolemia
    • Robinson, J.G., Nonstatins and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors: role in non-familial hypercholesterolemia. Prog. Cardiovasc. Dis. 59:2 (2016), 165–171.
    • (2016) Prog. Cardiovasc. Dis. , vol.59 , Issue.2 , pp. 165-171
    • Robinson, J.G.1
  • 44
    • 85017501819 scopus 로고    scopus 로고
    • PCSK9 inhibitors - clinical applications
    • Schmidli, R., PCSK9 inhibitors - clinical applications. Australian Prescriber 39:5 (2016), 168–170.
    • (2016) Australian Prescriber , vol.39 , Issue.5 , pp. 168-170
    • Schmidli, R.1
  • 45
    • 85026614597 scopus 로고    scopus 로고
    • PCSK9 inhibition: a promise fulfilled?
    • White, K., Mohan, C., Rocco, M., PCSK9 inhibition: a promise fulfilled?. Cleve Clin. J. Med. 83:11 Suppl 2 (2016), S36–s44.
    • (2016) Cleve Clin. J. Med. , vol.83 , Issue.11 , pp. S36-s44
    • White, K.1    Mohan, C.2    Rocco, M.3
  • 46
    • 84863221458 scopus 로고    scopus 로고
    • Furin inhibitors: importance of the positive formal charge and beyond
    • Lopez-Vallejo, F., Martinez-Mayorga, K., Furin inhibitors: importance of the positive formal charge and beyond. Bioorg. Med. Chem. Lett. 20:14 (2012), 4462–4471.
    • (2012) Bioorg. Med. Chem. Lett. , vol.20 , Issue.14 , pp. 4462-4471
    • Lopez-Vallejo, F.1    Martinez-Mayorga, K.2
  • 47
    • 77649083093 scopus 로고    scopus 로고
    • Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors
    • Tian, S., Jianhua, W., Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors. Int. J. Biol. Sci. 6:1 (2010), 89–95.
    • (2010) Int. J. Biol. Sci. , vol.6 , Issue.1 , pp. 89-95
    • Tian, S.1    Jianhua, W.2
  • 48
    • 0028818056 scopus 로고
    • Synthesis of tight binding inhibitors and their action on the proprotein-processing enzyme furin
    • Angliker, H., Synthesis of tight binding inhibitors and their action on the proprotein-processing enzyme furin. J. Med. Chem. 38:20 (1995), 4014–4018.
    • (1995) J. Med. Chem. , vol.38 , Issue.20 , pp. 4014-4018
    • Angliker, H.1
  • 49
    • 0036893450 scopus 로고    scopus 로고
    • The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo
    • Sarac, M.S., Cameron, A., Lindberg, I., The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo. Infect. Immun. 70:12 (2002), 7136–7139.
    • (2002) Infect. Immun. , vol.70 , Issue.12 , pp. 7136-7139
    • Sarac, M.S.1    Cameron, A.2    Lindberg, I.3
  • 51
    • 0034711298 scopus 로고    scopus 로고
    • Polyarginines are potent furin inhibitors
    • Cameron, A., Appel, J., Houghten, R.A., Lindberg, I., Polyarginines are potent furin inhibitors. J. Biol. Chem. 275:47 (2000), 36741–36749.
    • (2000) J. Biol. Chem. , vol.275 , Issue.47 , pp. 36741-36749
    • Cameron, A.1    Appel, J.2    Houghten, R.A.3    Lindberg, I.4
  • 52
    • 33845865278 scopus 로고    scopus 로고
    • Short polybasic peptide sequences are potent inhibitors of PC5/6 and PC7: Use of positional scanning-synthetic peptide combinatorial libraries as a tool for the optimization of inhibitory sequences
    • Fugere, M., Appel, J., Houghten, R.A., Lindberg, I., Day, R., Short polybasic peptide sequences are potent inhibitors of PC5/6 and PC7: Use of positional scanning-synthetic peptide combinatorial libraries as a tool for the optimization of inhibitory sequences. Mol. Pharmacol. 71:1 (2007), 323–332.
    • (2007) Mol. Pharmacol. , vol.71 , Issue.1 , pp. 323-332
    • Fugere, M.1    Appel, J.2    Houghten, R.A.3    Lindberg, I.4    Day, R.5
  • 54
    • 84989950483 scopus 로고    scopus 로고
    • Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism
    • 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. PNAS 113:40 (2016), 11196–11201.
    • (2016) PNAS , vol.113 , Issue.40 , pp. 11196-11201
    • Dahms, S.O.1    Arciniega, M.2    Steinmetzer, T.3    Huber, R.4    Than, M.E.5
  • 55
    • 9644281041 scopus 로고    scopus 로고
    • Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity
    • Henrich, S., Lindberg, I., Bode, W., Than, M.E., Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J. Mol. Biol. 345:2 (2005), 211–227.
    • (2005) J. Mol. Biol. , vol.345 , Issue.2 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 56
    • 33845922116 scopus 로고    scopus 로고
    • Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine
    • Jiao, G.S., Cregar, L., Wang, J., Millis, S.Z., Tang, C., O'Malley, S., et al. Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine. PNAS 103:52 (2006), 19707–19712.
    • (2006) PNAS , vol.103 , Issue.52 , pp. 19707-19712
    • Jiao, G.S.1    Cregar, L.2    Wang, J.3    Millis, S.Z.4    Tang, C.5    O'Malley, S.6
  • 58
    • 84862644095 scopus 로고    scopus 로고
    • Highly potent inhibitors of proprotein convertase furin as potential drugs for treatment of infectious diseases
    • Becker, G.L., Lu, Y., Hardes, K., Strehlow, B., Levesque, C., Lindberg, I., et al. Highly potent inhibitors of proprotein convertase furin as potential drugs for treatment of infectious diseases. J. Biol. Chem. 287:26 (2012), 21992–22003.
    • (2012) J. Biol. Chem. , vol.287 , Issue.26 , pp. 21992-22003
    • Becker, G.L.1    Lu, Y.2    Hardes, K.3    Strehlow, B.4    Levesque, C.5    Lindberg, I.6
  • 59
    • 84870985285 scopus 로고    scopus 로고
    • The Multi-Leu peptide inhibitor discriminates between PACE4 and furin and exhibits antiproliferative effects on prostate cancer cells
    • Levesque, C., Fugere, M., Kwiatkowska, A., Couture, F., Desjardins, R., Routhier, S., P., et al. The Multi-Leu peptide inhibitor discriminates between PACE4 and furin and exhibits antiproliferative effects on prostate cancer cells. J. Med. Chem. 55:23 (2012), 10501–10511.
    • (2012) J. Med. Chem. , vol.55 , Issue.23 , pp. 10501-10511
    • Levesque, C.1    Fugere, M.2    Kwiatkowska, A.3    Couture, F.4    Desjardins, R.5    Routhier, S.6    P.7
  • 60
    • 84957558906 scopus 로고    scopus 로고
    • Novel insights into structure-activity relationships of N-terminally modified PACE4 inhibitors
    • Kwiatkowska, A., Couture, F., Levesque, C., Ly, K., Beauchemin, S., Desjardins, R., Neugebauer, W., et al. Novel insights into structure-activity relationships of N-terminally modified PACE4 inhibitors. ChemMedChem 11:3 (2016), 289–301.
    • (2016) ChemMedChem , vol.11 , Issue.3 , pp. 289-301
    • Kwiatkowska, A.1    Couture, F.2    Levesque, C.3    Ly, K.4    Beauchemin, S.5    Desjardins, R.6    Neugebauer, W.7
  • 61
    • 84924264140 scopus 로고    scopus 로고
    • PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation
    • Levesque, C., Couture, F., Kwiatkowska, A., Desjardins, R., Guerin, B., Neugebauer, W.A., PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation. Oncotarget 6:6 (2015), 3680–3693.
    • (2015) Oncotarget , vol.6 , Issue.6 , pp. 3680-3693
    • Levesque, C.1    Couture, F.2    Kwiatkowska, A.3    Desjardins, R.4    Guerin, B.5    Neugebauer, W.A.6
  • 62
  • 63
    • 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, J.S., Basak, A., Benjannet, S., Mowla, S.J., Decroly, E., 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. 274:48 (1999), 33913–33920.
    • (1999) J. Biol. Chem. , vol.274 , Issue.48 , pp. 33913-33920
    • Zhong, M.1    Munzer, J.S.2    Basak, A.3    Benjannet, S.4    Mowla, S.J.5    Decroly, E.6
  • 64
    • 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., Bontemps, Y., Calvo, F., Seidah, N.G., 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. 67:19 (2007), 9030–9034.
    • (2007) Cancer Res. , vol.67 , Issue.19 , pp. 9030-9034
    • Lapierre, M.1    Siegfried, G.2    Scamuffa, N.3    Bontemps, Y.4    Calvo, F.5    Seidah, N.G.6
  • 65
    • 20144371230 scopus 로고    scopus 로고
    • Human carcinoma cell growth and invasiveness is impaired by the propeptide of the ubiquitous proprotein convertase furin
    • Lopez de Cicco, R., Bassi, D.E., Zucker, S., Seidah, N.G., Klein-Szanto, A.J., Human carcinoma cell growth and invasiveness is impaired by the propeptide of the ubiquitous proprotein convertase furin. Cancer Res. 65:10 (2005), 4162–4171.
    • (2005) Cancer Res. , vol.65 , Issue.10 , pp. 4162-4171
    • Lopez de Cicco, R.1    Bassi, D.E.2    Zucker, S.3    Seidah, N.G.4    Klein-Szanto, A.J.5
  • 66
    • 54349122894 scopus 로고    scopus 로고
    • Regulation of prohepcidin processing and activity by the subtilisin-like proprotein convertases Furin, PC5, PACE4 and PC7
    • Scamuffa, N., Basak, A., Lalou, C., Wargnier, A., Marcinkiewicz, J., Siegfried, G., et al. Regulation of prohepcidin processing and activity by the subtilisin-like proprotein convertases Furin, PC5, PACE4 and PC7. Gut 57:11 (2008), 1573–1582.
    • (2008) Gut , vol.57 , Issue.11 , pp. 1573-1582
    • Scamuffa, N.1    Basak, A.2    Lalou, C.3    Wargnier, A.4    Marcinkiewicz, J.5    Siegfried, G.6
  • 67
    • 84923651483 scopus 로고    scopus 로고
    • Furin mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation
    • Chen, Y., Zhang, J., Deng, M., Furin mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation. J. Neurosci. Res. 93:1 (2015), 189–194.
    • (2015) J. Neurosci. Res. , vol.93 , Issue.1 , pp. 189-194
    • Chen, Y.1    Zhang, J.2    Deng, M.3
  • 68
    • 0020510606 scopus 로고
    • Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder
    • Owen, M.C., Brennan, S.O., Lewis, J.H., Carrell, R.W., Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder. NEJM 309:12 (1983), 694–698.
    • (1983) NEJM , vol.309 , Issue.12 , pp. 694-698
    • Owen, M.C.1    Brennan, S.O.2    Lewis, J.H.3    Carrell, R.W.4
  • 69
    • 0032560449 scopus 로고    scopus 로고
    • alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent
    • Jean, F., Stella, K., Thomas, L., Liu, G., Xiang, Y., Reason, A.J., et al. alpha1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent. PNAS 95:13 (1998), 7293–7298.
    • (1998) PNAS , vol.95 , Issue.13 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Reason, A.J.6
  • 70
    • 0032502868 scopus 로고    scopus 로고
    • Serpin-like properties of alpha1-antitrypsin Portland towards furin convertase
    • Dufour, E.K., Denault, J.B., Hopkins, P.C., Leduc, R., Serpin-like properties of alpha1-antitrypsin Portland towards furin convertase. FEBS Lett. 426:1 (1998), 41–46.
    • (1998) FEBS Lett. , vol.426 , Issue.1 , pp. 41-46
    • Dufour, E.K.1    Denault, J.B.2    Hopkins, P.C.3    Leduc, R.4
  • 71
    • 0032865255 scopus 로고    scopus 로고
    • Inactivation of proprotein convertase, PACE4, by alpha1-antitrypsin Portland (alpha1-PDX), a blocker of proteolytic activation of bone morphogenetic protein during embryogenesis: evidence that PACE4 is able to form an SDS-stable acyl intermediate with alpha1-PDX
    • Tsuji, A., Hashimoto, E., Ikoma, T., Taniguchi, T., Mori, K., Nagahama, M., et al. Inactivation of proprotein convertase, PACE4, by alpha1-antitrypsin Portland (alpha1-PDX), a blocker of proteolytic activation of bone morphogenetic protein during embryogenesis: evidence that PACE4 is able to form an SDS-stable acyl intermediate with alpha1-PDX. J. Biochem. 126:3 (1999), 591–603.
    • (1999) J. Biochem. , vol.126 , Issue.3 , pp. 591-603
    • Tsuji, A.1    Hashimoto, E.2    Ikoma, T.3    Taniguchi, T.4    Mori, K.5    Nagahama, M.6
  • 72
    • 0035964398 scopus 로고    scopus 로고
    • Furin inhibition results in absent or decreased invasiveness and tumorigenicity of human cancer cells
    • Bassi, D.E., Lopez De Cicco, R., Mahloogi, H., Zucker, S., Thomas, G., Klein-Szanto, A.J., Furin inhibition results in absent or decreased invasiveness and tumorigenicity of human cancer cells. PNAS 98:18 (2001), 10326–10331.
    • (2001) PNAS , vol.98 , Issue.18 , pp. 10326-10331
    • Bassi, D.E.1    Lopez De Cicco, R.2    Mahloogi, H.3    Zucker, S.4    Thomas, G.5    Klein-Szanto, A.J.6
  • 73
    • 34547905029 scopus 로고    scopus 로고
    • Inhibition of proprotein convertases: approaches to block squamous carcinoma development and progression
    • de Cicco, R.L., Bassi, D.E., Benavides, F., Conti, C.J., Klein-Szanto, A.J., Inhibition of proprotein convertases: approaches to block squamous carcinoma development and progression. Mol. Carcinogen. 46:8 (2007), 654–659.
    • (2007) Mol. Carcinogen. , vol.46 , Issue.8 , pp. 654-659
    • de Cicco, R.L.1    Bassi, D.E.2    Benavides, F.3    Conti, C.J.4    Klein-Szanto, A.J.5
  • 74
    • 38149024974 scopus 로고    scopus 로고
    • Selective inhibition of proprotein convertases represses the metastatic potential of human colorectal tumor cells
    • Scamuffa, N., Siegfried, G., Bontemps, Y., Ma, L., Basak, A., Cherel, G., et al. Selective inhibition of proprotein convertases represses the metastatic potential of human colorectal tumor cells. J. Clin. Invest. 118:1 (2008), 352–363.
    • (2008) J. Clin. Invest. , vol.118 , Issue.1 , pp. 352-363
    • Scamuffa, N.1    Siegfried, G.2    Bontemps, Y.3    Ma, L.4    Basak, A.5    Cherel, G.6
  • 75
    • 0027429771 scopus 로고
    • Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed alpha 1-antitrypsin variant
    • Anderson, E.D., Thomas, L., Hayflick, J.S., Thomas, G., Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed alpha 1-antitrypsin variant. J. Biol. Chem. 268:33 (1993), 24887–24891.
    • (1993) J. Biol. Chem. , vol.268 , Issue.33 , pp. 24887-24891
    • Anderson, E.D.1    Thomas, L.2    Hayflick, J.S.3    Thomas, G.4
  • 76
    • 0034646199 scopus 로고    scopus 로고
    • A protein-based therapeutic for human cytomegalovirus infection
    • Jean, F., Thomas, L., Molloy, S.S., Liu, G., Jarvis, M.A., Nelson, J.A., et al. A protein-based therapeutic for human cytomegalovirus infection. PNAS 97:6 (2000), 2864–2869.
    • (2000) PNAS , vol.97 , Issue.6 , pp. 2864-2869
    • Jean, F.1    Thomas, L.2    Molloy, S.S.3    Liu, G.4    Jarvis, M.A.5    Nelson, J.A.6
  • 77
    • 84872315938 scopus 로고    scopus 로고
    • Engineering of alpha1-antitrypsin variants with improved specificity for the proprotein convertase furin using site-directed random mutagenesis
    • Hada, K., Isshiki, K., Matsuda, S., Yuasa, K., Tsuji, A., Engineering of alpha1-antitrypsin variants with improved specificity for the proprotein convertase furin using site-directed random mutagenesis. Protein Eng. Des. Sel. 26:2 (2013), 123–131.
    • (2013) Protein Eng. Des. Sel. , vol.26 , Issue.2 , pp. 123-131
    • Hada, K.1    Isshiki, K.2    Matsuda, S.3    Yuasa, K.4    Tsuji, A.5
  • 78
    • 84989193408 scopus 로고    scopus 로고
    • The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers
    • Dahms, S.O., Creemers, J.W., Schaub, Y., Bourenkov, G.P., Zogg, T., Brandstetter, H., The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers. Sci. Rep., 6, 2016, 34303.
    • (2016) Sci. Rep. , vol.6 , pp. 34303
    • Dahms, S.O.1    Creemers, J.W.2    Schaub, Y.3    Bourenkov, G.P.4    Zogg, T.5    Brandstetter, H.6
  • 79
    • 84867762574 scopus 로고    scopus 로고
    • Generation and characterization of non-competitive furin-inhibiting nanobodies
    • Zhu, J., Declercq, J., Roucourt, B., Ghassabeh, G.H., Meulemans, S., Kinne, J., et al. Generation and characterization of non-competitive furin-inhibiting nanobodies. Biochem. J. 448:1 (2012), 73–82.
    • (2012) Biochem. J. , vol.448 , Issue.1 , pp. 73-82
    • Zhu, J.1    Declercq, J.2    Roucourt, B.3    Ghassabeh, G.H.4    Meulemans, S.5    Kinne, J.6
  • 80
    • 0030893704 scopus 로고    scopus 로고
    • Contrasting effects of TGF-beta 1 and TNF-alpha on the development of dendritic cells from progenitors in mouse bone marrow
    • Yamaguchi, Y., Tsumura, H., Miwa, M., Inaba, K., Contrasting effects of TGF-beta 1 and TNF-alpha on the development of dendritic cells from progenitors in mouse bone marrow. Stem Cells 15:2 (1997), 144–153.
    • (1997) Stem Cells , vol.15 , Issue.2 , pp. 144-153
    • Yamaguchi, Y.1    Tsumura, H.2    Miwa, M.3    Inaba, K.4
  • 81
    • 0023732890 scopus 로고
    • Molecular events in the processing of recombinant type 1 pre-pro-transforming growth factor beta to the mature polypeptide
    • Gentry, L.E., Lioubin, M.N., Purchio, A.F., Marquardt, H., Molecular events in the processing of recombinant type 1 pre-pro-transforming growth factor beta to the mature polypeptide. Mol. Cell Biol. 8:10 (1988), 4162–4168.
    • (1988) Mol. Cell Biol. , vol.8 , Issue.10 , pp. 4162-4168
    • Gentry, L.E.1    Lioubin, M.N.2    Purchio, A.F.3    Marquardt, H.4
  • 82
    • 0032773058 scopus 로고    scopus 로고
    • Xenopus nodal-related signaling is essential for mesendodermal patterning during early embryogenesis
    • Osada, S.I., Wright, C.V., Xenopus nodal-related signaling is essential for mesendodermal patterning during early embryogenesis. Development (Cambridge, England) 126:14 (1999), 3229–3240.
    • (1999) Development (Cambridge, England) , vol.126 , Issue.14 , pp. 3229-3240
    • Osada, S.I.1    Wright, C.V.2
  • 83
    • 77958085607 scopus 로고    scopus 로고
    • Enhanced target gene knockdown by a bifunctional shRNA: a novel approach of RNA interference
    • Rao, D.D., Maples, P.B., Senzer, N., Kumar, P., Wang, Z., Pappen, B.O., et al. Enhanced target gene knockdown by a bifunctional shRNA: a novel approach of RNA interference. Cancer Gene Ther. 17:11 (2010), 780–791.
    • (2010) Cancer Gene Ther. , vol.17 , Issue.11 , pp. 780-791
    • Rao, D.D.1    Maples, P.B.2    Senzer, N.3    Kumar, P.4    Wang, Z.5    Pappen, B.O.6
  • 84
    • 84902890484 scopus 로고    scopus 로고
    • Summary of bi-shRNA/GM-CSF augmented autologous tumor cell immunotherapy (FANG) in advanced cancer of the liver
    • Nemunaitis, J., Barve, M., Orr, D., Kuhn, J., Magee, M., Lamont, J., et al. Summary of bi-shRNA/GM-CSF augmented autologous tumor cell immunotherapy (FANG) in advanced cancer of the liver. Oncology 87:1 (2014), 21–29.
    • (2014) Oncology , vol.87 , Issue.1 , pp. 21-29
    • Nemunaitis, J.1    Barve, M.2    Orr, D.3    Kuhn, J.4    Magee, M.5    Lamont, J.6
  • 85
    • 84857782004 scopus 로고    scopus 로고
    • Phase I trial of “bi-shRNAifurin/GMCSF DNA/autologous tumor cell” vaccine (FANG) in advanced cancer
    • Senzer, N., Barve, M., Kuhn, J., Melnyk, A., Beitsch, P., Lazar, M., et al. Phase I trial of “bi-shRNAifurin/GMCSF DNA/autologous tumor cell” vaccine (FANG) in advanced cancer. Mol. Ther. 20:3 (2012), 679–686.
    • (2012) Mol. Ther. , vol.20 , Issue.3 , pp. 679-686
    • Senzer, N.1    Barve, M.2    Kuhn, J.3    Melnyk, A.4    Beitsch, P.5    Lazar, M.6
  • 86
    • 84978628970 scopus 로고    scopus 로고
    • Three-year follow up of GMCSF/bi-shRNA(furin) DNA-transfected autologous tumor immunotherapy (Vigil) in metastatic advanced ewing's sarcoma
    • Ghisoli, M., Barve, M., Mennel, R., Lenarsky, C., Horvath, S., Wallraven, G., et al. Three-year follow up of GMCSF/bi-shRNA(furin) DNA-transfected autologous tumor immunotherapy (Vigil) in metastatic advanced ewing's sarcoma. Mol. Ther. 24:8 (2016), 1478–1483.
    • (2016) Mol. Ther. , vol.24 , Issue.8 , pp. 1478-1483
    • Ghisoli, M.1    Barve, M.2    Mennel, R.3    Lenarsky, C.4    Horvath, S.5    Wallraven, G.6
  • 88
    • 84996553234 scopus 로고    scopus 로고
    • Phase II study of Vigil® DNA engineered immunotherapy as maintenance in advanced stage ovarian cancer
    • Oh, J., Barve, M., Matthews, C.M., Koon, E.C., Heffernan, T.P., Fine, B., et al. Phase II study of Vigil® DNA engineered immunotherapy as maintenance in advanced stage ovarian cancer. Gynecol. Oncol. 143:3 (2016), 504–510.
    • (2016) Gynecol. Oncol. , vol.143 , Issue.3 , pp. 504-510
    • Oh, J.1    Barve, M.2    Matthews, C.M.3    Koon, E.C.4    Heffernan, T.P.5    Fine, B.6
  • 89
    • 2442710211 scopus 로고    scopus 로고
    • Induction of potent TRAIL-mediated tumoricidal activity by hFLEX/Furin/TRAIL recombinant DNA construct
    • Wu, X., Hui, K.M., Induction of potent TRAIL-mediated tumoricidal activity by hFLEX/Furin/TRAIL recombinant DNA construct. Mol. Ther. 9:5 (2004), 674–681.
    • (2004) Mol. Ther. , vol.9 , Issue.5 , pp. 674-681
    • Wu, X.1    Hui, K.M.2
  • 90
    • 0037507288 scopus 로고    scopus 로고
    • Adenoviral gene transfer of tumor necrosis factor-related apoptosis-inducing ligand overcomes an impaired response of hepatoma cells but causes severe apoptosis in primary human hepatocytes
    • Armeanu, S., Lauer, U.M., Smirnow, I., Schenk, M., Weiss, T.S., Gregor, M., et al. Adenoviral gene transfer of tumor necrosis factor-related apoptosis-inducing ligand overcomes an impaired response of hepatoma cells but causes severe apoptosis in primary human hepatocytes. Cancer Res. 63:10 (2003), 2369–2372.
    • (2003) Cancer Res. , vol.63 , Issue.10 , pp. 2369-2372
    • Armeanu, S.1    Lauer, U.M.2    Smirnow, I.3    Schenk, M.4    Weiss, T.S.5    Gregor, M.6
  • 91
    • 78651347264 scopus 로고    scopus 로고
    • A novel recombinant immuno-tBid with a furin site effectively suppresses the growth of HER2-positive osteosarcoma cells in vitro
    • Shan, L.Q., Ma, S., Qiu, X.C., Wang, T., Yu, S.B., Ma, B.A., et al. A novel recombinant immuno-tBid with a furin site effectively suppresses the growth of HER2-positive osteosarcoma cells in vitro. Oncology Rep. 25:2 (2011), 325–331.
    • (2011) Oncology Rep. , vol.25 , Issue.2 , pp. 325-331
    • Shan, L.Q.1    Ma, S.2    Qiu, X.C.3    Wang, T.4    Yu, S.B.5    Ma, B.A.6
  • 92
    • 37549014941 scopus 로고    scopus 로고
    • Recombinant immunoproapoptotic proteins with furin site can translocate and kill HER2-positive cancer cells
    • Wang, T., Zhao, J., Ren, J.L., Zhang, L., Wen, W.H., Zhang, R., et al. Recombinant immunoproapoptotic proteins with furin site can translocate and kill HER2-positive cancer cells. Cancer Res. 67:24 (2007), 11830–11839.
    • (2007) Cancer Res. , vol.67 , Issue.24 , pp. 11830-11839
    • Wang, T.1    Zhao, J.2    Ren, J.L.3    Zhang, L.4    Wen, W.H.5    Zhang, R.6
  • 94
    • 0030948621 scopus 로고    scopus 로고
    • The expression of p185(HER-2/neu) correlates with the stage of disease and survival in colorectal cancer
    • Kapitanovic, S., Radosevic, S., Kapitanovic, M., Andelinovic, S., Ferencic, Z., Tavassoli, M., The expression of p185(HER-2/neu) correlates with the stage of disease and survival in colorectal cancer. Gastroenterology 112:4 (1997), 1103–1113.
    • (1997) Gastroenterology , vol.112 , Issue.4 , pp. 1103-1113
    • Kapitanovic, S.1    Radosevic, S.2    Kapitanovic, M.3    Andelinovic, S.4    Ferencic, Z.5    Tavassoli, M.6
  • 95
    • 27744600091 scopus 로고    scopus 로고
    • Serum levels of shed Her2/neu protein in men with prostate cancer correlate with disease progression
    • Osman, I., Mikhail, M., Shuch, B., Clute, M., Cheli, C.D., Ghani, F., et al. Serum levels of shed Her2/neu protein in men with prostate cancer correlate with disease progression. J. Urol. 174:6 (2005), 2174–2177.
    • (2005) J. Urol. , vol.174 , Issue.6 , pp. 2174-2177
    • Osman, I.1    Mikhail, M.2    Shuch, B.3    Clute, M.4    Cheli, C.D.5    Ghani, F.6
  • 96
    • 0141426787 scopus 로고    scopus 로고
    • Prevalence and prognostic value of c-erbB2 expression in non-small cell lung cancer (NSCLC)
    • Turken, O., Kunter, E., Cermik, H., Isitmangil, T., Kandemir, G., Yaylaci, M., et al. Prevalence and prognostic value of c-erbB2 expression in non-small cell lung cancer (NSCLC). Neoplasma 50:4 (2003), 257–261.
    • (2003) Neoplasma , vol.50 , Issue.4 , pp. 257-261
    • Turken, O.1    Kunter, E.2    Cermik, H.3    Isitmangil, T.4    Kandemir, G.5    Yaylaci, M.6
  • 97
    • 0038407472 scopus 로고    scopus 로고
    • Specific tumoricidal activity of a secreted proapoptotic protein consisting of HER2 antibody and constitutively active caspase-3
    • Jia, L.T., Zhang, L.H., Yu, C.J., Zhao, J., Xu, Y.M., Gui, J.H., et al. Specific tumoricidal activity of a secreted proapoptotic protein consisting of HER2 antibody and constitutively active caspase-3. Cancer Res. 63:12 (2003), 3257–3262.
    • (2003) Cancer Res. , vol.63 , Issue.12 , pp. 3257-3262
    • Jia, L.T.1    Zhang, L.H.2    Yu, C.J.3    Zhao, J.4    Xu, Y.M.5    Gui, J.H.6
  • 98
    • 4444363661 scopus 로고    scopus 로고
    • SU5416 is a potent inhibitor of hepatocyte growth factor receptor (c-Met) and blocks HGF-induced invasiveness of human HepG2 hepatoma cells
    • Wang, S.Y., Chen, B., Zhan, Y.Q., Xu, W.X., Li, C.Y., Yang, R.F., et al. SU5416 is a potent inhibitor of hepatocyte growth factor receptor (c-Met) and blocks HGF-induced invasiveness of human HepG2 hepatoma cells. J. Hepatol. 41:2 (2004), 267–273.
    • (2004) J. Hepatol. , vol.41 , Issue.2 , pp. 267-273
    • Wang, S.Y.1    Chen, B.2    Zhan, Y.Q.3    Xu, W.X.4    Li, C.Y.5    Yang, R.F.6
  • 99
    • 84934897412 scopus 로고    scopus 로고
    • Designing the furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A
    • Weldon, J.E., Skarzynski, M., Therres, J.A., Ostovitz, J.R., Zhou, H., Kreitman, R.J., et al. Designing the furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A. Bioconjugate Chem. 26:6 (2015), 1120–1128.
    • (2015) Bioconjugate Chem. , vol.26 , Issue.6 , pp. 1120-1128
    • Weldon, J.E.1    Skarzynski, M.2    Therres, J.A.3    Ostovitz, J.R.4    Zhou, H.5    Kreitman, R.J.6
  • 100
    • 0036547417 scopus 로고    scopus 로고
    • Death and anti-death: tumour resistance to apoptosis, nature reviews
    • Igney, F.H., Krammer, P.H., Death and anti-death: tumour resistance to apoptosis, nature reviews. Cancer 2:4 (2002), 277–288.
    • (2002) Cancer , vol.2 , Issue.4 , pp. 277-288
    • Igney, F.H.1    Krammer, P.H.2
  • 101
    • 0036623140 scopus 로고    scopus 로고
    • Immune escape of tumors: apoptosis resistance and tumor counterattack
    • Igney, F.H., Krammer, P.H., Immune escape of tumors: apoptosis resistance and tumor counterattack. J. Leukoc. Biol. 71:6 (2002), 907–920.
    • (2002) J. Leukoc. Biol. , vol.71 , Issue.6 , pp. 907-920
    • Igney, F.H.1    Krammer, P.H.2
  • 102
    • 0036679173 scopus 로고    scopus 로고
    • Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects
    • Zhu, X., Zhou, A., Dey, A., Norrbom, C., Carroll, R., Zhang, C., et al. Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects. PNAS 99:16 (2002), 10293–10298.
    • (2002) PNAS , vol.99 , Issue.16 , pp. 10293-10298
    • Zhu, X.1    Zhou, A.2    Dey, A.3    Norrbom, C.4    Carroll, R.5    Zhang, C.6
  • 104
    • 69449093447 scopus 로고    scopus 로고
    • Association of variants in the PCSK1 gene with obesity in the EPIC-Norfolk study
    • Kilpelainen, T.O., Bingham, S.A., Khaw, K.T., Wareham, N.J., Loos, R.J., Association of variants in the PCSK1 gene with obesity in the EPIC-Norfolk study. Hum. Mol. Gen. 18:18 (2009), 3496–3501.
    • (2009) Hum. Mol. Gen. , vol.18 , Issue.18 , pp. 3496-3501
    • Kilpelainen, T.O.1    Bingham, S.A.2    Khaw, K.T.3    Wareham, N.J.4    Loos, R.J.5
  • 105
    • 85009188337 scopus 로고    scopus 로고
    • Functional and clinical relevance of novel and known PCSK1 variants for childhood obesity and glucose metabolism
    • Loffler, D., Behrendt, S., Creemers, J.W., Klammt, J., Aust, G., Stanik, J., et al. Functional and clinical relevance of novel and known PCSK1 variants for childhood obesity and glucose metabolism. Mol. Metab. 6:3 (2017), 295–305.
    • (2017) Mol. Metab. , vol.6 , Issue.3 , pp. 295-305
    • Loffler, D.1    Behrendt, S.2    Creemers, J.W.3    Klammt, J.4    Aust, G.5    Stanik, J.6
  • 106
    • 85016400385 scopus 로고    scopus 로고
    • Next-generation sequencing of the monogenic obesity genes LEP, LEPR, MC4R, PCSK1 and POMC in a Norwegian cohort of patients with morbid obesity and normal weight controls
    • Nordang, G.B., Busk, O.L., Tveten, K., Hanevik, H.I., Fell, A.K., Hjelmesaeth, J., et al. Next-generation sequencing of the monogenic obesity genes LEP, LEPR, MC4R, PCSK1 and POMC in a Norwegian cohort of patients with morbid obesity and normal weight controls. Mol. Genet. Metab., 2017.
    • (2017) Mol. Genet. Metab.
    • Nordang, G.B.1    Busk, O.L.2    Tveten, K.3    Hanevik, H.I.4    Fell, A.K.5    Hjelmesaeth, J.6
  • 107
    • 85010876882 scopus 로고    scopus 로고
    • PC1/3 deficiency impacts pro-opiomelanocortin processing in human embryonic stem cell-derived hypothalamic neurons
    • Wang, L., Sui, L., Panigrahi, S.K., Meece, K., Xin, Y., Kim, J., et al. PC1/3 deficiency impacts pro-opiomelanocortin processing in human embryonic stem cell-derived hypothalamic neurons. Stem Cell Rep. 8:2 (2017), 264–277.
    • (2017) Stem Cell Rep. , vol.8 , Issue.2 , pp. 264-277
    • Wang, L.1    Sui, L.2    Panigrahi, S.K.3    Meece, K.4    Xin, Y.5    Kim, J.6
  • 108
    • 34548403935 scopus 로고    scopus 로고
    • Association of the proprotein convertase subtilisin/kexin-type 2 (PCSK2) gene with type 2 diabetes in an African American population
    • Leak, T.S., Keene, K.L., Langefeld, C.D., Gallagher, C.J., Mychaleckyj, J.C., Freedman, B.I., et al. Association of the proprotein convertase subtilisin/kexin-type 2 (PCSK2) gene with type 2 diabetes in an African American population. Mol. Genet. Metab. 92:1–2 (2007), 145–150.
    • (2007) Mol. Genet. Metab. , vol.92 , Issue.1-2 , pp. 145-150
    • Leak, T.S.1    Keene, K.L.2    Langefeld, C.D.3    Gallagher, C.J.4    Mychaleckyj, J.C.5    Freedman, B.I.6
  • 110
    • 12644251967 scopus 로고    scopus 로고
    • Impaired fertility in mice deficient for the testicular germ-cell protease PC4
    • Mbikay, M., Tadros, H., Ishida, N., Lerner, C.P., De Lamirande, E., Chen, A., et al. Impaired fertility in mice deficient for the testicular germ-cell protease PC4. PNAS 94:13 (1997), 6842–6846.
    • (1997) PNAS , vol.94 , Issue.13 , pp. 6842-6846
    • Mbikay, M.1    Tadros, H.2    Ishida, N.3    Lerner, C.P.4    De Lamirande, E.5    Chen, A.6
  • 111
    • 80755153564 scopus 로고    scopus 로고
    • Inactivation of endothelial proprotein convertase 5/6 decreases collagen deposition in the cardiovascular system: role of fibroblast autophagy
    • Marchesi, C., Essalmani, R., Lemarie, C.A., Leibovitz, E., Ebrahimian, T., Paradis, P., et al. Inactivation of endothelial proprotein convertase 5/6 decreases collagen deposition in the cardiovascular system: role of fibroblast autophagy. J. Mol. Med. (Berlin, Germany) 89:11 (2011), 1103–1111.
    • (2011) J. Mol. Med. (Berlin, Germany) , vol.89 , Issue.11 , pp. 1103-1111
    • Marchesi, C.1    Essalmani, R.2    Lemarie, C.A.3    Leibovitz, E.4    Ebrahimian, T.5    Paradis, P.6
  • 112
    • 79953191442 scopus 로고    scopus 로고
    • Proprotein convertase PC7 enhances the activation of the EGF receptor pathway through processing of the EGF precursor
    • Rousselet, E., Benjannet, S., Marcinkiewicz, E., Asselin, M.C., Lazure, C., Seidah, N.G., Proprotein convertase PC7 enhances the activation of the EGF receptor pathway through processing of the EGF precursor. J. Biol. Chem. 286:11 (2011), 9185–9195.
    • (2011) J. Biol. Chem. , vol.286 , Issue.11 , pp. 9185-9195
    • Rousselet, E.1    Benjannet, S.2    Marcinkiewicz, E.3    Asselin, M.C.4    Lazure, C.5    Seidah, N.G.6
  • 113
    • 84886441051 scopus 로고    scopus 로고
    • Disruption of the expression of the proprotein convertase PC7 reduces BDNF production and affects learning and memory in mice
    • Wetsel, W.C., Rodriguiz, R.M., Guillemot, J., Rousselet, E., Essalmani, R., Kim, I.H., et al. Disruption of the expression of the proprotein convertase PC7 reduces BDNF production and affects learning and memory in mice. PNAS 110:43 (2013), 17362–17367.
    • (2013) PNAS , vol.110 , Issue.43 , pp. 17362-17367
    • Wetsel, W.C.1    Rodriguiz, R.M.2    Guillemot, J.3    Rousselet, E.4    Essalmani, R.5    Kim, I.H.6
  • 114
    • 36349027096 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity
    • Bergeron, E., Vincent, M.J., Nichol, S.T., Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivity. J. Virol. 81:23 (2007), 13271–13276.
    • (2007) J. Virol. , vol.81 , Issue.23 , pp. 13271-13276
    • Bergeron, E.1    Vincent, M.J.2    Nichol, S.T.3
  • 115
    • 0037192792 scopus 로고    scopus 로고
    • Biosynthesis and cellular trafficking of the convertase SKI-1/S1P: ectodomain shedding requires SKI-1 activity
    • Elagoz, A., Benjannet, S., Mammarbassi, A., Wickham, L., Seidah, N.G., Biosynthesis and cellular trafficking of the convertase SKI-1/S1P: ectodomain shedding requires SKI-1 activity. J. Biol. Chem. 277:13 (2002), 11265–11275.
    • (2002) J. Biol. Chem. , vol.277 , Issue.13 , pp. 11265-11275
    • Elagoz, A.1    Benjannet, S.2    Mammarbassi, A.3    Wickham, L.4    Seidah, N.G.5
  • 116
    • 84861921405 scopus 로고    scopus 로고
    • Proprotein convertase subtilisin kexin9 (PCSK9): a novel target for cholesterol regulation
    • Basak, A., Palmer-Smith, H., Mishra, P., Proprotein convertase subtilisin kexin9 (PCSK9): a novel target for cholesterol regulation. Protine Pept. Lett. 19:6 (2012), 575–585.
    • (2012) Protine Pept. Lett. , vol.19 , Issue.6 , pp. 575-585
    • Basak, A.1    Palmer-Smith, H.2    Mishra, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.