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Volumn 57, Issue 1, 2014, Pages 98-109

Design, synthesis, and structure-activity relationship studies of a potent PACE4 inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; ARGININE; LEUCINE; PROPROTEIN CONVERTASE 4 INHIBITOR; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84892609855     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm401457n     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 19544393760 scopus 로고    scopus 로고
    • Cutting back on pro-protein convertases: The latest approaches to pharmacological inhibition
    • Fugere, M.; Day, R. Cutting back on pro-protein convertases: The latest approaches to pharmacological inhibition Trends Pharmacol. Sci. 2005, 26, 294-301
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 294-301
    • Fugere, M.1    Day, R.2
  • 2
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • Hosaka, M.; Nagahama, M.; Kim, W. S.; Watanabe, T.; Hatsuzawa, K.; Ikemizu, J.; Murakami, K.; Nakayama, K. Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway J. Biol. Chem. 1991, 266, 12127-12130
    • (1991) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 3
    • 33747636007 scopus 로고    scopus 로고
    • The proprotein convertase SKI-1/S1P. in vitro analysis of Lassa virus glycoprotein-derived substrates and ex vivo validation of irreversible peptide inhibitors
    • Pasquato, A.; Pullikotil, P.; Asselin, M. C.; Vacatello, M.; Paolillo, L.; Ghezzo, F.; Basso, F.; Di Bello, C.; Dettin, M.; Seidah, N. G. The proprotein convertase SKI-1/S1P. In vitro analysis of Lassa virus glycoprotein-derived substrates and ex vivo validation of irreversible peptide inhibitors J. Biol. Chem. 2006, 281, 23471-23481
    • (2006) J. Biol. Chem. , vol.281 , pp. 23471-23481
    • Pasquato, A.1    Pullikotil, P.2    Asselin, M.C.3    Vacatello, M.4    Paolillo, L.5    Ghezzo, F.6    Basso, F.7    Di Bello, C.8    Dettin, M.9    Seidah, N.G.10
  • 5
    • 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 2011, 2, 421-438
    • (2011) Biomol. Concepts , vol.2 , pp. 421-438
    • Couture, F.1    D'Anjou, F.2    Day, R.3
  • 6
    • 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 2003, 17, 1215-1227
    • (2003) FASEB J , vol.17 , pp. 1215-1227
    • Taylor, N.A.1    Van De Ven, W.J.2    Creemers, J.W.3
  • 7
    • 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 Discovery 2012, 11, 367-383
    • (2012) Nat. Rev. Drug Discovery , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 8
    • 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. 1993, 268, 24887-24891
    • (1993) J. Biol. Chem. , vol.268 , pp. 24887-24891
    • Anderson, E.D.1    Thomas, L.2    Hayflick, J.S.3    Thomas, G.4
  • 10
    • 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. 2007, 71, 323-332
    • (2007) Mol. Pharmacol. , vol.71 , pp. 323-332
    • Fugere, M.1    Appel, J.2    Houghten, R.A.3    Lindberg, I.4    Day, R.5
  • 15
    • 84855379737 scopus 로고    scopus 로고
    • Trial watch: PCSK9 antibody reduces LDL cholesterol
    • Crunkhorn, S. Trial watch: PCSK9 antibody reduces LDL cholesterol Nat. Rev. Drug Discovery 2012, 11, 11
    • (2012) Nat. Rev. Drug Discovery , vol.11 , pp. 11
    • Crunkhorn, S.1
  • 16
    • 0035903230 scopus 로고    scopus 로고
    • Inhibition of proprotein convertases is associated with loss of growth and tumorigenicity of HT-29 human colon carcinoma cells: Importance of insulin-like growth factor-1 (IGF-1) receptor processing in IGF-1-mediated functions
    • Khatib, A. M.; Siegfried, G.; Prat, A.; Luis, J.; Chretien, M.; Metrakos, P.; Seidah, N. G. Inhibition of proprotein convertases is associated with loss of growth and tumorigenicity of HT-29 human colon carcinoma cells: Importance of insulin-like growth factor-1 (IGF-1) receptor processing in IGF-1-mediated functions J. Biol. Chem. 2001, 276, 30686-30693
    • (2001) J. Biol. Chem. , vol.276 , pp. 30686-30693
    • Khatib, A.M.1    Siegfried, G.2    Prat, A.3    Luis, J.4    Chretien, M.5    Metrakos, P.6    Seidah, N.G.7
  • 17
    • 0032513136 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor
    • Maquoi, E.; Noel, A.; Frankenne, F.; Angliker, H.; Murphy, G.; Foidart, J. M. Inhibition of matrix metalloproteinase 2 maturation and HT1080 invasiveness by a synthetic furin inhibitor FEBS Lett. 1998, 424, 262-266
    • (1998) FEBS Lett. , vol.424 , pp. 262-266
    • Maquoi, E.1    Noel, A.2    Frankenne, F.3    Angliker, H.4    Murphy, G.5    Foidart, J.M.6
  • 19
    • 41649118952 scopus 로고    scopus 로고
    • A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness
    • Coppola, J. M.; Bhojani, M. S.; Ross, B. D.; Rehemtulla, A. A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness Neoplasia 2008, 10, 363-370
    • (2008) Neoplasia , vol.10 , pp. 363-370
    • Coppola, J.M.1    Bhojani, M.S.2    Ross, B.D.3    Rehemtulla, A.4
  • 22
    • 84869191516 scopus 로고    scopus 로고
    • Role of proprotein convertases in prostate cancer progression
    • Couture, F.; D'Anjou, F.; Desjardins, R.; Boudreau, F.; Day, R. Role of proprotein convertases in prostate cancer progression Neoplasia 2012, 14, 1032-1042
    • (2012) Neoplasia , vol.14 , pp. 1032-1042
    • Couture, F.1    D'Anjou, F.2    Desjardins, R.3    Boudreau, F.4    Day, R.5
  • 26
    • 0141615711 scopus 로고    scopus 로고
    • Inhibition of bovine plasma amine oxidase by 1,4-diamino-2-butenes and -2-butynes
    • Jeon, H. B.; Lee, Y.; Qiao, C.; Huang, H.; Sayre, L. M. Inhibition of bovine plasma amine oxidase by 1,4-diamino-2-butenes and -2-butynes Bioorg. Med. Chem. 2003, 11, 4631-4641
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 4631-4641
    • Jeon, H.B.1    Lee, Y.2    Qiao, C.3    Huang, H.4    Sayre, L.M.5
  • 27
    • 29944435240 scopus 로고    scopus 로고
    • Solid-phase synthesis of "mixed" peptidomimetics using Fmoc-protected aza-beta3-amino acids and alpha-amino acids
    • Busnel, O.; Bi, L.; Dali, H.; Cheguillaume, A.; Chevance, S.; Bondon, A.; Muller, S.; Baudy-Floc'h, M. Solid-phase synthesis of "mixed" peptidomimetics using Fmoc-protected aza-beta3-amino acids and alpha-amino acids J. Org. Chem. 2005, 70, 10701-10708
    • (2005) J. Org. Chem. , vol.70 , pp. 10701-10708
    • Busnel, O.1    Bi, L.2    Dali, H.3    Cheguillaume, A.4    Chevance, S.5    Bondon, A.6    Muller, S.7    Baudy-Floc'H, M.8
  • 28
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J. F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors Biochim. Biophys. Acta 1969, 185, 269-286
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 29
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams, J. W.; Morrison, J. F. The kinetics of reversible tight-binding inhibition Methods Enzymol. 1979, 63, 437-467
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 32
    • 79960914019 scopus 로고    scopus 로고
    • New substrate analogue furin inhibitors derived from 4-amidinobenzylamide
    • Becker, G. L.; Hardes, K.; Steinmetzer, T. New substrate analogue furin inhibitors derived from 4-amidinobenzylamide Bioorg. Med. Chem. Lett. 2011, 21, 4695-4697
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 4695-4697
    • Becker, G.L.1    Hardes, K.2    Steinmetzer, T.3
  • 33
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B.; Noble, R. L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids Int. J. Pept. Protein Res. 1990, 35, 161-214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 35
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction
    • Cheng, Y.; Prusoff, W. H. Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction Biochem. Pharmacol. 1973, 22, 3099-3108
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.