메뉴 건너뛰기




Volumn 23, Issue 8, 2016, Pages 748-762

Targeting "undruggable" proteins: Design of synthetic cyclopeptides

Author keywords

Cyclopeptides; Macrocycles; Protein protein interactions

Indexed keywords

ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; ANTINEOPLASTIC AGENT; BAMBERMYCIN; CYCLOPEPTIDE; CYCLOSPORIN; ERYTHROMYCIN; GRAMICIDIN S; IMMUNOMODULATING AGENT; IMMUNOSUPPRESSIVE AGENT; MACROCYCLIC COMPOUND; ORITAVANCIN; PEPTIDOMIMETIC AGENT; PROTEIN; RIFAMPICIN; SOMATOSTATIN; TACROLIMUS; TUBERCULOSTATIC AGENT; TYROCIDINE; CREB1 PROTEIN, HUMAN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; PROTEIN BINDING;

EID: 84964528884     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867323666160112122540     Document Type: Review
Times cited : (57)

References (122)
  • 1
    • 76149109071 scopus 로고    scopus 로고
    • Targeting protein-protein interactions for therapeutic intervention: A challenge for the future
    • Zinzalla, G.; Thurston, D.E. Targeting protein-protein interactions for therapeutic intervention: a challenge for the future. Future Med. Chem., 2009, 1(1), 65-93.
    • (2009) Future Med. Chem. , vol.1 , Issue.1 , pp. 65-93
    • Zinzalla, G.1    Thurston, D.E.2
  • 2
    • 23044496736 scopus 로고    scopus 로고
    • Protein-protein interactions in human disease
    • Ryan, D.P.; Matthews, J.M. Protein-protein interactions in human disease. Curr. Opin. Struct. Biol., 2005, 15(4), 441-446.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , Issue.4 , pp. 441-446
    • Ryan, D.P.1    Matthews, J.M.2
  • 3
    • 33746288394 scopus 로고    scopus 로고
    • Small molecule modulators of transcription
    • Arndt, H.D. Small molecule modulators of transcription. Angew. Chem. Int. Ed. Engl., 2006, 45(28), 4552-4560.
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , Issue.28 , pp. 4552-4560
    • Arndt, H.D.1
  • 4
    • 33847778677 scopus 로고    scopus 로고
    • Inhibiting protein-protein interactions as an emerging paradigm for drug discovery
    • Gerrard, J.A.; Hutton, C.A.; Perugini, M.A. Inhibiting protein-protein interactions as an emerging paradigm for drug discovery. Mini Rev. Med. Chem., 2007, 7(2), 151-157.
    • (2007) Mini Rev. Med. Chem. , vol.7 , Issue.2 , pp. 151-157
    • Gerrard, J.A.1    Hutton, C.A.2    Perugini, M.A.3
  • 5
    • 33750610998 scopus 로고    scopus 로고
    • Drugs targeting protein-protein interactions
    • Chene, P. Drugs targeting protein-protein interactions. Chem. Med. Chem., 2006, 1(4), 400-411.
    • (2006) Chem. Med. Chem. , vol.1 , Issue.4 , pp. 400-411
    • Chene, P.1
  • 6
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T.; Nash, P. Protein-protein interactions define specificity in signal transduction. Genes Dev., 2000, 14(9), 1027-1047.
    • (2000) Genes Dev. , vol.14 , Issue.9 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 7
    • 0030768266 scopus 로고    scopus 로고
    • Structural motifs at proteinprotein interfaces: Protein cores versus two-state and threestate model complexes
    • Tsai, C.J.; Xu, D; Nussinov, R. Structural motifs at proteinprotein interfaces: protein cores versus two-state and threestate model complexes. Protein Sci., 1997, 6(9), 1793-1805.
    • (1997) Protein Sci. , vol.6 , Issue.9 , pp. 1793-1805
    • Tsai, C.J.1    Xu, D.2    Nussinov, R.3
  • 8
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, C.J.; Lin, S.L.; Wolfson, H.J.; Nussinov, R. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci., 1997, 6(1), 53-64.
    • (1997) Protein Sci. , vol.6 , Issue.1 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 9
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L.; Jernigan, R.L.; Covell, D.G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci., 1994, 3(5), 717-729.
    • (1994) Protein Sci. , vol.3 , Issue.5 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 10
    • 0034769223 scopus 로고    scopus 로고
    • Electrostatic contributions to protein-protein interactions: Fast energetic filters for docking and their physical basis
    • Norel, R.; Sheinerman, F.; Petrey, D.; Honig, B. Electrostatic contributions to protein-protein interactions: fast energetic filters for docking and their physical basis. Protein Sci., 2001, 10(11), 2147-2161.
    • (2001) Protein Sci. , vol.10 , Issue.11 , pp. 2147-2161
    • Norel, R.1    Sheinerman, F.2    Petrey, D.3    Honig, B.4
  • 11
    • 0036306236 scopus 로고    scopus 로고
    • On the role of electrostatic interactions in the design of protein-protein interfaces
    • Sheinerman, F.B.; Honig, B. On the role of electrostatic interactions in the design of protein-protein interfaces. J. Mol. Biol., 2002, 318(1), 161-177.
    • (2002) J. Mol. Biol. , vol.318 , Issue.1 , pp. 161-177
    • Sheinerman, F.B.1    Honig, B.2
  • 12
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of protein-protein interactions
    • Sheinerman, F.B.; Norel, R.; Honig, B. Electrostatic aspects of protein-protein interactions. Curr. Opin. Struct. Biol., 2000, 10(2), 153-159.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , Issue.2 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 13
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu, D.; Lin, S.L.; Nussinov, R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J. Mol. Biol., 1997, 265(1), 68-84.
    • (1997) J. Mol. Biol. , vol.265 , Issue.1 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 15
    • 84927645757 scopus 로고    scopus 로고
    • Identification of inhibitors of biological interactions involving intrinsically disordered proteins
    • Marasco, D.; Scognamiglio, P.L. Identification of inhibitors of biological interactions involving intrinsically disordered proteins. Int. J. Mol. Sci., 2015, 16(4), 7394-7412.
    • (2015) Int. J. Mol. Sci. , vol.16 , Issue.4 , pp. 7394-7412
    • Marasco, D.1    Scognamiglio, P.L.2
  • 16
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren, I.M.; Thornton J.M. Diversity of protein-protein interactions. EMBO J., 2003, 22(14), 3486-3492.
    • (2003) EMBO J. , vol.22 , Issue.14 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 17
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J.; Wyman, J.; Changeux, J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol., 1965, 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 20
    • 0029809182 scopus 로고    scopus 로고
    • On the origin of the cooperativity of protein folding: Implications from model simulations
    • Kolinski, A.; Galazka, W.; Skolnick, J. On the origin of the cooperativity of protein folding: implications from model simulations. Proteins, 1996, 26(3), 271-287.
    • (1996) Proteins , vol.26 , Issue.3 , pp. 271-287
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 21
    • 0030756203 scopus 로고    scopus 로고
    • Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and to protein-protein association
    • Tsai, C.J.; Nussinov, R. Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association. Protein Sci., 1997, 6(7), 1426-1437.
    • (1997) Protein Sci. , vol.6 , Issue.7 , pp. 1426-1437
    • Tsai, C.J.1    Nussinov, R.2
  • 22
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: What are the preferred ways for proteins to interact?
    • Keskin, O.; Gursoy, A.; Ma, B.; Nussinov, R. Principles of protein-protein interactions: what are the preferred ways for proteins to interact? Chem. Rev., 2008, 108(4), 1225-1244.
    • (2008) Chem. Rev. , vol.108 , Issue.4 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 24
    • 11844249426 scopus 로고    scopus 로고
    • Hot regions in protein - Protein interactions: The organization and contribution of structurally conserved hot spot residues
    • Keskin, O.; Ma, B.; Nussinov, R. Hot regions in protein - protein interactions: the organization and contribution of structurally conserved hot spot residues. J. Mol. Biol., 2005, 345(5), 1281-1294.
    • (2005) J. Mol. Biol. , vol.345 , Issue.5 , pp. 1281-1294
    • Keskin, O.1    Ma, B.2    Nussinov, R.3
  • 25
    • 7944225979 scopus 로고    scopus 로고
    • Proteinprotein interactions: Hot spots and structurally conserved residues often locate in complemented pockets that preorganized in the unbound states: Implications for docking
    • Li, X.; Keskin, O.; Ma, B.; Nussinov, R.; Liang, J. Proteinprotein interactions: hot spots and structurally conserved residues often locate in complemented pockets that preorganized in the unbound states: implications for docking. J. Mol. Biol., 2004, 344(3), 781-795.
    • (2004) J. Mol. Biol. , vol.344 , Issue.3 , pp. 781-795
    • Li, X.1    Keskin, O.2    Ma, B.3    Nussinov, R.4    Liang, J.5
  • 26
    • 0024040620 scopus 로고
    • Brownian dynamics of cytochrome c and cytochrome c peroxidase association
    • Northrup, S.H.; Boles, J.O.; Reynolds, J.C. Brownian dynamics of cytochrome c and cytochrome c peroxidase association. Science, 1988, 241(4861), 67-70.
    • (1988) Science , vol.241 , Issue.4861 , pp. 67-70
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.3
  • 27
    • 84888430272 scopus 로고    scopus 로고
    • Formation of transient protein complexes
    • Schilder, J.; Ubbink, M. Formation of transient protein complexes. Curr. Opin. Struct. Biol., 2013, 23(6), 911-988.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , Issue.6 , pp. 911-988
    • Schilder, J.1    Ubbink, M.2
  • 28
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J.A.; McClendon, C.L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature, 2007, 450(7172), 1001-1009.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 29
    • 84924077519 scopus 로고    scopus 로고
    • An overview of recent advances in structural bioinformatics of proteinprotein interactions and a guide to their principles
    • Sudha, G.; Nussinov, R.; Srinivasan, N. An overview of recent advances in structural bioinformatics of proteinprotein interactions and a guide to their principles. Prog. Biophys. Mol. Biol., 2014, 116, 141-150.
    • (2014) Prog. Biophys. Mol. Biol. , vol.116 , pp. 141-150
    • Sudha, G.1    Nussinov, R.2    Srinivasan, N.3
  • 30
    • 78649846386 scopus 로고    scopus 로고
    • Update 1 of: Over one hundred peptideactivated G protein-coupled receptors recognize ligands with turn structure
    • Ruiz-Gomez, G.; Tyndall, J.D.; Pfeiffer, B.; Abbenante, G.; Fairlie, D.P. Update 1 of: Over one hundred peptideactivated G protein-coupled receptors recognize ligands with turn structure. Chem. Rev., 2010, 110(4), R1-R41.
    • (2010) Chem. Rev. , vol.110 , Issue.4 , pp. R1-R41
    • Ruiz-Gomez, G.1    Tyndall, J.D.2    Pfeiffer, B.3    Abbenante, G.4    Fairlie, D.P.5
  • 31
    • 79959886414 scopus 로고    scopus 로고
    • Design, synthesis, and validation of a β-turn mimetic library targeting protein-protein and peptide-receptor interactions
    • Whitby, L.R.; Ando, Y.; Setola, V.; Vogt, P.K.; Roth, B.L.; Boger, D.L. Design, synthesis, and validation of a β-turn mimetic library targeting protein-protein and peptide-receptor interactions. J. Am. Chem. Soc., 2011, 133(26), 10184-10194.
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.26 , pp. 10184-10194
    • Whitby, L.R.1    Ando, Y.2    Setola, V.3    Vogt, P.K.4    Roth, B.L.5    Boger, D.L.6
  • 32
    • 44949231073 scopus 로고    scopus 로고
    • Peptidomimetics, a synthetic tool of drug discovery
    • Vagner, J.; Qu, H.; Hruby, V.J. Peptidomimetics, a synthetic tool of drug discovery. Curr. Opin. Chem. Biol., 2008, 12(3), 292-296.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , Issue.3 , pp. 292-296
    • Vagner, J.1    Qu, H.2    Hruby, V.J.3
  • 33
    • 79959752282 scopus 로고    scopus 로고
    • Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease
    • Nie, Q.; Du,X.G.; Geng, M.Y. Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease. Acta Pharmacol. Sin., 2011, 32(5), 545-551.
    • (2011) Acta Pharmacol. Sin. , vol.32 , Issue.5 , pp. 545-551
    • Nie, Q.1    Du, X.G.2    Geng, M.Y.3
  • 34
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of alpha-helix-mediated protein-protein interactions using designed molecules
    • Azzarito, V.; Long, K.; Murphy, N.S.; Wilson, A.J. Inhibition of alpha-helix-mediated protein-protein interactions using designed molecules. Nat. Chem., 2013, 5(3), 161-173.
    • (2013) Nat. Chem. , vol.5 , Issue.3 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3    Wilson, A.J.4
  • 36
    • 34548141882 scopus 로고    scopus 로고
    • Secondary structure based analysis and classification of biological interfaces: Identification of binding motifs in protein-protein interactions
    • Guharoy, M.; Chakrabarti, P. Secondary structure based analysis and classification of biological interfaces: identification of binding motifs in protein-protein interactions. Bioinformatics, 2007, 23(15), 1909-1918.
    • (2007) Bioinformatics , vol.23 , Issue.15 , pp. 1909-1918
    • Guharoy, M.1    Chakrabarti, P.2
  • 37
    • 84906327241 scopus 로고    scopus 로고
    • Comprehensive analysis of loops at protein-protein interfaces for macrocycle design
    • Gavenonis, J.; Sheneman, B.A.; Siegert, T.R.; Eshelman, M.R.; Kritzer, J.A. Comprehensive analysis of loops at protein-protein interfaces for macrocycle design. Nat. Chem. Biol. 2014, 10(9), 716-722.
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.9 , pp. 716-722
    • Gavenonis, J.1    Sheneman, B.A.2    Siegert, T.R.3    Eshelman, M.R.4    Kritzer, J.A.5
  • 38
    • 73649124584 scopus 로고    scopus 로고
    • Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolution
    • Vollmuth, F.; Blankenfeldt, W.; Geyer, M. Structures of the dual bromodomains of the P-TEFb-activating protein Brd4 at atomic resolution. J. Biol. Chem., 2009, 284(52), 36547-36556.
    • (2009) J. Biol. Chem. , vol.284 , Issue.52 , pp. 36547-36556
    • Vollmuth, F.1    Blankenfeldt, W.2    Geyer, M.3
  • 40
    • 84870249445 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C.A.; Lombardo, F.; Dominy, B.W.; Feeney, P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev., 2012, 64, 4-17.
    • (2012) Adv. Drug Deliv. Rev. , vol.64 , pp. 4-17
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 41
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: What can medicinal chemists learn from their properties?
    • Giordanetto, F.; Kihlberg, J. Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties? J. Med. Chem., 2014, 57(2), 278-295.
    • (2014) J. Med. Chem. , vol.57 , Issue.2 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 42
    • 0034032705 scopus 로고    scopus 로고
    • Synthesis of natural-product-based compound libraries
    • Wessjohann, L.A. Synthesis of natural-product-based compound libraries. Curr. Opin. Chem. Biol., 2000, 4(3), 303-309.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , Issue.3 , pp. 303-309
    • Wessjohann, L.A.1
  • 43
    • 44249098800 scopus 로고    scopus 로고
    • Natural products to drugs: Natural productderived compounds in clinical trials
    • Butler, M.S. Natural products to drugs: natural productderived compounds in clinical trials. Nat. Prod. Rep., 2008, 25(3), 475-516.
    • (2008) Nat. Prod. Rep. , vol.25 , Issue.3 , pp. 475-516
    • Butler, M.S.1
  • 44
    • 33644535147 scopus 로고    scopus 로고
    • Natural products - The future scaffolds for novel antibiotics?
    • Butler, M.S.; Buss, A.D. Natural products - the future scaffolds for novel antibiotics? Biochem. Pharmacol., 2006, 71(7), 919-929.
    • (2006) Biochem. Pharmacol. , vol.71 , Issue.7 , pp. 919-929
    • Butler, M.S.1    Buss, A.D.2
  • 45
    • 0036165478 scopus 로고    scopus 로고
    • Tacrolimus and pimecrolimus: From clever prokaryotes to inhibiting calcineurin and treating atopic dermatitis
    • Nghiem, P.; Pearson, G.; Langley, R.G. Tacrolimus and pimecrolimus: from clever prokaryotes to inhibiting calcineurin and treating atopic dermatitis. J. Am. Acad. Dermatol., 2002, 46(2), 228-241.
    • (2002) J. Am. Acad. Dermatol. , vol.46 , Issue.2 , pp. 228-241
    • Nghiem, P.1    Pearson, G.2    Langley, R.G.3
  • 47
    • 79959580534 scopus 로고    scopus 로고
    • Contemporary strategies for peptide macrocyclization
    • White, C.J.; Yudin, A.K. Contemporary strategies for peptide macrocyclization. Nat. Chem., 2011, 3(7), 509-524.
    • (2011) Nat. Chem. , vol.3 , Issue.7 , pp. 509-524
    • White, C.J.1    Yudin, A.K.2
  • 49
    • 61649120635 scopus 로고    scopus 로고
    • Recent progress of synthetic studies to peptide and peptidomimetic cyclization
    • Jiang, S.; Li, Z.; Ding, K.; Roller, P.P. Recent progress of synthetic studies to peptide and peptidomimetic cyclization. Curr. Org. Chem., 2008, 12(17), 1502-1542.
    • (2008) Curr. Org. Chem. , vol.12 , Issue.17 , pp. 1502-1542
    • Jiang, S.1    Li, Z.2    Ding, K.3    Roller, P.P.4
  • 50
    • 46449115901 scopus 로고    scopus 로고
    • The exploration of macrocycles for drug discovery - An underexploited structural class
    • Driggers, E.M.; Hale, S.P.; Lee, J.; Terrett, N.K. The exploration of macrocycles for drug discovery - an underexploited structural class. Nat. Rev. Drug Discov., 2008, 7, 608-624.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 608-624
    • Driggers, E.M.1    Hale, S.P.2    Lee, J.3    Terrett, N.K.4
  • 51
    • 26844576835 scopus 로고    scopus 로고
    • Amide bond formation and peptide coupling
    • Montalbetti, C.; Falque, V. Amide bond formation and peptide coupling. Tetrahedron, 2005, 61(46), 10827-10852.
    • (2005) Tetrahedron , vol.61 , Issue.46 , pp. 10827-10852
    • Montalbetti, C.1    Falque, V.2
  • 52
    • 33645364955 scopus 로고    scopus 로고
    • Macrolactonizations in the total synthesis of natural products
    • Parenty, A.; Moreau, X; Campagne, J.M. Macrolactonizations in the total synthesis of natural products. Chem. Rev., 2006, 106(3), 911-939.
    • (2006) Chem. Rev. , vol.106 , Issue.3 , pp. 911-939
    • Parenty, A.1    Moreau, X.2    Campagne, J.M.3
  • 54
    • 0037136487 scopus 로고    scopus 로고
    • A new tri-orthogonal strategy for peptide cyclization
    • Lundquist, J.T. 4th; Pelletier, J.C. A new tri-orthogonal strategy for peptide cyclization. Org. Lett., 2002, 4(19), 3219-3221.
    • (2002) Org. Lett. , vol.4 , Issue.19 , pp. 3219-3221
    • Lundquist, I.V.J.T.1    Pelletier, J.C.2
  • 55
    • 84942928809 scopus 로고    scopus 로고
    • Enantioselective synthesis of 3-arylquinazolin-4(3H)-ones via peptide-catalyzed atroposelective bromination
    • Diener, M.E.; Metrano, A.J.; Kusano, S.; Miller, S.J. Enantioselective synthesis of 3-arylquinazolin-4(3H)-ones via peptide-catalyzed atroposelective bromination. J. Am. Chem. Soc., 2015, 137(38), 12369-12377.
    • (2015) J. Am. Chem. Soc. , vol.137 , Issue.38 , pp. 12369-12377
    • Diener, M.E.1    Metrano, A.J.2    Kusano, S.3    Miller, S.J.4
  • 56
    • 84863121468 scopus 로고    scopus 로고
    • Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction
    • Kawamoto, S.A.; Coleska, A.; Ran, X.; Yi, H.; Yang, C.Y.; Wang, S. Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction. J. Med. Chem., 2012, 55(3), 1137-1146.
    • (2012) J. Med. Chem. , vol.55 , Issue.3 , pp. 1137-1146
    • Kawamoto, S.A.1    Coleska, A.2    Ran, X.3    Yi, H.4    Yang, C.Y.5    Wang, S.6
  • 57
    • 77957298854 scopus 로고    scopus 로고
    • Structural and pharmacological effects of ring-closing metathesis in peptides
    • Jacobsen, O.; Klaveness, J.; Rongved, P. Structural and pharmacological effects of ring-closing metathesis in peptides. Molecules, 2010, 15(9), 6638-6677.
    • (2010) Molecules , vol.15 , Issue.9 , pp. 6638-6677
    • Jacobsen, O.1    Klaveness, J.2    Rongved, P.3
  • 58
    • 3843049165 scopus 로고    scopus 로고
    • An improved method for the solution cyclization of peptides under pseudo-high dilution conditions
    • Malesevic, M.; Strijowski, U.; Bachle, D. An improved method for the solution cyclization of peptides under pseudo-high dilution conditions. J. Biotechnol., 2004, 112(1-2), 73-77.
    • (2004) J. Biotechnol. , vol.112 , Issue.1-2 , pp. 73-77
    • Malesevic, M.1    Strijowski, U.2    Bachle, D.3
  • 59
    • 10444281979 scopus 로고    scopus 로고
    • New developments in polymer-supported reagents, scavengers and catalysts for organic synthesis
    • Bhattacharyya, S. New developments in polymer-supported reagents, scavengers and catalysts for organic synthesis. Curr. Opin. Drug Discov. Devel., 2004, 7(6), 752-764.
    • (2004) Curr. Opin. Drug Discov. Devel. , vol.7 , Issue.6 , pp. 752-764
    • Bhattacharyya, S.1
  • 60
    • 0034119855 scopus 로고    scopus 로고
    • Polymer-supported reagents and catalysts: Recent advances in synthetic applications
    • Bhattacharyya, S. Polymer-supported reagents and catalysts: recent advances in synthetic applications. Comb. Chem. High Throughput Screen., 2000, 3(2), 65-92.
    • (2000) Comb. Chem. High Throughput Screen. , vol.3 , Issue.2 , pp. 65-92
    • Bhattacharyya, S.1
  • 62
    • 0030999396 scopus 로고    scopus 로고
    • Cyclotetrapeptides and cyclopentapeptides: Occurrence and synthesis
    • Schmidt, U.; Langner, J. Cyclotetrapeptides and cyclopentapeptides: occurrence and synthesis. J. Pept. Res., 1997, 49(1), 67-73.
    • (1997) J. Pept. Res. , vol.49 , Issue.1 , pp. 67-73
    • Schmidt, U.1    Langner, J.2
  • 63
    • 76749155787 scopus 로고    scopus 로고
    • Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains
    • Daidone, I.; Neuweiler, H.; Doose, S.; Sauer, M.; Smith, J.C., Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains. PLoS Comp. Biol., 2010, 6(1), e1000645.
    • (2010) PLoS Comp. Biol. , vol.6 , Issue.1
    • Daidone, I.1    Neuweiler, H.2    Doose, S.3    Sauer, M.4    Smith, J.C.5
  • 64
    • 0033620414 scopus 로고    scopus 로고
    • Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template
    • Favre, M.; Jiang, L.; Robinson, J.A.; Moehle, K. Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template. J. Am. Chem. Soc., 1999, 121(12), 2679-2685.
    • (1999) J. Am. Chem. Soc. , vol.121 , Issue.12 , pp. 2679-2685
    • Favre, M.1    Jiang, L.2    Robinson, J.A.3    Moehle, K.4
  • 65
    • 0031028387 scopus 로고    scopus 로고
    • Pseudo-Prolines as a Molecular Hinge: Reversible induction of cis amide bonds into peptide backbones
    • Dumy, P.; Keller, M.; Ryan, D.E.; Rohwedder, B.; Wohr, T.; Mutter, M. Pseudo-Prolines as a Molecular Hinge: Reversible induction of cis amide bonds into peptide backbones. J. Am. Chem. Soc., 1997, 119(5), 918-925.
    • (1997) J. Am. Chem. Soc. , vol.119 , Issue.5 , pp. 918-925
    • Dumy, P.1    Keller, M.2    Ryan, D.E.3    Rohwedder, B.4    Wohr, T.5    Mutter, M.6
  • 67
    • 0032482050 scopus 로고    scopus 로고
    • Facile synthesis of cyclic tetrapeptides from nonactivated peptide esters on metal centers
    • Haas, K.; Ponikwar, W.; Noeth, H.; Beck,W. Facile synthesis of cyclic tetrapeptides from nonactivated peptide esters on metal centers. Angew. Chem. Int. Ed. Engl., 1998, 37(8), 1086-1089.
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , Issue.8 , pp. 1086-1089
    • Haas, K.1    Ponikwar, W.2    Noeth, H.3    Beck, W.4
  • 68
    • 10044225838 scopus 로고    scopus 로고
    • Pseudoprolines as removable turn inducers: Tools for the cyclization of small peptides
    • Skropeta, D.; Jolliffe, K.A.; Turner, P. Pseudoprolines as removable turn inducers: tools for the cyclization of small peptides. J. Org. Chem., 2004, 69(25), 8804-8809.
    • (2004) J. Org. Chem. , vol.69 , Issue.25 , pp. 8804-8809
    • Skropeta, D.1    Jolliffe, K.A.2    Turner, P.3
  • 69
    • 84897014318 scopus 로고    scopus 로고
    • Isocyanidebased multicomponent reactions towards cyclic constrained peptidomimetics
    • Koopmanschap, G.; Ruijter, E.; Orru, R.V. Isocyanidebased multicomponent reactions towards cyclic constrained peptidomimetics. Beilstein J. Org. Chem., 2014, 10, 544-598.
    • (2014) Beilstein J. Org. Chem. , vol.10 , pp. 544-598
    • Koopmanschap, G.1    Ruijter, E.2    Orru, R.V.3
  • 71
    • 84901681947 scopus 로고    scopus 로고
    • Hydrocarbon-stapled peptides: Principles, practice, and progress
    • Walensky, L.D.; Bird, G.H. Hydrocarbon-stapled peptides: principles, practice, and progress. J. Med. Chem., 2014, 57(15), 6275-6288.
    • (2014) J. Med. Chem. , vol.57 , Issue.15 , pp. 6275-6288
    • Walensky, L.D.1    Bird, G.H.2
  • 72
    • 84916912015 scopus 로고    scopus 로고
    • Peptide stapling techniques based on different macrocyclisation chemistries
    • Lau, Y.H.; de Andrade, P.; Wu, Y.; Spring, D.R. Peptide stapling techniques based on different macrocyclisation chemistries. Chem. Soc. Rev., 2015, 44(1), 91-102.
    • (2015) Chem. Soc. Rev. , vol.44 , Issue.1 , pp. 91-102
    • Lau, Y.H.1    De Andrade, P.2    Wu, Y.3    Spring, D.R.4
  • 73
    • 33750554051 scopus 로고    scopus 로고
    • Naturallyoccurring cyclopeptides: Structures and bioactivity
    • Pomilio, A.B.; Battista, M.E.; Vitale, A.A. Naturallyoccurring cyclopeptides: Structures and bioactivity. Curr. Org. Chem., 2006, 10(16), 2075-2121.
    • (2006) Curr. Org. Chem. , vol.10 , Issue.16 , pp. 2075-2121
    • Pomilio, A.B.1    Battista, M.E.2    Vitale, A.A.3
  • 74
    • 0036495674 scopus 로고    scopus 로고
    • Circular proteins - No end in sight
    • Trabi, M.C.; Craik, D.J. Circular proteins - no end in sight. Trends Biochem. Sci., 2002, 27(3), 132-138.
    • (2002) Trends Biochem. Sci. , vol.27 , Issue.3 , pp. 132-138
    • Trabi, M.C.1    Craik, D.J.2
  • 75
    • 84964565511 scopus 로고    scopus 로고
    • Antimicrobial and immunosuppressive activitites of cyclopeptides as targets for medicinal chemistry
    • Mercader, A.G.; Duchowicz, P.R.; Sivakumar, P.M.; Eds. Apple Academic Press Inc., exclusive worldwide distribution by CRC Press, a Taylor & Francis Group
    • Pomilio A.B.; Battista, S.M.; Vitale, A.A. Antimicrobial and immunosuppressive activitites of cyclopeptides as targets for medicinal chemistry. In: Chemometrics Applications and Research: QSAR in Medicinal Chemistry. Mercader, A.G.; Duchowicz, P.R.; Sivakumar, P.M.; Eds. Apple Academic Press Inc., exclusive worldwide distribution by CRC Press, a Taylor & Francis Group, 2015. ISBN: 978-1-77188-113-5
    • (2015) Chemometrics Applications and Research: QSAR in Medicinal Chemistry
    • Pomilio, A.B.1    Battista, S.M.2    Vitale, A.A.3
  • 76
    • 84862014605 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship (QSAR) studies on bioactive cyclopeptides
    • Chapter 1 Castro, E.A.; chief editor. Pandalai, S.G.; Managing Ed. Research Signpost: Kerala, India
    • Pomilio A.B.; Battista, S.M.; Vitale, A.A. Quantitative structure-activity relationship (QSAR) studies on bioactive cyclopeptides. In: QSPR-QSAR Studies on desired properties for drug design. Castro, E.A.; chief editor. Pandalai, S.G.; Managing Ed. Research Signpost: Kerala, India, 2010; Chapter 1, pp. 1-34. ISBN: 978-81-308-0404-0. http://issuu.com/researchsignpost/docs/castro-e-book
    • (2010) QSPR-QSAR Studies on Desired Properties for Drug Design , pp. 1-34
    • Pomilio, A.B.1    Battista, S.M.2    Vitale, A.A.3
  • 77
    • 78650277371 scopus 로고    scopus 로고
    • Inhibition of spoilage and toxigenic Bacillus species in dough from wheat flour by the cyclic peptide enterocin AS-48
    • Martinez Viedma, P.; Abriouel, H.; Omar, N.B.; Lopez, R.L.; Galvez, A. Inhibition of spoilage and toxigenic Bacillus species in dough from wheat flour by the cyclic peptide enterocin AS-48. Food Control, 2011, 22(5), 756-761.
    • (2011) Food Control , vol.22 , Issue.5 , pp. 756-761
    • Martinez Viedma, P.1    Abriouel, H.2    Omar, N.B.3    Lopez, R.L.4    Galvez, A.5
  • 78
    • 79251607581 scopus 로고    scopus 로고
    • Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos)
    • Borrero, J.; Brede, D.A.; Skaugen, M.; Diep, D.B.; Herranz, C.; Nes, I.F.; Cintas, L.M.; Hernandez, P.E. Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos). Appl. Environ. Microb., 2011, 77(1), 369-373.
    • (2011) Appl. Environ. Microb. , vol.77 , Issue.1 , pp. 369-373
    • Borrero, J.1    Brede, D.A.2    Skaugen, M.3    Diep, D.B.4    Herranz, C.5    Nes, I.F.6    Cintas, L.M.7    Hernandez, P.E.8
  • 79
    • 62149087459 scopus 로고    scopus 로고
    • Identification and characterization of lactocyclicin Q, a novel cyclic bacteriocin produced by Lactococcus sp. Strain QU 12
    • Sawa, N.; Zendo, T.; Kiyofuji, J.; Fujita, K.; Himeno, K.; Nakayama, J.; Sonomoto, K. Identification and characterization of lactocyclicin Q, a novel cyclic bacteriocin produced by Lactococcus sp. strain QU 12. Appl. Environ. Microb., 2009, 75(6), 1552-1558.
    • (2009) Appl. Environ. Microb. , vol.75 , Issue.6 , pp. 1552-1558
    • Sawa, N.1    Zendo, T.2    Kiyofuji, J.3    Fujita, K.4    Himeno, K.5    Nakayama, J.6    Sonomoto, K.7
  • 83
    • 0005132333 scopus 로고
    • Studies on a bactericidal agent extracted from a soil bacillus: III. Preparation and activity of a protein-free fraction
    • Dubos, R.J.; Cattaneo, C. Studies on a bactericidal agent extracted from a soil bacillus: III. Preparation and activity of a protein-free fraction. J. Exp. Med., 1939, 70(3), 249-256.
    • (1939) J. Exp. Med. , vol.70 , Issue.3 , pp. 249-256
    • Dubos, R.J.1    Cattaneo, C.2
  • 84
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature, 2002, 415(6870), 389-395.
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 85
    • 34548538972 scopus 로고    scopus 로고
    • Development of Tyrocidine A analogues with improved antibacterial activity
    • Marques, M.A.; Citron, D.M.; Wang, C.C. Development of Tyrocidine A analogues with improved antibacterial activity. Bioorg. Med. Chem., 2007, 15(21), 6667-6677.
    • (2007) Bioorg. Med. Chem. , vol.15 , Issue.21 , pp. 6667-6677
    • Marques, M.A.1    Citron, D.M.2    Wang, C.C.3
  • 86
    • 0017072249 scopus 로고
    • Cyclosporin A, a peptide metabolite from trichoderma polysporum (Link ex Pers.) Rifai, with a remarkable immunosuppressive activity
    • Ruegger, A.; Kuhn, M.; Lichti, H.; Loosli, H.R., Huguenin, R., Quiquerez, C.; von Wartburg, A. Cyclosporin A, a peptide metabolite from trichoderma polysporum (Link ex Pers.) Rifai, with a remarkable immunosuppressive activity. Helv. Chim. Acta, 1976, 59(4), 1075-1092.
    • (1976) Helv. Chim. Acta , vol.59 , Issue.4 , pp. 1075-1092
    • Ruegger, A.1    Kuhn, M.2    Lichti, H.3    Loosli, H.R.4    Huguenin, R.5    Quiquerez, C.6    Von Wartburg, A.7
  • 87
    • 0032053123 scopus 로고    scopus 로고
    • Structural characterization of two novel oxidative derivatives of cyclosporine generated by a chemical method
    • Liu, W.T.; Marat, K.; Ren, Y.; Eng, R.T.; Wong, P.Y. Structural characterization of two novel oxidative derivatives of cyclosporine generated by a chemical method. Clin. Biochem., 1998, 31(3), 173-180.
    • (1998) Clin. Biochem. , vol.31 , Issue.3 , pp. 173-180
    • Liu, W.T.1    Marat, K.2    Ren, Y.3    Eng, R.T.4    Wong, P.Y.5
  • 90
    • 0034885143 scopus 로고    scopus 로고
    • Vancomycin, teicoplanin, and ramoplanin: Synthetic and mechanistic studies
    • Boger, D.L. Vancomycin, teicoplanin, and ramoplanin: synthetic and mechanistic studies. Med. Res. Rev., 2001, 21(5), 356-381.
    • (2001) Med. Res. Rev. , vol.21 , Issue.5 , pp. 356-381
    • Boger, D.L.1
  • 91
    • 0025281763 scopus 로고
    • Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein
    • Knox, J.R.; Pratt, R.F. Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein. Antimicrob. Agents Chemother., 1990, 34(7), 1342-1347.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , Issue.7 , pp. 1342-1347
    • Knox, J.R.1    Pratt, R.F.2
  • 92
    • 33644654444 scopus 로고    scopus 로고
    • Synthesis of alkyne-bridged cyclic tripeptides toward constrained mimics of vancomycin
    • ten Brink, H.T.; Rijkers, D.T.; Liskamp, R.M. Synthesis of alkyne-bridged cyclic tripeptides toward constrained mimics of vancomycin. J. Org. Chem., 2006, 71(5), 1817-1824.
    • (2006) J. Org. Chem. , vol.71 , Issue.5 , pp. 1817-1824
    • Ten Brink, H.T.1    Rijkers, D.T.2    Liskamp, R.M.3
  • 93
    • 84949115155 scopus 로고    scopus 로고
    • Total synthesis of [Psi[C( horizontal lineNH)NH]Tpg (4)]vancomycin and its (4-chlorobiphenyl)methyl derivative: Impact of peripheral modifications on vancomycin analogues redesigned for dual D-Ala-D-Ala and D-Ala-D-Lac binding
    • Okano, A.; Nakayama, A.; Schammel, A.W.; Boger, D.L. Total synthesis of [Psi[C( horizontal lineNH)NH]Tpg (4)]vancomycin and its (4-chlorobiphenyl)methyl derivative: impact of peripheral modifications on vancomycin analogues redesigned for dual D-Ala-D-Ala and D-Ala-D-Lac binding. J. Am. Chem. Soc., 2014, 136(39), 13522-13525.
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.39 , pp. 13522-13525
    • Okano, A.1    Nakayama, A.2    Schammel, A.W.3    Boger, D.L.4
  • 94
    • 0033574743 scopus 로고    scopus 로고
    • Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala
    • Ge, M.; Chen, Z.; Onishi, H.R.; Kohler, J.; Silver, L.L.; Kerns, R.; Fukuzawa, S.; Thompson, C.; Kahne, D. Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Science, 1999, 284(5413), 507-511.
    • (1999) Science , vol.284 , Issue.5413 , pp. 507-511
    • Ge, M.1    Chen, Z.2    Onishi, H.R.3    Kohler, J.4    Silver, L.L.5    Kerns, R.6    Fukuzawa, S.7    Thompson, C.8    Kahne, D.9
  • 95
    • 0000915203 scopus 로고
    • Bioactive sponge peptides
    • Fusetani, N.; Matsunaga, S. Bioactive sponge peptides. Chem. Rev., 1993, 93(5), 1793-1806.
    • (1993) Chem. Rev. , vol.93 , Issue.5 , pp. 1793-1806
    • Fusetani, N.1    Matsunaga, S.2
  • 96
    • 0029133970 scopus 로고
    • Cyclotheonamide derivatives: Synthesis and thrombin inhibition. Exploration of specific structure-function issues
    • Maryanoff, B.E.; Zhang, H.C.; Greco, M.N.; Glover, K.A.; Kauffman, J.A.; Andrade-Gordon, P. Cyclotheonamide derivatives: synthesis and thrombin inhibition. Exploration of specific structure-function issues. Bioorg. Med. Chem., 1995, 3(8), 1025-1038.
    • (1995) Bioorg. Med. Chem. , vol.3 , Issue.8 , pp. 1025-1038
    • Maryanoff, B.E.1    Zhang, H.C.2    Greco, M.N.3    Glover, K.A.4    Kauffman, J.A.5    Andrade-Gordon, P.6
  • 97
    • 84857147068 scopus 로고    scopus 로고
    • Cyclic peptides as therapeutic agents and biochemical tools
    • Joo, S.H. Cyclic peptides as therapeutic agents and biochemical tools. Biomol. Ther., 2012, 20(1), 19-26.
    • (2012) Biomol. Ther. , vol.20 , Issue.1 , pp. 19-26
    • Joo, S.H.1
  • 98
    • 0023839836 scopus 로고
    • Inhibition of in vitro tumor cell invasion by Arg-Gly-ASP-containing synthetic peptides
    • Gehlsen, K.R.; Argraves, W.S.; Pierschbacher, M.D.; Ruoslahti, E. Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides. J. Cell. Biol., 1988, 106(3), 925-930.
    • (1988) J. Cell. Biol. , vol.106 , Issue.3 , pp. 925-930
    • Gehlsen, K.R.1    Argraves, W.S.2    Pierschbacher, M.D.3    Ruoslahti, E.4
  • 99
    • 0027102818 scopus 로고
    • Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides
    • Gurrath, M.; Muller, G.; Kessler, H.; Aumailley, M.; Timpl, R., Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides. Eur. J. Biochem., 1992, 210(3), 911-921.
    • (1992) Eur. J. Biochem. , vol.210 , Issue.3 , pp. 911-921
    • Gurrath, M.1    Muller, G.2    Kessler, H.3    Aumailley, M.4    Timpl, R.5
  • 101
    • 84863722013 scopus 로고    scopus 로고
    • Encapsulation of cell-adhesive RGD peptides into a polymeric physical hydrogel to prevent postoperative tissue adhesion
    • Zhang, Z.; Ni, J.; Chen, L.; Yu, L.; Xu, J.; Ding, J. Encapsulation of cell-adhesive RGD peptides into a polymeric physical hydrogel to prevent postoperative tissue adhesion. J. Biomed. Mater. Res., Part B, 2012, 100B(6), 1599-1609.
    • (2012) J. Biomed. Mater. Res., Part B , vol.100 B , Issue.6 , pp. 1599-1609
    • Zhang, Z.1    Ni, J.2    Chen, L.3    Yu, L.4    Xu, J.5    Ding, J.6
  • 105
    • 0036976236 scopus 로고    scopus 로고
    • Design, synthesis, conformational analysis, and biological studies of urotensin-II lactam analogues
    • Grieco, P.; Carotenuto, A.; Patacchini, R.; Maggi, C.A.; Novellino, E.; Rovero, P. Design, synthesis, conformational analysis, and biological studies of urotensin-II lactam analogues. Bioorg. Med. Chem., 2002, 10(12), 3731-3739.
    • (2002) Bioorg. Med. Chem. , vol.10 , Issue.12 , pp. 3731-3739
    • Grieco, P.1    Carotenuto, A.2    Patacchini, R.3    Maggi, C.A.4    Novellino, E.5    Rovero, P.6
  • 107
    • 84940600691 scopus 로고    scopus 로고
    • Sortase Amediated synthesis of ligand-grafted cyclized peptides for modulating a model protein-protein interaction
    • Zhang, J.; Yamaguchi, S.; Nagamune, T. Sortase Amediated synthesis of ligand-grafted cyclized peptides for modulating a model protein-protein interaction. Biotechnol. J., 2015, 10(9), 1499-1505.
    • (2015) Biotechnol. J. , vol.10 , Issue.9 , pp. 1499-1505
    • Zhang, J.1    Yamaguchi, S.2    Nagamune, T.3
  • 108
    • 84887918731 scopus 로고    scopus 로고
    • From peptides to small molecules: An intriguing but intricated way to new drugs
    • Scognamiglio, P.L.; Di Natale, C.; Perretta, G.; Marasco, D. From peptides to small molecules: an intriguing but intricated way to new drugs. Curr. Med. Chem., 2013, 20(31), 3803-3817.
    • (2013) Curr. Med. Chem. , vol.20 , Issue.31 , pp. 3803-3817
    • Scognamiglio, P.L.1    Di Natale, C.2    Perretta, G.3    Marasco, D.4
  • 109
    • 84955151762 scopus 로고    scopus 로고
    • Synthetic and structural routes for the rational conversion of peptides into small molecules
    • Scognamiglio, P.L.; Morelli, G.; Marasco, D. Synthetic and structural routes for the rational conversion of peptides into small molecules. Methods Mol. Biol., 2015, 1268(10), 159-193.
    • (2015) Methods Mol. Biol. , vol.1268 , Issue.10 , pp. 159-193
    • Scognamiglio, P.L.1    Morelli, G.2    Marasco, D.3
  • 111
    • 84925258831 scopus 로고    scopus 로고
    • Cationic peptides as RNA compaction agents: A study on the polyA compaction activity of a linear alpha,epsilon-oligo-L-lysine
    • Roviello, G.N.; Musumeci, D.; Roviello, V. Cationic peptides as RNA compaction agents: a study on the polyA compaction activity of a linear alpha,epsilon-oligo-L-lysine. Int. J. Pharm., 2015, 485(1-2), 244-248.
    • (2015) Int. J. Pharm. , vol.485 , Issue.1-2 , pp. 244-248
    • Roviello, G.N.1    Musumeci, D.2    Roviello, V.3
  • 114
    • 84929018299 scopus 로고    scopus 로고
    • Intracellular delivery of peptidyl ligands by reversible cyclization: Discovery of a PDZ domain inhibitor that rescues CFTR activity
    • Qian, Z.; Xu, X.; Amacher, J.F.; Madden, D.R.; Cormet-Boyaka, E.; Pei, D. Intracellular delivery of peptidyl ligands by reversible cyclization: discovery of a PDZ domain inhibitor that rescues CFTR activity. Angew. Chem., 2015, 54(20), 5874-5878.
    • (2015) Angew. Chem. , vol.54 , Issue.20 , pp. 5874-5878
    • Qian, Z.1    Xu, X.2    Amacher, J.F.3    Madden, D.R.4    Cormet-Boyaka, E.5    Pei, D.6
  • 115
    • 84907940003 scopus 로고    scopus 로고
    • Rationally designed macrocyclic peptides as synergistic agonists of LPSinduced inflammatory response
    • Gao, M.; Londonb, N.; Chengc, K.; Tamurac, R.; Jina, J.; Schueler-Furmanb, O.; Yina, H. Rationally designed macrocyclic peptides as synergistic agonists of LPSinduced inflammatory response. Tetrahedron, 2014, 70(42), 7664-7668.
    • (2014) Tetrahedron , vol.70 , Issue.42 , pp. 7664-7668
    • Gao, M.1    Londonb, N.2    Chengc, K.3    Tamurac, R.4    Jina, J.5    Schueler-Furmanb, O.6    Yina, H.7
  • 116
    • 84906935431 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of scaffoldbased tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4)
    • Zachariassen, Z.G.; Thiele, S.; Berg, E.A.; Rasmussen, P.; Fossen, T.; Rosenkilde, M,M.; Vabeno, J.; Haug, B.E. Design, synthesis, and biological evaluation of scaffoldbased tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4). Bioorg. Med. Chem., 2014, 22(17), 4759-4769.
    • (2014) Bioorg. Med. Chem. , vol.22 , Issue.17 , pp. 4759-4769
    • Zachariassen, Z.G.1    Thiele, S.2    Berg, E.A.3    Rasmussen, P.4    Fossen, T.5    Rosenkilde, M.M.6    Vabeno, J.7    Haug, B.E.8
  • 119
    • 84929094259 scopus 로고    scopus 로고
    • Cyclization of the urokinase receptorderived ser-arg-ser-arg-tyr Peptide generates a potent inhibitor of trans-endothelial migration of monocytes
    • Yousif, A.M.; Minopoli, M.; Bifulco, K.; Ingangi, V.; Di Carluccio, G.; Merlino, F.; Motti, M.L.; Grieco, P.; Carriero, M.V. Cyclization of the urokinase receptorderived ser-arg-ser-arg-tyr Peptide generates a potent inhibitor of trans-endothelial migration of monocytes. PloS One, 2015, 10(5), e0126172.
    • (2015) PloS One , vol.10 , Issue.5
    • Yousif, A.M.1    Minopoli, M.2    Bifulco, K.3    Ingangi, V.4    Di Carluccio, G.5    Merlino, F.6    Motti, M.L.7    Grieco, P.8    Carriero, M.V.9
  • 120
    • 84920860615 scopus 로고    scopus 로고
    • Computational de novo design of a selfassembling peptide with predefined structure
    • Kaltofen, S.; Li, C.; Huang P.S.; Serpell, L.C. Barth, A.; Andre, I. Computational de novo design of a selfassembling peptide with predefined structure. J. Mol. Biol., 2015, 427(2), 550-62.
    • (2015) J. Mol. Biol. , vol.427 , Issue.2 , pp. 550-562
    • Kaltofen, S.1    Li, C.2    Huang, P.S.3    Serpell, L.C.4    Barth, A.5    Andre, I.6
  • 122
    • 84865514143 scopus 로고    scopus 로고
    • Flexible or fixed: A comparative review of linear and cyclic cancer-targeting peptides
    • Roxin, A.; Zheng, G. Flexible or fixed: a comparative review of linear and cyclic cancer-targeting peptides. Future Med. Chem., 2012, 4(12), 1601-1618.
    • (2012) Future Med. Chem. , vol.4 , Issue.12 , pp. 1601-1618
    • Roxin, A.1    Zheng, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.