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Volumn 99, Issue 5, 2015, Pages 2023-2040

Antimicrobial peptides: an alternative for innovative medicines?

Author keywords

Antitumoral; Bioinformatics; Salivary peptide; Synthesis

Indexed keywords

BACTERIA; BIOINFORMATICS; COST EFFECTIVENESS; MICROORGANISMS; MOLECULES; PEPTIDES; SYNTHESIS (CHEMICAL); VIRUSES;

EID: 84925465535     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-6375-x     Document Type: Review
Times cited : (172)

References (253)
  • 1
    • 84894142802 scopus 로고    scopus 로고
    • Magnetic nanoparticles for selective capture and purification of an antimicrobial peptide secreted by food-grade lactic acid bacteria
    • COI: 1:CAS:528:DC%2BC2cXisFSisbw%3D
    • Adhikari MD, Mukherjee S, Saikia J, Das G, Ramesh A (2014) Magnetic nanoparticles for selective capture and purification of an antimicrobial peptide secreted by food-grade lactic acid bacteria. J Mater Chem B Mater Biol Med 2(10):1432–1438
    • (2014) J Mater Chem B Mater Biol Med , vol.2 , Issue.10 , pp. 1432-1438
    • Adhikari, M.D.1    Mukherjee, S.2    Saikia, J.3    Das, G.4    Ramesh, A.5
  • 2
    • 84887847992 scopus 로고    scopus 로고
    • Structure and orientation study of Ebola fusion peptide inserted in lipid membrane models
    • COI: 1:CAS:528:DC%2BC3sXhvFOlsb7F, PID: 24055820
    • Agopian A, Castano S (2014) Structure and orientation study of Ebola fusion peptide inserted in lipid membrane models. Biochim Biophys Acta 1838(1, Part B):117–126
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.1 , pp. 117-126
    • Agopian, A.1    Castano, S.2
  • 3
    • 84862555645 scopus 로고    scopus 로고
    • Identification and design of antimicrobial peptides for therapeutic applications
    • COI: 1:CAS:528:DC%2BC38XhtFSgtbrM, PID: 22612781
    • Ahmad A, Ahmad E, Rabbani G, Haque S, Arshad M, Hasan Khan R (2012) Identification and design of antimicrobial peptides for therapeutic applications. Curr Protein Pept Sci 13(3):211–223
    • (2012) Curr Protein Pept Sci , vol.13 , Issue.3 , pp. 211-223
    • Ahmad, A.1    Ahmad, E.2    Rabbani, G.3    Haque, S.4    Arshad, M.5    Hasan Khan, R.6
  • 4
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • COI: 1:CAS:528:DyaK2sXlvFyhu7w%3D, PID: 9254694
    • Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25(17):3389–3402
    • (1997) Nucleic Acids Res , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 5
    • 84901030066 scopus 로고    scopus 로고
    • Salivary lactoferrin in HIV-infected children: correlation with Candida albicans carriage, oral manifestations, HIV infection and its antifungal activity
    • COI: 1:CAS:528:DC%2BC2cXpvFSqsbc%3D, PID: 24837476
    • Alves TP, Simões ACDC, Soares RMA, Moreno DSA, Portela MB, Castro GFBA (2014) Salivary lactoferrin in HIV-infected children: correlation with Candida albicans carriage, oral manifestations, HIV infection and its antifungal activity. Arch Oral Biol 59(8):775–782
    • (2014) Arch Oral Biol , vol.59 , Issue.8 , pp. 775-782
    • Alves, T.P.1    Simões, A.C.D.C.2    Soares, R.M.A.3    Moreno, D.S.A.4    Portela, M.B.5    Castro, G.F.B.A.6
  • 6
    • 84878640947 scopus 로고    scopus 로고
    • One decade of salivary proteomics: current approaches and outstanding challenges
    • COI: 1:CAS:528:DC%2BC38XhvVeku7nN, PID: 23103441
    • Amado FML, Ferreira RP, Vitorino R (2013) One decade of salivary proteomics: current approaches and outstanding challenges. Clin Biochem 46(6):506–517
    • (2013) Clin Biochem , vol.46 , Issue.6 , pp. 506-517
    • Amado, F.M.L.1    Ferreira, R.P.2    Vitorino, R.3
  • 7
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: crystallographic structure analysis and refinement at 2·8 Å resolution
    • COI: 1:CAS:528:DyaK3cXltVOitQ%3D%3D, PID: 2585506
    • Anderson BF, Baker HM, Norris GE, Rice DW, Baker EN (1989) Structure of human lactoferrin: crystallographic structure analysis and refinement at 2·8 Å resolution. J Mol Biol 209(4):711–734
    • (1989) J Mol Biol , vol.209 , Issue.4 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 9
    • 84907228975 scopus 로고    scopus 로고
    • Peptides as drugs
    • Badiani K (2012) Peptides as drugs. Manufacturing 4(2)
    • (2012) Manufacturing , vol.4 , Issue.2
    • Badiani, K.1
  • 10
    • 80052336721 scopus 로고    scopus 로고
    • Antimicrobial peptides—promising alternatives to conventional antibiotics
    • COI: 1:CAS:528:DC%2BC3MXht12gsbzO, PID: 21894027
    • Baltzer SA, Brown MH (2011) Antimicrobial peptides—promising alternatives to conventional antibiotics. J Mol Microbiol Biotechnol 20(4):228–235
    • (2011) J Mol Microbiol Biotechnol , vol.20 , Issue.4 , pp. 228-235
    • Baltzer, S.A.1    Brown, M.H.2
  • 11
    • 84857681286 scopus 로고    scopus 로고
    • Antimicrobial activity of lysozyme and lactoferrin incorporated in cellulose-based food packaging
    • COI: 1:CAS:528:DC%2BC38XlsVaiu78%3D
    • Barbiroli A, Bonomi F, Capretti G, Iametti S, Manzoni M, Piergiovanni L, Rollini M (2012) Antimicrobial activity of lysozyme and lactoferrin incorporated in cellulose-based food packaging. Food Control 26(2):387–392
    • (2012) Food Control , vol.26 , Issue.2 , pp. 387-392
    • Barbiroli, A.1    Bonomi, F.2    Capretti, G.3    Iametti, S.4    Manzoni, M.5    Piergiovanni, L.6    Rollini, M.7
  • 12
    • 80052503897 scopus 로고    scopus 로고
    • Lactoferrin-derived antimicrobial peptide induces a micellar cubic phase in a model membrane system
    • COI: 1:CAS:528:DC%2BC3MXpsFeiu70%3D, PID: 21806917
    • Bastos M, Silva T, Teixeira V, Nazmi K, Bolscher JG, Funari SS, Uhríková D (2011) Lactoferrin-derived antimicrobial peptide induces a micellar cubic phase in a model membrane system. Biophys J 101(3):L20–L22
    • (2011) Biophys J , vol.101 , Issue.3 , pp. 20-22
    • Bastos, M.1    Silva, T.2    Teixeira, V.3    Nazmi, K.4    Bolscher, J.G.5    Funari, S.S.6    Uhríková, D.7
  • 13
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N‐terminal region of bovine lactoferrin
    • COI: 1:CAS:528:DyaK3sXkt1Cnt7g%3D, PID: 1490908
    • Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M (1992) Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N‐terminal region of bovine lactoferrin. J Appl Bacteriol 73(6):472–479
    • (1992) J Appl Bacteriol , vol.73 , Issue.6 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 14
    • 70350608319 scopus 로고    scopus 로고
    • Association of human cathelicidin (hCAP-18/LL-37) gene expression with cardiovascular disease risk factors
    • COI: 1:CAS:528:DC%2BD1MXhs1aitL%2FO, PID: 19346112
    • Benachour H, Zaiou M, Samara A, Herbeth B, Pfister M, Lambert D, Siest G, Visvikis-Siest S (2009) Association of human cathelicidin (hCAP-18/LL-37) gene expression with cardiovascular disease risk factors. Nutr Metab Cardiovasc Dis 19(10):720–728
    • (2009) Nutr Metab Cardiovasc Dis , vol.19 , Issue.10 , pp. 720-728
    • Benachour, H.1    Zaiou, M.2    Samara, A.3    Herbeth, B.4    Pfister, M.5    Lambert, D.6    Siest, G.7    Visvikis-Siest, S.8
  • 15
    • 0020480352 scopus 로고
    • Salivary proline-rich proteins
    • COI: 1:CAS:528:DyaL38Xks1OqsLY%3D, PID: 6810092
    • Bennick A (1982) Salivary proline-rich proteins. Mol Cell Biochem 45(2):83–99
    • (1982) Mol Cell Biochem , vol.45 , Issue.2 , pp. 83-99
    • Bennick, A.1
  • 16
    • 79954915318 scopus 로고    scopus 로고
    • Paneth cells, antimicrobial peptides and maintenance of intestinal homeostasis
    • COI: 1:CAS:528:DC%2BC3MXjsF2hsrs%3D, PID: 21423246
    • Bevins CL, Salzman NH (2011) Paneth cells, antimicrobial peptides and maintenance of intestinal homeostasis. Nat Rev Microbiol 9(5):356–368
    • (2011) Nat Rev Microbiol , vol.9 , Issue.5 , pp. 356-368
    • Bevins, C.L.1    Salzman, N.H.2
  • 17
    • 84890294468 scopus 로고    scopus 로고
    • Development of oligopeptide-based novel biosensor by solid-phase peptide synthesis on microchip
    • COI: 1:CAS:528:DC%2BC2cXptFCj
    • Bhardwaj R, Lightson N, Ukita Y, Takamura Y (2014) Development of oligopeptide-based novel biosensor by solid-phase peptide synthesis on microchip. Sensors Actuators B Chem 192:818–825
    • (2014) Sensors Actuators B Chem , vol.192 , pp. 818-825
    • Bhardwaj, R.1    Lightson, N.2    Ukita, Y.3    Takamura, Y.4
  • 18
    • 79952988935 scopus 로고    scopus 로고
    • Designing carbohydrate nanoparticles for prolonged efficacy of antimicrobial peptide
    • COI: 1:CAS:528:DC%2BC3MXjvVSmtrk%3D, PID: 21115078
    • Bi L, Yang L, Narsimhan G, Bhunia AK, Yao Y (2011) Designing carbohydrate nanoparticles for prolonged efficacy of antimicrobial peptide. J Control Release 150(2):150–156
    • (2011) J Control Release , vol.150 , Issue.2 , pp. 150-156
    • Bi, L.1    Yang, L.2    Narsimhan, G.3    Bhunia, A.K.4    Yao, Y.5
  • 19
    • 84902051285 scopus 로고    scopus 로고
    • Biomolecular display technology: a new tool for drug discovery
    • Verma AS, Singh A, (eds), Academic, San Diego:
    • Biyani M, Nishigaki K, Biyani M (2014) Biomolecular display technology: a new tool for drug discovery. In: Verma AS, Singh A (eds) Animal biotechnology. Academic, San Diego, pp 369–384
    • (2014) Animal biotechnology , pp. 369-384
    • Biyani, M.1    Nishigaki, K.2    Biyani, M.3
  • 20
    • 84878544428 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of antimicrobial activity of N-terminal modified Leucocin A analogues
    • COI: 1:CAS:528:DC%2BC3sXnslCitbc%3D, PID: 23673216
    • Bodapati KC, Soudy R, Etayash H, Stiles M, Kaur K (2013) Design, synthesis and evaluation of antimicrobial activity of N-terminal modified Leucocin A analogues. Bioorg Med Chem 21(13):3715–3722
    • (2013) Bioorg Med Chem , vol.21 , Issue.13 , pp. 3715-3722
    • Bodapati, K.C.1    Soudy, R.2    Etayash, H.3    Stiles, M.4    Kaur, K.5
  • 21
  • 22
    • 33748117424 scopus 로고    scopus 로고
    • Immunomodulatory properties of defensins and cathelicidins. Antimicrobial Peptides and Human Disease
    • Bowdish D, Davidson D, Hancock R (2006) Immunomodulatory properties of defensins and cathelicidins. Antimicrobial Peptides and Human Disease. Springer, pp 27-66
    • (2006) Springer , pp. 27-66
    • Bowdish, D.1    Davidson, D.2    Hancock, R.3
  • 23
    • 0037667047 scopus 로고    scopus 로고
    • Large-scale manufacture of peptide therapeutics by chemical synthesis
    • COI: 1:CAS:528:DC%2BD3sXks1Oqsr4%3D, PID: 12815383
    • Bray BL (2003) Large-scale manufacture of peptide therapeutics by chemical synthesis. Nat Rev Drug Discov 2(7):587–593
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.7 , pp. 587-593
    • Bray, B.L.1
  • 26
    • 84883622617 scopus 로고    scopus 로고
    • Molecular mechanics force field-based general map for the solvation effect on amide I probe of peptide in different micro-environments
    • COI: 1:CAS:528:DC%2BC3sXhslWhsL3J, PID: 24036186
    • Cai K, Su T, Lin S, Zheng R (2014) Molecular mechanics force field-based general map for the solvation effect on amide I probe of peptide in different micro-environments. Spectrochim Acta A Mol Biomol Spectrosc 117:548–556
    • (2014) Spectrochim Acta A Mol Biomol Spectrosc , vol.117 , pp. 548-556
    • Cai, K.1    Su, T.2    Lin, S.3    Zheng, R.4
  • 27
    • 33845426262 scopus 로고    scopus 로고
    • Identification of a new Schistosoma mansoni membrane-bound protein through bioinformatic analysis
    • COI: 1:CAS:528:DC%2BD28XhtFGitb7O, PID: 17183472
    • Cardoso F, Pinho J, Azevedo V, Oliveira S (2006) Identification of a new Schistosoma mansoni membrane-bound protein through bioinformatic analysis. Genet Mol Res 5(4):609–618
    • (2006) Genet Mol Res , vol.5 , Issue.4 , pp. 609-618
    • Cardoso, F.1    Pinho, J.2    Azevedo, V.3    Oliveira, S.4
  • 28
    • 84908279095 scopus 로고    scopus 로고
    • Antibacterial activity of hen egg white lysozyme modified by heat and enzymatic treatments against oenological lactic acid bacteria and acetic acid bacteria
    • COI: 1:CAS:528:DC%2BC2cXitFWhur%2FP, PID: 25285490
    • Carrillo W, García-Ruiz A, Recio I, Moreno-Arribas MV (2014) Antibacterial activity of hen egg white lysozyme modified by heat and enzymatic treatments against oenological lactic acid bacteria and acetic acid bacteria. J Food Prot 77(10):1732–1739
    • (2014) J Food Prot , vol.77 , Issue.10 , pp. 1732-1739
    • Carrillo, W.1    García-Ruiz, A.2    Recio, I.3    Moreno-Arribas, M.V.4
  • 30
    • 84881118027 scopus 로고    scopus 로고
    • Analysis and prediction of highly effective antiviral peptides based on random forests
    • COI: 1:CAS:528:DC%2BC3sXhtlSmsLfI, PID: 23940542
    • Chang KY, Yang J-R (2013) Analysis and prediction of highly effective antiviral peptides based on random forests. PLoS One 8(8):e70166
    • (2013) PLoS One , vol.8 , Issue.8
    • Chang, K.Y.1    Yang, J.-R.2
  • 31
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: a protein structure and structural feature prediction server
    • COI: 1:CAS:528:DC%2BD2MXlslyrurc%3D, PID: 15980571
    • Cheng J, Randall AZ, Sweredoski MJ, Baldi P (2005) SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res 33(2):W72–W76
    • (2005) Nucleic Acids Res , vol.33 , Issue.2 , pp. 72-76
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 32
    • 0030038197 scopus 로고    scopus 로고
    • Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
    • COI: 1:CAS:528:DyaK28XhtVWqtb4%3D, PID: 8621683
    • Chertov O, Michiel DF, Xu L, Wang JM, Tani K, Murphy WJ, Longo DL, Taub DD, Oppenheim JJ (1996) Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J Biol Chem 271(6):2935–2940
    • (1996) J Biol Chem , vol.271 , Issue.6 , pp. 2935-2940
    • Chertov, O.1    Michiel, D.F.2    Xu, L.3    Wang, J.M.4    Tani, K.5    Murphy, W.J.6    Longo, D.L.7    Taub, D.D.8    Oppenheim, J.J.9
  • 33
    • 84866558088 scopus 로고    scopus 로고
    • Antimicrobial peptide pleurocidin synergizes with antibiotics through hydroxyl radical formation and membrane damage, and exerts antibiofilm activity
    • COI: 1:CAS:528:DC%2BC38XhsFClu7%2FE, PID: 22921812
    • Choi H, Lee DG (2012a) Antimicrobial peptide pleurocidin synergizes with antibiotics through hydroxyl radical formation and membrane damage, and exerts antibiofilm activity. Biochim Biophys Acta 1820(12):1831–1838
    • (2012) Biochim Biophys Acta , vol.1820 , Issue.12 , pp. 1831-1838
    • Choi, H.1    Lee, D.G.2
  • 34
    • 84865599210 scopus 로고    scopus 로고
    • Synergistic effect of antimicrobial peptide arenicin-1 in combination with antibiotics against pathogenic bacteria
    • COI: 1:CAS:528:DC%2BC38Xhtlaitr%2FJ, PID: 22705395
    • Choi H, Lee DG (2012b) Synergistic effect of antimicrobial peptide arenicin-1 in combination with antibiotics against pathogenic bacteria. Res Microbiol 163(6–7):479–486
    • (2012) Res Microbiol , vol.163 , Issue.6-7 , pp. 479-486
    • Choi, H.1    Lee, D.G.2
  • 36
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: automatic comparative molecular modelling of protein
    • COI: 1:CAS:528:DC%2BD38Xhs1eksrk%3D, PID: 11836238
    • Combet C, Jambon M, Deleage G, Geourjon C (2002) Geno3D: automatic comparative molecular modelling of protein. Bioinformatics 18(1):213–214
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deleage, G.3    Geourjon, C.4
  • 37
    • 84872111755 scopus 로고    scopus 로고
    • Structural and functional studies on a proline-rich peptide isolated from swine saliva endowed with antifungal activity towards Cryptococcus neoformans
    • COI: 1:CAS:528:DC%2BC3sXhs1Cgs74%3D, PID: 23274276
    • Conti S, Radicioni G, Ciociola T, Longhi R, Polonelli L, Gatti R, Cabras T, Messana I, Castagnola M, Vitali A (2013) Structural and functional studies on a proline-rich peptide isolated from swine saliva endowed with antifungal activity towards Cryptococcus neoformans. Biochim Biophys Acta 1828(3):1066–1074
    • (2013) Biochim Biophys Acta , vol.1828 , Issue.3 , pp. 1066-1074
    • Conti, S.1    Radicioni, G.2    Ciociola, T.3    Longhi, R.4    Polonelli, L.5    Gatti, R.6    Cabras, T.7    Messana, I.8    Castagnola, M.9    Vitali, A.10
  • 38
    • 84875451768 scopus 로고    scopus 로고
    • Bacterial expression and antibiotic activities of recombinant variants of human β-defensins on pathogenic bacteria and M. tuberculosis
    • COI: 1:CAS:528:DC%2BC3sXlvVCrtb8%3D, PID: 23459290
    • Corrales-Garcia L, Ortiz E, Castañeda-Delgado J, Rivas-Santiago B, Corzo G (2013) Bacterial expression and antibiotic activities of recombinant variants of human β-defensins on pathogenic bacteria and M. tuberculosis. Protein Expr Purif 89(1):33–43
    • (2013) Protein Expr Purif , vol.89 , Issue.1 , pp. 33-43
    • Corrales-Garcia, L.1    Ortiz, E.2    Castañeda-Delgado, J.3    Rivas-Santiago, B.4    Corzo, G.5
  • 39
    • 79952187401 scopus 로고    scopus 로고
    • Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces
    • COI: 1:CAS:528:DC%2BC3MXisFaiur4%3D, PID: 21056701
    • Costa F, Carvalho IF, Montelaro RC, Gomes P, Martins MCL (2011) Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces. Acta Biomater 7(4):1431–1440
    • (2011) Acta Biomater , vol.7 , Issue.4 , pp. 1431-1440
    • Costa, F.1    Carvalho, I.F.2    Montelaro, R.C.3    Gomes, P.4    Martins, M.C.L.5
  • 40
    • 80051596010 scopus 로고    scopus 로고
    • Nanovesicle encapsulation of antimicrobial peptide P34: physicochemical characterization and mode of action on Listeria monocytogenes
    • da Silva Malheiros P, Sant’Anna V, Micheletto YMS, da Silveira NP, Brandelli A (2011) Nanovesicle encapsulation of antimicrobial peptide P34: physicochemical characterization and mode of action on Listeria monocytogenes. J Nanoparticle Res 13(8):3545–3552
    • (2011) J Nanoparticle Res , vol.13 , Issue.8 , pp. 3545-3552
    • da Silva Malheiros, P.1    Sant’Anna, V.2    Micheletto, Y.M.S.3    da Silveira, N.P.4    Brandelli, A.5
  • 41
    • 22944435825 scopus 로고    scopus 로고
    • Antimicrobial peptides in the oral environment: expression and function in health and disease
    • COI: 1:CAS:528:DC%2BD2MXotFarurs%3D, PID: 16053246
    • Dale BA, Fredericks LP (2005) Antimicrobial peptides in the oral environment: expression and function in health and disease. Curr Issues Mol Biol 7(2):119–133
    • (2005) Curr Issues Mol Biol , vol.7 , Issue.2 , pp. 119-133
    • Dale, B.A.1    Fredericks, L.P.2
  • 42
    • 84862871084 scopus 로고    scopus 로고
    • Salivary concentration of the antimicrobial peptide LL-37 in children
    • COI: 1:CAS:528:DC%2BC38Xpt1Sitbs%3D, PID: 22336091
    • Davidopoulou S, Diza E, Menexes G, Kalfas S (2012) Salivary concentration of the antimicrobial peptide LL-37 in children. Arch Oral Biol 57(7):865–869
    • (2012) Arch Oral Biol , vol.57 , Issue.7 , pp. 865-869
    • Davidopoulou, S.1    Diza, E.2    Menexes, G.3    Kalfas, S.4
  • 43
  • 46
    • 77957837910 scopus 로고    scopus 로고
    • A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes
    • COI: 1:CAS:528:DC%2BC3cXht1OmtLvO, PID: 20705109
    • Dean R, O’Brien L, Thwaite J, Fox M, Atkins H, Ulaeto D (2010) A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes. Peptides 31(11):1966–1972
    • (2010) Peptides , vol.31 , Issue.11 , pp. 1966-1972
    • Dean, R.1    O’Brien, L.2    Thwaite, J.3    Fox, M.4    Atkins, H.5    Ulaeto, D.6
  • 47
    • 0035029214 scopus 로고    scopus 로고
    • ANTHEPROT: an integrated protein sequence analysis software with client/server capabilities
    • PID: 11334635
    • Deléage G, Combet C, Blanchet C, Geourjon C (2001) ANTHEPROT: an integrated protein sequence analysis software with client/server capabilities. Comput Biol Med 31(4):259–267
    • (2001) Comput Biol Med , vol.31 , Issue.4 , pp. 259-267
    • Deléage, G.1    Combet, C.2    Blanchet, C.3    Geourjon, C.4
  • 49
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • COI: 1:CAS:528:DC%2BD28XhtVanu7fF, PID: 16978580
    • Dhople V, Krukemeyer A, Ramamoorthy A (2006) The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim Biophys Acta 1758(9):1499–1512
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.9 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 50
    • 84908200723 scopus 로고    scopus 로고
    • Treatment of microbial biofilms in the post-antibiotic era: prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools
    • PID: 24515391
    • Di Luca M, Maccari G, Nifosi R (2014) Treatment of microbial biofilms in the post-antibiotic era: prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools. Pathog Dis 70(3):257–270
    • (2014) Pathog Dis , vol.70 , Issue.3 , pp. 257-270
    • Di Luca, M.1    Maccari, G.2    Nifosi, R.3
  • 51
    • 58149252357 scopus 로고    scopus 로고
    • Host defense peptides in the oral cavity and the lung: similarities and differences
    • COI: 1:CAS:528:DC%2BD1cXht1KqtrbM, PID: 18809744
    • Diamond G, Beckloff N, Ryan LK (2008) Host defense peptides in the oral cavity and the lung: similarities and differences. J Dent Res 87(10):915–927
    • (2008) J Dent Res , vol.87 , Issue.10 , pp. 915-927
    • Diamond, G.1    Beckloff, N.2    Ryan, L.K.3
  • 52
    • 84875974241 scopus 로고    scopus 로고
    • Bacterial membrane disrupting dodecapeptide SC4 improves survival of mice challenged with Pseudomonas aeruginosa
    • COI: 1:CAS:528:DC%2BC3sXmsFertbg%3D, PID: 23403135
    • Dings RPM, Haseman JR, Leslie DB, Luong M, Dunn DL, Mayo KH (2013) Bacterial membrane disrupting dodecapeptide SC4 improves survival of mice challenged with Pseudomonas aeruginosa. Biochim Biophys Acta 1830(6):3454–3457
    • (2013) Biochim Biophys Acta , vol.1830 , Issue.6 , pp. 3454-3457
    • Dings, R.P.M.1    Haseman, J.R.2    Leslie, D.B.3    Luong, M.4    Dunn, D.L.5    Mayo, K.H.6
  • 54
    • 27944433008 scopus 로고    scopus 로고
    • Protein semi-synthesis: new proteins for functional and structural studies
    • COI: 1:CAS:528:DC%2BD2MXht1GnurbJ, PID: 16188500
    • Durek T, Becker CFW (2005) Protein semi-synthesis: new proteins for functional and structural studies. Biomol Eng 22(5–6):153–172
    • (2005) Biomol Eng , vol.22 , Issue.5-6 , pp. 153-172
    • Durek, T.1    Becker, C.F.W.2
  • 55
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • PID: 16716248
    • Dürr UHN, Sudheendra US, Ramamoorthy A (2006) LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 1758(9):1408–1425
    • (2006) Biochim Biophys Acta , vol.1758 , Issue.9 , pp. 1408-1425
    • Dürr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 56
    • 84881368685 scopus 로고    scopus 로고
    • Solid phase synthesis of Smac/DIABLO-derived peptides using a ‘Safety-Catch’ resin: identification of potent XIAP BIR3 antagonists
    • COI: 1:CAS:528:DC%2BC3sXhtFCqtrfO, PID: 23886811
    • Elsawy MA, Martin L, Tikhonova IG, Walker B (2013) Solid phase synthesis of Smac/DIABLO-derived peptides using a ‘Safety-Catch’ resin: identification of potent XIAP BIR3 antagonists. Bioorg Med Chem 21(17):5004–5011
    • (2013) Bioorg Med Chem , vol.21 , Issue.17 , pp. 5004-5011
    • Elsawy, M.A.1    Martin, L.2    Tikhonova, I.G.3    Walker, B.4
  • 57
    • 84876552582 scopus 로고    scopus 로고
    • Release of antimicrobial peptides from electrospun nanofibres as a drug delivery system
    • COI: 1:CAS:528:DC%2BC3sXltlGqt74%3D, PID: 23621006
    • Eriksen TH, Skovsen E, Fojan P (2013) Release of antimicrobial peptides from electrospun nanofibres as a drug delivery system. J Biomed Nanotechnol 9(3):492–498
    • (2013) J Biomed Nanotechnol , vol.9 , Issue.3 , pp. 492-498
    • Eriksen, T.H.1    Skovsen, E.2    Fojan, P.3
  • 58
    • 69549105611 scopus 로고    scopus 로고
    • The role of molecular chaperones (HSPAs/HSP70s) in oral health and oral inflammatory diseases: a review
    • Fábián T, Gótai L, Beck A, Fejérdy P (2009) The role of molecular chaperones (HSPAs/HSP70s) in oral health and oral inflammatory diseases: a review. Eur J Inflamm 7:53–61
    • (2009) Eur J Inflamm , vol.7 , pp. 53-61
    • Fábián, T.1    Gótai, L.2    Beck, A.3    Fejérdy, P.4
  • 59
    • 84860204140 scopus 로고    scopus 로고
    • Salivary defense proteins: their network and role in innate and acquired oral immunity
    • PID: 22605979
    • Fábián TK, Hermann P, Beck A, Fejérdy P, Fábián G (2012) Salivary defense proteins: their network and role in innate and acquired oral immunity. Int J Mol Sci 13(4):4295–4320
    • (2012) Int J Mol Sci , vol.13 , Issue.4 , pp. 4295-4320
    • Fábián, T.K.1    Hermann, P.2    Beck, A.3    Fejérdy, P.4    Fábián, G.5
  • 60
    • 77449107565 scopus 로고    scopus 로고
    • Efficacy of hexapeptide-7 on menopausal skin
    • PID: 20120425
    • Falla TJ, Zhang L (2010) Efficacy of hexapeptide-7 on menopausal skin. J Drugs Dermatol 9(1):49–54
    • (2010) J Drugs Dermatol , vol.9 , Issue.1 , pp. 49-54
    • Falla, T.J.1    Zhang, L.2
  • 61
    • 84868530499 scopus 로고    scopus 로고
    • The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism
    • COI: 1:CAS:528:DC%2BC38XhsF2kur%2FL, PID: 23093307
    • Fernandez DI, Le Brun AP, Whitwell TC, Sani M-A, James M, Separovic F (2012) The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism. Phys Chem Chem Phys 14(45):15739–15751
    • (2012) Phys Chem Chem Phys , vol.14 , Issue.45 , pp. 15739-15751
    • Fernandez, D.I.1    Le Brun, A.P.2    Whitwell, T.C.3    Sani, M.-A.4    James, M.5    Separovic, F.6
  • 62
    • 84925465266 scopus 로고    scopus 로고
    • Fidelis K, Kryshtafovych A. Accessed 21 Feb 2014
    • Fidelis K, Kryshtafovych A (2014) Protein Structure Prediction Center. http://predictioncenter.org/. Accessed 21 Feb 2014
    • (2014) Protein Structure Prediction Center
  • 63
    • 34249858459 scopus 로고    scopus 로고
    • AMPer: a database and an automated discovery tool for antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD2sXmtVKqu7w%3D, PID: 17341497
    • Fjell CD, Hancock REW, Cherkasov A (2007) AMPer: a database and an automated discovery tool for antimicrobial peptides. Bioinformatics 23(9):1148–1155
    • (2007) Bioinformatics , vol.23 , Issue.9 , pp. 1148-1155
    • Fjell, C.D.1    Hancock, R.E.W.2    Cherkasov, A.3
  • 65
    • 84857046993 scopus 로고    scopus 로고
    • The development of Byetta (exenatide) from the venom of the Gila monster as an anti-diabetic agent
    • COI: 1:CAS:528:DC%2BC38XisVGltbY%3D, PID: 21194543
    • Furman BL (2012) The development of Byetta (exenatide) from the venom of the Gila monster as an anti-diabetic agent. Toxicon 59(4):464–471
    • (2012) Toxicon , vol.59 , Issue.4 , pp. 464-471
    • Furman, B.L.1
  • 66
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • COI: 1:CAS:528:DC%2BD3sXmvVWmtLc%3D, PID: 12949495
    • Ganz T (2003) Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 3(9):710–720
    • (2003) Nat Rev Immunol , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 67
    • 78650153738 scopus 로고    scopus 로고
    • Musite, a tool for global prediction of general and kinase-specific phosphorylation sites
    • COI: 1:CAS:528:DC%2BC3MXhs12rsg%3D%3D, PID: 20702892
    • Gao J, Thelen JJ, Dunker AK, Xu D (2010) Musite, a tool for global prediction of general and kinase-specific phosphorylation sites. Mol Cell Proteomics 9(12):2586–2600
    • (2010) Mol Cell Proteomics , vol.9 , Issue.12 , pp. 2586-2600
    • Gao, J.1    Thelen, J.J.2    Dunker, A.K.3    Xu, D.4
  • 69
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server. The proteomics protocols handbook
    • Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD, Bairoch A (2005) Protein identification and analysis tools on the ExPASy server. The proteomics protocols handbook. Springer, pp 571-607
    • (2005) Springer , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2    Gattiker, A.3    Wilkins, M.R.4    Appel, R.D.5    Bairoch, A.6
  • 70
    • 79952818106 scopus 로고    scopus 로고
    • Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis
    • COI: 1:CAS:528:DC%2BC3MXjsFOjt7Y%3D, PID: 21262297
    • Gauri SS, Mandal SM, Pati BR, Dey S (2011) Purification and structural characterization of a novel antibacterial peptide from Bellamya bengalensis: activity against ampicillin and chloramphenicol resistant Staphylococcus epidermidis. Peptides 32(4):691–696
    • (2011) Peptides , vol.32 , Issue.4 , pp. 691-696
    • Gauri, S.S.1    Mandal, S.M.2    Pati, B.R.3    Dey, S.4
  • 71
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • COI: 1:CAS:528:DyaK28XjtFOgtL4%3D, PID: 8637016
    • Gazit E, Miller IR, Biggin PC, Sansom MS, Shai Y (1996) Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J Mol Biol 258(5):860–870
    • (1996) J Mol Biol , vol.258 , Issue.5 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.4    Shai, Y.5
  • 72
    • 34547566008 scopus 로고    scopus 로고
    • Toward rational protein crystallization: a Web server for the design of crystallizable protein variants
    • COI: 1:CAS:528:DC%2BD2sXos12qtrs%3D, PID: 17656576
    • Goldschmidt L, Cooper DR, Derewenda ZS, Eisenberg D (2007) Toward rational protein crystallization: a Web server for the design of crystallizable protein variants. Protein Sci 16(8):1569–1576
    • (2007) Protein Sci , vol.16 , Issue.8 , pp. 1569-1576
    • Goldschmidt, L.1    Cooper, D.R.2    Derewenda, Z.S.3    Eisenberg, D.4
  • 73
    • 84868020147 scopus 로고    scopus 로고
    • Peptides as therapeutics with enhanced bioactivity
    • COI: 1:CAS:528:DC%2BC3sXhtlens74%3D, PID: 22830348
    • Goodwin D, Simerska P, Toth I (2012) Peptides as therapeutics with enhanced bioactivity. Curr Med Chem 19(26):4451–4461
    • (2012) Curr Med Chem , vol.19 , Issue.26 , pp. 4451-4461
    • Goodwin, D.1    Simerska, P.2    Toth, I.3
  • 74
    • 58149515937 scopus 로고    scopus 로고
    • Acyclic and cyclic thioenamino peptides: solution- and solid-phase synthesis
    • COI: 1:CAS:528:DC%2BD1MXpsVWhsg%3D%3D
    • Goren L, Pappo D, Goldberg I, Kashman Y (2009) Acyclic and cyclic thioenamino peptides: solution- and solid-phase synthesis. Tetrahedron Lett 50(9):1048–1050
    • (2009) Tetrahedron Lett , vol.50 , Issue.9 , pp. 1048-1050
    • Goren, L.1    Pappo, D.2    Goldberg, I.3    Kashman, Y.4
  • 75
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • PID: 19878474
    • Gorr S-U (2009) Antimicrobial peptides of the oral cavity. Periodontol 2000 51(1):152–180
    • (2009) Periodontol 2000 , vol.51 , Issue.1 , pp. 152-180
    • Gorr, S.-U.1
  • 76
    • 84855522617 scopus 로고    scopus 로고
    • Antimicrobial peptides in periodontal innate defense
    • PID: 22142958
    • Gorr S-U (2011) Antimicrobial peptides in periodontal innate defense. Front Oral Biol 15:84–98
    • (2011) Front Oral Biol , vol.15 , pp. 84-98
    • Gorr, S.-U.1
  • 77
    • 84873633825 scopus 로고    scopus 로고
    • 2012 in review—part I: the year’s new drugs & biologics
    • COI: 1:STN:280:DC%2BC3szjs12rsw%3D%3D
    • Graul AI, Lupone B, Cruces E, Stringer M (2013) 2012 in review—part I: the year’s new drugs & biologics. Drugs Today (Barc) 49(1):33–68
    • (2013) Drugs Today (Barc) , vol.49 , Issue.1 , pp. 33-68
    • Graul, A.I.1    Lupone, B.2    Cruces, E.3    Stringer, M.4
  • 78
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: general overview and clinical implications in human health and disease
    • PID: 20116332
    • Guaní-Guerra E, Santos-Mendoza T, Lugo-Reyes SO, Terán LM (2010) Antimicrobial peptides: general overview and clinical implications in human health and disease. Clin Immunol 135(1):1–11
    • (2010) Clin Immunol , vol.135 , Issue.1 , pp. 1-11
    • Guaní-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Terán, L.M.4
  • 80
    • 84892170602 scopus 로고    scopus 로고
    • Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance
    • Guilhelmelli F, Vilela N, Albuquerque P, Derengowski LD, Silva-Pereira I, Kyaw CM (2013) Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front Microbiol 9(4):353
    • (2013) Front Microbiol , vol.9 , Issue.4 , pp. 353
    • Guilhelmelli, F.1    Vilela, N.2    Albuquerque, P.3    Derengowski, L.D.4    Silva-Pereira, I.5    Kyaw, C.M.6
  • 81
    • 0035951376 scopus 로고    scopus 로고
    • Salivary histatin 5 is a potent competitive inhibitor of the cysteine proteinase clostripain
    • COI: 1:CAS:528:DC%2BD3MXhsFSht74%3D, PID: 11231021
    • Gusman H, Grogan J, Kagan HM, Troxler RF, Oppenheim FG (2001) Salivary histatin 5 is a potent competitive inhibitor of the cysteine proteinase clostripain. FEBS Lett 489(1):97–100
    • (2001) FEBS Lett , vol.489 , Issue.1 , pp. 97-100
    • Gusman, H.1    Grogan, J.2    Kagan, H.M.3    Troxler, R.F.4    Oppenheim, F.G.5
  • 83
    • 84925478419 scopus 로고    scopus 로고
    • Habib-Valdhorn S (2013) Credit Suisse: Copaxone sales to plunge 90%.Globes Online
    • Habib-Valdhorn S (2013) Credit Suisse: Copaxone sales to plunge 90%.Globes Online
  • 84
    • 77954313195 scopus 로고    scopus 로고
    • Current trends in antimicrobial agent research: chemo- and bioinformatics approaches
    • COI: 1:CAS:528:DC%2BC3cXosVKjurY%3D, PID: 20546918
    • Hammami R, Fliss I (2010) Current trends in antimicrobial agent research: chemo- and bioinformatics approaches. Drug Discov Today 15(13–14):540–546
    • (2010) Drug Discov Today , vol.15 , Issue.13-14 , pp. 540-546
    • Hammami, R.1    Fliss, I.2
  • 86
    • 58149200923 scopus 로고    scopus 로고
    • PhytAMP: a database dedicated to antimicrobial plant peptides
    • COI: 1:CAS:528:DC%2BD1cXhsFejtb3M, PID: 18836196
    • Hammami R, Ben Hamida J, Vergoten G, Fliss I (2009) PhytAMP: a database dedicated to antimicrobial plant peptides. Nucleic Acids Res 37:D963–D968
    • (2009) Nucleic Acids Res , vol.37 , pp. 963-968
    • Hammami, R.1    Ben Hamida, J.2    Vergoten, G.3    Fliss, I.4
  • 87
    • 77249117208 scopus 로고    scopus 로고
    • BACTIBASE second release: a database and tool platform for bacteriocin characterization
    • Hammami R, Zouhir A, Le Lay C, Ben Hamida J, Fliss I (2010) BACTIBASE second release: a database and tool platform for bacteriocin characterization. BMC Microbiol 27(10):22
    • (2010) BMC Microbiol , vol.27 , Issue.10 , pp. 22
    • Hammami, R.1    Zouhir, A.2    Le Lay, C.3    Ben Hamida, J.4    Fliss, I.5
  • 88
    • 0033042432 scopus 로고    scopus 로고
    • Peptide antibiotics
    • COI: 1:CAS:528:DyaK1MXjs12nsrc%3D
    • Hancock RE, Chapple DS (1999) Peptide antibiotics. Antimicrob Agents Ch 43(6):1317–1323
    • (1999) Antimicrob Agents Ch , vol.43 , Issue.6 , pp. 1317-1323
    • Hancock, R.E.1    Chapple, D.S.2
  • 89
    • 84881296268 scopus 로고    scopus 로고
    • Development of antimicrobial packaging materials with immobilized glucose oxidase and lysozyme
    • Hanušová K, Vápenka L, Dobiáš J, Mišková L (2013) Development of antimicrobial packaging materials with immobilized glucose oxidase and lysozyme. Cent Eur J Chem 11(7):1066–1078
    • (2013) Cent Eur J Chem , vol.11 , Issue.7 , pp. 1066-1078
    • Hanušová, K.1    Vápenka, L.2    Dobiáš, J.3    Mišková, L.4
  • 90
    • 65649114368 scopus 로고    scopus 로고
    • Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface
    • COI: 1:CAS:528:DC%2BD1MXkvFGms7o%3D, PID: 19332808
    • Harris M, Mora-Montes HM, Gow NA, Coote PJ (2009) Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface. Microbiology 155(4):1058–1070
    • (2009) Microbiology , vol.155 , Issue.4 , pp. 1058-1070
    • Harris, M.1    Mora-Montes, H.M.2    Gow, N.A.3    Coote, P.J.4
  • 91
    • 84866290009 scopus 로고    scopus 로고
    • Natural antimicrobial peptides from bacteria: characteristics and potential applications to fight against antibiotic resistance
    • COI: 1:CAS:528:DC%2BC38XhtlehsbnF, PID: 22583565
    • Hassan M, Kjos M, Nes IF, Diep DB, Lotfipour F (2012) Natural antimicrobial peptides from bacteria: characteristics and potential applications to fight against antibiotic resistance. J Appl Microbiol 113(4):723–736
    • (2012) J Appl Microbiol , vol.113 , Issue.4 , pp. 723-736
    • Hassan, M.1    Kjos, M.2    Nes, I.F.3    Diep, D.B.4    Lotfipour, F.5
  • 92
    • 46649110555 scopus 로고    scopus 로고
    • Antimicrobial peptides, skin infections and atopic dermatitis. In: Seminars in cutaneous medicine and surgery. Vol 27. NIH Public Access
    • Hata TR, Gallo RL (2008) Antimicrobial peptides, skin infections and atopic dermatitis. In: Seminars in cutaneous medicine and surgery. Vol 27. NIH Public Access, p 144
    • (2008) p 144
    • Hata, T.R.1    Gallo, R.L.2
  • 93
    • 38549127781 scopus 로고    scopus 로고
    • PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor
    • COI: 1:CAS:528:DC%2BD1cXhtVSkurk%3D, PID: 17984086
    • Heazlewood JL, Durek P, Hummel J, Selbig J, Weckwerth W, Walther D, Schulze WX (2008) PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor. Nucleic Acids Res 36(suppl 1):D1015–D1021
    • (2008) Nucleic Acids Res , vol.36 , pp. 1015-1021
    • Heazlewood, J.L.1    Durek, P.2    Hummel, J.3    Selbig, J.4    Weckwerth, W.5    Walther, D.6    Schulze, W.X.7
  • 94
    • 4844229791 scopus 로고    scopus 로고
    • Congenital dyserythropoietic anemias: epidemiology, clinical significance, and progress in understanding their pathogenesis
    • PID: 15278299
    • Heimpel H (2004) Congenital dyserythropoietic anemias: epidemiology, clinical significance, and progress in understanding their pathogenesis. Ann Hematol 83(10):613–621
    • (2004) Ann Hematol , vol.83 , Issue.10 , pp. 613-621
    • Heimpel, H.1
  • 95
    • 79959865281 scopus 로고    scopus 로고
    • Fragment condensation of C‐terminal pseudoproline peptides without racemization on the solid phase
    • COI: 1:CAS:528:DC%2BC3MXmvFahsr0%3D, PID: 21630399
    • Heinlein C, Varón Silva D, Tröster A, Schmidt J, Gross A, Unverzagt C (2011) Fragment condensation of C‐terminal pseudoproline peptides without racemization on the solid phase. Angew Chem Int Ed Engl 50(28):6406–6410
    • (2011) Angew Chem Int Ed Engl , vol.50 , Issue.28 , pp. 6406-6410
    • Heinlein, C.1    Varón Silva, D.2    Tröster, A.3    Schmidt, J.4    Gross, A.5    Unverzagt, C.6
  • 97
    • 77957359728 scopus 로고    scopus 로고
    • Mass spectrometric identification of key proteolytic cleavage sites in statherin affecting mineral homeostasis and bacterial binding domains
    • COI: 1:CAS:528:DC%2BC3cXhtFGrtbfE, PID: 20731414
    • Helmerhorst EJ, Traboulsi G, Salih E, Oppenheim FG (2010) Mass spectrometric identification of key proteolytic cleavage sites in statherin affecting mineral homeostasis and bacterial binding domains. J Proteome Res 9(10):5413–5421
    • (2010) J Proteome Res , vol.9 , Issue.10 , pp. 5413-5421
    • Helmerhorst, E.J.1    Traboulsi, G.2    Salih, E.3    Oppenheim, F.G.4
  • 98
    • 84892616326 scopus 로고    scopus 로고
    • Implications of salivary protein binding to commensal and pathogenic bacteria
    • COI: 1:CAS:528:DC%2BC2cXit12ltbk%3D, PID: 24707190
    • Heo S-M, Ruhl S, Scannapieco FA (2013) Implications of salivary protein binding to commensal and pathogenic bacteria. J Oral Biosci 55(4):169–174
    • (2013) J Oral Biosci , vol.55 , Issue.4 , pp. 169-174
    • Heo, S.-M.1    Ruhl, S.2    Scannapieco, F.A.3
  • 99
    • 79952815718 scopus 로고    scopus 로고
    • Optimized grafting of antimicrobial peptides on stainless steel surface and biofilm resistance tests
    • PID: 21310597
    • Héquet A, Humblot V, Berjeaud J-M, Pradier C-M (2011) Optimized grafting of antimicrobial peptides on stainless steel surface and biofilm resistance tests. Colloids Surf B: Biointerfaces 84(2):301–309
    • (2011) Colloids Surf B: Biointerfaces , vol.84 , Issue.2 , pp. 301-309
    • Héquet, A.1    Humblot, V.2    Berjeaud, J.-M.3    Pradier, C.-M.4
  • 100
    • 34547629994 scopus 로고    scopus 로고
    • Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci
    • PID: 17676995
    • Herbert S, Bera A, Nerz C, Kraus D, Peschel A, Goerke C, Meehl M, Cheung A, Gotz F (2007) Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog 3(7):e102
    • (2007) PLoS Pathog , vol.3 , Issue.7 , pp. 102
    • Herbert, S.1    Bera, A.2    Nerz, C.3    Kraus, D.4    Peschel, A.5    Goerke, C.6    Meehl, M.7    Cheung, A.8    Gotz, F.9
  • 101
    • 0000617857 scopus 로고
    • Phagocytin—a bactericidal substance from polymorphonuclear leucocytes
    • COI: 1:CAS:528:DyaG28Xot12jsA%3D%3D, PID: 13319580
    • Hirsch JG (1956) Phagocytin—a bactericidal substance from polymorphonuclear leucocytes. J Exp Med 103(5):589–611
    • (1956) J Exp Med , vol.103 , Issue.5 , pp. 589-611
    • Hirsch, J.G.1
  • 102
    • 0842332277 scopus 로고    scopus 로고
    • Solid-phase peptide synthesis in water. Part 3: a water-soluble N-protecting group, 2-[phenyl (methyl) sulfonio] ethoxycarbonyl tetrafluoroborate, and its application to solid phase peptide synthesis in water
    • COI: 1:CAS:528:DC%2BD2cXpvFCmtA%3D%3D
    • Hojo K, Maeda M, Kawasaki K (2004) Solid-phase peptide synthesis in water. Part 3: a water-soluble N-protecting group, 2-[phenyl (methyl) sulfonio] ethoxycarbonyl tetrafluoroborate, and its application to solid phase peptide synthesis in water. Tetrahedron 60(8):1875–1886
    • (2004) Tetrahedron , vol.60 , Issue.8 , pp. 1875-1886
    • Hojo, K.1    Maeda, M.2    Kawasaki, K.3
  • 103
    • 79958803250 scopus 로고    scopus 로고
    • Peptide synthesis ‘in water’ by a solution-phase method using water-dispersible nanoparticle Boc-amino acid
    • COI: 1:CAS:528:DC%2BC3MXntlOqtbc%3D, PID: 21495120
    • Hojo K, Ichikawa H, Onishi M, Fukumori Y, Kawasaki K (2011) Peptide synthesis ‘in water’ by a solution-phase method using water-dispersible nanoparticle Boc-amino acid. J Pept Sci 17(7):487–492
    • (2011) J Pept Sci , vol.17 , Issue.7 , pp. 487-492
    • Hojo, K.1    Ichikawa, H.2    Onishi, M.3    Fukumori, Y.4    Kawasaki, K.5
  • 104
    • 78650678043 scopus 로고    scopus 로고
    • Potent antimicrobial action of triclosan–lysozyme complex against skin pathogens mediated through drug-targeted delivery mechanism
    • COI: 1:CAS:528:DC%2BC3cXhs1agtLnM, PID: 21078387
    • Hoq MI, Ibrahim HR (2011) Potent antimicrobial action of triclosan–lysozyme complex against skin pathogens mediated through drug-targeted delivery mechanism. Eur J Pharm Sci 42(1–2):130–137
    • (2011) Eur J Pharm Sci , vol.42 , Issue.1-2 , pp. 130-137
    • Hoq, M.I.1    Ibrahim, H.R.2
  • 105
    • 84890588697 scopus 로고    scopus 로고
    • Dispersion state and fiber toughness: antibacterial lysozyme-single walled carbon nanotubes
    • COI: 1:CAS:528:DC%2BC3sXhtVOisrrO
    • Horn DW, Ao G, Maugey M, Zakri C, Poulin P, Davis VA (2013) Dispersion state and fiber toughness: antibacterial lysozyme-single walled carbon nanotubes. Adv Funct Mater 23(48):6082–6090
    • (2013) Adv Funct Mater , vol.23 , Issue.48 , pp. 6082-6090
    • Horn, D.W.1    Ao, G.2    Maugey, M.3    Zakri, C.4    Poulin, P.5    Davis, V.A.6
  • 107
    • 84863414476 scopus 로고    scopus 로고
    • A spectral algorithm for learning hidden Markov models
    • Hsu D, Kakade SM, Zhang T (2012) A spectral algorithm for learning hidden Markov models. J Comp Syst Sci 78(5):1460–1480
    • (2012) J Comp Syst Sci , vol.78 , Issue.5 , pp. 1460-1480
    • Hsu, D.1    Kakade, S.M.2    Zhang, T.3
  • 108
    • 14544293955 scopus 로고    scopus 로고
    • The interactions of antimicrobial peptides derived from lysozyme with model membrane systems
    • COI: 1:CAS:528:DC%2BD2MXhvVSlu7o%3D, PID: 15737328
    • Hunter HN, Jing W, Schibli DJ, Trinh T, Park IY, Kim SC, Vogel HJ (2005) The interactions of antimicrobial peptides derived from lysozyme with model membrane systems. Biochim Biophys Acta 1668(2):175–189
    • (2005) Biochim Biophys Acta , vol.1668 , Issue.2 , pp. 175-189
    • Hunter, H.N.1    Jing, W.2    Schibli, D.J.3    Trinh, T.4    Park, I.Y.5    Kim, S.C.6    Vogel, H.J.7
  • 109
    • 80051550004 scopus 로고    scopus 로고
    • Antimicrobial and DNA-binding activities of the peptide fragments of human lactoferrin and histatin 5 against Streptococcus mutans
    • COI: 1:CAS:528:DC%2BC3MXpvFCgsb4%3D, PID: 21382611
    • Huo L, Zhang K, Ling J, Peng Z, Huang X, Liu H, Gu L (2011) Antimicrobial and DNA-binding activities of the peptide fragments of human lactoferrin and histatin 5 against Streptococcus mutans. Arch Oral Biol 56(9):869–876
    • (2011) Arch Oral Biol , vol.56 , Issue.9 , pp. 869-876
    • Huo, L.1    Zhang, K.2    Ling, J.3    Peng, Z.4    Huang, X.5    Liu, H.6    Gu, L.7
  • 110
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • COI: 1:STN:280:DC%2BD3MnnvVCruw%3D%3D, PID: 11560930
    • Ibrahim HR, Thomas U, Pellegrini A (2001) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J Biol Chem 276(47):43767–43774
    • (2001) J Biol Chem , vol.276 , Issue.47 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 111
    • 84896712019 scopus 로고    scopus 로고
    • Salivary histatin 3 inhibits heat shock cognate protein 70-mediated inflammatory cytokine production through toll-like receptors in human gingival fibroblasts
    • Imamura Y, Wang PL (2014) Salivary histatin 3 inhibits heat shock cognate protein 70-mediated inflammatory cytokine production through toll-like receptors in human gingival fibroblasts. J Inflamm (Lond) 11(1):4
    • (2014) J Inflamm (Lond) , vol.11 , Issue.1 , pp. 4
    • Imamura, Y.1    Wang, P.L.2
  • 113
    • 33746532309 scopus 로고    scopus 로고
    • Peptide antimicrobial agents
    • COI: 1:CAS:528:DC%2BD28XosVaqsrk%3D, PID: 16847082
    • Jenssen H, Hamill P, Hancock REW (2006) Peptide antimicrobial agents. Clin Microbiol Rev 19(3):491–511
    • (2006) Clin Microbiol Rev , vol.19 , Issue.3 , pp. 491-511
    • Jenssen, H.1    Hamill, P.2    Hancock, R.E.W.3
  • 114
    • 79952614254 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, ‘specificity determinants’, total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio
    • PID: 21219588
    • Jiang Z, Vasil AI, Gera L, Vasil ML, Hodges RS (2011) Rational design of α-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, ‘specificity determinants’, total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio. Chem Biol Drug Des 77(4):225–240
    • (2011) Chem Biol Drug Des , vol.77 , Issue.4 , pp. 225-240
    • Jiang, Z.1    Vasil, A.I.2    Gera, L.3    Vasil, M.L.4    Hodges, R.S.5
  • 115
    • 84858307872 scopus 로고    scopus 로고
    • The design and construction of K11: a novel α-helical antimicrobial peptide
    • PID: 22518150
    • Jin-Jiang H, Jin-Chun L, Min L, Qing-Shan H, Guo-Dong L (2012) The design and construction of K11: a novel α-helical antimicrobial peptide. Int J Microbiol 2012:764834
    • (2012) Int J Microbiol , vol.2012 , pp. 764834
    • Jin-Jiang, H.1    Jin-Chun, L.2    Min, L.3    Qing-Shan, H.4    Guo-Dong, L.5
  • 117
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction—the Phobius web server
    • PID: 17483518
    • Käll L, Krogh A, Sonnhammer ELL (2007) Advantages of combined transmembrane topology and signal peptide prediction—the Phobius web server. Nucleic Acids Res 35(2):W429–W432
    • (2007) Nucleic Acids Res , vol.35 , Issue.2 , pp. 429-432
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 118
    • 84883256420 scopus 로고    scopus 로고
    • Future directions for peptide therapeutics development
    • COI: 1:CAS:528:DC%2BC3sXpsV2ksbs%3D, PID: 23726889
    • Kaspar AA, Reichert JM (2013) Future directions for peptide therapeutics development. Drug Discov Today 18(17–18):807–817
    • (2013) Drug Discov Today , vol.18 , Issue.17-18 , pp. 807-817
    • Kaspar, A.A.1    Reichert, J.M.2
  • 119
    • 1642267482 scopus 로고    scopus 로고
    • Histatins: antimicrobial peptides with therapeutic potential
    • COI: 1:CAS:528:DC%2BD2cXjt1Ors7Y%3D, PID: 15025852
    • Kavanagh K, Dowd S (2004) Histatins: antimicrobial peptides with therapeutic potential. J Pharm Pharmacol 56(3):285–289
    • (2004) J Pharm Pharmacol , vol.56 , Issue.3 , pp. 285-289
    • Kavanagh, K.1    Dowd, S.2
  • 120
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • COI: 1:CAS:528:DyaK3cXkvFCgtr4%3D, PID: 2370661
    • Kneller DG, Cohen FE, Langridge R (1990) Improvements in protein secondary structure prediction by an enhanced neural network. J Mol Biol 214(1):171–182
    • (1990) J Mol Biol , vol.214 , Issue.1 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 121
    • 84890427506 scopus 로고    scopus 로고
    • Cheminformatics at the interface of medicinal chemistry and proteomics
    • COI: 1:CAS:528:DC%2BC3sXptFKnt7Y%3D, PID: 23707564
    • Koch U, Hamacher M, Nussbaumer P (2014) Cheminformatics at the interface of medicinal chemistry and proteomics. Biochim Biophys Acta 1844(1, Part A):156–161
    • (2014) Biochim Biophys Acta , vol.1844 , Issue.1 , pp. 156-161
    • Koch, U.1    Hamacher, M.2    Nussbaumer, P.3
  • 122
    • 0034491241 scopus 로고    scopus 로고
    • The effect of statherin and its shortened analogues on anaerobic bacteria isolated from the oral cavity
    • Kochańska B, Kedzia A, Kamysz W, Maćkiewicz Z, Kupryszewski G (1999) The effect of statherin and its shortened analogues on anaerobic bacteria isolated from the oral cavity. Acta Microbiol Pol 49(3–4):243–251
    • (1999) Acta Microbiol Pol , vol.49 , Issue.3-4 , pp. 243-251
    • Kochańska, B.1    Kedzia, A.2    Kamysz, W.3    Maćkiewicz, Z.4    Kupryszewski, G.5
  • 125
    • 0842328805 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 activates murine natural interferon-producing cells through toll-like receptor 9
    • COI: 1:CAS:528:DC%2BD2cXhsVSlurw%3D, PID: 14563635
    • Krug A, Luker GD, Barchet W, Leib DA, Akira S, Colonna M (2004) Herpes simplex virus type 1 activates murine natural interferon-producing cells through toll-like receptor 9. Blood 103(4):1433–1437
    • (2004) Blood , vol.103 , Issue.4 , pp. 1433-1437
    • Krug, A.1    Luker, G.D.2    Barchet, W.3    Leib, D.A.4    Akira, S.5    Colonna, M.6
  • 126
    • 84885340770 scopus 로고    scopus 로고
    • BaCoCa—a heuristic software tool for the parallel assessment of sequence biases in hundreds of gene and taxon partitions
    • PID: 24076250
    • Kück P, Struck TH (2014) BaCoCa—a heuristic software tool for the parallel assessment of sequence biases in hundreds of gene and taxon partitions. Mol Phylogenet Evol 70:94–98
    • (2014) Mol Phylogenet Evol , vol.70 , pp. 94-98
    • Kück, P.1    Struck, T.H.2
  • 127
    • 0027284291 scopus 로고
    • Structural features of salivary function
    • COI: 1:STN:280:DyaK3szosFekuw%3D%3D, PID: 8373982
    • Lamkin MS, Oppenheim FG (1993) Structural features of salivary function. Crit Rev Oral Biol Med 4(3):251–259
    • (1993) Crit Rev Oral Biol Med , vol.4 , Issue.3 , pp. 251-259
    • Lamkin, M.S.1    Oppenheim, F.G.2
  • 128
    • 35448929949 scopus 로고    scopus 로고
    • Analysis and prediction of antibacterial peptides
    • Lata S, Sharma B, Raghava G (2007) Analysis and prediction of antibacterial peptides. BMC Bioinforma 8(1):263
    • (2007) BMC Bioinforma , vol.8 , Issue.1 , pp. 263
    • Lata, S.1    Sharma, B.2    Raghava, G.3
  • 130
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • COI: 1:CAS:528:DC%2BD2MXksFyqsLk%3D, PID: 15911882
    • Lee S, Jilani SM, Nikolova GV, Carpizo D, Iruela-Arispe ML (2005) Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J Cell Biol 169(4):681–691
    • (2005) J Cell Biol , vol.169 , Issue.4 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3    Carpizo, D.4    Iruela-Arispe, M.L.5
  • 131
    • 34447093904 scopus 로고    scopus 로고
    • N-Nosyl-α-amino acids in solution phase peptide synthesis
    • COI: 1:CAS:528:DC%2BD2sXnslKmt7c%3D
    • Leggio A, Di Gioia ML, Perri F, Liguori A (2007) N-Nosyl-α-amino acids in solution phase peptide synthesis. Tetrahedron 63(34):8164–8173
    • (2007) Tetrahedron , vol.63 , Issue.34 , pp. 8164-8173
    • Leggio, A.1    Di Gioia, M.L.2    Perri, F.3    Liguori, A.4
  • 132
    • 47949084527 scopus 로고    scopus 로고
    • Ecallantide (DX-88), a plasma kallikrein inhibitor for the treatment of hereditary angioedema and the prevention of blood loss in on-pump cardiothoracic surgery
    • COI: 1:CAS:528:DC%2BD1cXos1Chtr8%3D, PID: 18613770
    • Lehmann A (2008) Ecallantide (DX-88), a plasma kallikrein inhibitor for the treatment of hereditary angioedema and the prevention of blood loss in on-pump cardiothoracic surgery. Expert Opin Biol Ther 8(8):1187–1199
    • (2008) Expert Opin Biol Ther , vol.8 , Issue.8 , pp. 1187-1199
    • Lehmann, A.1
  • 133
    • 85018150491 scopus 로고    scopus 로고
    • Evolution of antimicrobial peptides: a view from the cystine chapel antimicrobial peptides and innate immunity
    • Lehrer RI (2013) Evolution of antimicrobial peptides: a view from the cystine chapel antimicrobial peptides and innate immunity. Springer, pp 1-27
    • (2013) Springer , pp. 1-27
    • Lehrer, R.I.1
  • 134
    • 80054062747 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in Escherichia coli: a review
    • COI: 1:CAS:528:DC%2BC3MXhtlejtLvI, PID: 21843642
    • Li Y (2011) Recombinant production of antimicrobial peptides in Escherichia coli: a review. Protein Expr Purif 80(2):260–267
    • (2011) Protein Expr Purif , vol.80 , Issue.2 , pp. 260-267
    • Li, Y.1
  • 135
    • 56649106249 scopus 로고    scopus 로고
    • RAPD: a database of recombinantly-produced antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD1cXhsFWgsLfI, PID: 19054102
    • Li Y, Chen Z (2008) RAPD: a database of recombinantly-produced antimicrobial peptides. FEMS Microbiol Lett 289(2):126–129
    • (2008) FEMS Microbiol Lett , vol.289 , Issue.2 , pp. 126-129
    • Li, Y.1    Chen, Z.2
  • 136
    • 0033855722 scopus 로고    scopus 로고
    • Possible release of an ArgGlyArgProGln pentapeptide with innate immunity properties from acidic proline-rich proteins by proteolytic activity in commensal Streptococcus and Actinomyces species
    • COI: 1:CAS:528:DC%2BD3cXmtVektL8%3D, PID: 10948176
    • Li T, Bratt P, Jonsson AP, Ryberg M, Johansson I, Griffiths WJ, Bergman T, Strömberg N (2000) Possible release of an ArgGlyArgProGln pentapeptide with innate immunity properties from acidic proline-rich proteins by proteolytic activity in commensal Streptococcus and Actinomyces species. Infect Immun 68(9):5425–5429
    • (2000) Infect Immun , vol.68 , Issue.9 , pp. 5425-5429
    • Li, T.1    Bratt, P.2    Jonsson, A.P.3    Ryberg, M.4    Johansson, I.5    Griffiths, W.J.6    Bergman, T.7    Strömberg, N.8
  • 137
    • 83455173437 scopus 로고    scopus 로고
    • Antimicrobial lysozyme-containing starch microgel to target and inhibit amylase-producing microorganisms
    • COI: 1:CAS:528:DC%2BC38XhsFKjsL8%3D
    • Li Y, Kadam S, Abee T, Slaghek TM, Timmermans JW, Cohen Stuart MA, Norde W, Kleijn MJ (2012) Antimicrobial lysozyme-containing starch microgel to target and inhibit amylase-producing microorganisms. Food Hydrocoll 28(1):28–35
    • (2012) Food Hydrocoll , vol.28 , Issue.1 , pp. 28-35
    • Li, Y.1    Kadam, S.2    Abee, T.3    Slaghek, T.M.4    Timmermans, J.W.5    Cohen Stuart, M.A.6    Norde, W.7    Kleijn, M.J.8
  • 139
    • 0022886732 scopus 로고
    • In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes
    • COI: 1:CAS:528:DyaL2sXkvVGjsA%3D%3D, PID: 3779104
    • Lichtenstein A, Ganz T, Selsted ME, Lehrer RI (1986) In vitro tumor cell cytolysis mediated by peptide defensins of human and rabbit granulocytes. Blood 68(6):1407–1410
    • (1986) Blood , vol.68 , Issue.6 , pp. 1407-1410
    • Lichtenstein, A.1    Ganz, T.2    Selsted, M.E.3    Lehrer, R.I.4
  • 140
    • 84856962893 scopus 로고    scopus 로고
    • The use of plants for the production of therapeutic human peptides
    • COI: 1:CAS:528:DC%2BC38XitFamurY%3D, PID: 22218674
    • Lico C, Santi L, Twyman R, Pezzotti M, Avesani L (2012) The use of plants for the production of therapeutic human peptides. Plant Cell Rep 31(3):439–451
    • (2012) Plant Cell Rep , vol.31 , Issue.3 , pp. 439-451
    • Lico, C.1    Santi, L.2    Twyman, R.3    Pezzotti, M.4    Avesani, L.5
  • 143
    • 84925478417 scopus 로고    scopus 로고
    • Lupron Worldwide Sales
    • Lupron Worldwide Sales (2011a) http://www.evaluategroup.com/Universal/View.aspx?type=Entity&entityType=Product&id=21572&lType=modData&componentID=1002.
    • (2011)
  • 144
    • 84894634969 scopus 로고    scopus 로고
    • Ma T, Liu Y, Dai Q, Yao Y, He P-a (in press) A graphical representation of protein based on a novel iterated function system. Physica A: Statistical Mechanics and its Applications(0)
    • Ma T, Liu Y, Dai Q, Yao Y, He P-a (in press) A graphical representation of protein based on a novel iterated function system. Physica A: Statistical Mechanics and its Applications(0)
  • 145
    • 0021280786 scopus 로고
    • Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans
    • COI: 1:CAS:528:DyaL2cXkt1WqsLk%3D, PID: 6724693
    • Mackay BJ, Denepitiya L, Iacono V, Krost S, Pollock J (1984) Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans. Infect Immun 44(3):695–701
    • (1984) Infect Immun , vol.44 , Issue.3 , pp. 695-701
    • Mackay, B.J.1    Denepitiya, L.2    Iacono, V.3    Krost, S.4    Pollock, J.5
  • 146
    • 33746842648 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment
    • COI: 1:CAS:528:DC%2BD28Xnt1ahsbk%3D, PID: 16859395
    • Mader JS, Hoskin DW (2006) Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin Investig Drugs 15(8):933–946
    • (2006) Expert Opin Investig Drugs , vol.15 , Issue.8 , pp. 933-946
    • Mader, J.S.1    Hoskin, D.W.2
  • 147
    • 84869229709 scopus 로고    scopus 로고
    • Rapid microwave-assisted solution-phase peptide synthesis.Tetrahedron
    • COI: 1:CAS:528:DC%2BC38Xhs1SqurbE
    • Mahindra A, Sharma KK, Jain R (2012) Rapid microwave-assisted solution-phase peptide synthesis.Tetrahedron. Lett 53(51):6931–6935
    • (2012) Lett , vol.53 , Issue.51 , pp. 6931-6935
    • Mahindra, A.1    Sharma, K.K.2    Jain, R.3
  • 148
    • 0035717170 scopus 로고    scopus 로고
    • Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin
    • COI: 1:CAS:528:DC%2BD3MXitlaqurY%3D, PID: 11281721
    • Martemyanov KA, Shirokov VA, Kurnasov OV, Gudkov AT, Spirin AS (2001) Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin. Protein Expr Purif 21(3):456–461
    • (2001) Protein Expr Purif , vol.21 , Issue.3 , pp. 456-461
    • Martemyanov, K.A.1    Shirokov, V.A.2    Kurnasov, O.V.3    Gudkov, A.T.4    Spirin, A.S.5
  • 149
    • 84873718371 scopus 로고    scopus 로고
    • Salivary proteins as a biomarker for dental caries—a systematic review
    • COI: 1:CAS:528:DC%2BC38Xhslaku7vO, PID: 23142096
    • Martins C, Buczynski AK, Maia LC, Siqueira WL, Castro GFBA (2013) Salivary proteins as a biomarker for dental caries—a systematic review. J Dent 41(1):2–8
    • (2013) J Dent , vol.41 , Issue.1 , pp. 2-8
    • Martins, C.1    Buczynski, A.K.2    Maia, L.C.3    Siqueira, W.L.4    Castro, G.F.B.A.5
  • 150
    • 10944268735 scopus 로고    scopus 로고
    • Suppression of cold ischemic injury in stored kidneys by the antimicrobial peptide bactenecin
    • COI: 1:CAS:528:DC%2BD2cXhtFahs7bK, PID: 15615609
    • McAnulty JF, Foley JD, Reid TW, Heath TD, Waller KR, Murphy CJ (2004) Suppression of cold ischemic injury in stored kidneys by the antimicrobial peptide bactenecin. Cryobiology 49(3):230–240
    • (2004) Cryobiology , vol.49 , Issue.3 , pp. 230-240
    • McAnulty, J.F.1    Foley, J.D.2    Reid, T.W.3    Heath, T.D.4    Waller, K.R.5    Murphy, C.J.6
  • 152
    • 28044469064 scopus 로고    scopus 로고
    • Function and therapeutic potential of host defence peptides
    • COI: 1:CAS:528:DC%2BD2MXht1ehtL7E, PID: 16103989
    • Mcphee JB, Hancock RE (2005) Function and therapeutic potential of host defence peptides. J Pept Sci 11(11):677–687
    • (2005) J Pept Sci , vol.11 , Issue.11 , pp. 677-687
    • Mcphee, J.B.1    Hancock, R.E.2
  • 153
    • 33845921608 scopus 로고    scopus 로고
    • Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5
    • COI: 1:CAS:528:DC%2BD28Xht1Kitb7O, PID: 17176059
    • Melino S, Gallo M, Trotta E, Mondello F, Paci M, Petruzzelli R (2006) Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5. Biochemistry 45(51):15373–15383
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15373-15383
    • Melino, S.1    Gallo, M.2    Trotta, E.3    Mondello, F.4    Paci, M.5    Petruzzelli, R.6
  • 154
    • 84897033162 scopus 로고    scopus 로고
    • Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications
    • COI: 1:CAS:528:DC%2BC2cXht1Onurc%3D, PID: 24219363
    • Melino S, Santone C, Di Nardo P, Sarkar B (2014) Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications. FEBS J 281(3):657–672
    • (2014) FEBS J , vol.281 , Issue.3 , pp. 657-672
    • Melino, S.1    Santone, C.2    Di Nardo, P.3    Sarkar, B.4
  • 155
    • 84857690289 scopus 로고    scopus 로고
    • A novel antioxidant and antimicrobial peptide from hen egg white lysozyme hydrolysates
    • COI: 1:CAS:528:DC%2BC38Xjt1ansL0%3D
    • Memarpoor-Yazdi M, Asoodeh A, Chamani J (2012) A novel antioxidant and antimicrobial peptide from hen egg white lysozyme hydrolysates. J Funct Foods 4(1):278–286
    • (2012) J Funct Foods , vol.4 , Issue.1 , pp. 278-286
    • Memarpoor-Yazdi, M.1    Asoodeh, A.2    Chamani, J.3
  • 156
    • 79951512574 scopus 로고    scopus 로고
    • Antibacterial activity of products of depolymerization of chitosans with lysozyme and chitosanase against Campylobacter jejuni
    • Mengíbar M, Ganan M, Miralles B, Carrascosa AV, Martínez-Rodriguez AJ, Peter MG, Heras A (2011) Antibacterial activity of products of depolymerization of chitosans with lysozyme and chitosanase against Campylobacter jejuni. Carbohydr Polym 84(2):844–848
    • (2011) Carbohydr Polym , vol.84 , Issue.2 , pp. 844-848
    • Mengíbar, M.1    Ganan, M.2    Miralles, B.3    Carrascosa, A.V.4    Martínez-Rodriguez, A.J.5    Peter, M.G.6    Heras, A.7
  • 157
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • COI: 1:CAS:528:DyaF3sXksVajsLg%3D
    • Merrifield RB (1963) Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J Am Chem Soc 85(14):2149–2154
    • (1963) J Am Chem Soc , vol.85 , Issue.14 , pp. 2149-2154
    • Merrifield, R.B.1
  • 159
    • 84893092108 scopus 로고    scopus 로고
    • The evolution of peptide synthesis: from early days to small molecular machines
    • COI: 1:CAS:528:DC%2BC2cXhvVWqtL0%3D
    • Mollica A, Pinnen F, Azzurra S, Costante R (2013) The evolution of peptide synthesis: from early days to small molecular machines. Curr Bioact Compd 9(3):184–202
    • (2013) Curr Bioact Compd , vol.9 , Issue.3 , pp. 184-202
    • Mollica, A.1    Pinnen, F.2    Azzurra, S.3    Costante, R.4
  • 160
    • 84862663258 scopus 로고    scopus 로고
    • Group A streptococcus adheres to pharyngeal epithelial cells with salivary proline-rich proteins via GrpE chaperone protein
    • COI: 1:CAS:528:DC%2BC38XptVWru7o%3D, PID: 22566698
    • Murakami J, Terao Y, Morisaki I, Hamada S, Kawabata S (2012) Group A streptococcus adheres to pharyngeal epithelial cells with salivary proline-rich proteins via GrpE chaperone protein. J Biol Chem 287(26):22266–22275
    • (2012) J Biol Chem , vol.287 , Issue.26 , pp. 22266-22275
    • Murakami, J.1    Terao, Y.2    Morisaki, I.3    Hamada, S.4    Kawabata, S.5
  • 161
    • 33847022308 scopus 로고    scopus 로고
    • The synergistic effect of nisin and lactoferrin on the inhibition of Listeria monocytogenes and Escherichia coli O157: H7
    • COI: 1:CAS:528:DC%2BD2sXkt1WltLc%3D, PID: 17309501
    • Murdock C, Cleveland J, Matthews K, Chikindas M (2007) The synergistic effect of nisin and lactoferrin on the inhibition of Listeria monocytogenes and Escherichia coli O157: H7. Lett Appl Microbiol 44(3):255–261
    • (2007) Lett Appl Microbiol , vol.44 , Issue.3 , pp. 255-261
    • Murdock, C.1    Cleveland, J.2    Matthews, K.3    Chikindas, M.4
  • 162
    • 68449097384 scopus 로고    scopus 로고
    • Species-independent translational leaders facilitate cell-free expression
    • COI: 1:CAS:528:DC%2BD1MXpt1Ogsbk%3D, PID: 19648909
    • Mureev S, Kovtun O, Nguyen UTT, Alexandrov K (2009) Species-independent translational leaders facilitate cell-free expression. Nat Biotechnol 27(8):747–752
    • (2009) Nat Biotechnol , vol.27 , Issue.8 , pp. 747-752
    • Mureev, S.1    Kovtun, O.2    Nguyen, U.T.T.3    Alexandrov, K.4
  • 163
    • 52449119580 scopus 로고    scopus 로고
    • Skin peptides: biological activity and therapeutic opportunities
    • COI: 1:CAS:528:DC%2BD1cXotF2murg%3D, PID: 17914716
    • Namjoshi S, Caccetta R, Benson HAE (2008) Skin peptides: biological activity and therapeutic opportunities. J Pharm Sci 97(7):2524–2542
    • (2008) J Pharm Sci , vol.97 , Issue.7 , pp. 2524-2542
    • Namjoshi, S.1    Caccetta, R.2    Benson, H.A.E.3
  • 164
    • 1442314720 scopus 로고    scopus 로고
    • Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides
    • COI: 1:CAS:528:DC%2BD2cXht1GjtLs%3D, PID: 14656995
    • Nekhotiaeva N, Elmquist A, Rajarao GK, Hällbrink M, Langel U, Good L (2004) Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides. FASEB J 18(2):394–396
    • (2004) FASEB J , vol.18 , Issue.2 , pp. 394-396
    • Nekhotiaeva, N.1    Elmquist, A.2    Rajarao, G.K.3    Hällbrink, M.4    Langel, U.5    Good, L.6
  • 165
    • 77949772551 scopus 로고    scopus 로고
    • Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome
    • COI: 1:CAS:528:DC%2BC3cXitFelsrc%3D, PID: 20154731
    • Neumann H, Wang K, Davis L, Garcia-Alai M, Chin JW (2010) Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome. Nature 464(7287):441–444
    • (2010) Nature , vol.464 , Issue.7287 , pp. 441-444
    • Neumann, H.1    Wang, K.2    Davis, L.3    Garcia-Alai, M.4    Chin, J.W.5
  • 166
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • COI: 1:CAS:528:DC%2BC3MXhtVGktrnM, PID: 21680034
    • Nguyen LT, Haney EF, Vogel HJ (2011) The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol 29(9):464–472
    • (2011) Trends Biotechnol , vol.29 , Issue.9 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 167
    • 67649262194 scopus 로고    scopus 로고
    • The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD1MXnt1Ght7o%3D, PID: 18929530
    • Nicolas P, El Amri C (2009) The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides. Biochim Biophys Acta 1788(8):1537–1550
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.8 , pp. 1537-1550
    • Nicolas, P.1    El Amri, C.2
  • 168
    • 84873733394 scopus 로고    scopus 로고
    • Selective induction of antimicrobial peptides from keratinocytes by staphylococcal bacteria
    • COI: 1:CAS:528:DC%2BC3sXisVaksL8%3D, PID: 23178253
    • Ommori R, Ouji N, Mizuno F, Kita E, Ikada Y, Asada H (2013) Selective induction of antimicrobial peptides from keratinocytes by staphylococcal bacteria. Microb Pathog 56:35–39
    • (2013) Microb Pathog , vol.56 , pp. 35-39
    • Ommori, R.1    Ouji, N.2    Mizuno, F.3    Kita, E.4    Ikada, Y.5    Asada, H.6
  • 169
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • COI: 1:CAS:528:DyaL1cXltVKluro%3D, PID: 3286634
    • Oppenheim F, Xu T, McMillian F, Levitz S, Diamond R, Offner G, Troxler R (1988) Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J Biol Chem 263(16):7472–7477
    • (1988) J Biol Chem , vol.263 , Issue.16 , pp. 7472-7477
    • Oppenheim, F.1    Xu, T.2    McMillian, F.3    Levitz, S.4    Diamond, R.5    Offner, G.6    Troxler, R.7
  • 170
    • 0142218765 scopus 로고    scopus 로고
    • Roles of antimicrobial peptides such as defensins in innate and adaptive immunity
    • COI: 1:CAS:528:DC%2BD3sXpvVyjt7k%3D, PID: 14532141
    • Oppenheim J, Biragyn A, Kwak L, Yang D (2003) Roles of antimicrobial peptides such as defensins in innate and adaptive immunity. Ann Rheum Dis 62(suppl 2):ii17–ii21
    • (2003) Ann Rheum Dis , vol.62 , pp. 17-21
    • Oppenheim, J.1    Biragyn, A.2    Kwak, L.3    Yang, D.4
  • 171
    • 80053622234 scopus 로고    scopus 로고
    • Computational approaches to selecting and optimising targets for structural biology
    • COI: 1:CAS:528:DC%2BC3MXhtlaqt73N, PID: 21906678
    • Overton IM, Barton GJ (2011) Computational approaches to selecting and optimising targets for structural biology. Methods 55(1):3–11
    • (2011) Methods , vol.55 , Issue.1 , pp. 3-11
    • Overton, I.M.1    Barton, G.J.2
  • 173
    • 58949086491 scopus 로고    scopus 로고
    • Solution- and solid-phase synthesis and anti-HIV activity of maslinic acid derivatives containing amino acids and peptides
    • COI: 1:CAS:528:DC%2BD1MXhtlOhtr0%3D, PID: 19135380
    • Parra A, Rivas F, Lopez PE, Garcia-Granados A, Martinez A, Albericio F, Marquez N, Muñoz E (2009) Solution- and solid-phase synthesis and anti-HIV activity of maslinic acid derivatives containing amino acids and peptides. Bioorg Med Chem 17(3):1139–1145
    • (2009) Bioorg Med Chem , vol.17 , Issue.3 , pp. 1139-1145
    • Parra, A.1    Rivas, F.2    Lopez, P.E.3    Garcia-Granados, A.4    Martinez, A.5    Albericio, F.6    Marquez, N.7    Muñoz, E.8
  • 175
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • COI: 1:CAS:528:DC%2BD28XlvVGltbY%3D, PID: 16778838
    • Peschel A, Sahl HG (2006) The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat Rev Microbiol 4(7):529–536
    • (2006) Nat Rev Microbiol , vol.4 , Issue.7 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 176
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: primeval molecules or future drugs?
    • PID: 21060861
    • Peters BM, Shirtliff ME, Jabra-Rizk MA (2010) Antimicrobial peptides: primeval molecules or future drugs? PLoS Pathog 6(10):e1001067
    • (2010) PLoS Pathog , vol.6 , Issue.10
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 177
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • COI: 1:CAS:528:DC%2BC3MXht1CrtrbL, PID: 21959131
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8(10):785–786
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 178
    • 84891569071 scopus 로고    scopus 로고
    • Antimicrobial peptides: their history, evolution, and functional promiscuity antimicrobial peptides. Wiley-VCH Verlag GmbH & Co
    • Phoenix DA, Dennison SR, Harris F (2013) Antimicrobial peptides: their history, evolution, and functional promiscuity antimicrobial peptides. Wiley-VCH Verlag GmbH & Co. KGaA, pp 1-37
    • (2013) KGaA , pp. 1-37
    • Phoenix, D.A.1    Dennison, S.R.2    Harris, F.3
  • 179
    • 84858277472 scopus 로고    scopus 로고
    • YADAMP: yet another database of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC38XitVWlsr4%3D, PID: 22325123
    • Piotto SP, Sessa L, Concilio S, Iannelli P (2012) YADAMP: yet another database of antimicrobial peptides. Int J Antimicrob Agents 39(4):346–351
    • (2012) Int J Antimicrob Agents , vol.39 , Issue.4 , pp. 346-351
    • Piotto, S.P.1    Sessa, L.2    Concilio, S.3    Iannelli, P.4
  • 180
    • 0021263092 scopus 로고
    • Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans
    • COI: 1:CAS:528:DyaL2cXkvVOhu70%3D, PID: 6373615
    • Pollock JJ, Denepitiya L, MacKay B, Iacono V (1984) Fungistatic and fungicidal activity of human parotid salivary histidine-rich polypeptides on Candida albicans. Infect Immun 44(3):702–707
    • (1984) Infect Immun , vol.44 , Issue.3 , pp. 702-707
    • Pollock, J.J.1    Denepitiya, L.2    MacKay, B.3    Iacono, V.4
  • 181
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • COI: 1:CAS:528:DC%2BD2cXhtFWmtLc%3D, PID: 15019199
    • Powers J-PS, Hancock RE (2003) The relationship between peptide structure and antibacterial activity. Peptides 24(11):1681–1691
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.-P.S.1    Hancock, R.E.2
  • 182
    • 84907463396 scopus 로고    scopus 로고
    • How does it kill?: understanding the candidacidal mechanism of salivary histatin 5
    • COI: 1:CAS:528:DC%2BC2cXhs1emurjK, PID: 24951439
    • Puri S, Edgerton M (2014) How does it kill?: understanding the candidacidal mechanism of salivary histatin 5. Eukaryot Cell 13(8):958–964
    • (2014) Eukaryot Cell , vol.13 , Issue.8 , pp. 958-964
    • Puri, S.1    Edgerton, M.2
  • 183
    • 84880166527 scopus 로고    scopus 로고
    • Antimicrobial peptides: versatile biological properties
    • PID: 23935642
    • Pushpanathan M, Gunasekaran P, Rajendhran J (2013) Antimicrobial peptides: versatile biological properties. Int J Pept 2013:675391
    • (2013) Int J Pept , vol.2013 , pp. 675391
    • Pushpanathan, M.1    Gunasekaran, P.2    Rajendhran, J.3
  • 184
    • 84872851002 scopus 로고    scopus 로고
    • HIPdb: a database of experimentally validated HIV inhibiting peptides
    • Qureshi A, Thakur N, Kumar M (2013) HIPdb: a database of experimentally validated HIV inhibiting peptides. PLoS One 8(1):e5490
    • (2013) PLoS One , vol.8 , Issue.1 , pp. 5490
    • Qureshi, A.1    Thakur, N.2    Kumar, M.3
  • 185
    • 77957373321 scopus 로고    scopus 로고
    • Quantitative understanding of cell signaling: the importance of membrane organization
    • COI: 1:CAS:528:DC%2BC3cXht1OmsrbK, PID: 20829029
    • Radhakrishnan K, Halász Á, Vlachos D, Edwards JS (2010) Quantitative understanding of cell signaling: the importance of membrane organization. Curr Opin Biotechnol 21(5):677–682
    • (2010) Curr Opin Biotechnol , vol.21 , Issue.5 , pp. 677-682
    • Radhakrishnan, K.1    Halász, Á.2    Vlachos, D.3    Edwards, J.S.4
  • 187
    • 48949110015 scopus 로고    scopus 로고
    • Antimicrobial peptides: a new dawn for regulating fertility and reproductive tract infections
    • Rana M, Chatterjee S, Kochhar S, Pereira B (2006) Antimicrobial peptides: a new dawn for regulating fertility and reproductive tract infections. J Endocrinol Reprod 10(2):88–95
    • (2006) J Endocrinol Reprod , vol.10 , Issue.2 , pp. 88-95
    • Rana, M.1    Chatterjee, S.2    Kochhar, S.3    Pereira, B.4
  • 188
    • 0026354984 scopus 로고
    • Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers
    • COI: 1:CAS:528:DyaK3MXmsFSjsr4%3D, PID: 1748653
    • Rapaport D, Shai Y (1991) Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J Biol Chem 266(35):23769–23775
    • (1991) J Biol Chem , vol.266 , Issue.35 , pp. 23769-23775
    • Rapaport, D.1    Shai, Y.2
  • 189
    • 0027933818 scopus 로고
    • A new LIM protein containing an autoepitope homologous to "senescent cell antigen"
    • COI: 1:CAS:528:DyaK2cXlslehurw%3D, PID: 7517666
    • Rearden A (1994) A new LIM protein containing an autoepitope homologous to "senescent cell antigen". Biochem Biophys Res Commun 201(3):1124–1131
    • (1994) Biochem Biophys Res Commun , vol.201 , Issue.3 , pp. 1124-1131
    • Rearden, A.1
  • 190
    • 65249175159 scopus 로고    scopus 로고
    • CC chemokine receptor 6–regulated entry of TH-17 cells into the CNS through the choroid plexus is required for the initiation of EAE
    • COI: 1:CAS:528:DC%2BD1MXjsVGjs7Y%3D, PID: 19305396
    • Reboldi A, Coisne C, Baumjohann D, Benvenuto F, Bottinelli D, Lira S, Uccelli A, Lanzavecchia A, Engelhardt B, Sallusto F (2009) CC chemokine receptor 6–regulated entry of TH-17 cells into the CNS through the choroid plexus is required for the initiation of EAE. Nat Immunol 10(5):514–523
    • (2009) Nat Immunol , vol.10 , Issue.5 , pp. 514-523
    • Reboldi, A.1    Coisne, C.2    Baumjohann, D.3    Benvenuto, F.4    Bottinelli, D.5    Lira, S.6    Uccelli, A.7    Lanzavecchia, A.8    Engelhardt, B.9    Sallusto, F.10
  • 191
    • 8844254807 scopus 로고    scopus 로고
    • Antimicrobial peptides: premises and promises
    • COI: 1:CAS:528:DC%2BD2cXhtVSntbnI, PID: 15555874
    • Reddy KVR, Yedery RD, Aranha C (2004) Antimicrobial peptides: premises and promises. Int J Antimicrob Agents 24(6):536–547
    • (2004) Int J Antimicrob Agents , vol.24 , Issue.6 , pp. 536-547
    • Reddy, K.V.R.1    Yedery, R.D.2    Aranha, C.3
  • 192
    • 70450200962 scopus 로고    scopus 로고
    • Development trends for peptide therapeutics
    • Reichert J (2010) Development trends for peptide therapeutics. In: Foundation PT (ed).
    • (2010) In: Foundation PT (ed)
    • Reichert, J.1
  • 193
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European molecular biology open software suite
    • COI: 1:CAS:528:DC%2BD3cXjvVygsbs%3D, PID: 10827456
    • Rice P, Longden I, Bleasby A (2000) EMBOSS: The European molecular biology open software suite. Trends Genet 16(6):276–277
    • (2000) Trends Genet , vol.16 , Issue.6 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 194
    • 84872433200 scopus 로고    scopus 로고
    • Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites
    • COI: 1:CAS:528:DC%2BC3sXislyqsbc%3D, PID: 23274811
    • Rico-Mata R, De Leon-Rodriguez LM, Avila EE (2013) Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites. Exp Parasitol 133(3):300–306
    • (2013) Exp Parasitol , vol.133 , Issue.3 , pp. 300-306
    • Rico-Mata, R.1    De Leon-Rodriguez, L.M.2    Avila, E.E.3
  • 195
    • 84896731463 scopus 로고    scopus 로고
    • Great expectorations: the potential of salivary ‘omic’ approaches in neonatal intensive care
    • COI: 1:STN:280:DC%2BC2czjs1Wqsw%3D%3D, PID: 24406743
    • Romano-Keeler J, Wynn JL, Maron JL (2014) Great expectorations: the potential of salivary ‘omic’ approaches in neonatal intensive care. J Perinatol 34(3):169–173
    • (2014) J Perinatol , vol.34 , Issue.3 , pp. 169-173
    • Romano-Keeler, J.1    Wynn, J.L.2    Maron, J.L.3
  • 197
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • COI: 1:CAS:528:DC%2BD3cXovVKku78%3D, PID: 11123901
    • Rozek A, Friedrich CL, Hancock RE (2000) Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39(51):15765–15774
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 198
    • 80053459095 scopus 로고    scopus 로고
    • Determining the effect of the incorporation of unnatural amino acids into antimicrobial peptides on the interactions with zwitterionic and anionic membrane model systems
    • COI: 1:CAS:528:DC%2BC3MXhtl2qs77L, PID: 21945566
    • Russell AL, Kennedy AM, Spuches AM, Gibson WS, Venugopal D, Klapper D, Srouji AH, Bhonsle JB, Hicks RP (2011) Determining the effect of the incorporation of unnatural amino acids into antimicrobial peptides on the interactions with zwitterionic and anionic membrane model systems. Chem Phys Lipids 164(8):740–758
    • (2011) Chem Phys Lipids , vol.164 , Issue.8 , pp. 740-758
    • Russell, A.L.1    Kennedy, A.M.2    Spuches, A.M.3    Gibson, W.S.4    Venugopal, D.5    Klapper, D.6    Srouji, A.H.7    Bhonsle, J.B.8    Hicks, R.P.9
  • 199
    • 84867888751 scopus 로고    scopus 로고
    • Membrane interaction and secondary structure of de novo designed arginine-and tryptophan peptides with dual function
    • COI: 1:CAS:528:DC%2BC38XhsVOgs7bE, PID: 22989747
    • Rydberg HA, Carlsson N, Nordén B (2012) Membrane interaction and secondary structure of de novo designed arginine-and tryptophan peptides with dual function. Biochem Biophys Res Commun 427(2):261–265
    • (2012) Biochem Biophys Res Commun , vol.427 , Issue.2 , pp. 261-265
    • Rydberg, H.A.1    Carlsson, N.2    Nordén, B.3
  • 200
    • 84903362494 scopus 로고    scopus 로고
    • Effect of hydrophobic modifications in antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC3sXhtF2hsrjO
    • Schmidtchen A, Pasupuleti M, Malmsten M (2014) Effect of hydrophobic modifications in antimicrobial peptides. Adv Colloid Interf Sci 205:265–274
    • (2014) Adv Colloid Interf Sci , vol.205 , pp. 265-274
    • Schmidtchen, A.1    Pasupuleti, M.2    Malmsten, M.3
  • 201
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • COI: 1:CAS:528:DyaK2MXksVajtbc%3D, PID: 7886453
    • Schonwetter BS, Stolzenberg ED, Zasloff MA (1995) Epithelial antibiotics induced at sites of inflammation. Science 267(5204):1645–1648
    • (1995) Science , vol.267 , Issue.5204 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 202
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • COI: 1:CAS:528:DC%2BD3sXltVWjsLg%3D, PID: 12824332
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31(13):3381–3385
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 203
    • 33846108632 scopus 로고    scopus 로고
    • Defensins knowledgebase: a manually curated database and information source focused on the defensins family of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD2sXivFGqtw%3D%3D, PID: 17090586
    • Seebah S, Suresh A, Zhuo SW, Choong YH, Chua H, Chuon D, Beuerman R, Verma C (2007) Defensins knowledgebase: a manually curated database and information source focused on the defensins family of antimicrobial peptides. Nucleic Acids Res 35:D265–D268
    • (2007) Nucleic Acids Res , vol.35 , pp. 265-268
    • Seebah, S.1    Suresh, A.2    Zhuo, S.W.3    Choong, Y.H.4    Chua, H.5    Chuon, D.6    Beuerman, R.7    Verma, C.8
  • 204
    • 0034824597 scopus 로고    scopus 로고
    • From “carpet” mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • COI: 1:CAS:528:DC%2BD3MXnt1SgsLg%3D, PID: 11587791
    • Shai Y, Oren Z (2001) From “carpet” mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22(10):1629–1641
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 205
    • 84868696288 scopus 로고    scopus 로고
    • Antimicrobial activity of human β-defensin 4 analogs: insights into the role of disulfide linkages in modulating activity
    • COI: 1:CAS:528:DC%2BC38XhslKqsrbE, PID: 23000475
    • Sharma H, Nagaraj R (2012) Antimicrobial activity of human β-defensin 4 analogs: insights into the role of disulfide linkages in modulating activity. Peptides 38(2):255–265
    • (2012) Peptides , vol.38 , Issue.2 , pp. 255-265
    • Sharma, H.1    Nagaraj, R.2
  • 206
    • 33645015808 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action: studies of indolicidin assembly at model membrane interfaces by in situ atomic force microscopy
    • COI: 1:CAS:528:DC%2BD28XivValt7w%3D, PID: 16459101
    • Shaw JE, Alattia J-R, Verity JE, Privé GG, Yip CM (2006) Mechanisms of antimicrobial peptide action: studies of indolicidin assembly at model membrane interfaces by in situ atomic force microscopy. J Struct Biol 154(1):42–58
    • (2006) J Struct Biol , vol.154 , Issue.1 , pp. 42-58
    • Shaw, J.E.1    Alattia, J.-R.2    Verity, J.E.3    Privé, G.G.4    Yip, C.M.5
  • 207
    • 17344389389 scopus 로고    scopus 로고
    • Sensitivity and selectivity in protein similarity searches: a comparison of Smith–Waterman in hardware to BLAST and FASTA
    • COI: 1:CAS:528:DyaK28XnsFaht74%3D, PID: 8954800
    • Shpaer EG, Robinson M, Yee D, Candlin JD, Mines R, Hunkapiller T (1996) Sensitivity and selectivity in protein similarity searches: a comparison of Smith–Waterman in hardware to BLAST and FASTA. Genomics 38(2):179–191
    • (1996) Genomics , vol.38 , Issue.2 , pp. 179-191
    • Shpaer, E.G.1    Robinson, M.2    Yee, D.3    Candlin, J.D.4    Mines, R.5    Hunkapiller, T.6
  • 208
    • 84879191482 scopus 로고    scopus 로고
    • Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein
    • Sinha M, Kaushik S, Kaur P, Sharma S, Singh TP (2013) Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein. Int J Pept 2013:12
    • (2013) Int J Pept , vol.2013 , pp. 12
    • Sinha, M.1    Kaushik, S.2    Kaur, P.3    Sharma, S.4    Singh, T.P.5
  • 210
    • 84895923109 scopus 로고    scopus 로고
    • Recent advances in modeling languages for pathway maps and computable biological networks
    • PID: 24444544
    • Slater T (2014) Recent advances in modeling languages for pathway maps and computable biological networks. Drug Discov Today 19(2):193–198
    • (2014) Drug Discov Today , vol.19 , Issue.2 , pp. 193-198
    • Slater, T.1
  • 212
    • 34547151206 scopus 로고    scopus 로고
    • Relationship between salivary histatin 5 levels and Candida CFU counts in healthy elderly
    • PID: 16919097
    • Sugimoto J, Kanehira T, Mizugai H, Chiba I, Morita M (2006) Relationship between salivary histatin 5 levels and Candida CFU counts in healthy elderly. Gerodontology 23(3):164–169
    • (2006) Gerodontology , vol.23 , Issue.3 , pp. 164-169
    • Sugimoto, J.1    Kanehira, T.2    Mizugai, H.3    Chiba, I.4    Morita, M.5
  • 213
    • 84890029384 scopus 로고    scopus 로고
    • Template-based structure modeling of protein–protein interactions
    • COI: 1:CAS:528:DC%2BC2cXmtVamsr8%3D, PID: 24721449
    • Szilagyi A, Zhang Y (2014) Template-based structure modeling of protein–protein interactions. Curr Opin Struct Biol 24:10–23
    • (2014) Curr Opin Struct Biol , vol.24 , pp. 10-23
    • Szilagyi, A.1    Zhang, Y.2
  • 214
    • 77950472075 scopus 로고    scopus 로고
    • Methods for building quantitative structure-activity relationship (QSAR) descriptors and predictive models for computer-aided design of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC3cXhtVSlu7rO, PID: 20094859
    • Taboureau O (2010) Methods for building quantitative structure-activity relationship (QSAR) descriptors and predictive models for computer-aided design of antimicrobial peptides. Methods Mol Biol 618:77–86
    • (2010) Methods Mol Biol , vol.618 , pp. 77-86
    • Taboureau, O.1
  • 215
    • 84868019079 scopus 로고    scopus 로고
    • Making peptides at large scale
    • Thayer A (2011) Making peptides at large scale. Chem Eng News 89(22):81–85
    • (2011) Chem Eng News , vol.89 , Issue.22 , pp. 81-85
    • Thayer, A.1
  • 216
    • 84894934931 scopus 로고    scopus 로고
    • The mechanisms by which pardaxin, a natural cationic antimicrobial peptide, targets the endoplasmic reticulum and induces c-FOS
    • COI: 1:CAS:528:DC%2BC2cXht1yrs70%3D, PID: 24477193
    • Ting C-H, Huang H-N, Huang T-C, Wu C-J, Chen J-Y (2014) The mechanisms by which pardaxin, a natural cationic antimicrobial peptide, targets the endoplasmic reticulum and induces c-FOS. Biomaterials 35(11):3627–3640
    • (2014) Biomaterials , vol.35 , Issue.11 , pp. 3627-3640
    • Ting, C.-H.1    Huang, H.-N.2    Huang, T.-C.3    Wu, C.-J.4    Chen, J.-Y.5
  • 217
    • 84855164403 scopus 로고    scopus 로고
    • Andreu D (2012) AMPA: an automated web server for prediction of protein antimicrobial regions
    • COI: 1:CAS:528:DC%2BC3MXhs1yms7bI, PID: 22053077
    • Torrent M, Di Tommaso P, Pulido D, Nogues MV, Notredame C, Boix E (2012) Andreu D (2012) AMPA: an automated web server for prediction of protein antimicrobial regions. Bioinformatics 28(1):130–131
    • (2012) Bioinformatics , vol.28 , Issue.1 , pp. 130-131
    • Torrent, M.1    Di Tommaso, P.2    Pulido, D.3    Nogues, M.V.4    Notredame, C.5    Boix, E.6
  • 218
    • 84874284256 scopus 로고    scopus 로고
    • Safety, formulation and in vitro antiviral activity of the antimicrobial peptide subtilosin against herpes simplex virus type 1
    • COI: 1:CAS:528:DC%2BC3sXjtVahsbw%3D
    • Torres NI, Noll KS, Xu S, Li J, Huang Q, Sinko PJ, Wachsman MB, Chikindas ML (2013) Safety, formulation and in vitro antiviral activity of the antimicrobial peptide subtilosin against herpes simplex virus type 1. Probiotics Antimicrob Protein 5(1):26–35
    • (2013) Probiotics Antimicrob Protein , vol.5 , Issue.1 , pp. 26-35
    • Torres, N.I.1    Noll, K.S.2    Xu, S.3    Li, J.4    Huang, Q.5    Sinko, P.J.6    Wachsman, M.B.7    Chikindas, M.L.8
  • 219
    • 11444259936 scopus 로고    scopus 로고
    • New consensus hydrophobicity scale extended to non-proteinogenic amino acids
    • Tossi A, Sandri L, Giangaspero A (2002) New consensus hydrophobicity scale extended to non-proteinogenic amino acids. Peptides 27:416
    • (2002) Peptides , vol.27 , pp. 416
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 220
    • 84863638716 scopus 로고    scopus 로고
    • Antimicrobial peptides as therapeutic agents
    • Upton M, Cotter P, Tagg J (2012) Antimicrobial peptides as therapeutic agents. Int J Microbiol 2012:326503
    • (2012) Int J Microbiol , vol.2012
    • Upton, M.1    Cotter, P.2    Tagg, J.3
  • 221
    • 84864538606 scopus 로고    scopus 로고
    • Fernandez-Busquets X (2012) Nanotools for the delivery of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC38Xht1Wjs7rJ, PID: 22664075
    • Urban P, Valle-Delgado JJ, Moles E, Marques J, Diez C (2012) Fernandez-Busquets X (2012) Nanotools for the delivery of antimicrobial peptides. Curr Drug Targets 13(9):1158–1172
    • (2012) Curr Drug Targets , vol.13 , Issue.9 , pp. 1158-1172
    • Urban, P.1    Valle-Delgado, J.J.2    Moles, E.3    Marques, J.4    Diez, C.5
  • 223
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • COI: 1:CAS:528:DC%2BC3sXhvFSnurs%3D, PID: 23246832
    • Vandamme D, Landuyt B, Luyten W, Schoofs L (2012) A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell Immunol 280(1):22–35
    • (2012) Cell Immunol , vol.280 , Issue.1 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 225
    • 74149094591 scopus 로고    scopus 로고
    • Synthetic therapeutic peptides: science and market
    • COI: 1:CAS:528:DC%2BC3cXnsV2iug%3D%3D, PID: 19879957
    • Vlieghe P, Lisowski V, Martinez J, Khrestchatisky M (2010) Synthetic therapeutic peptides: science and market. Drug Discov Today 15(1–2):40–56
    • (2010) Drug Discov Today , vol.15 , Issue.1-2 , pp. 40-56
    • Vlieghe, P.1    Lisowski, V.2    Martinez, J.3    Khrestchatisky, M.4
  • 226
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • COI: 1:CAS:528:DC%2BD1cXhtVKntrfF, PID: 17658458
    • Vollmer W, Bertsche U (2008) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim Biophys Acta 1778(9):1714–1734
    • (2008) Biochim Biophys Acta , vol.1778 , Issue.9 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 227
    • 84891799288 scopus 로고    scopus 로고
    • CAMP: collection of sequences and structures of antimicrobial peptides
    • COI: 1:CAS:528:DC%2BC2cXoslGj, PID: 24265220
    • Waghu FH, Gopi L, Barai RS, Ramteke P, Nizami B, Idicula-Thomas S (2014) CAMP: collection of sequences and structures of antimicrobial peptides. Nucleic Acids Res 42(D1):D1154–D1158
    • (2014) Nucleic Acids Res , vol.42 , Issue.D1 , pp. 1154-1158
    • Waghu, F.H.1    Gopi, L.2    Barai, R.S.3    Ramteke, P.4    Nizami, B.5    Idicula-Thomas, S.6
  • 228
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • COI: 1:CAS:528:DC%2BD1cXhtlOjtLvN, PID: 18818205
    • Wang G (2008) Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem 283(47):32637–32643
    • (2008) J Biol Chem , vol.283 , Issue.47 , pp. 32637-32643
    • Wang, G.1
  • 229
    • 38549134937 scopus 로고    scopus 로고
    • CyBase: a database of cyclic protein sequences and structures, with applications in protein discovery and engineering
    • COI: 1:CAS:528:DC%2BD1cXhtVWiurw%3D, PID: 17986451
    • Wang CKL, Kaas Q, Chiche L, Craik DJ (2008) CyBase: a database of cyclic protein sequences and structures, with applications in protein discovery and engineering. Nucleic Acids Res 36(1):D206–D210
    • (2008) Nucleic Acids Res , vol.36 , Issue.1 , pp. 206-210
    • Wang, C.K.L.1    Kaas, Q.2    Chiche, L.3    Craik, D.J.4
  • 230
    • 58149187882 scopus 로고    scopus 로고
    • APD2: the updated antimicrobial peptide database and its application in peptide design
    • COI: 1:CAS:528:DC%2BD1cXhsFejtL3L, PID: 18957441
    • Wang G, Li X, Wang Z (2009) APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res 37:D933–D937
    • (2009) Nucleic Acids Res , vol.37 , pp. 933-937
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 231
    • 75149139976 scopus 로고    scopus 로고
    • The efficacy of self-assembled cationic antimicrobial peptide nanoparticles against Cryptococcus neoformans for the treatment of meningitis
    • COI: 1:CAS:528:DC%2BC3cXht1yisLo%3D, PID: 20044131
    • Wang H, Xu K, Liu L, Tan JPK, Chen Y, Li Y, Fan W, Wei Z, Sheng J, Yang Y-Y, Li L (2010) The efficacy of self-assembled cationic antimicrobial peptide nanoparticles against Cryptococcus neoformans for the treatment of meningitis. Biomaterials 31(10):2874–2881
    • (2010) Biomaterials , vol.31 , Issue.10 , pp. 2874-2881
    • Wang, H.1    Xu, K.2    Liu, L.3    Tan, J.P.K.4    Chen, Y.5    Li, Y.6    Fan, W.7    Wei, Z.8    Sheng, J.9    Yang, Y.-Y.10    Li, L.11
  • 232
    • 84863229777 scopus 로고    scopus 로고
    • Reprogramming the genetic code: from triplet to quadruplet codes
    • COI: 1:CAS:528:DC%2BC38XhtFSmur4%3D, PID: 22262408
    • Wang K, Schmied WH, Chin JW (2012) Reprogramming the genetic code: from triplet to quadruplet codes. Angew Chem Int Ed Engl 51(10):2288–2297
    • (2012) Angew Chem Int Ed Engl , vol.51 , Issue.10 , pp. 2288-2297
    • Wang, K.1    Schmied, W.H.2    Chin, J.W.3
  • 233
    • 84903701599 scopus 로고    scopus 로고
    • High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments
    • COI: 1:CAS:528:DC%2BC2cXisFenurw%3D, PID: 24463069
    • Wang G, Mishra B, Epand RF, Epand RM (2014) High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments. Biochim Biophys Acta 1838(9):2160–2172
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.9 , pp. 2160-2172
    • Wang, G.1    Mishra, B.2    Epand, R.F.3    Epand, R.M.4
  • 235
    • 2442550833 scopus 로고    scopus 로고
    • Encapsulation of nisin and lysozyme in liposomes enhances efficacy against Listeria monocytogenes
    • COI: 1:CAS:528:DC%2BD2cXksleqtro%3D, PID: 15151228
    • Were LM, Bruce B, Davidson PM, Weiss J (2004) Encapsulation of nisin and lysozyme in liposomes enhances efficacy against Listeria monocytogenes. J Food Prot 67(5):922–927
    • (2004) J Food Prot , vol.67 , Issue.5 , pp. 922-927
    • Were, L.M.1    Bruce, B.2    Davidson, P.M.3    Weiss, J.4
  • 236
    • 0346494756 scopus 로고    scopus 로고
    • The Peptaibol database: a database for sequences and structures of naturally occurring peptaibols
    • COI: 1:CAS:528:DC%2BD3sXhtVSrurjK, PID: 14681489
    • Whitmore L, Wallace BA (2004) The Peptaibol database: a database for sequences and structures of naturally occurring peptaibols. Nucleic Acids Res 32:D593–D594
    • (2004) Nucleic Acids Res , vol.32 , pp. 593-594
    • Whitmore, L.1    Wallace, B.A.2
  • 237
    • 84887989699 scopus 로고    scopus 로고
    • Antiviral mechanisms of human defensins
    • COI: 1:CAS:528:DC%2BC3sXhs1CrtLnN, PID: 24095897
    • Wilson SS, Wiens ME, Smith JG (2013) Antiviral mechanisms of human defensins. J Mol Biol 425(24):4965–4980
    • (2013) J Mol Biol , vol.425 , Issue.24 , pp. 4965-4980
    • Wilson, S.S.1    Wiens, M.E.2    Smith, J.G.3
  • 238
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • COI: 1:CAS:528:DC%2BC3cXhtVGgsLbF, PID: 20698568
    • Wimley WC (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem Biol 5(10):905–917
    • (2010) ACS Chem Biol , vol.5 , Issue.10 , pp. 905-917
    • Wimley, W.C.1
  • 239
    • 79955669580 scopus 로고    scopus 로고
    • Antimicrobial peptides: successes, challenges and unanswered questions
    • COI: 1:CAS:528:DC%2BC3MXht1Clsbo%3D, PID: 21225255
    • Wimley W, Hristova K (2011) Antimicrobial peptides: successes, challenges and unanswered questions. J Membr Biol 239(1–2):27–34
    • (2011) J Membr Biol , vol.239 , Issue.1-2 , pp. 27-34
    • Wimley, W.1    Hristova, K.2
  • 240
    • 0029952823 scopus 로고    scopus 로고
    • Pseudo-prolines as a solubilizing, structure-disrupting protection technique in peptide synthesis
    • Wöhr T, Wahl F, Nefzi A, Rohwedder B, Sato T, Sun X, Mutter M (1996) Pseudo-prolines as a solubilizing, structure-disrupting protection technique in peptide synthesis. J Am Chem Soc 118(39):9218–9227
    • (1996) J Am Chem Soc , vol.118 , Issue.39 , pp. 9218-9227
    • Wöhr, T.1    Wahl, F.2    Nefzi, A.3    Rohwedder, B.4    Sato, T.5    Sun, X.6    Mutter, M.7
  • 241
    • 84902056021 scopus 로고    scopus 로고
    • Modern cancer drug discovery: integrating targets, technologies, and treatments for personalized medicine
    • Neidle S, (ed), Academic, San Diego:
    • Workman P, Collins I (2014) Modern cancer drug discovery: integrating targets, technologies, and treatments for personalized medicine. In: Neidle S (ed) Cancer drug design and discovery, 2nd edn. Academic, San Diego, pp 3–53
    • (2014) Cancer drug design and discovery , pp. 3-53
    • Workman, P.1    Collins, I.2
  • 242
    • 84875887004 scopus 로고    scopus 로고
    • Design, expression and characterization of the hybrid antimicrobial peptide LHP7, connected by a flexible linker, against Staphylococcus and Streptococcus
    • COI: 1:CAS:528:DC%2BC3sXislymtrk%3D
    • Xi D, Teng D, Wang X, Mao R, Yang Y, Xiang W, Wang J (2013) Design, expression and characterization of the hybrid antimicrobial peptide LHP7, connected by a flexible linker, against Staphylococcus and Streptococcus. Process Biochem 48(3):453–461
    • (2013) Process Biochem , vol.48 , Issue.3 , pp. 453-461
    • Xi, D.1    Teng, D.2    Wang, X.3    Mao, R.4    Yang, Y.5    Xiang, W.6    Wang, J.7
  • 243
    • 0036467968 scopus 로고    scopus 로고
    • Inhibition of intracellular macromolecular synthesis in Staphylococcus aureus by thrombin-induced platelet microbicidal proteins
    • COI: 1:CAS:528:DC%2BD38XhsVKkurw%3D, PID: 11807717
    • Xiong Y-Q, Bayer AS, Yeaman MR (2002) Inhibition of intracellular macromolecular synthesis in Staphylococcus aureus by thrombin-induced platelet microbicidal proteins. J Infect Dis 185(3):348–356
    • (2002) J Infect Dis , vol.185 , Issue.3 , pp. 348-356
    • Xiong, Y.-Q.1    Bayer, A.S.2    Yeaman, M.R.3
  • 244
    • 39649091872 scopus 로고    scopus 로고
    • Eukaryotic expression and antimicrobial spectrum determination of the peptide tachyplesin II
    • COI: 1:CAS:528:DC%2BD1cXitlCjt70%3D, PID: 18249136
    • Xu F, Meng K, Wang Y-R, Luo H-Y, Yang P-L, Wu N-F, Fan Y-L, Yao B (2008) Eukaryotic expression and antimicrobial spectrum determination of the peptide tachyplesin II. Protein Expr Purif 58(2):175–183
    • (2008) Protein Expr Purif , vol.58 , Issue.2 , pp. 175-183
    • Xu, F.1    Meng, K.2    Wang, Y.-R.3    Luo, H.-Y.4    Yang, P.-L.5    Wu, N.-F.6    Fan, Y.-L.7    Yao, B.8
  • 245
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • COI: 1:CAS:528:DC%2BD3sXisVKgsLg%3D, PID: 12615953
    • Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55(1):27–55
    • (2003) Pharmacol Rev , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 246
    • 79960936612 scopus 로고    scopus 로고
    • Multifunctional cationic host defence peptides and their clinical applications
    • COI: 1:CAS:528:DC%2BC3MXntlajurk%3D, PID: 21573784
    • Yeung AT, Gellatly SL, Hancock RE (2011) Multifunctional cationic host defence peptides and their clinical applications. Cell Mol Life Sci 68(13):2161–2176
    • (2011) Cell Mol Life Sci , vol.68 , Issue.13 , pp. 2161-2176
    • Yeung, A.T.1    Gellatly, S.L.2    Hancock, R.E.3
  • 247
    • 0023818378 scopus 로고
    • Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae
    • COI: 1:CAS:528:DyaL1cXktVWltr8%3D, PID: 2829884
    • Yoshimura K, Toibana A, Nakahama K (1988) Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae. Biochem Biophys Res Commun 150(2):794–801
    • (1988) Biochem Biophys Res Commun , vol.150 , Issue.2 , pp. 794-801
    • Yoshimura, K.1    Toibana, A.2    Nakahama, K.3
  • 248
    • 67049107801 scopus 로고    scopus 로고
    • Antifungal activities of natural and synthetic iron chelators alone and in combination with azole and polyene antibiotics against Aspergillus fumigatus
    • COI: 1:CAS:528:DC%2BD1MXntFGksLc%3D
    • Zarember KA, Cruz AR, Huang C-Y, Gallin JI (2009) Antifungal activities of natural and synthetic iron chelators alone and in combination with azole and polyene antibiotics against Aspergillus fumigatus. Antimicrob Agents Ch 53(6):2654–2656
    • (2009) Antimicrob Agents Ch , vol.53 , Issue.6 , pp. 2654-2656
    • Zarember, K.A.1    Cruz, A.R.2    Huang, C.-Y.3    Gallin, J.I.4
  • 249
    • 0013866176 scopus 로고
    • Cationic proteins of polymorphonuclear leukocyte lysosomes. 2. Composition properties and mechanism of antibacterial action
    • COI: 1:CAS:528:DyaF28XltlWrsg%3D%3D, PID: 5934974
    • Zeya HI, Spitznag JK (1966) Cationic proteins of polymorphonuclear leukocyte lysosomes. 2. Composition properties and mechanism of antibacterial action. J Bacteriol 91(2):755
    • (1966) J Bacteriol , vol.91 , Issue.2 , pp. 755
    • Zeya, H.I.1    Spitznag, J.K.2
  • 250
    • 77958124580 scopus 로고    scopus 로고
    • Dual functions of the human antimicrobial peptide LL-37—target membrane perturbation and host cell cargo delivery
    • COI: 1:CAS:528:DC%2BC3cXhtlequr7I, PID: 20036634
    • Zhang X, Oglęcka K, Sandgren S, Belting M, Esbjörner EK, Nordén B, Gräslund A (2010) Dual functions of the human antimicrobial peptide LL-37—target membrane perturbation and host cell cargo delivery. Biochim Biophys Acta 1798(12):2201–2208
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.12 , pp. 2201-2208
    • Zhang, X.1    Oglęcka, K.2    Sandgren, S.3    Belting, M.4    Esbjörner, E.K.5    Nordén, B.6    Gräslund, A.7
  • 251
    • 85028101466 scopus 로고    scopus 로고
    • Evolutionary origin of β-defensins
    • COI: 1:CAS:528:DC%2BC38XlslSgur0%3D, PID: 22369779
    • Zhu S, Gao B (2013) Evolutionary origin of β-defensins. Dev Comp Immunol 39(1–2):79–84
    • (2013) Dev Comp Immunol , vol.39 , Issue.1-2 , pp. 79-84
    • Zhu, S.1    Gao, B.2
  • 252
    • 79952265946 scopus 로고    scopus 로고
    • Unraveling the mechanism of nanotube formation by chiral self-assembly of amphiphiles
    • COI: 1:CAS:528:DC%2BC3MXmslKisA%3D%3D, PID: 21244023
    • Ziserman L, Lee H-Y, Raghavan SR, Mor A, Danino D (2011) Unraveling the mechanism of nanotube formation by chiral self-assembly of amphiphiles. J Am Chem Soc 133(8):2511–2517
    • (2011) J Am Chem Soc , vol.133 , Issue.8 , pp. 2511-2517
    • Ziserman, L.1    Lee, H.-Y.2    Raghavan, S.R.3    Mor, A.4    Danino, D.5
  • 253
    • 84925478412 scopus 로고    scopus 로고
    • Zoladex Worldwide Sales
    • Zoladex Worldwide Sales (2011b) http://www.evaluategroup.com/Universal/View.aspx?type=Entity&entityType=Product&id=21572&lType=modData&componentID=1002#&&_ViewArgs=%7b%22_EntityType%22%3a0%2c%22_Parameters%22%3a%7b%22_ContextData%22%3a%22zoladex%22%7d%2c%22_Type%22%3a5%7d.
    • (2011)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.