메뉴 건너뛰기




Volumn 16, Issue 2, 2016, Pages 206-219

Disulfide bridges in defensins

Author keywords

Antibiotics; Chemotactic activity; Defensin; Disulfide bond; Structure function relationship; Truncated peptide; hairpin structure

Indexed keywords

ALPHA DEFENSIN; ANTIMICROBIAL CATIONIC PEPTIDE; BETA DEFENSIN; BOVINE NEUTROPHIL BETA DEFENSIN 12; CRYPTDIN 4; DEFENSIN; DISULFIDE; DITHIOTHREITOL; HUMAN NEUTROPHIL PEPTIDE 1; HUMAN NEUTROPHIL PEPTIDE 2; HUMAN NEUTROPHIL PEPTIDE 3; INSECT DEFENSIN; MATRILYSIN; PLECTASIN; PROTEIN HBD1; PROTEIN HBD2; PROTEIN HBD3; PROTEIN RTD 1; PROTEIN RTD 2; RETROCYCLIN 1; RETROCYCLIN 2; THETA DEFENSIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT;

EID: 84974622234     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026615666150701115911     Document Type: Review
Times cited : (28)

References (76)
  • 1
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • Lehrer, R. I. Primate defensins. Nat. Rev. Micro., 2004, 2 (9), 727-738
    • (2004) Nat. Rev. Micro. , vol.2 , Issue.9 , pp. 727-738
    • Lehrer, R.I.1
  • 2
    • 33745698864 scopus 로고    scopus 로고
    • Defensins in innate antiviral immunity
    • Klotman, M. E.; Chang, T. L. Defensins in innate antiviral immunity. Nat. Rev. Immunol., 2006, 6 (6), 447-456
    • (2006) Nat. Rev. Immunol. , vol.6 , Issue.6 , pp. 447-456
    • Klotman, M.E.1    Chang, T.L.2
  • 3
    • 34548039239 scopus 로고    scopus 로고
    • Defensins in the immunology of bacterial infections
    • Menendez, A.; Brett Finlay, B. Defensins in the immunology of bacterial infections. Curr. Opin. Immunol., 2007, 19 (4), 385-391
    • (2007) Curr. Opin. Immunol. , vol.19 , Issue.4 , pp. 385-391
    • Menendez, A.1    Brett Finlay, B.2
  • 4
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz, T. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol., 2003, 3 (9), 710-720
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 6
    • 67349088413 scopus 로고    scopus 로고
    • Plant defensins-Prospects for the biological functions and biotechnological properties
    • Carvalho, A. d. O.; Gomes, V. M. Plant defensins-Prospects for the biological functions and biotechnological properties. Peptides, 2009, 30 (5), 1007-1020
    • (2009) Peptides , vol.30 , Issue.5 , pp. 1007-1020
    • Carvalho, A.D.O.1    Gomes, V.M.2
  • 7
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • Lehrer, R. I.; Ganz, T. Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol., 1999, 11 (1), 23-27
    • (1999) Curr. Opin. Immunol. , vol.11 , Issue.1 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 8
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer, R. I.; Ganz, T. Defensins of vertebrate animals. Curr. Opin. Immunol., 2002, 14 (1), 96-102
    • (2002) Curr. Opin. Immunol. , vol.14 , Issue.1 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 9
    • 83655193502 scopus 로고    scopus 로고
    • α-Defensins in human innate immunity
    • Lehrer, R. I.; Lu, W. α-Defensins in human innate immunity. Immunol. Rev., 2012, 245 (1), 84-112
    • (2012) Immunol. Rev. , vol.245 , Issue.1 , pp. 84-112
    • Lehrer, R.I.1    Lu, W.2
  • 11
    • 85028101466 scopus 로고    scopus 로고
    • Evolutionary origin of beta-defensins
    • Zhu, S.; Gao, B. Evolutionary origin of beta-defensins. Dev. Comp. Immunol., 2013, 39 (1-2), 79-84
    • (2013) Dev. Comp. Immunol. , vol.39 , Issue.1-2 , pp. 79-84
    • Zhu, S.1    Gao, B.2
  • 13
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople, V.; Krukemeyer, A.; Ramamoorthy, A. The human beta-defensin-3, an antibacterial peptide with multiple biological functions. Biochim. Biophys. Acta., 2006, 1758 (9), 1499-1512
    • (2006) Biochim. Biophys. Acta. , vol.1758 , Issue.9 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 16
    • 0037407586 scopus 로고    scopus 로고
    • Retrocyclin, an Antiretroviral θ-Defensin, Is a Lectin
    • Wang, W.; Cole, A. M.; Hong, T.; Waring, A. J.; Lehrer, R. I. Retrocyclin, an Antiretroviral θ-Defensin, Is a Lectin. J. Immunol., 2003, 170 (9), 4708-4716
    • (2003) J. Immunol. , vol.170 , Issue.9 , pp. 4708-4716
    • Wang, W.1    Cole, A.M.2    Hong, T.3    Waring, A.J.4    Lehrer, R.I.5
  • 17
    • 84896735396 scopus 로고    scopus 로고
    • An Insect Defensin-Derived β-Hairpin Peptide with Enhanced Antibacterial Activity
    • Gao, B.; Zhu, S. An Insect Defensin-Derived β-Hairpin Peptide with Enhanced Antibacterial Activity. ACS Chem. Bio., 2014, 9 (2), 405-413
    • (2014) ACS Chem. Bio. , vol.9 , Issue.2 , pp. 405-413
    • Gao, B.1    Zhu, S.2
  • 18
    • 0037260694 scopus 로고    scopus 로고
    • The Three-dimensional Solution Structure of NaD1, a New Floral Defensin from Nicotiana alata and its Application to a Homology Model of the Crop Defense Protein alfAFP
    • Lay, F. T.; Schirra, H. J.; Scanlon, M. J.; Anderson, M. A.; Craik, D. J. The Three-dimensional Solution Structure of NaD1, a New Floral Defensin from Nicotiana alata and its Application to a Homology Model of the Crop Defense Protein alfAFP. J. Mol. Biol., 2003, 325 (1), 175-188
    • (2003) J. Mol. Biol. , vol.325 , Issue.1 , pp. 175-188
    • Lay, F.T.1    Schirra, H.J.2    Scanlon, M.J.3    Anderson, M.A.4    Craik, D.J.5
  • 19
  • 20
    • 27144432006 scopus 로고    scopus 로고
    • Phyligenetic distribution, functional epitopes and evolution of the CSαβ superfamily
    • Zhu, S.; Gao, B.; Tytgat, J. Phyligenetic distribution, functional epitopes and evolution of the CSαβ superfamily. Cell. Mol. Life Sci., 2005, 62, 2257-2269
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2257-2269
    • Zhu, S.1    Gao, B.2    Tytgat, J.3
  • 21
    • 0029645290 scopus 로고
    • Solution Structure of the Cardiostimulant Polypeptide Anthopleurin-B and Comparison with Anthopleurin-A
    • Monks, S. A.; Pallaghy, P. K.; Scanlon, M. J.; Norton, R. S. Solution Structure of the Cardiostimulant Polypeptide Anthopleurin-B and Comparison with Anthopleurin-A. Structure, 1995, 3 (8), 791-803
    • (1995) Structure , vol.3 , Issue.8 , pp. 791-803
    • Monks, S.A.1    Pallaghy, P.K.2    Scanlon, M.J.3    Norton, R.S.4
  • 22
    • 0036159378 scopus 로고    scopus 로고
    • A proposed 3D structure for crotamine based on homology building, molecular simulations and circular dichroism
    • Siqueira, A. M.; Martins, N. F.; De Lima, M. E.; Diniz, C. R.; Cartier, A.; Brown, D.; Maigret, B. A proposed 3D structure for crotamine based on homology building, molecular simulations and circular dichroism. J. Mol. Graph. Model., 2002, 20 (5), 389-398
    • (2002) J. Mol. Graph. Model. , vol.20 , Issue.5 , pp. 389-398
    • Siqueira, A.M.1    Martins, N.F.2    De Lima, M.E.3    Diniz, C.R.4    Cartier, A.5    Brown, D.6    Maigret, B.7
  • 23
    • 14244258642 scopus 로고    scopus 로고
    • The β-defensin-fold family of polypeptides
    • Torres, A. M.; Kuchel, P. W. The β-defensin-fold family of polypeptides. Toxicon, 2004, 44 (6), 581-588
    • (2004) Toxicon , vol.44 , Issue.6 , pp. 581-588
    • Torres, A.M.1    Kuchel, P.W.2
  • 25
    • 0024973385 scopus 로고
    • Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus
    • Kem, W. R.; Parten, B.; Pennington, M. W.; Price, D. A.; Dunn, B. M. Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus. Biochemistry, 1989, 28 (8), 3483-3489
    • (1989) Biochemistry , vol.28 , Issue.8 , pp. 3483-3489
    • Kem, W.R.1    Parten, B.2    Pennington, M.W.3    Price, D.A.4    Dunn, B.M.5
  • 26
    • 0024595937 scopus 로고
    • Determination of the three-dimensional solution structure of the anti-hypertensive and anti-viral protein BDS-I from the sea anemone Anemonia sulcata: A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Driscoll, P. C.; Gronenborn, A. M.; Beress, L.; Clore, G. M. Determination of the three-dimensional solution structure of the anti-hypertensive and anti-viral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry, 1989, 28, 2188-2198
    • (1989) Biochemistry , vol.28 , pp. 2188-2198
    • Driscoll, P.C.1    Gronenborn, A.M.2    Beress, L.3    Clore, G.M.4
  • 27
    • 0028061984 scopus 로고
    • Interactions between Human Defensins and Lipid Bilayers-Evidence for Formation of Multimeric Pores
    • Wimley, W. C.; Selsted, M. E.; White, S. H. Interactions between Human Defensins and Lipid Bilayers-Evidence for Formation of Multimeric Pores. Protein Sci., 1994, 3 (9), 1362-1373
    • (1994) Protein Sci. , vol.3 , Issue.9 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 28
    • 0037407586 scopus 로고    scopus 로고
    • Retrocyclin, an antiretroviral theta-defensin, is a lectin
    • Wang, W.; Cole, A. M.; Hong, T.; Waring, A. J.; Lehrer, R. I. Retrocyclin, an antiretroviral theta-defensin, is a lectin. J. Immunol., 2003, 170 (9), 4708-4716
    • (2003) J. Immunol. , vol.170 , Issue.9 , pp. 4708-4716
    • Wang, W.1    Cole, A.M.2    Hong, T.3    Waring, A.J.4    Lehrer, R.I.5
  • 29
    • 77958085274 scopus 로고    scopus 로고
    • Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model
    • Wimley, W. C. Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model. ACS Chem. Biol., 2010, 5 (10), 905-917
    • (2010) ACS Chem. Biol. , vol.5 , Issue.10 , pp. 905-917
    • Wimley, W.C.1
  • 31
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted, M. E.; Ouellette, A. J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol., 2005, 6 (6), 551-557
    • (2005) Nat. Immunol. , vol.6 , Issue.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 34
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman, N. H.; Ghosh, D.; Huttner, K. M.; Paterson, Y.; Bevins, C. L. Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature, 2003, 422 (6931), 522-526
    • (2003) Nature , vol.422 , Issue.6931 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 37
    • 0035576242 scopus 로고    scopus 로고
    • Mediators of Innate Immunity That Target Immature, But Not Mature, Dendritic Cells Induce Antitumor Immunity When Genetically Fused with Nonimmunogenic Tumor Antigens
    • Biragyn, A.; Surenhu, M.; Yang, D.; Ruffini, P. A.; Haines, B. A.; Klyushnenkova, E.; Oppenheim, J. J.; Kwak, L. W. Mediators of Innate Immunity That Target Immature, But Not Mature, Dendritic Cells Induce Antitumor Immunity When Genetically Fused with Nonimmunogenic Tumor Antigens. J. Immunol., 2001, 167 (11), 6644-6653
    • (2001) J. Immunol. , vol.167 , Issue.11 , pp. 6644-6653
    • Biragyn, A.1    Surenhu, M.2    Yang, D.3    Ruffini, P.A.4    Haines, B.A.5    Klyushnenkova, E.6    Oppenheim, J.J.7    Kwak, L.W.8
  • 44
    • 34548222649 scopus 로고    scopus 로고
    • Antimicrobial activity of truncated α-defensin (Human neutrophil peptide (HNP)-1) analogues without disulphide bridges
    • Lundy, F. T.; Nelson, J.; Lockhart, D.; Greer, B.; Harriott, P.; Marley, J. J. Antimicrobial activity of truncated α-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges. Mol. Immunol., 2008, 45 (1), 190-193
    • (2008) Mol. Immunol. , vol.45 , Issue.1 , pp. 190-193
    • Lundy, F.T.1    Nelson, J.2    Lockhart, D.3    Greer, B.4    Harriott, P.5    Marley, J.J.6
  • 46
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and Characterization of Human β-Defensin-3, a Novel Human Inducible Peptide Antibiotic
    • Harder, J.; Bartels, J.; Christophers, E.; Schröder, J.-M. Isolation and Characterization of Human β-Defensin-3, a Novel Human Inducible Peptide Antibiotic. J. Biol. Chem., 2001, 276 (8), 5707-5713
    • (2001) J. Biol. Chem. , vol.276 , Issue.8 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.-M.4
  • 48
    • 22244480342 scopus 로고    scopus 로고
    • Structure−Activity Relation of Human β-Defensin 3: Influence of Disulfide Bonds and Cysteine Substitution on Antimicrobial Activity and Cytotoxicity
    • Klüver, E.; Schulz-Maronde, S.; Scheid, S.; Meyer, B.; Forssmann, W.-G.; Adermann, K. Structure−Activity Relation of Human β-Defensin 3: Influence of Disulfide Bonds and Cysteine Substitution on Antimicrobial Activity and Cytotoxicity. Biochemistry, 2005, 44 (28), 9804-9816
    • (2005) Biochemistry , vol.44 , Issue.28 , pp. 9804-9816
    • Klüver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.-G.5    Adermann, K.6
  • 49
    • 0021792199 scopus 로고
    • Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes
    • Lehrer R. I.; Daher K.; Ganz T. E. S. M. Direct inactivation of viruses by MCP-1 and MCP-2, natural peptide antibiotics from rabbit leukocytes. J. Virol., 1986, 54 (2), 467-472
    • (1986) J. Virol. , vol.54 , Issue.2 , pp. 467-472
    • Lehrer, R.I.1    Daher, K.2    Ganz, T.E.S.M.3
  • 52
    • 0028825285 scopus 로고
    • Solution Structure of Bovine Neutrophil.Beta.-Defensin-12: The Peptide Fold of the. Beta.-Defensins Is Identical to That of the Classical Defensins
    • Zimmermann, G. R.; Legault, P.; Selsted, M. E.; Pardi, A. Solution Structure of Bovine Neutrophil.beta.-Defensin-12: The Peptide Fold of the. beta.-Defensins Is Identical to That of the Classical Defensins. Biochemistry, 1995, 34 (41), 13663-13671
    • (1995) Biochemistry , vol.34 , Issue.41 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4
  • 53
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C.; Selsted, M. E.; White, S. H. Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores. Protein Sci., 1994, 3 (9), 1362-1373
    • (1994) Protein Sci. , vol.3 , Issue.9 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 54
    • 0035885441 scopus 로고    scopus 로고
    • Human α-defensin 1 (HNP-1) inhibits adenoviral infection in vitro
    • Bastian, A.; Schäfer, H. Human α-defensin 1 (HNP-1) inhibits adenoviral infection in vitro. Regul. Pept., 2001, 101 (1-3), 157-161
    • (2001) Regul. Pept. , vol.101 , Issue.1-3 , pp. 157-161
    • Bastian, A.1    Schäfer, H.2
  • 58
    • 0033582302 scopus 로고    scopus 로고
    • Synthetic Peptides Corresponding to the β-Hairpin Loop of Rabbit Defensin NP-2 Show Antimicrobial Activity
    • Thennarasu, S.; Nagaraj, R. Synthetic Peptides Corresponding to the β-Hairpin Loop of Rabbit Defensin NP-2 Show Antimicrobial Activity. Biochem. Biophys. Res. Commun., 1999, 254 (2), 281-283
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , Issue.2 , pp. 281-283
    • Thennarasu, S.1    Nagaraj, R.2
  • 59
    • 0036196119 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of synthetic α-defensin HNP-1 and analogs with one, two and three disulfide bridges
    • Mandal, M.; Nagaraj, R. Antibacterial activities and conformations of synthetic α-defensin HNP-1 and analogs with one, two and three disulfide bridges. J. Pept. Res., 2002, 59 (3), 95-104
    • (2002) J. Pept. Res. , vol.59 , Issue.3 , pp. 95-104
    • Mandal, M.1    Nagaraj, R.2
  • 60
    • 0042072743 scopus 로고    scopus 로고
    • Single Disulfide and Linear Analogues Corresponding to the Carboxy-Terminal Segment of Bovine β-Defensin-2: Effects of Introducing the β-Hairpin Nucleating Sequence d-Pro-Gly on Antibacterial Activity and Biophysical Properties
    • Krishnakumari, V.; Sharadadevi, A.; Singh, S.; Nagaraj, R. Single Disulfide and Linear Analogues Corresponding to the Carboxy-Terminal Segment of Bovine β-Defensin-2: Effects of Introducing the β-Hairpin Nucleating Sequence d-Pro-Gly on Antibacterial Activity and Biophysical Properties. Biochemistry, 2003, 42 (31), 9307-9315
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9307-9315
    • Krishnakumari, V.1    Sharadadevi, A.2    Singh, S.3    Nagaraj, R.4
  • 64
    • 33846424608 scopus 로고    scopus 로고
    • Structure-dependent functional properties of human defensin 5
    • Leeuw, D. E.; Burks, S. R.; Li, X.; Kao, J. P. Y.; Lu, W. Structure-dependent functional properties of human defensin 5. FEBS Lett., 2007, 581 (3), 515-520
    • (2007) FEBS Lett. , vol.581 , Issue.3 , pp. 515-520
    • Leeuw, D.E.1    Burks, S.R.2    Li, X.3    Kao, J.P.Y.4    Lu, W.5
  • 65
    • 67650081577 scopus 로고    scopus 로고
    • Structure, Dynamics, and Activity of an All-Cysteine Mutated Human β Defensin-3 Peptide Analogue
    • Chandrababu, K. B.; Ho, B.; Yang, D. Structure, Dynamics, and Activity of an All-Cysteine Mutated Human β Defensin-3 Peptide Analogue. Biochemistry, 2009, 48 (26), 6052-6061
    • (2009) Biochemistry , vol.48 , Issue.26 , pp. 6052-6061
    • Chandrababu, K.B.1    Ho, B.2    Yang, D.3
  • 66
    • 44049109194 scopus 로고    scopus 로고
    • Linear Analogues of Human β-Defensin 3: Concepts for Design of Antimicrobial Peptides with Reduced Cytotoxicity to Mammalian Cells
    • Liu, S.; Zhou, L.; Li, J.; Suresh, A.; Verma, C.; Foo, Y. H.; Yap, E. P. H.; Tan, D. T. H.; Beuerman, R. W. Linear Analogues of Human β-Defensin 3: Concepts for Design of Antimicrobial Peptides with Reduced Cytotoxicity to Mammalian Cells. ChemBioChem, 2008, 9 (6), 964-973
    • (2008) Chembiochem , vol.9 , Issue.6 , pp. 964-973
    • Liu, S.1    Zhou, L.2    Li, J.3    Suresh, A.4    Verma, C.5    Foo, Y.H.6    Yap, E.P.H.7    Tan, D.T.H.8    Beuerman, R.W.9
  • 69
  • 70
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine β-defensin BNBD-12 and analogs:Structural and disulfide bridge requirements for activity
    • Mandal, M.; Jagannadham, M. V.; Nagaraj, R. Antibacterial activities and conformations of bovine β-defensin BNBD-12 and analogs:structural and disulfide bridge requirements for activity. Peptides, 2002, 23 (3), 413-418
    • (2002) Peptides , vol.23 , Issue.3 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 73
    • 80052735816 scopus 로고    scopus 로고
    • Human Defensin 5 Disulfide Array Mutants: Disulfide Bond Deletion Attenuates Antibacterial Activity against Staphylococcus aureus
    • Wanniarachchi, Y. A.; Kaczmarek, P.; Wan, A.; Nolan, E. M. Human Defensin 5 Disulfide Array Mutants: Disulfide Bond Deletion Attenuates Antibacterial Activity against Staphylococcus aureus. Biochemistry, 2011, 50 (37), 8005-8017
    • (2011) Biochemistry , vol.50 , Issue.37 , pp. 8005-8017
    • Wanniarachchi, Y.A.1    Kaczmarek, P.2    Wan, A.3    Nolan, E.M.4
  • 74
    • 27644584146 scopus 로고    scopus 로고
    • Antibacterial Activity of Human Neutrophil Defensin HNP-1 Analogs without Cysteines
    • Varkey, J.; Nagaraj, R. Antibacterial Activity of Human Neutrophil Defensin HNP-1 Analogs without Cysteines. Antimicrob. Agents Chemother., 2005, 49 (11), 4561-4566
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.11 , pp. 4561-4566
    • Varkey, J.1    Nagaraj, R.2
  • 75
    • 16844382886 scopus 로고    scopus 로고
    • Defensin deficiency, intestinal microbes, and the clinical phenotypes of Crohn’s disease
    • Wehkamp, J.; Schmid, M.; Fellermann, K.; Stange, E. F. Defensin deficiency, intestinal microbes, and the clinical phenotypes of Crohn’s disease. J. Leukoc. Biol., 2005, 77 (4), 460-465
    • (2005) J. Leukoc. Biol. , vol.77 , Issue.4 , pp. 460-465
    • Wehkamp, J.1    Schmid, M.2    Fellermann, K.3    Stange, E.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.