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Volumn 51, Issue 2, 2012, Pages 653-664

Structure, dynamics, and antimicrobial and immune modulatory activities of human LL-23 and its single-residue variants mutated on the basis of homologous primate cathelicidins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; AMPHIPATHIC; ANTI-BACTERIAL ACTIVITY; ANTI-MICROBIAL ACTIVITY; BACKBONE DYNAMICS; CATHELICIDIN; CHEMOKINES; CYTOKINES; HELICAL STRUCTURES; HETERONUCLEAR; HOST DEFENSE; HOT SPOT; HUMAN PERIPHERAL BLOOD; HYDROGEN-DEUTERIUM EXCHANGE; HYDROPHOBIC SURFACES; IMMUNE MODULATORS; LIPOPOLYSACCHARIDES; MAMMALIAN CELLS; N-TERMINALS; NATURAL PEPTIDE; NMR STRUCTURES; SECONDARY STRUCTURES; TWO DOMAINS;

EID: 84862907676     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2016266     Document Type: Article
Times cited : (50)

References (63)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms Nature 415, 389-395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • DOI 10.1046/j.1365-2796.2003.01228.x
    • Boman, H. G. (2003) Antibacterial peptides: Basic facts and emerging concepts J. Intern. Med. 254, 197-215 (Pubitemid 37070221)
    • (2003) Journal of Internal Medicine , vol.254 , Issue.3 , pp. 197-215
    • Boman, H.G.1
  • 3
    • 69949086979 scopus 로고    scopus 로고
    • Potential of immunomodulatory host defense peptides as novel anti-infectives
    • Easton, D. M., Nijnik, A., Mayer, M. L., and Hancock, R. E. W. (2009) Potential of immunomodulatory host defense peptides as novel anti-infectives Trends Biotechnol. 27, 582-590
    • (2009) Trends Biotechnol. , vol.27 , pp. 582-590
    • Easton, D.M.1    Nijnik, A.2    Mayer, M.L.3    Hancock, R.E.W.4
  • 4
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • DOI 10.1016/S0952-7915(01)00303-X
    • Lehrer, R. I. and Ganz, T. (2002) Defensins of vertebrate animals Curr. Opin. Immunol. 14, 96-102 (Pubitemid 34085112)
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 5
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti, M. (2005) The role of cathelicidins in the innate host defenses of mammals Curr. Issues Mol. Biol. 7, 179-196 (Pubitemid 41051685)
    • (2005) Current Issues in Molecular Biology , vol.7 , Issue.2 , pp. 179-196
    • Zanetti, M.1
  • 6
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y. and Gallo, R. L. (2009) AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense Trends Immunol. 30, 131-141
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 7
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang, Z. and Wang, G. (2004) APD: The antimicrobial peptide database Nucleic Acids Res. 32, D590-D592
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.2
  • 8
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • Wang, G., Li, X., and 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
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 9
    • 33645051715 scopus 로고    scopus 로고
    • Antimicrobial skin peptides and proteins
    • Schroder, J. M. and Harder, J. (2006) Antimicrobial skin peptides and proteins Cell. Mol. Life Sci. 63, 469-486
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 469-486
    • Schroder, J.M.1    Harder, J.2
  • 10
    • 38549098276 scopus 로고    scopus 로고
    • Antimicrobial peptides in human skin disease
    • Yamasaki, K. and Gallo, R. L. (2008) Antimicrobial peptides in human skin disease Eur. J. Dermatol. 18, 1-11
    • (2008) Eur. J. Dermatol. , vol.18 , pp. 1-11
    • Yamasaki, K.1    Gallo, R.L.2
  • 17
    • 34548487515 scopus 로고    scopus 로고
    • On-resin cleavage of bacterially expressed fusion proteins for purification of active recombinant peptides SK-29, KR-20, LL-29, and LL-23 from human sweat or skin
    • DOI 10.1016/j.pep.2007.04.023, PII S104659280700126X
    • Li, Y., Li, X., and Wang, G. (2007) On-resin cleavage of bacterially expressed fusion proteins for purification of active recombinant peptides SK-29, KR-20, LL-29, and LL-23 from human sweat or skin Protein Expression Purif. 55, 395-405 (Pubitemid 47376882)
    • (2007) Protein Expression and Purification , vol.55 , Issue.2 , pp. 395-405
    • Li, Y.1    Li, X.2    Wang, G.3
  • 18
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • 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, 32637-32643
    • (2008) J. Biol. Chem. , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 19
    • 14044268292 scopus 로고    scopus 로고
    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor
    • DOI 10.1074/jbc.M410116200
    • Wang, G., Li, Y., and Li, X. (2005) Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor J. Biol. Chem. 280, 5803-5811 (Pubitemid 40280061)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5803-5811
    • Wang, G.1    Li, Y.2    Li, X.3
  • 20
    • 30744475282 scopus 로고    scopus 로고
    • The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides
    • DOI 10.1096/fj.05-4406com
    • Dorschner, R. A., Lopez-Garcia, B., Peschel, A., Kraus, D., Morikawa, K., Nizet, V., and Gallo, R. L. (2006) The mammalian ionic environment dictates microbial susceptibility to antimicrobial defense peptides FASEB J. 20, 35-42 (Pubitemid 43100473)
    • (2006) FASEB Journal , vol.20 , Issue.1 , pp. 35-42
    • Dorschner, R.A.1    Lopez-Garcia, B.2    Peschel, A.3    Kraus, D.4    Morikawa, K.5    Nizet, V.6    Gallo, R.L.7
  • 21
    • 39449086721 scopus 로고    scopus 로고
    • Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances
    • DOI 10.1038/nprot.2007.521, PII NPROT.2007.521
    • Wiegand, I., Hilpert, K., and Hancock, R. E. W. (2008) Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances Nat. Protoc. 3, 163-175 (Pubitemid 351266501)
    • (2008) Nature Protocols , vol.3 , Issue.2 , pp. 163-175
    • Wiegand, I.1    Hilpert, K.2    Hancock, R.E.W.3
  • 23
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • DOI 10.1074/jbc.274.1.29
    • Wu, M. and Hancock, R. E. W. (1999) Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane J. Biol. Chem. 274, 29-35 (Pubitemid 29035025)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 29-35
    • Wu, M.1    Hancock, R.E.W.2
  • 24
    • 3042746872 scopus 로고    scopus 로고
    • Effects of detergent alkyl chain length and chemical structure on the properties of a micelle-bound bacterial membrane targeting peptide
    • DOI 10.1016/j.ab.2004.03.074, PII S0003269704003677
    • Keifer, P. A., Peterkofsky, A. P., and Wang, G. (2004) Effects of detergent alkyl chain length and chemical structure on the properties of a micelle-bound bacterial membrane targeting peptide Anal. Biochem. 331, 33-39 (Pubitemid 38881555)
    • (2004) Analytical Biochemistry , vol.331 , Issue.1 , pp. 33-39
    • Keifer, P.A.1    Peterkofsky, A.2    Wang, G.3
  • 25
    • 0001098519 scopus 로고
    • Diffusion-ordered two-dimensional nuclear magnetic resonance spectroscopy
    • Morris, K. F. and Johnson, C. S. (1992) Diffusion-ordered two-dimensional nuclear magnetic resonance spectroscopy J. Am. Chem. Soc. 114, 3139-3141
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3139-3141
    • Morris, K.F.1    Johnson, C.S.2
  • 26
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy J. Chem. Phys. 71, 4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 27
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. and Davis, D. G. (1985) MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy J. Magn. Reson. 65, 355-360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 29
    • 33646010991 scopus 로고    scopus 로고
    • Structural biology of antimicrobial peptides by NMR spectroscopy
    • Wang, G. (2006) Structural biology of antimicrobial peptides by NMR spectroscopy Curr. Org. Chem. 10, 569-581
    • (2006) Curr. Org. Chem. , vol.10 , pp. 569-581
    • Wang, G.1
  • 30
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P. A., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114, 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.A.2    Saarinen, T.3
  • 31
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A. and Grzesiek, S. (1993) Methodological advances in protein NMR Acc. Chem. Res. 26, 131-138
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 32
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids: IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., and Wüthrich, K. (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy J. Biomol. NMR 12, 1-23 (Pubitemid 128512831)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wuthrich, K.8
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 0000041361 scopus 로고
    • A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. (1991) A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams J. Magn. Reson. 95, 214-220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 36
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 38
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures J. Mol. Graphics 14, 51-55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 42
    • 1542724426 scopus 로고    scopus 로고
    • The Human Cationic Peptide LL-37 Induces Activation of the Extracellular Signal-Regulated Kinase and p38 Kinase Pathways in Primary Human Monocytes
    • Bowdish, D. M., Davidson, D. J., Speert, D. P., and Hancock, R. E. W. (2004) The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes J. Immunol. 172, 3758-3765 (Pubitemid 38337960)
    • (2004) Journal of Immunology , vol.172 , Issue.6 , pp. 3758-3765
    • Bowdish, D.M.E.1    Davidson, D.J.2    Speert, D.P.3    Hancock, R.E.W.4
  • 43
    • 0037406076 scopus 로고    scopus 로고
    • Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles
    • DOI 10.1110/ps.0301503
    • Wang, G., Keifer, P. A., and Peterkofsky, A. (2003) Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles Protein Sci. 12, 1087-1096 (Pubitemid 36505442)
    • (2003) Protein Science , vol.12 , Issue.5 , pp. 1087-1096
    • Wang, G.1    Keifer, P.A.2    Peterkofsky, A.3
  • 44
    • 2442681552 scopus 로고    scopus 로고
    • Short-chain diacyl phosphatidylglycerols: Which one to choose for the NMR structural determination of a membrane-associated peptide from Escherichia coli?
    • Second International Conference on Biomedical Spectroscopy: From the Bench to the Clinic
    • Wang, G., Keifer, P. A., and Peterkofsky, A. (2004) Short-chain diacyl phosphatidylglycerols: Which one to choose for NMR structural determination of a membrane-associated peptide from Escherichia coli ? Spectroscopy 18, 257-264 (Pubitemid 38668503)
    • (2004) Spectroscopy , vol.18 , Issue.2 , pp. 257-264
    • Wang, G.1    Keifer, P.A.2    Peterkofsky, A.3
  • 46
    • 57749108450 scopus 로고    scopus 로고
    • NMR studies of a model antimicrobial peptide in the micelles of SDS, dodecylphosphocholine, or dioctanoylphosphatidylglycerol
    • Wang, G. (2008) NMR studies of a model antimicrobial peptide in the micelles of SDS, dodecylphosphocholine, or dioctanoylphosphatidylglycerol Open Magn. Reson. J. 1, 9-15
    • (2008) Open Magn. Reson. J. , vol.1 , pp. 9-15
    • Wang, G.1
  • 48
    • 43949083747 scopus 로고    scopus 로고
    • NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles
    • DOI 10.1021/bi702036s
    • Porcelli, F., Verardi, R., Shi, L., Henzler-Wilderman, K. A., Ramamoorthy, A., and Veglia, G. (2008) NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles Biochemistry 47, 5565-5572 (Pubitemid 351705167)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5565-5572
    • Porcelli, F.1    Verardi, R.2    Shi, L.3    Henzler-Wildman, K.A.4    Ramamoorthy, A.5    Veglia, G.6
  • 49
    • 33646597266 scopus 로고    scopus 로고
    • Solution structures of human ll-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region
    • DOI 10.1021/ja0584875
    • Li, X., Li, Y., Han, H., Miller, D. W., and Wang, G. (2006) Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region J. Am. Chem. Soc. 128, 5776-5785 (Pubitemid 43724381)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.17 , pp. 5776-5785
    • Li, X.1    Li, Y.2    Han, H.3    Miller, D.W.4    Wang, G.5
  • 50
    • 33746014692 scopus 로고    scopus 로고
    • Evolution of the primate cathelicidin: Correlation between structural variations and antimicrobial activity
    • DOI 10.1074/jbc.M511108200
    • Zelezetsky, I., Pontillo, A., Puzzi, L., Antcheva, N., Segat, L., Pacor, S., Crovella, S., and Tossi, A. (2006) Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity J. Biol. Chem. 281, 19861-19871 (Pubitemid 44065759)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.29 , pp. 19861-19871
    • Zelezetsky, I.1    Pontillo, A.2    Puzzi, L.3    Antcheva, N.4    Segat, L.5    Pacor, S.6    Crovella, S.7    Tossi, A.8
  • 51
    • 11144348648 scopus 로고    scopus 로고
    • Interaction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells
    • DOI 10.1128/IAI.73.1.583-591.2005
    • Lau, Y. E., Rozek, A., Scott, M. G., Goosney, D. L., Davidson, D. J., and Hancock, R. E. W. (2005) Interaction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells Infect. Immun. 73, 583-591 (Pubitemid 40041153)
    • (2005) Infection and Immunity , vol.73 , Issue.1 , pp. 583-591
    • Lau, Y.E.1    Rozek, A.2    Scott, M.G.3    Goosney, D.L.4    Davidson, D.J.5    Hancock, R.E.W.6
  • 55
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides
    • Rosenfeld, Y., Papo, N., and Shai, Y. (2006) Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides J. Biol. Chem. 281, 1636-1643
    • (2006) J. Biol. Chem. , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 56
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner, J., Cho, Y., Dinh, N.-N., Waring, A. J., and Lehrer, R. I. (1998) Activities of LL-37, a cathelin-associated antimicrobial peptides of human neutrophils Antimicrob. Agents Chemother. 42, 2206-2214 (Pubitemid 28420351)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.9 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.-N.3    Waring, A.J.4    Lehrer, R.I.5
  • 57
    • 0036731921 scopus 로고    scopus 로고
    • Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues
    • DOI 10.1128/CDLI.9.5.972-982.2002
    • Nagaoka, I., Hirota, S., Niyonsaba, F., Hirata, M., Adachi, Y., Tamura, H., Tanaka, S., and Heumann, D. (2002) Augmentation of the lipopolysaccharide- neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobal peptides by replacement with hydrophbic and cationic amino acid residues Clin. Diagn. Lab. Immunol. 9, 972-982 (Pubitemid 34988462)
    • (2002) Clinical and Diagnostic Laboratory Immunology , vol.9 , Issue.5 , pp. 972-982
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3    Hirata, M.4    Adachi, Y.5    Tamura, H.6    Tanaka, S.7    Heumann, D.8
  • 59
    • 77956363683 scopus 로고    scopus 로고
    • Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications
    • Wu, W. K. K., Wang, G., Coffelt, S. B., Betancourt, A. M., Lee, C. W., Yu, J., Sung, J. J. Y., and Cho, C. H. (2010) Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications Int. J. Cancer 127, 1741-1747
    • (2010) Int. J. Cancer , vol.127 , pp. 1741-1747
    • Wu, W.K.K.1    Wang, G.2    Coffelt, S.B.3    Betancourt, A.M.4    Lee, C.W.5    Yu, J.6    Sung, J.J.Y.7    Cho, C.H.8
  • 62
    • 0842325226 scopus 로고    scopus 로고
    • MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance
    • DOI 10.1016/S0378-1097(03)00921-2
    • Staubiz, P., Neumann, H., Schneider, T., Wiedemann, I., and Peschel, A. (2004) MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance FEMS Microbiol. Lett. 231, 67-71 (Pubitemid 38180561)
    • (2004) FEMS Microbiology Letters , vol.231 , Issue.1 , pp. 67-71
    • Staubitz, P.1    Neumann, H.2    Schneider, T.3    Wiedemann, I.4    Peschel, A.5


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