메뉴 건너뛰기




Volumn 31, Issue 22, 2015, Pages 6164-6171

Atomic Force Microscopy Reveals the Mechanobiology of Lytic Peptide Action on Bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; BACTERIA; CELLS; CYTOLOGY; ELASTIC MODULI; MICROORGANISMS;

EID: 84931267681     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/acs.langmuir.5b01011     Document Type: Article
Times cited : (43)

References (60)
  • 1
    • 70349739265 scopus 로고    scopus 로고
    • The Clinical Consequences of Antimicrobial Resistance
    • Rice, L. B. The Clinical Consequences of Antimicrobial Resistance Curr. Opin. Microbiol. 2009, 12 (5) 476-481
    • (2009) Curr. Opin. Microbiol. , vol.12 , Issue.5 , pp. 476-481
    • Rice, L.B.1
  • 2
    • 79958844972 scopus 로고    scopus 로고
    • Pathogens Resistant to Antibacterial Agents
    • Chen, L. F.; Chopra, T.; Kaye, K. S. Pathogens Resistant to Antibacterial Agents Med. Clin. North Am. 2011, 95 (4) 647-676
    • (2011) Med. Clin. North Am. , vol.95 , Issue.4 , pp. 647-676
    • Chen, L.F.1    Chopra, T.2    Kaye, K.S.3
  • 3
    • 47749093130 scopus 로고    scopus 로고
    • The Bacteria Fight Back
    • Taubes, G. The Bacteria Fight Back Science 2008, 321 (5887) 356-361
    • (2008) Science , vol.321 , Issue.5887 , pp. 356-361
    • Taubes, G.1
  • 4
    • 33748098214 scopus 로고    scopus 로고
    • Antimicrobial Peptides Versus Invasive Infections
    • Shafer, W., Ed.; Springer: Berlin
    • Yeaman, M. R.; Bayer, A. S. Antimicrobial Peptides Versus Invasive Infections. In Antimicrobial Peptides and Human Disease; Shafer, W., Ed.; Springer: Berlin, 2006; Vol. 306, pp 111-152.
    • (2006) Antimicrobial Peptides and Human Disease , vol.306 , pp. 111-152
    • Yeaman, M.R.1    Bayer, A.S.2
  • 5
    • 0036948138 scopus 로고    scopus 로고
    • Mode of Action of Membrane Active Antimicrobial Peptides
    • Shai, Y. Mode of Action of Membrane Active Antimicrobial Peptides J. Pept. Sci. 2002, 66 (4) 236-248
    • (2002) J. Pept. Sci. , vol.66 , Issue.4 , pp. 236-248
    • Shai, Y.1
  • 6
    • 67649259180 scopus 로고    scopus 로고
    • Membrane Interactions of Antimicrobial Peptides from Australian Frogs
    • Fernandez, D. I.; Gehman, J. D.; Separovic, F. Membrane Interactions of Antimicrobial Peptides from Australian Frogs Biochim. Biophys. Acta, Biomembr. 2009, 1788 (8) 1630-1638
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , Issue.8 , pp. 1630-1638
    • Fernandez, D.I.1    Gehman, J.D.2    Separovic, F.3
  • 7
    • 0031039956 scopus 로고    scopus 로고
    • Peptide Antibiotics
    • Hancock, R. E. W. Peptide Antibiotics Lancet 1997, 349 (9049) 418-422
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 10
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores
    • Yang, L.; Harroun, T. A.; Weiss, T. M.; Ding, L.; Huang, H. W. Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores Biophys. J. 2001, 81 (3) 1475-1485
    • (2001) Biophys. J. , vol.81 , Issue.3 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 11
  • 12
    • 0032443219 scopus 로고    scopus 로고
    • Mode of Action of Linear Amphipathic α-helical Antimicrobial Peptides
    • Oren, Z.; Shai, Y. Mode of Action of Linear Amphipathic α-helical Antimicrobial Peptides J. Pept. Sci. 1998, 47 (6) 451-463
    • (1998) J. Pept. Sci. , vol.47 , Issue.6 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 13
    • 84856455720 scopus 로고    scopus 로고
    • Slow Insertion Kinetics during Interaction of a Model Antimicrobial Peptide with Unilamellar Phospholipid Vesicles
    • Ningsih, Z.; Hossain, M. A.; Wade, J. D.; Clayton, A. H. A.; Gee, M. L. Slow Insertion Kinetics during Interaction of a Model Antimicrobial Peptide with Unilamellar Phospholipid Vesicles Langmuir 2011, 28 (4) 2217-2224
    • (2011) Langmuir , vol.28 , Issue.4 , pp. 2217-2224
    • Ningsih, Z.1    Hossain, M.A.2    Wade, J.D.3    Clayton, A.H.A.4    Gee, M.L.5
  • 14
    • 84887665716 scopus 로고    scopus 로고
    • Translocation of Cationic Amphipathic Peptides across the Membranes of Pure Phospholipid Giant Vesicles
    • Wheaten, S. A.; Ablan, F. D. O.; Spaller, B. L.; Trieu, J. M.; Almeida, P. F. Translocation of Cationic Amphipathic Peptides across the Membranes of Pure Phospholipid Giant Vesicles J. Am. Chem. Soc. 2013, 135 (44) 16517-16525
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.44 , pp. 16517-16525
    • Wheaten, S.A.1    Ablan, F.D.O.2    Spaller, B.L.3    Trieu, J.M.4    Almeida, P.F.5
  • 15
    • 1042267410 scopus 로고    scopus 로고
    • Can we Predict Biological Activity of Antimicrobial Peptides from Their Interactions with Model Phospholipid Membranes?
    • Papo, N.; Shai, Y. Can we Predict Biological Activity of Antimicrobial Peptides from Their Interactions with Model Phospholipid Membranes? Peptides 2003, 24 (11) 1693-1703
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1693-1703
    • Papo, N.1    Shai, Y.2
  • 17
    • 0037960262 scopus 로고    scopus 로고
    • Direct Comparison of Membrane Interactions of Model Peptides Composed of only Leu and Lys Residues
    • Epand, R. F.; Lehrer, R. I.; Waring, A.; Wang, W.; Maget-Dana, R.; Lelièvre, D.; Epand, R. M. Direct Comparison of Membrane Interactions of Model Peptides Composed of only Leu and Lys Residues J. Pept. Sci. 2003, 71 (1) 2-16
    • (2003) J. Pept. Sci. , vol.71 , Issue.1 , pp. 2-16
    • Epand, R.F.1    Lehrer, R.I.2    Waring, A.3    Wang, W.4    Maget-Dana, R.5    Lelièvre, D.6    Epand, R.M.7
  • 18
    • 27744587245 scopus 로고    scopus 로고
    • Force Measurements with the Atomic Force Microscope: Technique, Interpretation and Applications
    • Butt, H. J. R.; Cappella, B.; Kappl, M. Force Measurements with the Atomic Force Microscope: Technique, Interpretation and Applications Surf. Sci. Rep. 2005, 59 (1) 1-152
    • (2005) Surf. Sci. Rep. , vol.59 , Issue.1 , pp. 1-152
    • Butt, H.J.R.1    Cappella, B.2    Kappl, M.3
  • 19
    • 0031106327 scopus 로고    scopus 로고
    • Measuring the Elastic Properties of Biological Samples with the AFM
    • Radmacher, M. Measuring the Elastic Properties of Biological Samples with the AFM Eng. Med. Biol. Mag., IEEE 1997, 16 (2) 47-57
    • (1997) Eng. Med. Biol. Mag., IEEE , vol.16 , Issue.2 , pp. 47-57
    • Radmacher, M.1
  • 21
  • 24
    • 0035907067 scopus 로고    scopus 로고
    • Bacterial Recognition of Mineral Surfaces: Nanoscale Interactions Between Shewanella and α-FeOOH
    • Lower, S. K.; Hochella, M. F.; Beveridge, T. J. Bacterial Recognition of Mineral Surfaces: Nanoscale Interactions Between Shewanella and α-FeOOH Science 2001, 292 (5520) 1360-1363
    • (2001) Science , vol.292 , Issue.5520 , pp. 1360-1363
    • Lower, S.K.1    Hochella, M.F.2    Beveridge, T.J.3
  • 27
    • 79957872824 scopus 로고    scopus 로고
    • Bacterial Surface Appendages Strongly Impact Nanomechanical and Electrokinetic Properties of Escherichia coli Cells Subjected to Osmotic Stress
    • Francius, G.; Polyakov, P.; Merlin, J.; Abe, Y.; Ghigo, J. M.; Merlin, C.; Beloin, C.; Duval, J. F. L. Bacterial Surface Appendages Strongly Impact Nanomechanical and Electrokinetic Properties of Escherichia coli Cells Subjected to Osmotic Stress PLoS One 2011, 6 (5) e20066
    • (2011) PLoS One , vol.6 , Issue.5
    • Francius, G.1    Polyakov, P.2    Merlin, J.3    Abe, Y.4    Ghigo, J.M.5    Merlin, C.6    Beloin, C.7    Duval, J.F.L.8
  • 28
    • 41649105098 scopus 로고    scopus 로고
    • Cationic Peptide-Induced Remodelling of Model Membranes: Direct Visualization by in Situ Atomic Force Microscopy
    • Shaw, J. E.; Epand, R. F.; Hsu, J. C. Y.; Mo, G. C. H.; Epand, R. M.; Yip, C. M. Cationic Peptide-Induced Remodelling of Model Membranes: Direct Visualization by in Situ Atomic Force Microscopy J. Struct. Biol. 2008, 162 (1) 121-138
    • (2008) J. Struct. Biol. , vol.162 , Issue.1 , pp. 121-138
    • Shaw, J.E.1    Epand, R.F.2    Hsu, J.C.Y.3    Mo, G.C.H.4    Epand, R.M.5    Yip, C.M.6
  • 29
    • 70449635387 scopus 로고    scopus 로고
    • Binding, Inactivation, and Adhesion Forces between Antimicrobial Peptide Cecropin P1 and Pathogenic E. coli
    • Strauss, J.; Kadilak, A.; Cronin, C.; Mello, C. M.; Camesano, T. A. Binding, Inactivation, and Adhesion Forces between Antimicrobial Peptide Cecropin P1 and Pathogenic E. coli Colloids Surf., B 2010, 75 (1) 156-164
    • (2010) Colloids Surf., B , vol.75 , Issue.1 , pp. 156-164
    • Strauss, J.1    Kadilak, A.2    Cronin, C.3    Mello, C.M.4    Camesano, T.A.5
  • 30
    • 84865323284 scopus 로고    scopus 로고
    • Efficacy Verification and Microscopic Observations of an Anticancer Peptide, CB1a, on Single Lung Cancer Cell
    • Kao, F. S.; Pan, Y. R.; Hsu, R. Q.; Chen, H. M. Efficacy Verification and Microscopic Observations of an Anticancer Peptide, CB1a, on Single Lung Cancer Cell Biochim. Biophys. Acta, Biomembr. 2012, 1818 (12) 2927-2935
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , Issue.12 , pp. 2927-2935
    • Kao, F.S.1    Pan, Y.R.2    Hsu, R.Q.3    Chen, H.M.4
  • 31
    • 18944366367 scopus 로고    scopus 로고
    • Surface Structure and Nanomechanical Properties of Shewanella putrefaciens Bacteria at Two pH Values (4 and 10) Determined by Atomic Force Microscopy
    • Gaboriaud, F.; Bailet, S.; Dague, E.; Jorand, F. Surface Structure and Nanomechanical Properties of Shewanella putrefaciens Bacteria at Two pH Values (4 and 10) Determined by Atomic Force Microscopy J. Bacteriol. 2005, 187 (11) 3864-3868
    • (2005) J. Bacteriol. , vol.187 , Issue.11 , pp. 3864-3868
    • Gaboriaud, F.1    Bailet, S.2    Dague, E.3    Jorand, F.4
  • 32
    • 84880911323 scopus 로고    scopus 로고
    • Nanomechanics Measurements of Live Bacteria Reveal a Mechanism for Bacterial Cell Protection: the Polysaccharide Capsule in Klebsiella is a Responsive Polymer Hydrogel That Adapts to Osmotic Stress
    • Wang, H.; Wilksch, J. J.; Lithgow, T.; Strugnell, R. A.; Gee, M. L. Nanomechanics Measurements of Live Bacteria Reveal a Mechanism for Bacterial Cell Protection: the Polysaccharide Capsule in Klebsiella is a Responsive Polymer Hydrogel That Adapts to Osmotic Stress Soft Matter 2013, 9 (31) 7560-7567
    • (2013) Soft Matter , vol.9 , Issue.31 , pp. 7560-7567
    • Wang, H.1    Wilksch, J.J.2    Lithgow, T.3    Strugnell, R.A.4    Gee, M.L.5
  • 35
    • 0037458180 scopus 로고    scopus 로고
    • Role of Capsule in Klebsiella pneumoniae Virulence: Lack of Correlation between in Vitro and in Vivo Studies
    • Struve, C.; Krogfelt, K. A. Role of Capsule in Klebsiella pneumoniae Virulence: Lack of Correlation between in Vitro and in Vivo Studies FEMS Microbiol. Lett. 2003, 218 (1) 149-154
    • (2003) FEMS Microbiol. Lett. , vol.218 , Issue.1 , pp. 149-154
    • Struve, C.1    Krogfelt, K.A.2
  • 36
    • 23344443133 scopus 로고    scopus 로고
    • Capsule and Fimbria Interaction in Klebsiella pneumoniae
    • Schembri, M. A.; Blom, J.; Krogfelt, K. A.; Klemm, P. Capsule and Fimbria Interaction in Klebsiella pneumoniae Infect. Immun. 2005, 73 (8) 4626-4633
    • (2005) Infect. Immun. , vol.73 , Issue.8 , pp. 4626-4633
    • Schembri, M.A.1    Blom, J.2    Krogfelt, K.A.3    Klemm, P.4
  • 37
    • 58949097012 scopus 로고    scopus 로고
    • Capsule Polysaccharide is a Bacterial Decoy for Antimicrobial Peptides
    • Llobet, E.; Tomas, J. M.; Bengoechea, J. A. Capsule Polysaccharide is a Bacterial Decoy for Antimicrobial Peptides Microbiology 2008, 154 (Pt 12) 3877-86
    • (2008) Microbiology , vol.154 , pp. 3877-86
    • Llobet, E.1    Tomas, J.M.2    Bengoechea, J.A.3
  • 38
    • 0026768029 scopus 로고
    • Melittin-Induced Changes in Lipid Multilayers. A Solid-State NMR Study
    • Smith, R.; Separovic, F.; Bennett, F. C.; Cornell, B. A. Melittin-Induced Changes in Lipid Multilayers. A Solid-State NMR Study Biophys. J. 1992, 63 (2) 469-474
    • (1992) Biophys. J. , vol.63 , Issue.2 , pp. 469-474
    • Smith, R.1    Separovic, F.2    Bennett, F.C.3    Cornell, B.A.4
  • 39
    • 0020479083 scopus 로고
    • The Structure of Melittin. I. Structure Determination and Partial Refinement
    • Terwilliger, T. C.; Eisenberg, D. The Structure of Melittin. I. Structure Determination and Partial Refinement J. Biol. Chem. 1982, 257 (11) 6010-6015
    • (1982) J. Biol. Chem. , vol.257 , Issue.11 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 40
  • 42
    • 84893818582 scopus 로고    scopus 로고
    • Transcriptional Activation of the mrkA Promoter of the Klebsiella pneumoniae Type 3 Fimbrial Operon by the c-di-GMP-Dependent MrkH Protein
    • Yang, J.; Wilksch, J. J.; Tan, J. W. H.; Hocking, D. M.; Webb, C. T.; Lithgow, T.; Robins-Browne, R. M.; Strugnell, R. A. Transcriptional Activation of the mrkA Promoter of the Klebsiella pneumoniae Type 3 Fimbrial Operon by the c-di-GMP-Dependent MrkH Protein PLoS One 2013, 8 (11) e79038
    • (2013) PLoS One , vol.8 , Issue.11
    • Yang, J.1    Wilksch, J.J.2    Tan, J.W.H.3    Hocking, D.M.4    Webb, C.T.5    Lithgow, T.6    Robins-Browne, R.M.7    Strugnell, R.A.8
  • 43
    • 0025195680 scopus 로고
    • Mini-Tn5 Transposon Derivatives for Insertion Mutagenesis, Promoter Probing, and Chromosomal Insertion of Cloned DNA in Gram-Negative Eubacteria
    • de Lorenzo, V.; Herrero, M.; Jakubzik, U.; Timmis, K. N. Mini-Tn5 Transposon Derivatives for Insertion Mutagenesis, Promoter Probing, and Chromosomal Insertion of Cloned DNA in Gram-Negative Eubacteria J. Bacteriol. 1990, 172 (11) 6568-6572
    • (1990) J. Bacteriol. , vol.172 , Issue.11 , pp. 6568-6572
    • De Lorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 44
    • 0033846629 scopus 로고    scopus 로고
    • Efficient Amplification of Multiple Transposon-Flanking Sequences
    • Kwon, Y. M.; Ricke, S. C. Efficient Amplification of Multiple Transposon-Flanking Sequences J. Microbiol. Methods 2000, 41 (3) 195-199
    • (2000) J. Microbiol. Methods , vol.41 , Issue.3 , pp. 195-199
    • Kwon, Y.M.1    Ricke, S.C.2
  • 47
    • 36449007442 scopus 로고
    • Calibration of Atomic-Force Microscope Tips
    • Hutter, J. L.; Bechhoefer, J. Calibration of Atomic-Force Microscope Tips Rev. Sci. Instrum. 1993, 64 (7) 1868-1873
    • (1993) Rev. Sci. Instrum. , vol.64 , Issue.7 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 48
    • 0037173283 scopus 로고    scopus 로고
    • Contributions of Bacterial Surface Polymers, Electrostatics, and Cell Elasticity to the Shape of AFM Force Curves
    • Velegol, S. B.; Logan, B. E. Contributions of Bacterial Surface Polymers, Electrostatics, and Cell Elasticity to the Shape of AFM Force Curves Langmuir 2002, 18 (13) 5256-5262
    • (2002) Langmuir , vol.18 , Issue.13 , pp. 5256-5262
    • Velegol, S.B.1    Logan, B.E.2
  • 49
    • 0028997572 scopus 로고
    • Imaging Soft Samples with the Atomic Force Microscope: Gelatin in Water and Propanol
    • Radmacher, M.; Fritz, M.; Hansma, P. K. Imaging Soft Samples with the Atomic Force Microscope: Gelatin in Water and Propanol Biophys. J. 1995, 69 (1) 264-270
    • (1995) Biophys. J. , vol.69 , Issue.1 , pp. 264-270
    • Radmacher, M.1    Fritz, M.2    Hansma, P.K.3
  • 50
    • 39449137836 scopus 로고    scopus 로고
    • Spatially Resolved Force Spectroscopy of Bacterial Surfaces Using Force-Volume Imaging
    • Gaboriaud, F.; Parcha, B. S.; Gee, M. L.; Holden, J. A.; Strugnell, R. A. Spatially Resolved Force Spectroscopy of Bacterial Surfaces Using Force-Volume Imaging Colloids Surf., B 2008, 62 (2) 206-213
    • (2008) Colloids Surf., B , vol.62 , Issue.2 , pp. 206-213
    • Gaboriaud, F.1    Parcha, B.S.2    Gee, M.L.3    Holden, J.A.4    Strugnell, R.A.5
  • 51
    • 65249143305 scopus 로고    scopus 로고
    • Bacteria Survive Multiple Puncturings of Their Cell Walls
    • Suo, Z.; Avci, R.; Deliorman, M.; Yang, X.; Pascual, D. W. Bacteria Survive Multiple Puncturings of Their Cell Walls Langmuir 2009, 25 (8) 4588-4594
    • (2009) Langmuir , vol.25 , Issue.8 , pp. 4588-4594
    • Suo, Z.1    Avci, R.2    Deliorman, M.3    Yang, X.4    Pascual, D.W.5
  • 52
    • 85025744188 scopus 로고
    • A Simple Algorithm for the Calculation of the Electrostatic Repulsion between Identical Charged Surfaces in Electrolyte
    • Chan, D. Y. C.; Pashley, R. M.; White, L. R. A Simple Algorithm for the Calculation of the Electrostatic Repulsion between Identical Charged Surfaces in Electrolyte J. Colloid Interface Sci. 1980, 77 (1) 283-285
    • (1980) J. Colloid Interface Sci. , vol.77 , Issue.1 , pp. 283-285
    • Chan, D.Y.C.1    Pashley, R.M.2    White, L.R.3
  • 53
    • 0035797971 scopus 로고    scopus 로고
    • Force of Interaction between a Biocolloid and an Inorganic Oxide: Complexity of Surface Deformation, Roughness, and Brushlike Behavior
    • Considine, R. F.; Drummond, C. J.; Dixon, D. R. Force of Interaction between a Biocolloid and an Inorganic Oxide: Complexity of Surface Deformation, Roughness, and Brushlike Behavior Langmuir 2001, 17 (20) 6325-6335
    • (2001) Langmuir , vol.17 , Issue.20 , pp. 6325-6335
    • Considine, R.F.1    Drummond, C.J.2    Dixon, D.R.3
  • 54
    • 0008943229 scopus 로고
    • On the Contact of Elastic Solids
    • Macmillan: London
    • Hertz, H. On the Contact of Elastic Solids. In Miscellaneous Papers by H. Hertz; Macmillan: London, 1896.
    • (1896) Miscellaneous Papers by H. Hertz
    • Hertz, H.1
  • 55
    • 54549107854 scopus 로고    scopus 로고
    • Coupled Electrostatic, Hydrodynamic, and Mechanical Properties of Bacterial Interfaces in Aqueous Media
    • Gaboriaud, F.; Gee, M. L.; Strugnell, R.; Duval, J. F. L. Coupled Electrostatic, Hydrodynamic, and Mechanical Properties of Bacterial Interfaces in Aqueous Media Langmuir 2008, 24 (19) 10988-10995
    • (2008) Langmuir , vol.24 , Issue.19 , pp. 10988-10995
    • Gaboriaud, F.1    Gee, M.L.2    Strugnell, R.3    Duval, J.F.L.4
  • 56
    • 78649876670 scopus 로고    scopus 로고
    • Antibacterial Action of Dispersed Single-Walled Carbon Nanotubes on Escherichia coli and Bacillus subtilis Investigated by Atomic Force Microscopy
    • Liu, S.; Ng, A. K.; Xu, R.; Wei, J.; Tan, C. M.; Yang, Y.; Chen, Y. Antibacterial Action of Dispersed Single-Walled Carbon Nanotubes on Escherichia coli and Bacillus subtilis Investigated by Atomic Force Microscopy Nanoscale 2010, 2 (12) 2744-2750
    • (2010) Nanoscale , vol.2 , Issue.12 , pp. 2744-2750
    • Liu, S.1    Ng, A.K.2    Xu, R.3    Wei, J.4    Tan, C.M.5    Yang, Y.6    Chen, Y.7
  • 57
    • 84865532003 scopus 로고    scopus 로고
    • Functional Convergence of Hopanoids and Sterols in Membrane Ordering
    • Sáenz, J. P.; Sezgin, E.; Schwille, P.; Simons, K. Functional Convergence of Hopanoids and Sterols in Membrane Ordering Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (35) 14236-14240
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.35 , pp. 14236-14240
    • Sáenz, J.P.1    Sezgin, E.2    Schwille, P.3    Simons, K.4
  • 58
    • 84864951944 scopus 로고    scopus 로고
    • Variation in Streptococcus pneumoniae Susceptibility to Human Antimicrobial Peptides May Mediate Intraspecific Competition
    • Habets, M. G. J. L.; Rozen, D. E.; Brockhurst, M. A. Variation in Streptococcus pneumoniae Susceptibility to Human Antimicrobial Peptides May Mediate Intraspecific Competition Proc. R. Soc. B 2012, 279, 3803-3811
    • (2012) Proc. R. Soc. B , vol.279 , pp. 3803-3811
    • Habets, M.G.J.L.1    Rozen, D.E.2    Brockhurst, M.A.3
  • 59
    • 0020485149 scopus 로고
    • The Capsular Polysaccharide from Klebsiella serotype K54; Location of the O-acyl Groups, and a Revised Structure
    • Dutton, G. G. S.; Merrifield, E. H. The Capsular Polysaccharide from Klebsiella serotype K54; Location of the O-acyl Groups, and a Revised Structure Carbohydr. Res. 1982, 105 (2) 189-203
    • (1982) Carbohydr. Res. , vol.105 , Issue.2 , pp. 189-203
    • Dutton, G.G.S.1    Merrifield, E.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.