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Volumn 11, Issue 4, 2012, Pages

Lactoferricin B inhibits the phosphorylation of the two-component system response regulators BasR and CreB

Author keywords

[No Author keywords available]

Indexed keywords

COGNATE SENSOR KINASE BASS; COGNATE SENSOR KINASE CREC; FERRIC ION; LACTOFERRICIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN KINASE; PROTEOME; REGULATOR PROTEIN; REGULATOR PROTEIN BASR; REGULATOR PROTEIN CREB; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; LACTOFERRIN;

EID: 84859862508     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.014720     Document Type: Article
Times cited : (45)

References (63)
  • 1
    • 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, D590-592 (Pubitemid 38081727)
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATABASE ISS.
    • Wang, Z.1    Wang, G.2
  • 2
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 3
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto, K., Hirao, K., Oshima, T., Aiba, H., Utsumi, R., and Ishihama, A. (2005) Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J. Biol. Chem. 280, 1448-1456
    • (2005) J. Biol. Chem. , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 4
    • 50049106044 scopus 로고    scopus 로고
    • System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids
    • Gao, R., Tao, Y., and Stock, A. M. (2008) System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids. Mol. Microbiol. 69, 1358-1372
    • (2008) Mol. Microbiol. , vol.69 , pp. 1358-1372
    • Gao, R.1    Tao, Y.2    Stock, A.M.3
  • 5
    • 4644294727 scopus 로고    scopus 로고
    • A genome-wide view of the Escherichia coli BasS-BasR two-component system implicated in iron-responses
    • DOI 10.1271/bbb.68.1758
    • Hagiwara, D., Yamashino, T., and Mizuno, T. (2004) A Genome-wide view of the Escherichia coli BasS-BasR two-component system implicated in iron-responses. Biosci Biotechnol Biochem. 68, 1758-1767 (Pubitemid 39260307)
    • (2004) Bioscience, Biotechnology and Biochemistry , vol.68 , Issue.8 , pp. 1758-1767
    • Hagiwara, D.1    Yamashino, T.2    Mizuno, T.3
  • 7
    • 23744504984 scopus 로고    scopus 로고
    • Recognition of antimicrobial peptides by a bacterial sensor kinase
    • DOI 10.1016/j.cell.2005.05.030, PII S0092867405005532
    • Bader, M. W., Sanowar, S., Daley, M. E., Schneider, A. R., Cho, U., Xu, W., Klevit, R. E., Le Moual, H., and Miller, S. I. (2005) Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122, 461-472 (Pubitemid 41127146)
    • (2005) Cell , vol.122 , Issue.3 , pp. 461-472
    • Bader, M.W.1    Sanowar, S.2    Daley, M.E.3    Schneider, A.R.4    Cho, U.5    Xu, W.6    Klevit, R.E.7    Le, M.H.8    Miller, S.I.9
  • 8
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman, E. A. (2001) The pleiotropic two-component regulatory system PhoP-PhoQ. J. Bacteriol. 183, 1835-1842
    • (2001) J. Bacteriol. , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 9
    • 30344480252 scopus 로고    scopus 로고
    • A bacterial sensory system that activates resistance to innate immune defenses: Potential targets for antimicrobial therapeutics
    • DOI 10.1124/mi.5.6.4
    • Brodsky, I. E., and Gunn, J. S. (2005) A bacterial sensory system that activates resistance to innate immune defenses: potential targets for antimicrobial therapeutics. Mol. Interv. 5, 335-337 (Pubitemid 43060712)
    • (2005) Molecular Interventions , vol.5 , Issue.6 , pp. 335-337
    • Brodsky, I.E.1    Gunn, J.S.2
  • 10
    • 0141484326 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • DOI 10.1046/j.1365-2958.2003.03673.x
    • McPhee, J. B., Lewenza, S., and Hancock, R. E. (2003) Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa. Mol. Microbiol. 50, 205-217 (Pubitemid 37222798)
    • (2003) Molecular Microbiology , vol.50 , Issue.1 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.W.3
  • 12
    • 4143102460 scopus 로고    scopus 로고
    • Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis
    • DOI 10.1016/j.femsle.2004.07.001, PII S0378109704004896
    • Ulvatne, H., Samuelsen, O., Haukland, H. H., Kramer, M., and Vorland, L. H. (2004) Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis. FEMS Microbiol. Lett. 237, 377-384 (Pubitemid 39091973)
    • (2004) FEMS Microbiology Letters , vol.237 , Issue.2 , pp. 377-384
    • Ulvatne, H.1    Samuelsen, O.2    Haukland, H.H.3    Kramer, M.4    Vorland, L.H.5
  • 13
    • 0036168570 scopus 로고    scopus 로고
    • Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli
    • DOI 10.1128/AAC.46.3.605-614.2002
    • Patrzykat, A., Friedrich, C. L., Zhang, L., Mendoza, V., and Hancock, R. E. (2002) Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46, 605-614 (Pubitemid 34162506)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.3 , pp. 605-614
    • Patrzykat, A.1    Friedrich, C.L.2    Zhang, L.3    Mendoza, V.4    Hancock, R.E.W.5
  • 16
    • 0027669173 scopus 로고
    • Forms of lactoferrin: Their antibacterial effect on enterotoxigenic Escherichia coli
    • Dionysius, D. A., Grieve, P. A., and Milne, J. M. (1993) Forms of lactoferrin: their antibacterial effect on enterotoxigenic Escherichia coli. J. Dairy Sci. 76, 2597-2600
    • (1993) J. Dairy Sci. , vol.76 , pp. 2597-2600
    • Dionysius, D.A.1    Grieve, P.A.2    Milne, J.M.3
  • 17
    • 18044397724 scopus 로고    scopus 로고
    • Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines
    • DOI 10.1158/1535-7163.MCT-04-0077
    • Mader, J. S., Salsman, J., Conrad, D. M., and Hoskin, D. W. (2005) Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol. Cancer Ther. 4, 612-624 (Pubitemid 40601843)
    • (2005) Molecular Cancer Therapeutics , vol.4 , Issue.4 , pp. 612-624
    • Mader, J.S.1    Salsman, J.2    Conrad, D.M.3    Hoskin, D.W.4
  • 18
    • 38348999283 scopus 로고    scopus 로고
    • 165-induced angiogenesis by competing for heparin-like binding sites on endothelial cells
    • DOI 10.2353/ajpath.2006.051229
    • Mader, J. S., Smyth, D., Marshall, J., and Hoskin, D. W. (2006) Bovine lactoferricin inhibits basic fibroblast growth factor- and vascular endothelial growth factor165-induced angiogenesis by competing for heparin- like binding sites on endothelial cells. Am. J. Pathol. 169, 1753-1766 (Pubitemid 351182006)
    • (2006) American Journal of Pathology , vol.169 , Issue.5 , pp. 1753-1766
    • Mader, J.S.1    Smyth, D.2    Marshall, J.3    Hoskin, D.W.4
  • 19
    • 0035831078 scopus 로고    scopus 로고
    • Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes
    • DOI 10.1016/S0014-5793(01)02233-5, PII S0014579301022335
    • Ulvatne, H., Haukland, H. H., Olsvik, O., and Vorland, L. H. (2001) Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes. FEBS Lett. 492, 62-65 (Pubitemid 32206721)
    • (2001) FEBS Letters , vol.492 , Issue.1-2 , pp. 62-65
    • Ulvatne, H.1    Haukland, H.H.2    Olsvik, O.3    Vorland, L.H.4
  • 20
    • 0035941062 scopus 로고    scopus 로고
    • The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
    • DOI 10.1016/S0014-5793(01)03100-3, PII S0014579301031003
    • Haukland, H. H., Ulvatne, H., Sandvik, K., and Vorland, L. H. (2001) The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett. 508, 389-393 (Pubitemid 33135477)
    • (2001) FEBS Letters , vol.508 , Issue.3 , pp. 389-393
    • Haukland, H.H.1    Ulvatne, H.2    Sandvik, K.3    Vorland, L.H.4
  • 22
    • 37749048465 scopus 로고    scopus 로고
    • A proteome chip approach reveals new DNA damage recognition activities in Escherichia coli
    • Chen, C. S., Korobkova, E., Chen, H., Zhu, J., Jian, X., Tao, S. C., He, C., and Zhu, H. (2008) A proteome chip approach reveals new DNA damage recognition activities in Escherichia coli. Nat. Methods 5, 69-74
    • (2008) Nat. Methods , vol.5 , pp. 69-74
    • Chen, C.S.1    Korobkova, E.2    Chen, H.3    Zhu, J.4    Jian, X.5    Tao, S.C.6    He, C.7    Zhu, H.8
  • 23
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H., and Mori, H. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12, 291-299
    • (2005) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 24
    • 33847705714 scopus 로고    scopus 로고
    • ProCAT: A data analysis approach for protein microarrays
    • Zhu, X., Gerstein, M., and Snyder, M. (2006) ProCAT: a data analysis approach for protein microarrays. Genome Biol. 7, R110
    • (2006) Genome Biol. , vol.7
    • Zhu, X.1    Gerstein, M.2    Snyder, M.3
  • 25
    • 31344459012 scopus 로고    scopus 로고
    • A pmrA constitutive mutant sensitizes Escherichia coli to deoxycholic acid
    • DOI 10.1128/JB.188.3.1180-1183.2006
    • Froelich, J. M., Tran, K., and Wall, D. (2006) A pmrA constitutive mutant sensitizes Escherichia coli to deoxycholic acid. J. Bacteriol. 188, 1180-1183 (Pubitemid 43146436)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 1180-1183
    • Froelich, J.M.1    Tran, K.2    Wall, D.3
  • 26
    • 0035920119 scopus 로고    scopus 로고
    • Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media
    • Avison, M. B., Horton, R. E., Walsh, T. R., and Bennett, P. M. (2001) Escherichia coli CreBC is a global regulator of gene expression that responds to growth in minimal media. J. Biol. Chem. 276, 26955-26961
    • (2001) J. Biol. Chem. , vol.276 , pp. 26955-26961
    • Avison, M.B.1    Horton, R.E.2    Walsh, T.R.3    Bennett, P.M.4
  • 27
    • 4444286595 scopus 로고    scopus 로고
    • Focused proteomics: Monoclonal antibody-based isolation of the oxidative phosphorylation machinery and detection of phosphoproteins using a fluorescent phosphoprotein gel stain
    • DOI 10.1002/elps.200406006
    • Murray, J., Marusich, M. F., Capaldi, R. A., and Aggeler, R. (2004) Focused proteomics: monoclonal antibody-based isolation of the oxidative phosphorylation machinery and detection of phosphoproteins using a fluorescent phosphoprotein gel stain. Electrophoresis 25, 2520-2525 (Pubitemid 39193661)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2520-2525
    • Murray, J.1    Marusich, M.F.2    Capaldi, R.A.3    Aggeler, R.4
  • 28
    • 4444305698 scopus 로고    scopus 로고
    • Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry
    • DOI 10.1002/elps.200406007
    • Schulenberg, B., Goodman, T. N., Aggeler, R., Capaldi, R. A., and Patton, W. F. (2004) Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry. Electrophoresis 25, 2526-2532 (Pubitemid 39193662)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2526-2532
    • Schulenberg, B.1    Goodman, T.N.2    Aggeler, R.3    Capaldi, R.A.4    Patton, W.F.5
  • 29
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • DOI 10.1074/jbc.C300189200
    • Schulenberg, B., Aggeler, R., Beechem, J. M., Capaldi, R. A., and Patton, W. F. (2003) Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278, 27251-27255 (Pubitemid 36876882)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 31
    • 4444236379 scopus 로고    scopus 로고
    • A two-dimensional electrophoresis map of Chinese hamster ovary cell proteins based on fluorescence staining
    • DOI 10.1002/elps.200406010
    • Hayduk, E. J., Choe, L. H., and Lee, K. H. (2004) A two-dimensional electrophoresis map of Chinese hamster ovary cell proteins based on fluorescence staining. Electrophoresis 25, 2545-2556 (Pubitemid 39193665)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2545-2556
    • Hayduk, E.J.1    Choe, L.H.2    Lee, K.H.3
  • 32
    • 8744300809 scopus 로고    scopus 로고
    • Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness
    • DOI 10.1002/pmic.200400957
    • Ge, Y., Rajkumar, L., Guzman, R. C., Nandi, S., Patton, W. F., and Agnew, B. J. (2004) Multiplexed fluorescence detection of phosphorylation, glycosylation, and total protein in the proteomic analysis of breast cancer refractoriness. Proteomics 4, 3464-3467 (Pubitemid 39525296)
    • (2004) Proteomics , vol.4 , Issue.11 , pp. 3464-3467
    • Ge, Y.1    Rajkumar, L.2    Guzman, R.C.3    Nandi, S.4    Patton, W.F.5    Agnew, B.J.6
  • 34
    • 0035045954 scopus 로고    scopus 로고
    • The OmpR-family of proteins: Insight into the tertiary structure and functions of two-component regulator proteins
    • Itou, H., and Tanaka, I. (2001) The OmpR-family of proteins: insight into the tertiary structure and functions of two-component regulator proteins. J. Biochem. 129, 343-350 (Pubitemid 32304107)
    • (2001) Journal of Biochemistry , vol.129 , Issue.3 , pp. 343-350
    • Itou, H.1    Tanaka, I.2
  • 35
    • 14244270197 scopus 로고    scopus 로고
    • Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo
    • DOI 10.1074/jbc.M412741200
    • Shin, D., and Groisman, E. A. (2005) Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo. J. Biol. Chem. 280, 4089-4094 (Pubitemid 40288572)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4089-4094
    • Shin, D.1    Groisman, E.A.2
  • 36
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch, J. A. (2000) Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 3, 165-170
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 37
    • 68949163858 scopus 로고    scopus 로고
    • Metabolic flux analysis of Escherichia coli creB and arcA mutants reveals shared control of carbon catabolism under microaerobic growth conditions
    • Nikel, P. I., Zhu, J., San, K. Y., Mendez, B. S., and Bennett, G. N. (2009) Metabolic flux analysis of Escherichia coli creB and arcA mutants reveals shared control of carbon catabolism under microaerobic growth conditions. J. Bacteriol. 191, 5538-5548
    • (2009) J. Bacteriol. , vol.191 , pp. 5538-5548
    • Nikel, P.I.1    Zhu, J.2    San, K.Y.3    Mendez, B.S.4    Bennett, G.N.5
  • 38
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • DOI 10.1016/S0952-7915(99)80005-3
    • Lehrer, R. I., and Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27 (Pubitemid 29082332)
    • (1999) Current Opinion in Immunology , vol.11 , Issue.1 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 39
    • 44349100490 scopus 로고    scopus 로고
    • Defining the growth conditions and promoter-proximal DNA sequences required for activation of gene expression by CreBC in Escherichia coli
    • DOI 10.1128/JB.00108-08
    • Cariss, S. J., Tayler, A. E., and Avison, M. B. (2008) Defining the growth conditions and promoter-proximal DNA sequences required for activation of gene expression by CreBC in Escherichia coli. J. Bacteriol. 190, 3930-3939 (Pubitemid 351732872)
    • (2008) Journal of Bacteriology , vol.190 , Issue.11 , pp. 3930-3939
    • Cariss, S.J.L.1    Tayler, A.E.2    Avison, M.B.3
  • 41
    • 32144464889 scopus 로고    scopus 로고
    • Small intestinal bacterial overgrowth: Roles of antibiotics, prebiotics, and probiotics
    • DOI 10.1053/j.gastro.2005.11.046, PII S0016508505024200
    • Quigley, E. M., and Quera, R. (2006) Small intestinal bacterial overgrowth: roles of antibiotics, prebiotics, and probiotics. Gastroenterology 130, S78-90 (Pubitemid 43208864)
    • (2006) Gastroenterology , vol.130 , Issue.2 SUPPL.
    • Quigley, E.M.M.1    Quera, R.2
  • 43
    • 0025141461 scopus 로고
    • Forms of soluble iron in mouse stomach and duodenal lumen: Significance for mucosal uptake
    • Simpson, R. J., and Peters, T. J. (1990) Forms of soluble iron in mouse stomach and duodenal lumen: significance for mucosal uptake. Br. J. Nutr. 63, 79-89 (Pubitemid 20053936)
    • (1990) British Journal of Nutrition , vol.63 , Issue.1 , pp. 79-89
    • Simpson, R.J.1    Peters, T.J.2
  • 45
    • 59449101520 scopus 로고    scopus 로고
    • A role for antimicrobial peptides in intestinal microsporidiosis
    • Leitch, G. J., and Ceballos, C. (2009) A role for antimicrobial peptides in intestinal microsporidiosis. Parasitology 136, 175-181
    • (2009) Parasitology , vol.136 , pp. 175-181
    • Leitch, G.J.1    Ceballos, C.2
  • 48
    • 70349131189 scopus 로고    scopus 로고
    • Persistence of colicinogenic Escherichia coli in the mouse gastrointestinal tract
    • Gillor, O., Giladi, I., and Riley, M. A. (2009) Persistence of colicinogenic Escherichia coli in the mouse gastrointestinal tract. BMC Microbiol. 9, 165
    • (2009) BMC Microbiol. , vol.9 , pp. 165
    • Gillor, O.1    Giladi, I.2    Riley, M.A.3
  • 49
    • 0036790373 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal-transduction systems as therapeutic targets
    • Stephenson, K., and Hoch, J. A. (2002) Two-component and phosphorelay signal-transduction systems as therapeutic targets. Curr. Opin. Pharmacol. 2, 507-512
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 507-512
    • Stephenson, K.1    Hoch, J.A.2
  • 50
    • 0036214541 scopus 로고    scopus 로고
    • Structure/function relationships in OmpR and other winged-helix transcription factors
    • Kenney, L. J. (2002) Structure/function relationships in OmpR and other winged-helix transcription factors. Curr. Opin. Microbiol. 5, 135-141
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 135-141
    • Kenney, L.J.1
  • 51
    • 34247170877 scopus 로고    scopus 로고
    • Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel three-protein two-component system from Mycobacterium tuberculosis
    • DOI 10.1016/j.febslet.2007.03.089, PII S0014579307003675
    • Shrivastava, R., Ghosh, A. K., and Das, A. K. (2007) Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel threeprotein two-component system from Mycobacterium tuberculosis. FEBS Lett. 581, 1903-1909 (Pubitemid 46602287)
    • (2007) FEBS Letters , vol.581 , Issue.9 , pp. 1903-1909
    • Shrivastava, R.1    Ghosh, A.K.2    Das, A.K.3
  • 52
    • 0032807458 scopus 로고    scopus 로고
    • Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems
    • Hilliard, J. J., Goldschmidt, R. M., Licata, L., Baum, E. Z., and Bush, K. (1999) Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems. Antimicrob. Agents Chemother. 43, 1693-1699 (Pubitemid 29331249)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.7 , pp. 1693-1699
    • Hilliard, J.J.1    Goldschmidt, R.M.2    Licata, L.3    Baum, E.Z.4    Bush, K.5
  • 53
    • 1642309791 scopus 로고    scopus 로고
    • Developing inhibitors to selectivity target two-component and phosphorelay signal transduction systems of pathogenic microorganisms
    • DOI 10.2174/0929867043455765
    • Stephenson, K., and Hoch, J. A. (2004) Developing inhibitors to selectively target two-component and phosphorelay signal transduction systems of pathogenic microorganisms. Curr. Med. Chem. 11, 765-773 (Pubitemid 38380050)
    • (2004) Current Medicinal Chemistry , vol.11 , Issue.6 , pp. 765-773
    • Stephenson, K.1    Hoch, J.A.2
  • 54
    • 77949916499 scopus 로고    scopus 로고
    • Two-component signal transduction as potential drug targets in pathogenic bacteria
    • Gotoh, Y., Eguchi, Y., Watanabe, T., Okamoto, S., Doi, A., and Utsumi, R. (2010) Two-component signal transduction as potential drug targets in pathogenic bacteria. Curr. Opin. Microbiol. 13, 232-239
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 232-239
    • Gotoh, Y.1    Eguchi, Y.2    Watanabe, T.3    Okamoto, S.4    Doi, A.5    Utsumi, R.6
  • 55
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • Bourret, R. B. Receiver domain structure and function in response regulator proteins. Curr. Opin. Microbiol. 13, 142-149
    • Curr. Opin. Microbiol. , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 56
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., Tomita, M., Giehl, T. J., and Ellison, R. T., 3rd (1993) Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61, 719-728 (Pubitemid 23030865)
    • (1993) Infection and Immunity , vol.61 , Issue.2 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4
  • 57
    • 3342928851 scopus 로고    scopus 로고
    • The antimicrobial activity of lactoferrin: Current status and perspectives
    • Orsi, N. (2004) The antimicrobial activity of lactoferrin: current status and perspectives. Biometals 17, 189-196
    • (2004) Biometals , vol.17 , pp. 189-196
    • Orsi, N.1
  • 58
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., and 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, 472-479
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 59
  • 60
    • 77953285465 scopus 로고    scopus 로고
    • Influence of bovine lactoferrin on selected probiotic bacteria and intestinal pathogens
    • Tian, H., Maddox, I. S., Ferguson, L. R., and Shu, Q. Influence of bovine lactoferrin on selected probiotic bacteria and intestinal pathogens. Biometals 23, 593-596
    • Biometals , vol.23 , pp. 593-596
    • Tian, H.1    Maddox, I.S.2    Ferguson, L.R.3    Shu, Q.4
  • 62
    • 33745889417 scopus 로고    scopus 로고
    • The role of lactoferrin in the proper development of newborns
    • Artym, J., and Zimecki, M. (2005) [The role of lactoferrin in the proper development of newborns]. Postepy Hig Med Dosw 59, 421-432
    • (2005) Postepy Hig Med Dosw , vol.59 , pp. 421-432
    • Artym, J.1    Zimecki, M.2
  • 63
    • 67449096940 scopus 로고    scopus 로고
    • Effects of dietary supplementation with an expressed fusion peptide bovine lactoferricin-lactoferrampin on performance, immune function and intestinal mucosal morphology in piglets weaned at age 21 d
    • Tang, Z., Yin, Y., Zhang, Y., Huang, R., Sun, Z., Li, T., Chu, W., Kong, X., Li, L., Geng, M., and Tu, Q. (2009) Effects of dietary supplementation with an expressed fusion peptide bovine lactoferricin-lactoferrampin on performance, immune function and intestinal mucosal morphology in piglets weaned at age 21 d. Br. J. Nutr. 101, 998-1005
    • (2009) Br. J. Nutr. , vol.101 , pp. 998-1005
    • Tang, Z.1    Yin, Y.2    Zhang, Y.3    Huang, R.4    Sun, Z.5    Li, T.6    Chu, W.7    Kong, X.8    Li, L.9    Geng, M.10    Tu, Q.11


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