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Volumn 23, Issue 4, 1997, Pages 737-749

Molecular characterization of hpuAB, the haemoglobin-haptoglobin-utilization operon of Neisseria meningitidis

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; RECEPTOR PROTEIN;

EID: 0031025513     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.2501619.x     Document Type: Article
Times cited : (119)

References (65)
  • 1
    • 0028308286 scopus 로고
    • Gonococcal transferrin binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson, J.E., Sparling, P.F., and Cornelissen, C.N. (1994) Gonococcal transferrin binding protein 2 facilitates but is not essential for transferrin utilization. J Bacteriol 176: 3162-3170.
    • (1994) J Bacteriol , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 2
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell, P.E., Nau, C.D., Brown, J.T., Konisky, J., and Kadner, R.J. (1990) Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J Bacteriol 172: 3826-3829.
    • (1990) J Bacteriol , vol.172 , pp. 3826-3829
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, R.J.5
  • 3
    • 0003272157 scopus 로고
    • Enzymatic amplifications of RNA by PCR
    • Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (eds). New York: John Wiley & Sons, Inc., and Green Publishing Associates, Inc.
    • Beverly, S.M. (1992) Enzymatic amplifications of RNA by PCR. In Current Protocols in Molecular Biology. Ausubel, P.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (eds). New York: John Wiley & Sons, Inc., and Green Publishing Associates, Inc., pp. 15.4.1-15.4.6.
    • (1992) Current Protocols in Molecular Biology , pp. 1541-1546
    • Beverly, S.M.1
  • 4
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor
    • Bonnah, R.A., Yu, R.-H., and Schryvers, A.B. (1995) Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor. Microb Pathog 19: 285-297.
    • (1995) Microb Pathog , vol.19 , pp. 285-297
    • Bonnah, R.A.1    Yu, R.-H.2    Schryvers, A.B.3
  • 5
    • 8044253575 scopus 로고    scopus 로고
    • Genetic and serological analysis of lactoferrin receptors in the Neisseriaceae: Evidence for the antigenically conserved nature of LbpB
    • Zollinger, W., Frasch C., and Deal, C. (eds). Baltimore, Maryland. September 8-13
    • Bonnah, R.A., Wong, H., and Schryvers, A.B. (1996) Genetic and serological analysis of lactoferrin receptors in the Neisseriaceae: evidence for the antigenically conserved nature of LbpB. Abstracts of the Tenth International Pathogenic Neisseria Conference. Zollinger, W., Frasch C., and Deal, C. (eds). Baltimore, Maryland. September 8-13. p. 560.
    • (1996) Abstracts of the Tenth International Pathogenic Neisseria Conference , pp. 560
    • Bonnah, R.A.1    Wong, H.2    Schryvers, A.B.3
  • 6
    • 0023576859 scopus 로고
    • Molecular mechanisms of regulation of siderophore-mediated iron assimilation
    • Bragg, A., and Neilands, J.B. (1987) Molecular mechanisms of regulation of siderophore-mediated iron assimilation. Microbiol Rev 51: 509-518.
    • (1987) Microbiol Rev , vol.51 , pp. 509-518
    • Bragg, A.1    Neilands, J.B.2
  • 8
    • 0027491241 scopus 로고
    • The ferric iron binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin
    • Chen, C.-Y., Berish, S.A., Morse, S.A., and Mietzner, T.A. (1993) The ferric iron binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol Microbiol 10: 311-318.
    • (1993) Mol Microbiol , vol.10 , pp. 311-318
    • Chen, C.-Y.1    Berish, S.A.2    Morse, S.A.3    Mietzner, T.A.4
  • 10
    • 0028073695 scopus 로고
    • Iron piracy: Acquisition of transferrin-bound iron by bacterial pathogens
    • Cornelissen, C.N., and Sparling, P.F. (1994) Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens. Mol Microbiol 14: 843-850.
    • (1994) Mol Microbiol , vol.14 , pp. 843-850
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 11
    • 0026768392 scopus 로고
    • Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors
    • Cornelissen, C., Biswas, G.D., Tsai, J., Paruchuri, D.K., Thompson, S.A., and Sparling, P.F. (1992) Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors. J Bacteriol 174: 5788-5797.
    • (1992) J Bacteriol , vol.174 , pp. 5788-5797
    • Cornelissen, C.1    Biswas, G.D.2    Tsai, J.3    Paruchuri, D.K.4    Thompson, S.A.5    Sparling, P.F.6
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucl Acids Res 12: 387-395.
    • (1984) Nucl Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 14
    • 0023193093 scopus 로고
    • Effects of serum carrier proteins on the growth of pathogenic Neisseriae with heme-bound iron
    • Dyer, D.W., West, E.P., and Sparling, P.P. (1987) Effects of serum carrier proteins on the growth of pathogenic Neisseriae with heme-bound iron. Infect Immun 55: 2171-2175.
    • (1987) Infect Immun , vol.55 , pp. 2171-2175
    • Dyer, D.W.1    West, E.P.2    Sparling, P.P.3
  • 15
  • 16
    • 0028905674 scopus 로고
    • Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi
    • Elkins, C. (1995) Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi. Infect Immun 63: 1241-1245.
    • (1995) Infect Immun , vol.63 , pp. 1241-1245
    • Elkins, C.1
  • 17
    • 0029061591 scopus 로고
    • Characterization of the hgbA locus encoding a hemoglobin receptor from Haemophilus ducreyi
    • Elkins, C., Chen, C.-J., and Thomas, C.E. (1995) Characterization of the hgbA locus encoding a hemoglobin receptor from Haemophilus ducreyi. Infect Immun 63: 2194-2200.
    • (1995) Infect Immun , vol.63 , pp. 2194-2200
    • Elkins, C.1    Chen, C.-J.2    Thomas, C.E.3
  • 19
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish, W., and States, D.J. (1993) Identification of protein coding regions by database similarity search. Nat Genet 3: 266-272.
    • (1993) Nat Genet , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 20
    • 0023886391 scopus 로고
    • Suppression of the btuB451 mutations by mutations in tonB gene suggests a direct interaction between TonB and TonB-dependent proteins in the outer membrane of Escherichia coli
    • Heller, K.J., Kadner, R.J., and Gunther, K. (1988) Suppression of the btuB451 mutations by mutations in tonB gene suggests a direct interaction between TonB and TonB-dependent proteins in the outer membrane of Escherichia coli. Gene 64: 147-153.
    • (1988) Gene , vol.64 , pp. 147-153
    • Heller, K.J.1    Kadner, R.J.2    Gunther, K.3
  • 21
    • 0016615657 scopus 로고
    • The fate of circulating hemoglobin
    • Hershko, C. (1975) The fate of circulating hemoglobin. Br J Haematol 29: 199-204.
    • (1975) Br J Haematol , vol.29 , pp. 199-204
    • Hershko, C.1
  • 22
    • 0018926512 scopus 로고
    • Iron-controlled infection with Neisseria meningitidis in mice
    • Holbein, B.E. (1980) Iron-controlled infection with Neisseria meningitidis in mice. Infect Immun 29: 886-891.
    • (1980) Infect Immun , vol.29 , pp. 886-891
    • Holbein, B.E.1
  • 23
    • 0019360750 scopus 로고
    • Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin
    • Holbein, B.E. (1981) Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin. Infect Immun 34: 120-125.
    • (1981) Infect Immun , vol.34 , pp. 120-125
    • Holbein, B.E.1
  • 24
    • 0018360061 scopus 로고
    • Neisseria meningitidis infection in mice: Influence of iron, variations in virulence among strains, and pathology
    • Holbein, B.E., Jericho, K.W.F., and Likes, G.C. (1979) Neisseria meningitidis infection in mice: Influence of iron, variations in virulence among strains, and pathology. Infect Immun 24: 545-551.
    • (1979) Infect Immun , vol.24 , pp. 545-551
    • Holbein, B.E.1    Jericho, K.W.F.2    Likes, G.C.3
  • 25
    • 0027252119 scopus 로고
    • Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis
    • Irwin, S.W., Averil, N., Cheng, C.Y., and Schryvers, A.B. (1993) Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis. Mol Microbiol 8: 1125-1133.
    • (1993) Mol Microbiol , vol.8 , pp. 1125-1133
    • Irwin, S.W.1    Averil, N.2    Cheng, C.Y.3    Schryvers, A.B.4
  • 26
    • 0028180667 scopus 로고
    • Cloning and sequence analysis of the fur gene encoding an iron-regulatory protein of Neisseria meningitidis
    • Karkhoff-Schweizer, R.R., Schryvers, A.B., and Schweizer, H.P. (1994) Cloning and sequence analysis of the fur gene encoding an iron-regulatory protein of Neisseria meningitidis. Gene 141: 139-140.
    • (1994) Gene , vol.141 , pp. 139-140
    • Karkhoff-Schweizer, R.R.1    Schryvers, A.B.2    Schweizer, H.P.3
  • 28
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope
    • Klebba, P.E., Rutz, J.M., Liu, J., and Murphy, C.K. (1993) Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J Bioenerg Biomembr 25: 603-611.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 29
    • 0025882007 scopus 로고
    • Iron sources for Haemophilus ducreyi
    • Lee, B.C. (1991) Iron sources for Haemophilus ducreyi. J Med Microbiol 34: 317-322.
    • (1991) J Med Microbiol , vol.34 , pp. 317-322
    • Lee, B.C.1
  • 30
    • 0027202149 scopus 로고
    • Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2
    • Legrain, M., Mazarin, V., Irwin, S.W., Bouchon, B., Quentin-Millet, M.J., Jacobs, E., and Schryvers, A.B. (1993) Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2. Gene 130: 73-80.
    • (1993) Gene , vol.130 , pp. 73-80
    • Legrain, M.1    Mazarin, V.2    Irwin, S.W.3    Bouchon, B.4    Quentin-Millet, M.J.5    Jacobs, E.6    Schryvers, A.B.7
  • 31
    • 0028937627 scopus 로고
    • Identification of an ironregulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin
    • Lewis, L.A., and Dyer, D.W. (1995) Identification of an ironregulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin. J Bacteriol 177: 1299-1306.
    • (1995) J Bacteriol , vol.177 , pp. 1299-1306
    • Lewis, L.A.1    Dyer, D.W.2
  • 32
    • 8044220434 scopus 로고    scopus 로고
    • Molecular analysis of IbpAB encoding the two component meningococcal lactoferrin receptor
    • Zollinger, W., Frasch, C., and Deal, C. (eds). Baltimore, Maryland. September 8-13
    • Lewis, L.A., Rohde, K.H., Behrens, B., Gray, E., Toth, S.I., Roe, B.A., and Dyer, D.W. (1996) Molecular analysis of IbpAB encoding the two component meningococcal lactoferrin receptor. Abstracts of the Tenth International Pathogenic Neisseria Conference. Zollinger, W., Frasch, C., and Deal, C. (eds). Baltimore, Maryland. September 8-13. p. 557.
    • (1996) Abstracts of the Tenth International Pathogenic Neisseria Conference , pp. 557
    • Lewis, L.A.1    Rohde, K.H.2    Behrens, B.3    Gray, E.4    Toth, S.I.5    Roe, B.A.6    Dyer, D.W.7
  • 33
    • 0028907131 scopus 로고
    • The changing epidemiology of invasive bacterial infections in Massachusetts children, 1984 through 1991
    • Loughlin, A.M., D.Marchant, C., and Lett, S.M. (1995) The changing epidemiology of invasive bacterial infections in Massachusetts children, 1984 through 1991. Public Health Briefs 85: 392-394.
    • (1995) Public Health Briefs , vol.85 , pp. 392-394
    • Loughlin, A.M.1    D.Marchant, C.2    Lett, S.M.3
  • 34
    • 0023027071 scopus 로고
    • Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli: Homology among outer membrane receptors that interact with TonB
    • Lundrigan, M.D., and Kadner, R.J. (1986) Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli: homology among outer membrane receptors that interact with TonB. J Biol Chem 261.
    • (1986) J Biol Chem , vol.261
    • Lundrigan, M.D.1    Kadner, R.J.2
  • 35
    • 0014360531 scopus 로고
    • Plasma concentration of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard, U., Javid, J., Leim, H.H., Hanstein, A., and Hanna, M. (1968) Plasma concentration of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 32: 811-815.
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Leim, H.H.3    Hanstein, A.4    Hanna, M.5
  • 36
    • 0002455633 scopus 로고
    • Molecular biology and regulation of iron acquisition by Escherichia coli K-12
    • Iglewski, B.H., and Clark, V.L. (eds). San Diego, California: Academic Press
    • Neilands, J.B. (1990) Molecular biology and regulation of iron acquisition by Escherichia coli K-12. In Molecular Basis of Bacterial Pathogenesis. Iglewski, B.H., and Clark, V.L. (eds). San Diego, California: Academic Press, pp. 205-223.
    • (1990) Molecular Basis of Bacterial Pathogenesis , pp. 205-223
    • Neilands, J.B.1
  • 37
    • 0008958082 scopus 로고
    • Periplasm and protein secretion
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology
    • Oliver, D.B. (1987) Periplasm and protein secretion. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology, pp. 56-69.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 56-69
    • Oliver, D.B.1
  • 38
    • 0026596453 scopus 로고
    • Transferrin and heme-compounds as iron sources for pathogenic bacteria
    • Otto, B.R., Vught, A.M.J.J.V.-v., and MacLaren, D.M. (1992) Transferrin and heme-compounds as iron sources for pathogenic bacteria. Crit Rev Microbiol 18: 217-233.
    • (1992) Crit Rev Microbiol , vol.18 , pp. 217-233
    • Otto, B.R.1    Vught, A.M.J.J.V.-V.2    MacLaren, D.M.3
  • 39
    • 0027364814 scopus 로고
    • Molecular characterization of the 98-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis
    • Pettersson, A., Ley, P.V.D., Poolman, J.T., and Tommassen, J. (1993) Molecular characterization of the 98-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis. Infect Immun 61: 4724-4733.
    • (1993) Infect Immun , vol.61 , pp. 4724-4733
    • Pettersson, A.1    Ley, P.V.D.2    Poolman, J.T.A.3    Tommassen, J.4
  • 40
    • 0028345373 scopus 로고
    • Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor
    • Pettersson, A., Maas, A., and Tommassen, J. (1994) Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor. J Bacteriol 176: 1764-1766.
    • (1994) J Bacteriol , vol.176 , pp. 1764-1766
    • Pettersson, A.1    Maas, A.2    Tommassen, J.3
  • 42
    • 0025666854 scopus 로고
    • TonB and the Gram-negative dilemma
    • Postle, K. (1990) TonB and the Gram-negative dilemma. Mol Microbiol 4: 2019-2025.
    • (1990) Mol Microbiol , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 43
    • 0027752437 scopus 로고
    • TonB protein and energy transduction between membranes
    • Postle, K. (1993) TonB protein and energy transduction between membranes. J Bioenerg Biomembr25: 591-601.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 591-601
    • Postle, K.1
  • 44
    • 0024022151 scopus 로고
    • Genetics of the iron dicitrate transport system of Escherichia coli
    • Pressler, U., Staudenmaier, H., Zimmerman, L., and Braun, V. (1988) Genetics of the iron dicitrate transport system of Escherichia coli. J Bacteriol 170: 2716-2724.
    • (1988) J Bacteriol , vol.170 , pp. 2716-2724
    • Pressler, U.1    Staudenmaier, H.2    Zimmerman, L.3    Braun, V.4
  • 45
    • 0028607079 scopus 로고
    • Insertional inactivation of the gene for the meningococcal lactoferrin binding protein
    • Quinn, M.L., Weyer, S.J., Lewis, L.A., Dyer, D.W., and Wagner, P.M. (1994) Insertional inactivation of the gene for the meningococcal lactoferrin binding protein. Microb Pathog 17: 227-237.
    • (1994) Microb Pathog , vol.17 , pp. 227-237
    • Quinn, M.L.1    Weyer, S.J.2    Lewis, L.A.3    Dyer, D.W.4    Wagner, P.M.5
  • 48
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R., and Wittinghofer, A. (1990) The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem Sci 15: 430-434.
    • (1990) Trends Biochem Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 49
    • 0001870287 scopus 로고
    • Detection of proteins
    • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., and Smith, J.A. (eds). New York: John Wiley and Sons, Inc.
    • Sasse, J., and Gallagher, S.R. (1987) Detection of proteins. In Current Protocols in Molecular Biology. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., and Smith, J.A. (eds). New York: John Wiley and Sons, Inc., pp. 10.6.1-10.6.8.
    • (1987) Current Protocols in Molecular Biology , pp. 1061-1068
    • Sasse, J.1    Gallagher, S.R.2
  • 50
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A.B., and Morris, L.J. (1988a) Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect Immun 56: 1144-1149.
    • (1988) Infect Immun , vol.56 , pp. 1144-1149
    • Schryvers, A.B.1    Morris, L.J.2
  • 51
    • 0023974498 scopus 로고
    • Identification and characterization of the transferrin receptor of Neisseria meningitidis
    • Schryvers, A.B., and Morris, L.J. (1988b) Identification and characterization of the transferrin receptor of Neisseria meningitidis. Mol Microbiol 2: 281-288.
    • (1988) Mol Microbiol , vol.2 , pp. 281-288
    • Schryvers, A.B.1    Morris, L.J.2
  • 52
    • 0001071291 scopus 로고
    • Shuttle mutagenesis: A method of introducing transposons into transformable organisms
    • Setlow, J.K., and Hollander, A. (eds). New York: Plenum Press
    • Seifert, H.S., So, M., and Heffron, F. (1986) Shuttle mutagenesis: A method of introducing transposons into transformable organisms. In: Genetic Engineering: Principles and Methods. Setlow, J.K., and Hollander, A. (eds). New York: Plenum Press, pp. 123-133.
    • (1986) Genetic Engineering: Principles and Methods , pp. 123-133
    • Seifert, H.S.1    So, M.2    Heffron, F.3
  • 53
    • 0029100970 scopus 로고
    • Escherichia coli periplasmic protein FepB binds ferrienterobactin
    • Stephens, D.L., Choe, M.D., and Earhart, C.F. (1995) Escherichia coli periplasmic protein FepB binds ferrienterobactin. Microbiology 141: 1647-1654.
    • (1995) Microbiology , vol.141 , pp. 1647-1654
    • Stephens, D.L.1    Choe, M.D.2    Earhart, C.F.3
  • 54
    • 0028968322 scopus 로고
    • The Neisseria meningitidis haemoglobin receptor: Its role in iron utilization and virulence
    • Stojiljkovic, I., Hwa, V., Martain, L.d.S., O'Gaora, P., Nassif, X., Heffron, F., and So, M. (1995) The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence. Mol Microbiol 15: 531-541.
    • (1995) Mol Microbiol , vol.15 , pp. 531-541
    • Stojiljkovic, I.1    Hwa, V.2    Martain, L.D.S.3    O'Gaora, P.4    Nassif, X.5    Heffron, F.6    So, M.7
  • 55
    • 0025976068 scopus 로고
    • Carboxyterminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyve, M., Moons, M., and Tommassen, J. (1991) Carboxyterminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218: 141-148.
    • (1991) J Mol Biol , vol.218 , pp. 141-148
    • Struyve, M.1    Moons, M.2    Tommassen, J.3
  • 56
    • 0026605978 scopus 로고
    • Molecular cloning, nucleotide sequence, and characterization of a 40,000-molecular weight lipoprotein of Haemophilus sommus
    • Theisen, M., Rioux, C.R., and Potter, A.A. (1992) Molecular cloning, nucleotide sequence, and characterization of a 40,000-molecular weight lipoprotein of Haemophilus sommus. Infect Immun 60: 826-831.
    • (1992) Infect Immun , vol.60 , pp. 826-831
    • Theisen, M.1    Rioux, C.R.2    Potter, A.A.3
  • 57
    • 0028308565 scopus 로고
    • Identification and cloning of a fur homologue from Neisseria meningitidis
    • Thomas, C.E., and Sparling, P.F. (1994) Identification and cloning of a fur homologue from Neisseria meningitidis. Mol Microbiol 11: 725-737.
    • (1994) Mol Microbiol , vol.11 , pp. 725-737
    • Thomas, C.E.1    Sparling, P.F.2
  • 58
    • 0026533769 scopus 로고
    • In vivo inhibition of TonB-dependent processes by a TonB box pentapeptide
    • Tuckman, M., and Osbourne, M.S. (1992) In vivo inhibition of TonB-dependent processes by a TonB box pentapeptide. J Bacteriol 174: 320-323.
    • (1992) J Bacteriol , vol.174 , pp. 320-323
    • Tuckman, M.A.1    Osbourne, M.S.2
  • 59
    • 8044247335 scopus 로고
    • The Neisseriaceae: Morphology and nutrition of the Neisseria
    • Barnes, D., Robinson, S.J., and Ewan, H. (eds). Philadelphia: J.B. Lippincott Co.
    • Volk, W.A., Benjamin, D.C., Kadner, R.J., and Parsons, J.T. (1986) The Neisseriaceae: morphology and nutrition of the Neisseria. In Essentials of Medical Microbiology. Barnes, D., Robinson, S.J., and Ewan, H. (eds). Philadelphia: J.B. Lippincott Co., pp. 382-394.
    • (1986) Essentials of Medical Microbiology , pp. 382-394
    • Volk, W.A.1    Benjamin, D.C.2    Kadner, R.J.3    Parsons, J.T.4
  • 60
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta- subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J., and Gay, N.J. (1982) Distantly related sequences in the alpha- and beta- subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1: 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 61
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E.D. (1978) Iron and infection. Microbiol Rev 42: 45-66.
    • (1978) Microbiol Rev , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 62
    • 0021356806 scopus 로고
    • Iron withholding: A defense against infection and neoplasia
    • Weinberg, E.D. (1984) Iron withholding: a defense against infection and neoplasia. Physiol Rev 64: 65-102.
    • (1984) Physiol Rev , vol.64 , pp. 65-102
    • Weinberg, E.D.1
  • 64
    • 0001323636 scopus 로고
    • Transcription elongation and termination in Escherichia coli
    • Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology
    • Yager, T.D., and vonHipple, P.H. (1987) Transcription elongation and termination in Escherichia coli. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., and Umbarger, H.E. (eds). Washington, DC: American Society for Microbiology, pp. 1241-1275.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1241-1275
    • Yager, T.D.1    Vonhipple, P.H.2
  • 65
    • 0028310423 scopus 로고
    • Lipooligosaccharide biosynthesis in pathogenic Neisseria: Cloning, identification and characterization of the phosphoglucomutase gene
    • Zhou, D., Stevens, D.S., Gibson, B.W., Engstrom, J.J., Mcallister, C.F., Lee, F.K.N., and Apicella, M.A. (1994) Lipooligosaccharide biosynthesis in pathogenic Neisseria: Cloning, identification and characterization of the phosphoglucomutase gene. J Biol Chem 269: 11162-11169.
    • (1994) J Biol Chem , vol.269 , pp. 11162-11169
    • Zhou, D.1    Stevens, D.S.2    Gibson, B.W.3    Engstrom, J.J.4    Mcallister, C.F.5    Lee, F.K.N.6    Apicella, M.A.7


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