메뉴 건너뛰기




Volumn 64, Issue 6, 1996, Pages 1950-1955

The conserved 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi has homology to PAL

Author keywords

[No Author keywords available]

Indexed keywords

CROSS REACTING ANTIBODY; GLOBOMYCIN; HYBRID PROTEIN; MONOCLONAL ANTIBODY; OUTER MEMBRANE PROTEIN; SIGNAL PEPTIDE;

EID: 0030010928     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.64.6.1950-1955.1996     Document Type: Article
Times cited : (41)

References (54)
  • 1
    • 0028878701 scopus 로고
    • Sexually transmitted diseases and human immunodeficiency virus control in Malawi: A field study of genital ulcer disease
    • Behets, F. M. T., G. Liomba, G. Lule, G. Dallabetta, I. F. Hoffman, H. A. Hamilton, S. Moeng, and M. S. Cohen. 1995. Sexually transmitted diseases and human immunodeficiency virus control in Malawi: a field study of genital ulcer disease. J. Infect. Dis. 171:451-455.
    • (1995) J. Infect. Dis. , vol.171 , pp. 451-455
    • Behets, F.M.T.1    Liomba, G.2    Lule, G.3    Dallabetta, G.4    Hoffman, I.F.5    Hamilton, H.A.6    Moeng, S.7    Cohen, M.S.8
  • 2
    • 0025879664 scopus 로고
    • Mutant MotB proteins in Escherichia coli
    • Blair, D. F., D. Y. Kim, and H. C. Berg. 1991. Mutant MotB proteins in Escherichia coli. J. Bacteriol. 173:4049-4055.
    • (1991) J. Bacteriol. , vol.173 , pp. 4049-4055
    • Blair, D.F.1    Kim, D.Y.2    Berg, H.C.3
  • 3
    • 0028807979 scopus 로고
    • Mapping of a surface-exposed. conformational epitope of the P6 protein of Haemophilus influenzae
    • Bogdan, J. A., Jr., and M. A. Apicella. 1995. Mapping of a surface-exposed. conformational epitope of the P6 protein of Haemophilus influenzae. Infect. Immun. 63:4395-4401.
    • (1995) Infect. Immun. , vol.63 , pp. 4395-4401
    • Bogdan Jr., J.A.1    Apicella, M.A.2
  • 4
    • 0029063793 scopus 로고
    • Monoclonal antibodies against Haemophilus lipopolysaccharides: Clone DP8 specific for Haemophilus ducreyi and clone DH24 binding to lacto-N-neotetraose
    • Borrelli, S., E. L. Roggen, D. Hendriksen, J. Jonasson, H. J. Ahmed, P. Piot, P.-E. Jansson, and A. A. Lindberg. 1995. Monoclonal antibodies against Haemophilus lipopolysaccharides: clone DP8 specific for Haemophilus ducreyi and clone DH24 binding to lacto-N-neotetraose. Infect. Immun. 63: 2665-2673.
    • (1995) Infect. Immun. , vol.63 , pp. 2665-2673
    • Borrelli, S.1    Roggen, E.L.2    Hendriksen, D.3    Jonasson, J.4    Ahmed, H.J.5    Piot, P.6    Jansson, P.-E.7    Lindberg, A.A.8
  • 5
    • 0030022898 scopus 로고    scopus 로고
    • Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili
    • Brentjens, R. J., M. Ketterer, M. A. Apicella, and S. M. Spinola. 1996. Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili. J. Bacteriol. 178:808-816.
    • (1996) J. Bacteriol. , vol.178 , pp. 808-816
    • Brentjens, R.J.1    Ketterer, M.2    Apicella, M.A.3    Spinola, S.M.4
  • 6
    • 0028338832 scopus 로고
    • Use of pyocin to select a Haemophilus ducreyi variant defective in lipooligosaccharide biosynthesis
    • Campagnari, A. A., R. Karalus, M. Apicella, W. Melaugh, A. J. Lesse, and B. W. Gibson. 1994. Use of pyocin to select a Haemophilus ducreyi variant defective in lipooligosaccharide biosynthesis. Infect. Immun. 62:2379-2386.
    • (1994) Infect. Immun. , vol.62 , pp. 2379-2386
    • Campagnari, A.A.1    Karalus, R.2    Apicella, M.3    Melaugh, W.4    Lesse, A.J.5    Gibson, B.W.6
  • 9
    • 0021909107 scopus 로고
    • Lack of deoxyribonucleic acid relatedness between Haemophilus ducreyi and other Haemophilus species
    • Casin, I., F. Grimont, P. A. D. Grimant, and M.-J. Sanson-Le Pors. 1985. Lack of deoxyribonucleic acid relatedness between Haemophilus ducreyi and other Haemophilus species. Int. J. Syst. Bacteriol. 35:23-25.
    • (1985) Int. J. Syst. Bacteriol. , vol.35 , pp. 23-25
    • Casin, I.1    Grimont, F.2    Grimant, P.A.D.3    Sanson-Le Pors, M.-J.4
  • 10
    • 0023117794 scopus 로고
    • Nucleotide sequence of the gene for the peptidoglycan-associated lipoprotein of Escherichia coli K12
    • Chen, R., and U. Henning. 1987. Nucleotide sequence of the gene for the peptidoglycan-associated lipoprotein of Escherichia coli K12. Eur. J. Biochem. 163:73-77.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 73-77
    • Chen, R.1    Henning, U.2
  • 11
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot, R., and J. Vanderleyden. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 12:333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 13
    • 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
  • 14
    • 0029061591 scopus 로고
    • Characterization of the hgbA locus encoding a hemoglobin receptor from Haemophilus ducreyi
    • Elkins, C., C.-J. Chen, and C. E. Thomas. 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
  • 15
    • 0027243733 scopus 로고
    • Evaluation of mixtures of purified Haemophilus influenzae outer membrane proteins in protection against challenge with nontypeable H. influenzae in the chinchilla otitis media model
    • Green, B. A., M. E. Vazquez, G. W. Zlotnick, G. Quigley-Reape, J. D. Swarts, I. Green, J. L. Cowell, C. D. Bluestone, and W. J. Doyle. 1993. Evaluation of mixtures of purified Haemophilus influenzae outer membrane proteins in protection against challenge with nontypeable H. influenzae in the chinchilla otitis media model. Infect. Immun. 61:1950-1957.
    • (1993) Infect. Immun. , vol.61 , pp. 1950-1957
    • Green, B.A.1    Vazquez, M.E.2    Zlotnick, G.W.3    Quigley-Reape, G.4    Swarts, J.D.5    Green, I.6    Cowell, J.L.7    Bluestone, C.D.8    Doyle, W.J.9
  • 17
    • 0028005246 scopus 로고
    • Induction of protective immunity to Haemophilus ducreyi in the temperature-dependent rabbit model of experimental chancroid
    • Hansen, E. J., S. R. Lumbley, J. A. Richardson, B. K. Purcell, M. K. Stevens, L. D. Cope, J. Datte, and J. D. Radolf. 1994. Induction of protective immunity to Haemophilus ducreyi in the temperature-dependent rabbit model of experimental chancroid. J. Immunol. 152:184-192.
    • (1994) J. Immunol. , vol.152 , pp. 184-192
    • Hansen, E.J.1    Lumbley, S.R.2    Richardson, J.A.3    Purcell, B.K.4    Stevens, M.K.5    Cope, L.D.6    Datte, J.7    Radolf, J.D.8
  • 19
    • 0028973961 scopus 로고
    • The cofactor effect of genital ulcers on the per-exposure risk of HIV transmission in sub-Saharan Africa
    • Hayes, R. J., K. F. Schulz, and F. A. Plummer. 1995. The cofactor effect of genital ulcers on the per-exposure risk of HIV transmission in sub-Saharan Africa. J. Trop. Med. Hyg. 98:1-8.
    • (1995) J. Trop. Med. Hyg. , vol.98 , pp. 1-8
    • Hayes, R.J.1    Schulz, K.F.2    Plummer, F.A.3
  • 21
    • 0020509679 scopus 로고
    • Termination of transcription in E. coli
    • Holmes, W. M., T. Platt, and M. Rosenberg. 1983. Termination of transcription in E. coli. Cell 32:1029-1032.
    • (1983) Cell , vol.32 , pp. 1029-1032
    • Holmes, W.M.1    Platt, T.2    Rosenberg, M.3
  • 22
    • 0019309069 scopus 로고
    • Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin
    • Hussain, M., S. Ichihara, and S. Mizushima. 1980. Accumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin. J. Biol. Chem. 255:3707-3712.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3707-3712
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 23
    • 0028916788 scopus 로고
    • Pasteurella multocida produces a protein with homology to the P6 outer membrane protein of Haemophilus influenzae
    • Kasten, R. W., L. M. Hansen, J. Hinojoza, D. Bieber, W. W. Ruehl, and D. C. Hirsh. 1995. Pasteurella multocida produces a protein with homology to the P6 outer membrane protein of Haemophilus influenzae. Infect. Immun. 63: 989-993.
    • (1995) Infect. Immun. , vol.63 , pp. 989-993
    • Kasten, R.W.1    Hansen, L.M.2    Hinojoza, J.3    Bieber, D.4    Ruehl, W.W.5    Hirsh, D.C.6
  • 24
    • 0023403378 scopus 로고
    • Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria
    • Kawula, T. H., S. M. Spinola, D. G. Klapper, and J. G. Cannon. 1987. Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria. Mol. Microbiol. 2:179-185.
    • (1987) Mol. Microbiol. , vol.2 , pp. 179-185
    • Kawula, T.H.1    Spinola, S.M.2    Klapper, D.G.3    Cannon, J.G.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0024414942 scopus 로고
    • Cloning of the excC and excD genes involved in the release of periplasmic proteins by Escherichia coli K12
    • Lazzaroni, J.-C., N. Fognini-Lefebvre, and R. Portalier. 1989. Cloning of the excC and excD genes involved in the release of periplasmic proteins by Escherichia coli K12. Mol. Gen. Genet. 218:460-464.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 460-464
    • Lazzaroni, J.-C.1    Fognini-Lefebvre, N.2    Portalier, R.3
  • 27
    • 0026588350 scopus 로고
    • The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (PAL)
    • Lazzaroni, J.-C., and R. Portalier. 1992. The excC gene of Escherichia coli K-12 required for cell envelope integrity encodes the peptidoglycan-associated lipoprotein (PAL). Mol. Microbiol. 6:735-742.
    • (1992) Mol. Microbiol. , vol.6 , pp. 735-742
    • Lazzaroni, J.-C.1    Portalier, R.2
  • 28
    • 0019473245 scopus 로고
    • Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12
    • Lazzaroni, J.-C., and R. C. Portalier. 1981. Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12. J. Bacteriol. 145:1351-1358.
    • (1981) J. Bacteriol. , vol.145 , pp. 1351-1358
    • Lazzaroni, J.-C.1    Portalier, R.C.2
  • 30
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 31
    • 0026632877 scopus 로고
    • Partial characterization of the major lipooligosaccharide from a strain of Haemophilus ducreyi, the causative agent of chancroid, a genital ulcer disease
    • Melaugh, W., N. J. Phillips, A. A. Campagnari, R. Karalus, and B. W. Gibson. 1992. Partial characterization of the major lipooligosaccharide from a strain of Haemophilus ducreyi, the causative agent of chancroid, a genital ulcer disease. J. Biol. Chem. 267:13434-13439.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13434-13439
    • Melaugh, W.1    Phillips, N.J.2    Campagnari, A.A.3    Karalus, R.4    Gibson, B.W.5
  • 32
    • 0018566728 scopus 로고
    • A novel peptidoglycan-associated lipoprotein found in the cell envelope of Pseudomonas aeruginosa and Escherichia coli
    • Mizuno, T. 1979. A novel peptidoglycan-associated lipoprotein found in the cell envelope of Pseudomonas aeruginosa and Escherichia coli. J. Biochem. 86:991-1000.
    • (1979) J. Biochem. , vol.86 , pp. 991-1000
    • Mizuno, T.1
  • 33
    • 85085225206 scopus 로고    scopus 로고
    • Personal communication
    • Morse, S. Personal communication.
    • Morse, S.1
  • 34
    • 0024603397 scopus 로고
    • Chancroid and Haemophilus ducreyi
    • Morse, S. A. 1989. Chancroid and Haemophilus ducreyi. Clin. Microbiol. Rev. 2:137-157.
    • (1989) Clin. Microbiol. Rev. , vol.2 , pp. 137-157
    • Morse, S.A.1
  • 35
    • 0022654454 scopus 로고
    • Genetic relationships of serologically nontypable and serotype b strains of Haemophilus influenzae
    • Musser, J. M., S. J. Barenkamp, D. M. Granoff, and R. K. Selander. 1986. Genetic relationships of serologically nontypable and serotype b strains of Haemophilus influenzae. Infect. Immun. 52:183-191.
    • (1986) Infect. Immun. , vol.52 , pp. 183-191
    • Musser, J.M.1    Barenkamp, S.J.2    Granoff, D.M.3    Selander, R.K.4
  • 36
    • 0025915020 scopus 로고
    • Molecular conservation of the P6 outer membrane protein among strains of Haemophilus influenzae: Analysis of antigenic determinants, gene sequences, and restriction fragment length polymorphisms
    • Nelson, M. B., R. S. Munson, Jr., M. A. Apicella, D. J. Sikkema, J. P. Molleston, and T. F. Murphy. 1991. Molecular conservation of the P6 outer membrane protein among strains of Haemophilus influenzae: analysis of antigenic determinants, gene sequences, and restriction fragment length polymorphisms. Infect. Immun. 59:2658-2663.
    • (1991) Infect. Immun. , vol.59 , pp. 2658-2663
    • Nelson, M.B.1    Munson Jr., R.S.2    Apicella, M.A.3    Sikkema, D.J.4    Molleston, J.P.5    Murphy, T.F.6
  • 37
  • 38
    • 0021020170 scopus 로고
    • Characterization of cell proteins of Haemophilus ducreyi by polyacrylamide gel electrophoresis
    • Odumeru, J. A., A. R. Ronald, and W. L. Albritton. 1983. Characterization of cell proteins of Haemophilus ducreyi by polyacrylamide gel electrophoresis. J. Infect. Dis. 148:710-714.
    • (1983) J. Infect. Dis. , vol.148 , pp. 710-714
    • Odumeru, J.A.1    Ronald, A.R.2    Albritton, W.L.3
  • 39
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 40
    • 0028006211 scopus 로고
    • Enzyme immunoassays (EIAs) for the detection of anti-Haemophilus ducreyi serum IgA, IgG, and IgM antibodies
    • Roggen, E. L., G. Hoofd, E. VanDyck, and P. Piot 1994. Enzyme immunoassays (EIAs) for the detection of anti-Haemophilus ducreyi serum IgA, IgG, and IgM antibodies. Sex. Transm. Dis. 21:36-42.
    • (1994) Sex. Transm. Dis. , vol.21 , pp. 36-42
    • Roggen, E.L.1    Hoofd, G.2    VanDyck, E.3    Piot, P.4
  • 42
    • 0025997619 scopus 로고
    • Molecular characterization of Haemophilus ducreyi by ribosomal DNA fingerprinting
    • Sarafian, S. K., T. C. Woods, J. S. Knapp, B. Swaminathan, and S. A. Morse. 1991. Molecular characterization of Haemophilus ducreyi by ribosomal DNA fingerprinting. J. Clin. Microbiol. 29:1949-1954.
    • (1991) J. Clin. Microbiol. , vol.29 , pp. 1949-1954
    • Sarafian, S.K.1    Woods, T.C.2    Knapp, J.S.3    Swaminathan, B.4    Morse, S.A.5
  • 43
    • 0028237058 scopus 로고
    • Structural studies of the cell envelope lipopolysaccharides from Haemophilus ducreyi strains ITM 2665 and ITM 4747
    • Schweda, E. K. H., A. C. Sundstrom, L. M. Eriksson, J. A. Jonasson, and A. A. Lindberg. 1994. Structural studies of the cell envelope lipopolysaccharides from Haemophilus ducreyi strains ITM 2665 and ITM 4747. J. Biol. Chem. 269:12040-12048.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12040-12048
    • Schweda, E.K.H.1    Sundstrom, A.C.2    Eriksson, L.M.3    Jonasson, J.A.4    Lindberg, A.A.5
  • 44
    • 0001071291 scopus 로고
    • Shuttle mutagenesis: A method of introducing transposons into transformable organisms
    • J. K. Setlow and A. Hollander (ed.), Plenum Press, New York
    • Seifert, H. S., M. So, and F. Heffron. 1986. Shuttle mutagenesis: a method of introducing transposons into transformable organisms, p. 123-134. In J. K. Setlow and A. Hollander (ed.), Genetic engineering, principles and methods. Plenum Press, New York.
    • (1986) Genetic Engineering, Principles and Methods , pp. 123-134
    • Seifert, H.S.1    So, M.2    Heffron, F.3
  • 45
    • 0025374676 scopus 로고
    • Cloning and expression in Escherichia coli of a Haemophilus influenzae type b lipooligosaccharide synthesis gene(s) that encode a 2-keto-3-deoxyoctulosonic acid epitope
    • Spinola, S. M., Y. Abu Kwaik, A. J. Lesse, A. A. Campagnari, and M. A. Apicella. 1990. Cloning and expression in Escherichia coli of a Haemophilus influenzae type b lipooligosaccharide synthesis gene(s) that encode a 2-keto-3-deoxyoctulosonic acid epitope. Infect. Immun. 58:1558-1564.
    • (1990) Infect. Immun. , vol.58 , pp. 1558-1564
    • Spinola, S.M.1    Abu Kwaik, Y.2    Lesse, A.J.3    Campagnari, A.A.4    Apicella, M.A.5
  • 46
    • 0026316139 scopus 로고
    • Characterization of an 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi that contains a conserved surface-exposed epitope
    • Spinola, S. M., G. E. Griffiths, J. A. Bogdan, and M. A. Menegus. 1992. Characterization of an 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi that contains a conserved surface-exposed epitope. Infect. Immun. 60:385-391.
    • (1992) Infect. Immun. , vol.60 , pp. 385-391
    • Spinola, S.M.1    Griffiths, G.E.2    Bogdan, J.A.3    Menegus, M.A.4
  • 47
    • 0027480724 scopus 로고
    • The major outer membrane protein of Haemophilus ducreyi is a member of the OmpA family of proteins
    • Spinola, S. M., G. E. Griffiths, K. L. Shanks, and M. S. Blake. 1993. The major outer membrane protein of Haemophilus ducreyi is a member of the OmpA family of proteins. Infect. Immun. 61:1346-1351.
    • (1993) Infect. Immun. , vol.61 , pp. 1346-1351
    • Spinola, S.M.1    Griffiths, G.E.2    Shanks, K.L.3    Blake, M.S.4
  • 49
    • 0027519580 scopus 로고
    • Characterization of an immunoreactive 17.5-kilodalton outer membrane protein of Haemophilus somnus by using a monoclonal antibody
    • Tagawa, Y., M. Haritani, and N. Yuasa. 1993. Characterization of an immunoreactive 17.5-kilodalton outer membrane protein of Haemophilus somnus by using a monoclonal antibody. Infect. Immun. 61:4153-4157.
    • (1993) Infect. Immun. , vol.61 , pp. 4153-4157
    • Tagawa, Y.1    Haritani, M.2    Yuasa, N.3
  • 50
    • 0021962622 scopus 로고
    • Antimicrobial susceptibility and characterization of outer membrane proteins of Haemophilus ducreyi isolated in Thailand
    • Taylor, D. N., P. Echeverria, S. Hanchalay, C. Pitarangsi, L. Slootmans, and P. Piot. 1985. Antimicrobial susceptibility and characterization of outer membrane proteins of Haemophilus ducreyi isolated in Thailand. J. Clin. Microbiol. 21:442-444.
    • (1985) J. Clin. Microbiol. , vol.21 , pp. 442-444
    • Taylor, D.N.1    Echeverria, P.2    Hanchalay, S.3    Pitarangsi, C.4    Slootmans, L.5    Piot, P.6
  • 52
    • 0028981507 scopus 로고
    • Chancroid and Haemophilus ducreyi: An update
    • Trees, D. L., and S. A. Morse. 1995. Chancroid and Haemophilus ducreyi: an update. Clin. Microbiol. Rev. 8:357-375.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 357-375
    • Trees, D.L.1    Morse, S.A.2
  • 53
    • 0027058409 scopus 로고
    • Epidemiological synergy. Interrelationships between human immunodeficiency virus infection and other sexually transmitted diseases
    • Wasserheit, J. N. 1992. Epidemiological synergy. Interrelationships between human immunodeficiency virus infection and other sexually transmitted diseases. Sex. Transm. Dis. 19:61-77.
    • (1992) Sex. Transm. Dis. , vol.19 , pp. 61-77
    • Wasserheit, J.N.1
  • 54
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli OmpA protein
    • Woodruff, W. A., and R. E. W. Hancock. 1989. Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J. Bacteriol. 171:3304-3309.
    • (1989) J. Bacteriol. , vol.171 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.