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Volumn 199, Issue 1, 2001, Pages 143-149

Neutrophil-activating protein (HP-NAP) versus ferritin (Pfr): Comparison of synthesis in Helicobacter pylori

Author keywords

Ferritin; Helicobacter pylori; HP NAP; Neutrophil activating protein; Pfr; Stress

Indexed keywords

ESCHERICHIA COLI; HELICOBACTER PYLORI;

EID: 0035873182     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(01)00174-4     Document Type: Article
Times cited : (37)

References (23)
  • 9
    • 0028843199 scopus 로고
    • Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences
    • D.J. Evans D.G. Evans H.C. Lampert H. Nakano Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori , Anabaena variabilis , Bacillus subtilis and Treponema pallidum , by analysis of gene sequences Gene 153 1995 123 127
    • (1995) Gene , vol.153 , pp. 123-127
    • Evans, D.J.1    Evans, D.G.2    Lampert, H.C.3    Nakano, H.4
  • 10
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • P.M. Harrison P. Arioso The ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta 1275 1996 161 203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arioso, P.2
  • 11
    • 1842370320 scopus 로고    scopus 로고
    • Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori
    • L. Dhaenens F. Szczebara O. Husson Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori Infect. Immun. 65 1997 514 518
    • (1997) Infect. Immun. , vol.65 , pp. 514-518
    • Dhaenens, L.1    Szczebara, F.2    Husson, O.3
  • 13
    • 0031685512 scopus 로고    scopus 로고
    • Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori
    • S. Bereswill U. Waidner S. Odenbreit F. Lichte F. Fassbinder G. Bode M. Kist Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori Microbiology 144 1998 2505 2516
    • (1998) Microbiology , vol.144 , pp. 2505-2516
    • Bereswill, S.1    Waidner, U.2    Odenbreit, S.3    Lichte, F.4    Fassbinder, F.5    Bode, G.6    Kist, M.7
  • 14
    • 0027462566 scopus 로고
    • Paracrystalline inclusions of a novel ferritin containing non-heme iron, produced by the human gastric pathogen Helicobacter pylori: evidence for a third class of ferritins
    • B.A. Frazier J.D. Peifer D.G. Russell P. Falk A.N. Olsen M. Hammar T.U. Westblom S.J. Normark Paracrystalline inclusions of a novel ferritin containing non-heme iron, produced by the human gastric pathogen Helicobacter pylori : evidence for a third class of ferritins J. Bacteriol. 175 1995 966 972
    • (1995) J. Bacteriol. , vol.175 , pp. 966-972
    • Frazier, B.A.1    Peifer, J.D.2    Russell, D.G.3    Falk, P.4    Olsen, A.N.5    Hammar, M.6    Westblom, T.U.7    Normark, S.J.8
  • 16
    • 85120101495 scopus 로고    scopus 로고
    • Majno, G. and Joris, I. (1996) Cells, Tissue and Disease: Principle of General Pathology. Blackwell Science, Oxford.
  • 17
    • 0040731249 scopus 로고    scopus 로고
    • Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress
    • S.N. Wai K. Nakayama K. Umene T. Moriya K. Amako Construction of a ferritin-deficient mutant of Campylobacter jejuni : contribution of ferritin to iron storage and protection against oxidative stress Mol. Microbiol. 20 1996 1127 1134
    • (1996) Mol. Microbiol. , vol.20 , pp. 1127-1134
    • Wai, S.N.1    Nakayama, K.2    Umene, K.3    Moriya, T.4    Amako, K.5
  • 18
    • 0016153291 scopus 로고
    • Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism of paraquat (methyl viologen) toxicity
    • J.S. Bus S.D. Aust J.E. Gibson Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism of paraquat (methyl viologen) toxicity Biochem. Biophys. Res. Commun. 58 1974 749 755
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 19
    • 85120140978 scopus 로고    scopus 로고
    • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A, and Strul K. (1987) Current Protocols in Molecular Biology. John Wiley and Sons, New York.
  • 21
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • M. Almiron A.J. Link D. Furlong R. Kolter A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli Genes Dev. 6 1992 2646 2654
    • (1992) Genes Dev. , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 23
    • 0033001042 scopus 로고    scopus 로고
    • Molecular and cellular activities of Helicobacter pylori pathogenic factors
    • C. Montecucco E. Papini M. de Bernard M. Zoratti Molecular and cellular activities of Helicobacter pylori pathogenic factors FEBS Lett. 452 1999 16 21
    • (1999) FEBS Lett. , vol.452 , pp. 16-21
    • Montecucco, C.1    Papini, E.2    de Bernard, M.3    Zoratti, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.