메뉴 건너뛰기




Volumn 323, Issue 1, 2002, Pages 125-130

Structure of the neutrophil-activating protein from Helicobacter pylori

Author keywords

Crystal structure; Ferritins; Helicobacter pylori; Iron storage; Neutrophil activating protein

Indexed keywords

BACTERIAL PROTEIN; FERRITIN; INTERLEUKIN 8;

EID: 0036398072     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00879-3     Document Type: Article
Times cited : (131)

References (23)
  • 1
    • 20644440421 scopus 로고    scopus 로고
    • Helicobacter pylori gastritis, peptic ulcer, and gastric cancer: Clinical and molecular aspects
    • Goodwin, C. S. (1997). Helicobacter pylori gastritis, peptic ulcer, and gastric cancer: clinical and molecular aspects. Clin. Infect. Dis. 25, 1017-1019.
    • (1997) Clin. Infect. Dis. , vol.25 , pp. 1017-1019
    • Goodwin, C.S.1
  • 2
    • 0035374653 scopus 로고    scopus 로고
    • Living dangerously: How Helicobacter pylori survives in the human stomach
    • Montecucco, C. & Rappuoli, R. (2001). Living dangerously: how Helicobacter pylori survives in the human stomach. Nature Rev. Cell Biol. 2, 457-466.
    • (2001) Nature Rev. Cell Biol. , vol.2 , pp. 457-466
    • Montecucco, C.1    Rappuoli, R.2
  • 3
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R. A., Filman, D. J., Finkel, S. E., Kolter, R. & Hogle, J. M. (1998). The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nature Struct. Biol. 5, 294-303.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 4
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari, A., Stefanini, S., Chiancone, E. & Tsernoglou, D. (2000). The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nature Struct. Biol. 7, 38-43.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 6
    • 0001413894 scopus 로고    scopus 로고
    • The Helicobacter pylori neutrohil-activating protein is an iron-binding protein with dodecameric structure
    • Tonello, F., Dundon, W. G., Satin, B., Molinari, M., Tognon, G., Grandi, G. et al. (1999). The Helicobacter pylori neutrohil-activating protein is an iron-binding protein with dodecameric structure. Mol. Microbiol. 34, 238-246.
    • (1999) Mol. Microbiol. , vol.34 , pp. 238-246
    • Tonello, F.1    Dundon, W.G.2    Satin, B.3    Molinari, M.4    Tognon, G.5    Grandi, G.6
  • 7
    • 0028843199 scopus 로고
    • Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences
    • Evans, D. J., Jr, Evans, D. G., Lampert, H. C. & Nakano, H. (1995). Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences. Gene, 153, 123-127.
    • (1995) Gene , vol.153 , pp. 123-127
    • Evans D.J., Jr.1    Evans, D.G.2    Lampert, H.C.3    Nakano, H.4
  • 9
    • 0035312988 scopus 로고    scopus 로고
    • Helicobacter pylori neutrophil-activating protein stimulates tissue factor and plasminogen activator inhibitor-2 production by human blood mononuclear cells
    • Montemurro, P., Barbuti, G., Dundon, W. G., Del Giudice, G., Rappuoli, R., Colucci, M. et al. (2001). Helicobacter pylori neutrophil-activating protein stimulates tissue factor and plasminogen activator inhibitor-2 production by human blood mononuclear cells. J. Infect. Dis. 183, 1055-1062.
    • (2001) J. Infect. Dis. , vol.183 , pp. 1055-1062
    • Montemurro, P.1    Barbuti, G.2    Dundon, W.G.3    Del Giudice, G.4    Rappuoli, R.5    Colucci, M.6
  • 12
    • 0031883873 scopus 로고    scopus 로고
    • Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin
    • Namavar, F., Sparrius, M., Veerman, E. C., Appelmelk, B. J. & Vandenbroucke-Grauls, C. M. (1998). Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin. Infect. Immun. 66, 444-447.
    • (1998) Infect. Immun. , vol.66 , pp. 444-447
    • Namavar, F.1    Sparrius, M.2    Veerman, E.C.3    Appelmelk, B.J.4    Vandenbroucke-Grauls, C.M.5
  • 14
    • 0026059720 scopus 로고
    • Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
    • Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M., Livingstone, J. C., Treffry, A. et al. (1991). Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature, 349, 541-544.
    • (1991) Nature , vol.349 , pp. 541-544
    • Lawson, D.M.1    Artymiuk, P.J.2    Yewdall, S.J.3    Smith, J.M.4    Livingstone, J.C.5    Treffry, A.6
  • 15
    • 0025999689 scopus 로고
    • Influence of site-directed modifications on the formation of iron cores in ferritin
    • Wade, V. J., Levi, S., Arosio, P., Treffry, A., Harrison, P. M. & Mann, S. (1991). Influence of site-directed modifications on the formation of iron cores in ferritin. J. Mol. Biol. 221, 1443-1452.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1443-1452
    • Wade, V.J.1    Levi, S.2    Arosio, P.3    Treffry, A.4    Harrison, P.M.5    Mann, S.6
  • 16
    • 0035942317 scopus 로고    scopus 로고
    • Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions
    • Laurence, J. S., Blanpain, C., De Leener, A., Parmentier, M. & LiWang, P. J. (2001). Importance of basic residues and quaternary structure in the function of MIP-1 beta: CCR5 binding and cell surface sugar interactions. Biochemistry, 40, 4990-4999.
    • (2001) Biochemistry , vol.40 , pp. 4990-4999
    • Laurence, J.S.1    Blanpain, C.2    De Leener, A.3    Parmentier, M.4    LiWang, P.J.5
  • 18
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras D., Podjarny, A. D. & Thierry, J. P., eds. Oxford University Press, Oxford
    • Leslie, A. G. W. (1991). Molecular data processing. In Crystallographic Computing V (Moras, D., Podjarny, A. D. & Thierry, J. P., eds), pp. 50-61, Oxford University Press, Oxford.
    • (1991) Crystallographic Computing V , pp. 50-61
    • Leslie, A.G.W.1
  • 19
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 20
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A, 50, 157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., McArthur, M. W., Moss, D. S. & Thornton, J. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.4
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.