메뉴 건너뛰기




Volumn 388, Issue 2, 2009, Pages 283-289

Characterizing the polymeric status of Helicobacter pylori heat shock protein 60

Author keywords

Heat shock protein 60; Helicobacter pylori; Inflammation

Indexed keywords

AMINO ACID; DIMER; GAMMA INTERFERON; HEAT SHOCK PROTEIN 60; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 10; INTERLEUKIN 1ALPHA; INTERLEUKIN 8; MELANOMA GROWTH STIMULATORY ACTIVITY FACTOR; OLIGOMER; RANTES; TETRAMER; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR ALPHA;

EID: 69249229490     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.07.159     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 33750075748 scopus 로고    scopus 로고
    • Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses
    • Algood H.M., and Cover T.L. Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses. Clin. Microbiol. Rev. 19 (2006) 597-613
    • (2006) Clin. Microbiol. Rev. , vol.19 , pp. 597-613
    • Algood, H.M.1    Cover, T.L.2
  • 2
    • 0036370334 scopus 로고    scopus 로고
    • Helicobacter pylori and gastrointestinal tract adenocarcinomas
    • Peek Jr. R.M., and Blaser M.J. Helicobacter pylori and gastrointestinal tract adenocarcinomas. Nat. Rev. Cancer 2 (2002) 28-37
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 28-37
    • Peek Jr., R.M.1    Blaser, M.J.2
  • 6
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca M., Borgia S., Hoffman P., and Lingwood C.A. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect. Immun. 64 (1996) 2643-2648
    • (1996) Infect. Immun. , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 7
    • 0023280905 scopus 로고
    • The 65 kDa antigen of mycobacteria-a common bacterial protein?
    • Ivanyi J., Young D.B., Cox J.H., and Lamb J.R. The 65 kDa antigen of mycobacteria-a common bacterial protein?. Immunol. Today 8 (1987) 215-219
    • (1987) Immunol. Today , vol.8 , pp. 215-219
    • Ivanyi, J.1    Young, D.B.2    Cox, J.H.3    Lamb, J.R.4
  • 8
    • 19544373825 scopus 로고    scopus 로고
    • Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes
    • Maguire M., Poole S., Coates A.R., Tormay P., Wheeler-Jones C., and Henderson B. Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes. Immunology 115 (2005) 231-238
    • (2005) Immunology , vol.115 , pp. 231-238
    • Maguire, M.1    Poole, S.2    Coates, A.R.3    Tormay, P.4    Wheeler-Jones, C.5    Henderson, B.6
  • 10
    • 33847226673 scopus 로고    scopus 로고
    • Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a Toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes
    • Zhao Y., Yokota K., Ayada K., Yamamoto Y., Okada T., Shen L., and Oguma K. Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a Toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes. J. Med. Microbiol. 56 (2007) 154-164
    • (2007) J. Med. Microbiol. , vol.56 , pp. 154-164
    • Zhao, Y.1    Yokota, K.2    Ayada, K.3    Yamamoto, Y.4    Okada, T.5    Shen, L.6    Oguma, K.7
  • 13
    • 4143134164 scopus 로고    scopus 로고
    • Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
    • Shimamura T., Koike-Takeshita A., Yokoyama K., Masui R., Murai N., Yoshida M., Taguchi H., and Iwata S. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure 12 (2004) 1471-1480
    • (2004) Structure , vol.12 , pp. 1471-1480
    • Shimamura, T.1    Koike-Takeshita, A.2    Yokoyama, K.3    Masui, R.4    Murai, N.5    Yoshida, M.6    Taguchi, H.7    Iwata, S.8
  • 14
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
    • Chen L., and Sigler P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell 99 (1999) 757-768
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 16
    • 0036359614 scopus 로고    scopus 로고
    • Inflammatory mediators in cystic fibrosis lung disease
    • Berger M. Inflammatory mediators in cystic fibrosis lung disease. Allergy Asthma Proc. 23 (2002) 19-25
    • (2002) Allergy Asthma Proc. , vol.23 , pp. 19-25
    • Berger, M.1
  • 17
    • 42949171833 scopus 로고    scopus 로고
    • Signalling, inflammation and arthritis: NF-kappaB and its relevance to arthritis and inflammation
    • Simmonds R.E., and Foxwell B.M. Signalling, inflammation and arthritis: NF-kappaB and its relevance to arthritis and inflammation. Rheumatology (Oxford) 47 (2008) 584-590
    • (2008) Rheumatology (Oxford) , vol.47 , pp. 584-590
    • Simmonds, R.E.1    Foxwell, B.M.2
  • 18
    • 0025293885 scopus 로고
    • Isolation and characterization of a Treponema pallidum major 60-kilodalton protein resembling the groEL protein of Escherichia coli
    • Houston L.S., Cook R.G., and Norris S.J. Isolation and characterization of a Treponema pallidum major 60-kilodalton protein resembling the groEL protein of Escherichia coli. J. Bacteriol. 172 (1990) 2862-2870
    • (1990) J. Bacteriol. , vol.172 , pp. 2862-2870
    • Houston, L.S.1    Cook, R.G.2    Norris, S.J.3
  • 19
    • 0018791204 scopus 로고
    • Purification and properties of groE: a host protein involved in bacteriophage assembly
    • Hendrix R.W. Purification and properties of groE: a host protein involved in bacteriophage assembly. J. Mol. Biol. 129 (1979) 375-392
    • (1979) J. Mol. Biol. , vol.129 , pp. 375-392
    • Hendrix, R.W.1
  • 20
    • 0028003639 scopus 로고
    • ATP induces non-identity of two rings in chaperonin GroEL
    • Bochkareva E.S., and Girshovich A.S. ATP induces non-identity of two rings in chaperonin GroEL. J. Biol. Chem. 269 (1994) 23869-23871
    • (1994) J. Biol. Chem. , vol.269 , pp. 23869-23871
    • Bochkareva, E.S.1    Girshovich, A.S.2
  • 22
    • 33644845097 scopus 로고    scopus 로고
    • Heat shock protein and innate immunity
    • Tsan M.F., and Gao B. Heat shock protein and innate immunity. Cell. Mol. Immunol. 1 (2004) 274-279
    • (2004) Cell. Mol. Immunol. , vol.1 , pp. 274-279
    • Tsan, M.F.1    Gao, B.2
  • 23
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T-cell regulation of chronic inflammation
    • van Eden W., van der Zee R., and Prakken B. Heat-shock proteins induce T-cell regulation of chronic inflammation. Nat. Rev. Immunol. 5 (2005) 318-330
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 318-330
    • van Eden, W.1    van der Zee, R.2    Prakken, B.3
  • 26
    • 0037300378 scopus 로고    scopus 로고
    • Chemokines: attractive mediators of the immune response
    • Wong M.M., and Fish E.N. Chemokines: attractive mediators of the immune response. Semin. Immunol. 15 (2003) 5-14
    • (2003) Semin. Immunol. , vol.15 , pp. 5-14
    • Wong, M.M.1    Fish, E.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.