메뉴 건너뛰기




Volumn 7, Issue 4, 2002, Pages 317-329

Chaperonin 60 unfolds its secrets of cellular communication

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; CYTOKINE;

EID: 12244263525     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2002)007<0317:CUISOC>2.0.CO;2     Document Type: Short Survey
Times cited : (71)

References (141)
  • 1
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin-1β involves exocytosis of endolysosome-related vesicles
    • Andrei C, Dazzi C, Lotti L, Torrisi MR, Chimini G, Rubartelli A. 1999. The secretory route of the leaderless protein interleukin-1β involves exocytosis of endolysosome-related vesicles. Mol Biol Cell 10: 1463-1475.
    • (1999) Mol Biol Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1    Dazzi, C.2    Lotti, L.3    Torrisi, M.R.4    Chimini, G.5    Rubartelli, A.6
  • 2
  • 3
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway
    • Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK. 2000. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 12: 1539-1546.
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 4
    • 0032765705 scopus 로고    scopus 로고
    • Plasma membrane expression of heat shock protein 60 in vivo in response to infection
    • Belles C, Kuhl A, Nosheny R, Carding SR. 1999. Plasma membrane expression of heat shock protein 60 in vivo in response to infection. Infect Immun 67: 4191-4200.
    • (1999) Infect Immun , vol.67 , pp. 4191-4200
    • Belles, C.1    Kuhl, A.2    Nosheny, R.3    Carding, S.R.4
  • 5
    • 0033952703 scopus 로고    scopus 로고
    • Tlr4: Central component of the sole mammalian LPS sensor
    • Beutler B. 2000. Tlr4: Central component of the sole mammalian LPS sensor. Curr Opin Immunol 12: 20-26.
    • (2000) Curr Opin Immunol , vol.12 , pp. 20-26
    • Beutler, B.1
  • 7
    • 0031869555 scopus 로고    scopus 로고
    • Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency
    • Botzler C, Schmidt J, Luz A, Jennen L, Issels R, Multhoff G. 1998. Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency. Int J Cancer 77: 942-948.
    • (1998) Int J Cancer , vol.77 , pp. 942-948
    • Botzler, C.1    Schmidt, J.2    Luz, A.3    Jennen, L.4    Issels, R.5    Multhoff, G.6
  • 8
    • 0035953547 scopus 로고    scopus 로고
    • TREM-1 amplifies inflammation and is a crucial mediator of septic shock
    • Bouchon A, Facchetti F, Weigand MA, Colonna M. 2001. TREM-1 amplifies inflammation and is a crucial mediator of septic shock. Nature 410: 1103-1107.
    • (2001) Nature , vol.410 , pp. 1103-1107
    • Bouchon, A.1    Facchetti, F.2    Weigand, M.A.3    Colonna, M.4
  • 9
    • 0033861419 scopus 로고    scopus 로고
    • The interleukin-1/Toll-like receptor superfamily: Signal generators for proinflammatory interleukins and microbial products
    • Bowie A, O'Neill LA. 2000. The interleukin-1/Toll-like receptor superfamily: Signal generators for proinflammatory interleukins and microbial products. J Leukoc Biol 67: 508-514.
    • (2000) J Leukoc Biol , vol.67 , pp. 508-514
    • Bowie, A.1    O'Neill, L.A.2
  • 11
    • 0034937409 scopus 로고    scopus 로고
    • Heat shock proteins as 'danger signals:' eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-gamma production in T cells
    • Breloer M, Dorner B, More SH, Roderian T, Fleischer B, von Bonin A. 2001. Heat shock proteins as 'danger signals:' eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-gamma production in T cells. Eur Immunol 31: 2051-2059.
    • (2001) Eur Immunol , vol.31 , pp. 2051-2059
    • Breloer, M.1    Dorner, B.2    More, S.H.3    Roderian, T.4    Fleischer, B.5    Von Bonin, A.6
  • 12
    • 0027178097 scopus 로고
    • Insulitis-caused redistribution of heat-shock protein Hsp60 inside beta-cells correlates with induction of Hsp60 autoantibodies
    • Brudzynski K. 1993. Insulitis-caused redistribution of heat-shock protein Hsp60 inside beta-cells correlates with induction of Hsp60 autoantibodies. Diabetes 42: 908-913.
    • (1993) Diabetes , vol.42 , pp. 908-913
    • Brudzynski, K.1
  • 13
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 14
    • 0031866651 scopus 로고    scopus 로고
    • Extracellular release of antigenic proteins by Helicobacter pylori
    • Cao P, McClain MS, Forsyth MH, Cover TL. 1998. Extracellular release of antigenic proteins by Helicobacter pylori. Infect Immun 66: 2984-2986.
    • (1998) Infect Immun , vol.66 , pp. 2984-2986
    • Cao, P.1    McClain, M.S.2    Forsyth, M.H.3    Cover, T.L.4
  • 15
    • 0033976869 scopus 로고    scopus 로고
    • Localisation of mitochondrial 60-kDa heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules
    • Cechetto JD, Soltys BJ, Gupta RS. 2000. Localisation of mitochondrial 60-kDa heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules. J Histochem Cytochem 48: 45-56.
    • (2000) J Histochem Cytochem , vol.48 , pp. 45-56
    • Cechetto, J.D.1    Soltys, B.J.2    Gupta, R.S.3
  • 18
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • Chen W, Syldath U, Bellmann K, Burkart V, Kolb H. 1999. Human 60-kDa heat-shock protein: A danger signal to the innate immune system. J Immunol 162: 3212-3219.
    • (1999) J Immunol , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 19
    • 0030615025 scopus 로고    scopus 로고
    • TH1 pattern of cytokine secretion by splenic cells from pyelonephritic mice after in-vitro stimulation with hsp-65 of Escherichia coli
    • Chopra U, Vohra H, Chhibber S, Ganguly NK, Sharma S. 1997. TH1 pattern of cytokine secretion by splenic cells from pyelonephritic mice after in-vitro stimulation with hsp-65 of Escherichia coli. J Med Microbiol 46: 139-144.
    • (1997) J Med Microbiol , vol.46 , pp. 139-144
    • Chopra, U.1    Vohra, H.2    Chhibber, S.3    Ganguly, N.K.4    Sharma, S.5
  • 20
    • 0031002736 scopus 로고    scopus 로고
    • Protein transport: The nonclassical ins and outs
    • Cleves AE. 1997. Protein transport: The nonclassical ins and outs. Curr Biol 7: R318-R320.
    • (1997) Curr Biol , vol.7
    • Cleves, A.E.1
  • 21
    • 0031851160 scopus 로고    scopus 로고
    • Chaperonins in health and disease
    • Coates AR, Henderson B. 1998. Chaperonins in health and disease. Ann N Y Acad Sci 851: 48-53.
    • (1998) Ann N Y Acad Sci , vol.851 , pp. 48-53
    • Coates, A.R.1    Henderson, B.2
  • 22
    • 0035253485 scopus 로고    scopus 로고
    • The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis
    • Corrigall VM, Bodman-Smith M, Fife MS, et al. 2001. The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis. J Immunol 166: 1492-498.
    • (2001) J Immunol , vol.166 , pp. 1492-1498
    • Corrigall, V.M.1    Bodman-Smith, M.2    Fife, M.S.3
  • 23
    • 0034292391 scopus 로고    scopus 로고
    • Exaggerated human monocyte IL-10 concomitant to minimal TNF-α induction by heat shock protein 27 (hsp27) suggests hsp27 is primarily an antiinflammatory stimulus
    • De AK, Kodys KM, Yeh BS, Miller-Graziano C. 2000. Exaggerated human monocyte IL-10 concomitant to minimal TNF-α induction by heat shock protein 27 (hsp27) suggests hsp27 is primarily an antiinflammatory stimulus. J Immunol 165:3951-3958.
    • (2000) J Immunol , vol.165 , pp. 3951-3958
    • De, A.K.1    Kodys, K.M.2    Yeh, B.S.3    Miller-Graziano, C.4
  • 24
    • 0034194396 scopus 로고    scopus 로고
    • Chaperone substrates inside the cell
    • Ellis RJ. 2000. Chaperone substrates inside the cell. Trends Biochem Sci 25: 210-212.
    • (2000) Trends Biochem Sci , vol.25 , pp. 210-212
    • Ellis, R.J.1
  • 25
    • 0035846548 scopus 로고    scopus 로고
    • Molecular chaperones: Inside and outside the Anfinsen cage
    • Ellis RJ. 2001. Molecular chaperones: Inside and outside the Anfinsen cage. Curr Biol 11: R1038-R1040.
    • (2001) Curr Biol , vol.11
    • Ellis, R.J.1
  • 26
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis RJ, Hartl FU. 1996. Protein folding in the cell: Competing models of chaperonin function. FASEB J 10: 20-26.
    • (1996) FASEB J , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 27
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis RJ, Hartl FU. 1999. Principles of protein folding in the cellular environment. Curr Opin Struct Biol 9: 102-110.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 28
    • 0027104883 scopus 로고
    • Surface expression of heat shock protein 90 by blood mononuclear cells from patients with systemic lupus erythematosus
    • Erkeller-Yuksel FM, Isenberg DA, Dhillon VB, Latchman DS, Lydyard PM. 1992. Surface expression of heat shock protein 90 by blood mononuclear cells from patients with systemic lupus erythematosus. J Autoimmun 5: 803-814.
    • (1992) J Autoimmun , vol.5 , pp. 803-814
    • Erkeller-Yuksel, F.M.1    Isenberg, D.A.2    Dhillon, V.B.3    Latchman, D.S.4    Lydyard, P.M.5
  • 29
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat shock proteins in human tumour cells
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C. 1992. Unusual expression and localization of heat shock proteins in human tumour cells. Int J Cancer 51: 613-619.
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 30
    • 0030572184 scopus 로고    scopus 로고
    • Adhesion molecules - Part 1
    • Frenette PS, Wagner DD. 1996. Adhesion molecules - Part 1. N Engl J Med 334: 1526-1529.
    • (1996) N Engl J Med , vol.334 , pp. 1526-1529
    • Frenette, P.S.1    Wagner, D.D.2
  • 31
    • 0027472869 scopus 로고
    • Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells
    • Friedland JS, Shattock R, Remick DG, Griffin GE. 1993. Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells. Clin Exp Immunol 91: 58-62.
    • (1993) Clin Exp Immunol , vol.91 , pp. 58-62
    • Friedland, J.S.1    Shattock, R.2    Remick, D.G.3    Griffin, G.E.4
  • 32
    • 0031888740 scopus 로고    scopus 로고
    • GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells
    • Frisk A, Ison CA, Lagergard T. 1998. GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells. Infect Immun 66: 1252-1257.
    • (1998) Infect Immun , vol.66 , pp. 1252-1257
    • Frisk, A.1    Ison, C.A.2    Lagergard, T.3
  • 34
    • 0031030347 scopus 로고    scopus 로고
    • Cytokine and adhesion molecule expression in human monocytes and endothelial cells stimulated with bacterial heat shock proteins
    • Galdiero M, de l'Ero GC, Marcatili A. 1997. Cytokine and adhesion molecule expression in human monocytes and endothelial cells stimulated with bacterial heat shock proteins. Infect Immun 65: 699-707.
    • (1997) Infect Immun , vol.65 , pp. 699-707
    • Galdiero, M.1    De l'Ero, G.C.2    Marcatili, A.3
  • 35
    • 0035139983 scopus 로고    scopus 로고
    • Danger signals: SOS to the immune system
    • Gallucci S, Matzinger P. 2001. Danger signals: SOS to the immune system. Curr Opin Immunol 13: 114-119.
    • (2001) Curr Opin Immunol , vol.13 , pp. 114-119
    • Gallucci, S.1    Matzinger, P.2
  • 37
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduno RA, Garduno E, Hoffman PS. 1998a. Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect Immun 66: 4602-4610.
    • (1998) Infect Immun , vol.66 , pp. 4602-4610
    • Garduno, R.A.1    Garduno, E.2    Hoffman, P.S.3
  • 39
    • 0017879067 scopus 로고
    • Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product)
    • Georgopoulos CP, Hohn B. 1978. Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product). Proc Natl Acad Sci U S A 75: 131-135.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 131-135
    • Georgopoulos, C.P.1    Hohn, B.2
  • 40
    • 0032438164 scopus 로고    scopus 로고
    • Subcellular localisation and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans
    • Goulhen F, Hafezi A, Uitto V-J, Hinode D, Nakamura R, Grenier D, Mayrand D. 1998. Subcellular localisation and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans. Infect Immun 66: 5307-5313.
    • (1998) Infect Immun , vol.66 , pp. 5307-5313
    • Goulhen, F.1    Hafezi, A.2    Uitto, V.-J.3    Hinode, D.4    Nakamura, R.5    Grenier, D.6    Mayrand, D.7
  • 41
    • 0035783391 scopus 로고    scopus 로고
    • Review: A structural view of the GroE chaperone cycle
    • Grallert H, Buchner J. 2001. Review: A structural view of the GroE chaperone cycle. J Struct Biol 135: 95-103.
    • (2001) J Struct Biol , vol.135 , pp. 95-103
    • Grallert, H.1    Buchner, J.2
  • 44
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • Gutsche I, Essen LO, Baumeister W. 1999. Group II chaperonins: New TRiC(k)s and turns of a protein folding machine. J Mol Biol 293: 295-312.
    • (1999) J Mol Biol , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3
  • 45
    • 0037080218 scopus 로고    scopus 로고
    • The receptor for heat shock protein 60 on macrophages is saturable, specific and distinct from receptors for other heat shock proteins
    • Habich C, Baumgart K, Kolb H, Burkart V. 2002. The receptor for heat shock protein 60 on macrophages is saturable, specific and distinct from receptors for other heat shock proteins. J Immunol 168:569-576,
    • (2002) J Immunol , vol.168 , pp. 569-576
    • Habich, C.1    Baumgart, K.2    Kolb, H.3    Burkart, V.4
  • 46
    • 0034647970 scopus 로고    scopus 로고
    • Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein
    • Haga A, Ninaka Y, Raz A. 2000. Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein. Biochim Biophys Acta 1480: 235-244.
    • (2000) Biochim Biophys Acta , vol.1480 , pp. 235-244
    • Haga, A.1    Ninaka, Y.2    Raz, A.3
  • 49
    • 0032189012 scopus 로고    scopus 로고
    • The GroEL-like protein from Campylobacter rectus: Immunological characterization and interleukin-6 and -8 induction in human gingival fibroblast
    • Hinode D, Yoshioka M, Tanabe S, Miki O, Masuda K, Nakamura R. 1998. The GroEL-like protein from Campylobacter rectus: Immunological characterization and interleukin-6 and -8 induction in human gingival fibroblast. FEMS Microbiol Lett 167: 1-6.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 1-6
    • Hinode, D.1    Yoshioka, M.2    Tanabe, S.3    Miki, O.4    Masuda, K.5    Nakamura, R.6
  • 50
    • 0031665599 scopus 로고    scopus 로고
    • Localization of pNT22 70 kDa heat shock cognate-like protein in the plasma membrane
    • Hirai I, Sato N, Qi W, Ohtani S, Torigoe T, Kikuchi K. 1998. Localization of pNT22 70 kDa heat shock cognate-like protein in the plasma membrane. Cell Struct Funct 23: 153-158.
    • (1998) Cell Struct Funct , vol.23 , pp. 153-158
    • Hirai, I.1    Sato, N.2    Qi, W.3    Ohtani, S.4    Torigoe, T.5    Kikuchi, K.6
  • 52
    • 0026610981 scopus 로고
    • An interaction between p21ras and heat shock protein hsp60, a chaperonin
    • Ikawa S, Weinberg RA. 1992. An interaction between p21ras and heat shock protein hsp60, a chaperonin. Proc Natl Acad Sci U S A 89: 2012-2016.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 2012-2016
    • Ikawa, S.1    Weinberg, R.A.2
  • 53
    • 2642618620 scopus 로고    scopus 로고
    • Presidential address to the American Association for Immunologists: The road less traveled by: The role of innate immunity in the adaptive immune response
    • Janeway CA. 1998. Presidential address to the American Association for Immunologists: The road less traveled by: The role of innate immunity in the adaptive immune response. J Immunol 161: 539-544.
    • (1998) J Immunol , vol.161 , pp. 539-544
    • Janeway, C.A.1
  • 54
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery CJ. 1999. Moonlighting proteins. Trends Biochem Sci 24: 8-11.
    • (1999) Trends Biochem Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 55
    • 0034633691 scopus 로고    scopus 로고
    • Heat shock protein 60 sequence comparisons: Duplications, lateral transfer, and mitochondrial evolution
    • Karlin S, Brocchieri L. 2000. Heat shock protein 60 sequence comparisons: Duplications, lateral transfer, and mitochondrial evolution. Proc Natl Acad Sci U S A 97: 11348-11353.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11348-11353
    • Karlin, S.1    Brocchieri, L.2
  • 56
    • 0035321067 scopus 로고    scopus 로고
    • The evolution and genetics of innate immunity
    • Kimbrell DA, Beutler B. 2001. The evolution and genetics of innate immunity. Nat Genet 2: 256-267.
    • (2001) Nat Genet , vol.2 , pp. 256-267
    • Kimbrell, D.A.1    Beutler, B.2
  • 57
    • 0034952318 scopus 로고    scopus 로고
    • Heat shock protein specific T-cell response in chlamydial infections
    • Kinnunen A, Paavonen J, Surcel H-M. 2001. Heat shock protein specific T-cell response in chlamydial infections. Scand J Immunol 54: 76-81.
    • (2001) Scand J Immunol , vol.54 , pp. 76-81
    • Kinnunen, A.1    Paavonen, J.2    Surcel, H.-M.3
  • 58
    • 0029091268 scopus 로고
    • The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL
    • Kirby AC, Meghji S, Nair SP, et al. 1995. The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL. J Clin Invest 96: 1185-1194.
    • (1995) J Clin Invest , vol.96 , pp. 1185-1194
    • Kirby, A.C.1    Meghji, S.2    Nair, S.P.3
  • 59
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol A, Bourcier T, Lichtman AH, Libby P. 1999. Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. J Clin Invest 103: 571-577.
    • (1999) J Clin Invest , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 60
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol A, Lichtman AH, Finberg RW, Libby P, Kurt-Jones EA. 2000. Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J Immunol 164: 13-17.
    • (2000) J Immunol , vol.164 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 62
    • 0035870143 scopus 로고    scopus 로고
    • Stimulatory effect of fibroblast growth factor on induction of heat shock protein 27 in osteoblasts: Role of protein kinase C
    • Kozawa O, Niwa M, Matsuno H, Ishisaki A, Kato K, Uematsu T. 2001. Stimulatory effect of fibroblast growth factor on induction of heat shock protein 27 in osteoblasts: Role of protein kinase C. Arch Biochem Biophys 388: 237-242.
    • (2001) Arch Biochem Biophys , vol.388 , pp. 237-242
    • Kozawa, O.1    Niwa, M.2    Matsuno, H.3    Ishisaki, A.4    Kato, K.5    Uematsu, T.6
  • 63
    • 0035183063 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain
    • Lewthwaite JC, Coates AR, Tormay P, et al. 2001. Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain. Infect Immun 69: 7349-7355.
    • (2001) Infect Immun , vol.69 , pp. 7349-7355
    • Lewthwaite, J.C.1    Coates, A.R.2    Tormay, P.3
  • 64
    • 0036556704 scopus 로고    scopus 로고
    • Rhizobium leguminosarum chaperonin 60-3, but not chaperonin 60.1, induces cytokine production by human leukocytes: Activity is dependent on interaction with cell surface CD14
    • Lewthwaite JC, George R, Lund PA, Poole S, Tormay P, Sharp L, Coates ARM, Henderson B. 2002. Rhizobium leguminosarum chaperonin 60-3, but not chaperonin 60.1, induces cytokine production by human leukocytes: Activity is dependent on interaction with cell surface CD14. Cell Stress Chaperones 7: 130-137.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 130-137
    • Lewthwaite, J.C.1    George, R.2    Lund, P.A.3    Poole, S.4    Tormay, P.5    Sharp, L.6    Coates, A.R.M.7    Henderson, B.8
  • 65
    • 0031756356 scopus 로고    scopus 로고
    • Are molecular chaperones microbial virulence factors?
    • Lewthwaite J, Skinner A, Henderson B. 1998. Are molecular chaperones microbial virulence factors? Trends Microbiol 6: 426-428.
    • (1998) Trends Microbiol , vol.6 , pp. 426-428
    • Lewthwaite, J.1    Skinner, A.2    Henderson, B.3
  • 66
  • 67
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
    • Lorimer GH. 1996. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J 10: 5-9.
    • (1996) FASEB J , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 68
    • 0031769504 scopus 로고    scopus 로고
    • Identification of a 71-kilodalton surface-associated Hsp70 homologue in Coxiella burnetii
    • Macellaro A, Tujulin E, Hjalmarsson K, Norlander L. 1998. Identification of a 71-kilodalton surface-associated Hsp70 homologue in Coxiella burnetii. Infect Immun 66: 5882-5888.
    • (1998) Infect Immun , vol.66 , pp. 5882-5888
    • Macellaro, A.1    Tujulin, E.2    Hjalmarsson, K.3    Norlander, L.4
  • 69
    • 1842412518 scopus 로고    scopus 로고
    • TNF-alpha, IL-1 alpha, IL-6 and ICAM-1 expression in human keratinocytes stimulated in vitro with Escherichia coli heat-shock proteins
    • Marcatili A, Cipollaro DL, Galdiero M, Folgore A, Petrillo G. 1997. TNF-alpha, IL-1 alpha, IL-6 and ICAM-1 expression in human keratinocytes stimulated in vitro with Escherichia coli heat-shock proteins. Microbiology 143: 45-53.
    • (1997) Microbiology , vol.143 , pp. 45-53
    • Marcatili, A.1    Cipollaro, D.L.2    Galdiero, M.3    Folgore, A.4    Petrillo, G.5
  • 70
    • 0028201732 scopus 로고
    • Tolerance, danger and the extended family
    • Matzinger P. 1994. Tolerance, danger and the extended family. Annu Rev Immunol 12: 991-1045.
    • (1994) Annu Rev Immunol , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 71
    • 0032191916 scopus 로고    scopus 로고
    • An innate sense of danger
    • Matzinger P. 1998. An innate sense of danger. Semin Immunol 10: 399-415.
    • (1998) Semin Immunol , vol.10 , pp. 399-415
    • Matzinger, P.1
  • 72
    • 0034956209 scopus 로고    scopus 로고
    • Essay 1: The Danger Model in its historical context
    • Matzinger P. 2001. Essay 1: The Danger Model in its historical context. Scand J Immunol 54: 4-9.
    • (2001) Scand J Immunol , vol.54 , pp. 4-9
    • Matzinger, P.1
  • 73
    • 0034702910 scopus 로고    scopus 로고
    • Infections, immunity, and atherosclerosis: Associations of antibodies to Chlamydia pneumoniae, Helicobacter pylori, and cytomegalovirus with immune reactions to heat-shock protein 60 and carotid or femoral atherosclerosis
    • Mayr M, Kiechl S, Willeit J, Wick G, Xu Q. 2000. Infections, immunity, and atherosclerosis: Associations of antibodies to Chlamydia pneumoniae, Helicobacter pylori, and cytomegalovirus with immune reactions to heat-shock protein 60 and carotid or femoral atherosclerosis. Circulation 102: 833-839.
    • (2000) Circulation , vol.102 , pp. 833-839
    • Mayr, M.1    Kiechl, S.2    Willeit, J.3    Wick, G.4    Xu, Q.5
  • 74
    • 2642659387 scopus 로고    scopus 로고
    • GroE is vital for cell-wall synthesis
    • McLennan N, Masters M. 1998. GroE is vital for cell-wall synthesis. Nature 392: 139.
    • (1998) Nature , vol.392 , pp. 139
    • McLennan, N.1    Masters, M.2
  • 75
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway CA, Jr. 1997. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388: 394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway C.A., Jr.3
  • 76
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R, Janeway CA, Jr. 1997. Innate immunity: The virtues of a nonclonal system of recognition. Cell 91: 295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 77
    • 0032191163 scopus 로고    scopus 로고
    • Innate immune recognition and control of adaptive immune responses
    • Medzhitov R, Janeway CA, Jr. 1998. Innate immune recognition and control of adaptive immune responses. Semin Immunol 10: 351-353.
    • (1998) Semin Immunol , vol.10 , pp. 351-353
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 78
    • 0030728057 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: A potential contributory factor in Pott's disease
    • Meghji S, White PA, Nair SP, et al. 1997. Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: A potential contributory factor in Pott's disease. J Exp Med 186: 1241-1246.
    • (1997) J Exp Med , vol.186 , pp. 1241-1246
    • Meghji, S.1    White, P.A.2    Nair, S.P.3
  • 79
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex
    • Mignatti P, Morimoto T, Rifkin DB. 1992. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J Cell Physiol 151: 81-93.
    • (1992) J Cell Physiol , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 81
    • 0028953056 scopus 로고
    • A stress inducible 72-kDa heat shock protein (HSP72) is expressed on the surface of human tumour cells, but not normal cells
    • Multhoff G, Botzler C, Weisnet M, Muller E, Meier T, Wilmanns W, Issels RD. 1995. A stress inducible 72-kDa heat shock protein (HSP72) is expressed on the surface of human tumour cells, but not normal cells. Int J Cancer 61: 272-279.
    • (1995) Int J Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Weisnet, M.3    Muller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 82
    • 0034819316 scopus 로고    scopus 로고
    • Essential roles of CD14 and lipopolysaccharide-binding protein for activation of toll-like receptor (TLR)2 as well as TLR4: Reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations
    • Muta T, Takeshige K. 2001. Essential roles of CD14 and lipopolysaccharide-binding protein for activation of toll-like receptor (TLR)2 as well as TLR4: Reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations. Eur J Immunol 268: 4580-4589.
    • (2001) Eur J Immunol , vol.268 , pp. 4580-4589
    • Muta, T.1    Takeshige, K.2
  • 84
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex
    • Ohashi K, Burkart V, Flohe S, Kolb H. 2000. Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J Immunol 164: 558-561.
    • (2000) J Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 85
    • 0033986771 scopus 로고    scopus 로고
    • Localization of heat shock proteins in clinical Actinobacillus actinomycetemcomitans strains and their effects on epithelial cell proliferation
    • Paju S, Goulhen F, Asikainen S, Grenier D, Mayrand D, Uitto V. 2000. Localization of heat shock proteins in clinical Actinobacillus actinomycetemcomitans strains and their effects on epithelial cell proliferation. FEMS Microbiol Lett 182: 231-235.
    • (2000) FEMS Microbiol Lett , vol.182 , pp. 231-235
    • Paju, S.1    Goulhen, F.2    Asikainen, S.3    Grenier, D.4    Mayrand, D.5    Uitto, V.6
  • 86
    • 0033868316 scopus 로고    scopus 로고
    • A self-hsp60 peptide acts as a partial agonist inducing expression of B7-2 on mycobacterial hsp60-specific T cells: A possible mechanism for inhibitory T cell regulation of adjuvant arthritis
    • Paul AGA, van der Zee R, Taams LS, van Eden W. 2000. A self-hsp60 peptide acts as a partial agonist inducing expression of B7-2 on mycobacterial hsp60-specific T cells: A possible mechanism for inhibitory T cell regulation of adjuvant arthritis. Int Immunol 12: 1041-1050.
    • (2000) Int Immunol , vol.12 , pp. 1041-1050
    • Paul, A.G.A.1    Van der Zee, R.2    Taams, L.S.3    Van Eden, W.4
  • 87
    • 0028816053 scopus 로고
    • Mucosal expression by B7-positive cells of the 60-kilodalton heat-shock protein in inflammatory bowel disease
    • Peetermans WE, D'Haens GR, Ceuppens JL, Rutgeerts P, Geboes K. 1995. Mucosal expression by B7-positive cells of the 60-kilodalton heat-shock protein in inflammatory bowel disease. Gastroenterology 108: 75-82.
    • (1995) Gastroenterology , vol.108 , pp. 75-82
    • Peetermans, W.E.1    D'Haens, G.R.2    Ceuppens, J.L.3    Rutgeerts, P.4    Geboes, K.5
  • 88
    • 0028364251 scopus 로고
    • Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes
    • Peetermans WE, Raats CJ, Langermans JA, van Furth R. 1994. Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes. Scand J Immunol 39: 613-617.
    • (1994) Scand J Immunol , vol.39 , pp. 613-617
    • Peetermans, W.E.1    Raats, C.J.2    Langermans, J.A.3    Van Furth, R.4
  • 89
    • 0032896726 scopus 로고    scopus 로고
    • Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals
    • Pockley AG, Bulmer J, Hanks BM, Wright BH. 1999. Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals. Cell Stress Chaperones 4: 29-35.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 29-35
    • Pockley, A.G.1    Bulmer, J.2    Hanks, B.M.3    Wright, B.H.4
  • 91
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in CEH/HeJ and C57BL/10CcCr mice: Mutations in the Tlr4 gene
    • Poltorak A, He X, Sminirva I, et al. 1998. Defective LPS signaling in CEH/HeJ and C57BL/10CcCr mice: Mutations in the Tlr4 gene. Science 282: 2085-2088.
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Sminirva, I.3
  • 92
    • 0025946853 scopus 로고
    • The aromatic amino acid content of the bacterial chaperone protein groEl (Cpn60): Evidence for the presence of a single tryptophan
    • Price N, Kelly SM, Wood S, auf de Mauer A. 1991. The aromatic amino acid content of the bacterial chaperone protein groEl (Cpn60): Evidence for the presence of a single tryptophan. FEBS Lett 292: 9-12.
    • (1991) FEBS Lett , vol.292 , pp. 9-12
    • Price, N.1    Kelly, S.M.2    Wood, S.3    De Mauer, A.4
  • 93
    • 0027446922 scopus 로고
    • Lipopolysaccharide activation of human endothelial and epithelial cells is mediated by lipopolysaccharide-binding protein and soluble CD14
    • Pugin J, Schurer-Maly CC, Leturcq D, Moriarty A, Ulevitch RJ, Tobias PS. 1993. Lipopolysaccharide activation of human endothelial and epithelial cells is mediated by lipopolysaccharide-binding protein and soluble CD14. Proc Natl Acad Sci U S A 90: 2744-2748.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2744-2748
    • Pugin, J.1    Schurer-Maly, C.C.2    Leturcq, D.3    Moriarty, A.4    Ulevitch, R.J.5    Tobias, P.S.6
  • 94
    • 0035500862 scopus 로고    scopus 로고
    • Lipopolysaccharides from distinct pathogens induce different classes of immune responses in vivo
    • Pulendran B, Kumar P, Cutler CW, Mohamadzadeh M, Van Dyke T, Banchereau J. 2001. Lipopolysaccharides from distinct pathogens induce different classes of immune responses in vivo. J Immunol 167: 5067-5076.
    • (2001) J Immunol , vol.167 , pp. 5067-5076
    • Pulendran, B.1    Kumar, P.2    Cutler, C.W.3    Mohamadzadeh, M.4    Van Dyke, T.5    Banchereau, J.6
  • 96
    • 0034955469 scopus 로고    scopus 로고
    • Heat shock protein-56 is induced by cardiotrophin-1 I and mediates its hypertropic effect
    • Railson JE, Lawrence K, Buddle JC, Pennica D, Latchman DS. 2001. Heat shock protein-56 is induced by cardiotrophin-1 I and mediates its hypertropic effect. J Mol Cell Cardiol 33: 1209-1221.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1209-1221
    • Railson, J.E.1    Lawrence, K.2    Buddle, J.C.3    Pennica, D.4    Latchman, D.S.5
  • 97
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (MRP) 8 and MRP14, calcium binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway
    • Rammes A, Roth J, Goebeler M, Klempt M, Hartmann M, Sorg C. 1997. Myeloid-related protein (MRP) 8 and MRP14, calcium binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J Biol Chem 272:9496-9502.
    • (1997) J Biol Chem , vol.272 , pp. 9496-9502
    • Rammes, A.1    Roth, J.2    Goebeler, M.3    Klempt, M.4    Hartmann, M.5    Sorg, C.6
  • 99
    • 0027525563 scopus 로고
    • Molecular characterization and outer membrane association of a Chlamydia trachomatis protein related to the hsp70 family of proteins
    • Raulston JE, Davis CH, Schmiel DH, Morgan MW, Wyrick PB. 1993. Molecular characterization and outer membrane association of a Chlamydia trachomatis protein related to the hsp70 family of proteins. J Biol Chem 268: 22139-22147.
    • (1993) J Biol Chem , vol.268 , pp. 22139-22147
    • Raulston, J.E.1    Davis, C.H.2    Schmiel, D.H.3    Morgan, M.W.4    Wyrick, P.B.5
  • 100
    • 0035944844 scopus 로고    scopus 로고
    • Beta-cell function in new-onset type I diabetes and immunomodulation with a heat shock protein peptide (DiaPep 277): A randomized, double blind, phase II trial
    • Raz I, Elias D, Avron A, Tamir M, Metzger M, Cohen IR. 2001. Beta-cell function in new-onset type I diabetes and immunomodulation with a heat shock protein peptide (DiaPep 277): A randomized, double blind, phase II trial. Lancet 358: 1749-1753.
    • (2001) Lancet , vol.358 , pp. 1749-1753
    • Raz, I.1    Elias, D.2    Avron, A.3    Tamir, M.4    Metzger, M.5    Cohen, I.R.6
  • 101
    • 0035114098 scopus 로고    scopus 로고
    • Serum heat shock protein and anti-heat shock protein antibody levels in aging
    • Rea IM, McNerlan S, Pockley AG. 2001. Serum heat shock protein and anti-heat shock protein antibody levels in aging. Exp Gerontol 36: 341-352.
    • (2001) Exp Gerontol , vol.36 , pp. 341-352
    • Rea, I.M.1    McNerlan, S.2    Pockley, A.G.3
  • 102
    • 0031830486 scopus 로고    scopus 로고
    • The Escherichia coli chaperonin 60 (GroEL) is a potent stimulator of osteoclast formation
    • Reddi K, Meghji S, Nair SP, et al. 1998. The Escherichia coli chaperonin 60 (GroEL) is a potent stimulator of osteoclast formation. J Bone Miner Res 13: 1260-1266.
    • (1998) J Bone Miner Res , vol.13 , pp. 1260-1266
    • Reddi, K.1    Meghji, S.2    Nair, S.P.3
  • 103
    • 0028113172 scopus 로고
    • Bacterial heat shock proteins directly induce cytokine mRNA and interleukin-1 secretion in macrophage cultures
    • Retzlaff C, Yamamoto Y, Hoffman PS, Friedman H, Klein TW. 1994. Bacterial heat shock proteins directly induce cytokine mRNA and interleukin-1 secretion in macrophage cultures. Infect Immun 62: 5689-5693.
    • (1994) Infect Immun , vol.62 , pp. 5689-5693
    • Retzlaff, C.1    Yamamoto, Y.2    Hoffman, P.S.3    Friedman, H.4    Klein, T.W.5
  • 104
    • 0034711676 scopus 로고    scopus 로고
    • Infections, inflammation, and the risk of coronary heart disease
    • Roivainen M, Viik-Kajender M, Palosuo T, et al. 2000. Infections, inflammation, and the risk of coronary heart disease. Circulation 101: 252-257.
    • (2000) Circulation , vol.101 , pp. 252-257
    • Roivainen, M.1    Viik-Kajender, M.2    Palosuo, T.3
  • 105
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • Rubartelli A, Cozzolino F, Talio M, Sitia R. 1990. A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EMBO J 9: 1503-1510.
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 106
    • 0033813317 scopus 로고    scopus 로고
    • Conformational changes studied by cryo-electron microscopy
    • Saibil HR. 2000a. Conformational changes studied by cryo-electron microscopy. Nat Struct Biol 7: 711-714.
    • (2000) Nat Struct Biol , vol.7 , pp. 711-714
    • Saibil, H.R.1
  • 107
    • 0034081637 scopus 로고    scopus 로고
    • Molecular chaperones: Containers and surfaces for folding, stabilising of unfolding proteins
    • Saibil HR. 2000b. Molecular chaperones: Containers and surfaces for folding, stabilising of unfolding proteins. Curr Opin Struct Biol 10: 251-258.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 251-258
    • Saibil, H.R.1
  • 108
    • 0032716118 scopus 로고    scopus 로고
    • Epidemiology of Chlamydia pneumoniae in atherosclerosis
    • Saikku P 1999. Epidemiology of Chlamydia pneumoniae in atherosclerosis. Am Heart J 138: S500-S503.
    • (1999) Am Heart J , vol.138
    • Saikku, P.1
  • 109
    • 0033561295 scopus 로고    scopus 로고
    • Presence of the pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in a mitochondrial fraction of Jurkat cells
    • Samali A, Cai J, Zhivotovsky B, Jone DP, Orrenius S. 1999. Presence of the pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in a mitochondrial fraction of Jurkat cells. EMBO J 18: 2024-2048.
    • (1999) EMBO J , vol.18 , pp. 2024-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jone, D.P.4    Orrenius, S.5
  • 110
    • 0033401220 scopus 로고    scopus 로고
    • Spontaneous apoptosis and expression of cell surface heatshock proteins in cultured EL-4 lymphoma cells
    • Sapozhnikov AM, Ponomarev ED, Tarasenko TN, Telford WG. 1999. Spontaneous apoptosis and expression of cell surface heatshock proteins in cultured EL-4 lymphoma cells. Cell Prolif 32: 363-378.
    • (1999) Cell Prolif , vol.32 , pp. 363-378
    • Sapozhnikov, A.M.1    Ponomarev, E.D.2    Tarasenko, T.N.3    Telford, W.G.4
  • 111
    • 0035800883 scopus 로고    scopus 로고
    • Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation
    • Sasu S, LaVerda D, Qureshi N, Golenbock DT, Beasley D. 2001. Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation. Circ Res 89: 244-250.
    • (2001) Circ Res , vol.89 , pp. 244-250
    • Sasu, S.1    LaVerda, D.2    Qureshi, N.3    Golenbock, D.T.4    Beasley, D.5
  • 113
    • 0028116493 scopus 로고
    • Subcellular localization of chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70
    • Scopio A, Johnson P, Laquerre A, Nelson DR. 1993. Subcellular localization of chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70. J Bacteriol 176: 6449-6456.
    • (1993) J Bacteriol , vol.176 , pp. 6449-6456
    • Scopio, A.1    Johnson, P.2    Laquerre, A.3    Nelson, D.R.4
  • 114
    • 0030816361 scopus 로고    scopus 로고
    • T-cell, antibody, and cytokine responses to homologs of the 60-kilodalton heat shock protein in Helicobacter pylori infection
    • Sharma SA, Miller GG, Peek RA, Perez-Perez G, Blaser MJ. 1997. T-cell, antibody, and cytokine responses to homologs of the 60-kilodalton heat shock protein in Helicobacter pylori infection. Clin Diagn Lab Immunol 4: 440-446.
    • (1997) Clin Diagn Lab Immunol , vol.4 , pp. 440-446
    • Sharma, S.A.1    Miller, G.G.2    Peek, R.A.3    Perez-Perez, G.4    Blaser, M.J.5
  • 115
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu R, Akashi S, Ogata H, Nagai Y, Fukudome K, Miyake K, Kimoto M. 1999. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 189: 1777-1782.
    • (1999) J Exp Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 116
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys BJ, Gupta RS. 1996. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp Cell Res 222: 16-27.
    • (1996) Exp Cell Res , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 117
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • Soltys BJ, Gupta RS. 1997. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol Int 21: 315-320.
    • (1997) Cell Biol Int , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 119
    • 7344240408 scopus 로고    scopus 로고
    • Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation
    • Tabona P, Reddi K, Khan S, et al. 1998. Homogeneous Escherichia coli chaperonin 60 induces IL-1 beta and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. J Immunol 161: 1414-1421.
    • (1998) J Immunol , vol.161 , pp. 1414-1421
    • Tabona, P.1    Reddi, K.2    Khan, S.3
  • 120
    • 0035070074 scopus 로고    scopus 로고
    • Identification of Tetrahymena hsp60 as a 14-nm filament protein/citrate synthase-binding protein and its possible involvement in the oral apparatus formation
    • Takeda T, Yoshihama I, Numata O. 2001. Identification of Tetrahymena hsp60 as a 14-nm filament protein/citrate synthase-binding protein and its possible involvement in the oral apparatus formation. Genes Cells 6: 139-149.
    • (2001) Genes Cells , vol.6 , pp. 139-149
    • Takeda, T.1    Yoshihama, I.2    Numata, O.3
  • 122
    • 0019760614 scopus 로고
    • Studies of Escherichia coli mutants which block bacteriophage morphogenesis
    • Tilly K, McKittrick N, Georgopoulos C, Murialdo H. 1981. Studies of Escherichia coli mutants which block bacteriophage morphogenesis. Prog Clin Biol Res 64: 35-45.
    • (1981) Prog Clin Biol Res , vol.64 , pp. 35-45
    • Tilly, K.1    McKittrick, N.2    Georgopoulos, C.3    Murialdo, H.4
  • 123
    • 0033006396 scopus 로고    scopus 로고
    • Moesin functions as a lipopolysaccharide receptor on human monocytes
    • Tohme ZN, Amar S, Van Dyke TE. 1999. Moesin functions as a lipopolysaccharide receptor on human monocytes. Infect Immun 67:3215-3220.
    • (1999) Infect Immun , vol.67 , pp. 3215-3220
    • Tohme, Z.N.1    Amar, S.2    Van Dyke, T.E.3
  • 124
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilise membranes under heat shock conditions
    • Torok Z, Horvath L, Goloubinoff P, Kovacs E, Glatz A, Balogh G, Vigh L. 1997. Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilise membranes under heat shock conditions. Proc Natl Acad Sci U S A 94:2192-2197.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2192-2197
    • Torok, Z.1    Horvath, L.2    Goloubinoff, P.3    Kovacs, E.4    Glatz, A.5    Balogh, G.6    Vigh, L.7
  • 126
    • 0034928401 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching reveals that LPS rapidly transfers from CD14 to hsp70 and hsp90 on the cell membrane
    • Triantafilou K, Triantafilou M, Ladha S, Mackie A, Fernandez N, Dedrick RL, Cherry R. 2001b. Fluorescence recovery after photobleaching reveals that LPS rapidly transfers from CD14 to hsp70 and hsp90 on the cell membrane. J Cell Sci 114: 2535-2545.
    • (2001) J Cell Sci , vol.114 , pp. 2535-2545
    • Triantafilou, K.1    Triantafilou, M.2    Ladha, S.3    Mackie, A.4    Fernandez, N.5    Dedrick, R.L.6    Cherry, R.7
  • 128
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas RM, Ahmad-Nejad P, da Costa C, Miethke T, Kirschning CJ, Hacker H, Wagner H. 2001. Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem 276:31332-31339.
    • (2001) J Biol Chem , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da Costa, C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 129
    • 0033765035 scopus 로고    scopus 로고
    • Induction and membrane expression of heat shock proteins in heat-treated HPC-4 cells is correlated with increased resistance to LAK-mediated lysis
    • Vendetti S, Cicconi R, Piselli P, Vismara D, Cassol M, Delpino A. 2000. Induction and membrane expression of heat shock proteins in heat-treated HPC-4 cells is correlated with increased resistance to LAK-mediated lysis. J Exp Clin Cancer Res 19: 329-334.
    • (2000) J Exp Clin Cancer Res , vol.19 , pp. 329-334
    • Vendetti, S.1    Cicconi, R.2    Piselli, P.3    Vismara, D.4    Cassol, M.5    Delpino, A.6
  • 130
    • 0029982220 scopus 로고    scopus 로고
    • Heat shock protein 65 induces CD62e, CD106, and CD54 on cultured human endothelial cells and increases their adhesiveness for monocytes and granulocytes
    • Verdegaal ME, Zegveld ST, van Furth R. 1996. Heat shock protein 65 induces CD62e, CD106, and CD54 on cultured human endothelial cells and increases their adhesiveness for monocytes and granulocytes. J Immunol 157: 369-376.
    • (1996) J Immunol , vol.157 , pp. 369-376
    • Verdegaal, M.E.1    Zegveld, S.T.2    Van Furth, R.3
  • 131
    • 0034163391 scopus 로고    scopus 로고
    • A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T-cells that cross react with the mammalian self-hsp70 homologue
    • Wendling U, Paul L, van der Zee R, Prakken B, Singh M, van Eden W. 2000. A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T-cells that cross react with the mammalian self-hsp70 homologue. J Immunol 164: 2711-2717.
    • (2000) J Immunol , vol.164 , pp. 2711-2717
    • Wendling, U.1    Paul, L.2    Van der Zee, R.3    Prakken, B.4    Singh, M.5    Van Eden, W.6
  • 132
    • 0034052160 scopus 로고    scopus 로고
    • Atherosclerosis - An autoimmune disease due to an immune reaction against heat-shock protein 60
    • Wick G. 2000. Atherosclerosis - An autoimmune disease due to an immune reaction against heat-shock protein 60. Herz 25: 87-90.
    • (2000) Herz , vol.25 , pp. 87-90
    • Wick, G.1
  • 135
    • 0033850839 scopus 로고    scopus 로고
    • Elevated levels of circulating heat shock protein 70 (Hsp70) in peripheral and renal vascular disease
    • Wright BH, Corton JM, El-Nahas AM, Wood RF, Pockley AG. 2000. Elevated levels of circulating heat shock protein 70 (Hsp70) in peripheral and renal vascular disease. Heart Vessels 15: 18-22.
    • (2000) Heart Vessels , vol.15 , pp. 18-22
    • Wright, B.H.1    Corton, J.M.2    El-Nahas, A.M.3    Wood, R.F.4    Pockley, A.G.5
  • 136
    • 0344959625 scopus 로고    scopus 로고
    • Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis
    • Xanthoudakis S, Roy S, Rasper D, et al. 1999. Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. EMBO J 18: 2049-2056.
    • (1999) EMBO J , vol.18 , pp. 2049-2056
    • Xanthoudakis, S.1    Roy, S.2    Rasper, D.3
  • 137
    • 0034604242 scopus 로고    scopus 로고
    • Serum soluble heat shock protein 60 is elevated in subjects with atherosclerosis in a general population
    • Xu Q, Schett G, Perschinka H, et al. 2000. Serum soluble heat shock protein 60 is elevated in subjects with atherosclerosis in a general population. Circulation 102: 14-20.
    • (2000) Circulation , vol.102 , pp. 14-20
    • Xu, Q.1    Schett, G.2    Perschinka, H.3
  • 138
    • 0033375716 scopus 로고    scopus 로고
    • Reactivity of monoclonal antibody to HSP60 homologue of Helicobacter pylori with human gastric epithelial cells and induction of IL-8 from these cells by purified H. pylori HSP60
    • Yamaguchi H, Osaki T, Kurihara N, Taguchi H, Kamiya S. 1999. Reactivity of monoclonal antibody to HSP60 homologue of Helicobacter pylori with human gastric epithelial cells and induction of IL-8 from these cells by purified H. pylori HSP60. J Gastroenterol 34(Suppl 11): 1-5.
    • (1999) J Gastroenterol , vol.34 , Issue.SUPPL. 11 , pp. 1-5
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Taguchi, H.4    Kamiya, S.5
  • 140
    • 0027176944 scopus 로고
    • Mechanisms of stimulation of interleukin-1 beta and tumor necrosis factor-alpha by Mycobacterium tuberculosis components
    • Zhang Y, Doerfler M, Lee TC, Guillemin B, Rom WN. 1993. Mechanisms of stimulation of interleukin-1 beta and tumor necrosis factor-alpha by Mycobacterium tuberculosis components. J Clin Invest 91: 2076-2083.
    • (1993) J Clin Invest , vol.91 , pp. 2076-2083
    • Zhang, Y.1    Doerfler, M.2    Lee, T.C.3    Guillemin, B.4    Rom, W.N.5
  • 141
    • 0035872251 scopus 로고    scopus 로고
    • Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinases
    • Zhang L, Pelech SL, Mayrand D, Grenier D, Heino J, Uitto VJ. 2001. Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinases. Exp Cell Res 266: 11-20.
    • (2001) Exp Cell Res , vol.266 , pp. 11-20
    • Zhang, L.1    Pelech, S.L.2    Mayrand, D.3    Grenier, D.4    Heino, J.5    Uitto, V.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.