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Volumn 72, Issue 1, 2004, Pages 38-45

Long-Term Effect of Heat Shock Protein 60 from Actinobacillus actinomycetemcomitans on Epithelial Cell Viability and Mitogen-Activated Protein Kinases

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 60; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHOPROTEIN PHOSPHATASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0347511932     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.72.1.38-45.2004     Document Type: Article
Times cited : (19)

References (48)
  • 1
    • 0035910411 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathways in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinase apoptosis
    • Avdi, N. J., J. A. Nick, B. B. Whitlock, M. A. Henson, G. L. Johnson, and G. S. Worthen. 2001. Tumor necrosis factor-alpha activation of the c-Jun N-terminal kinase pathways in human neutrophils. Integrin involvement in a pathway leading from cytoplasmic tyrosine kinase apoptosis. J. Biol. Chem. 276:2189-2199.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2189-2199
    • Avdi, N.J.1    Nick, J.A.2    Whitlock, B.B.3    Henson, M.A.4    Johnson, G.L.5    Worthen, G.S.6
  • 3
    • 0035023067 scopus 로고    scopus 로고
    • The role of protein kinase C isozymes in TNF-alpha-induced cytotoxicity to a rat intestinal epithelial cell line
    • Chang, Q., and B. L. Tepperman. 2001. The role of protein kinase C isozymes in TNF-alpha-induced cytotoxicity to a rat intestinal epithelial cell line. Am. J. Physiol. Gastrointest. Liver Physiol. 280:G572-G583.
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.280
    • Chang, Q.1    Tepperman, B.L.2
  • 4
    • 0035800855 scopus 로고    scopus 로고
    • Discordance between the binding affinity of mitogen-activated protein kinase subfamily members for MAP kinase phosphatase-2 and their ability to activate the phosphatase catalytically
    • Chen, P., D. Hutter, X. Yang, M. Gorospe, R. J. Davis, and Y. Liu. 2001. Discordance between the binding affinity of mitogen-activated protein kinase subfamily members for MAP kinase phosphatase-2 and their ability to activate the phosphatase catalytically. J. Biol. Chem. 276:29440-29449.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29440-29449
    • Chen, P.1    Hutter, D.2    Yang, X.3    Gorospe, M.4    Davis, R.J.5    Liu, Y.6
  • 5
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthesis kinase 3 represses transcriptional activation by heat shock factor-1
    • Chu, B., F. Soncin, B. D. Price, M. A. Stevenson, and S. K. Calderwood. 1996. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthesis kinase 3 represses transcriptional activation by heat shock factor-1. J. Biol. Chem. 271:30847-30857.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 6
    • 0034604623 scopus 로고    scopus 로고
    • p38 MAPK and NF-kappa B collaborate to induce interleukin-6 gene expression and release. Evidence for a cytoprotective autocrine signaling pathway in a cardiac myocyte model system
    • Craig, R., A. Larkin, A. M. Mingo, D. J. Thuerauf, C. Andrews, P. M. McDonough, and C. C. Glembotski. 2000. p38 MAPK and NF-kappa B collaborate to induce interleukin-6 gene expression and release. Evidence for a cytoprotective autocrine signaling pathway in a cardiac myocyte model system. J. Biol. Chem. 275:23814-23824.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23814-23824
    • Craig, R.1    Larkin, A.2    Mingo, A.M.3    Thuerauf, D.J.4    Andrews, C.5    McDonough, P.M.6    Glembotski, C.C.7
  • 7
    • 0034674061 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • Dai, R., W. Frejtag, B. He, Y. Zhang, and N. F. Mivechi. 2000. c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275:18210-18218.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18210-18218
    • Dai, R.1    Frejtag, W.2    He, B.3    Zhang, Y.4    Mivechi, N.F.5
  • 8
    • 0001215168 scopus 로고    scopus 로고
    • Virulence factors of the periodontopathogen Actinobacillus actinomycetemcomitans
    • Fives-Taylor, P., D. Meyer, and K. Mintz. 1996. Virulence factors of the periodontopathogen Actinobacillus actinomycetemcomitans. J. Periodontol. 67:291-297.
    • (1996) J. Periodontol. , vol.67 , pp. 291-297
    • Fives-Taylor, P.1    Meyer, D.2    Mintz, K.3
  • 9
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated Hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduño, R. A., E. Garduño, and P. S. Hoffman. 1998. 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
    • Garduño, R.A.1    Garduño, E.2    Hoffman, P.S.3
  • 10
    • 0032438164 scopus 로고    scopus 로고
    • Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans
    • Goulhen, F., A. Hafezi, V.-J. Uitto, D. Hinode, R. Nakamura, D. Grenier, and D. Mayrand. 1998. Subcellular localization 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
  • 11
    • 0032974306 scopus 로고    scopus 로고
    • The potential role of chemokines and inflammatory cytokine in periodontal disease progression
    • Graves, D. T. 1999. The potential role of chemokines and inflammatory cytokine in periodontal disease progression. Clin. Infect. Dis. 28:482-490.
    • (1999) Clin. Infect. Dis. , vol.28 , pp. 482-490
    • Graves, D.T.1
  • 12
    • 0032512847 scopus 로고    scopus 로고
    • Correlation between sustained c-Jun N-terminal protein kinase activation and apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells
    • Guo, Y. L., K. Baysal, B. Kang, L. J. Yang, and J. R. Williamson. 1998. Correlation between sustained c-Jun N-terminal protein kinase activation and apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells. J. Biol. Chem. 273:4027-4034.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4027-4034
    • Guo, Y.L.1    Baysal, K.2    Kang, B.3    Yang, L.J.4    Williamson, J.R.5
  • 13
    • 0032152824 scopus 로고    scopus 로고
    • A review of localized juvenile periodontitis (LJP): Part I. Clinical features, epidemiology, etiology, and pathogenesis
    • Gustke, C. J. 1998. A review of localized juvenile periodontitis (LJP): part I. Clinical features, epidemiology, etiology, and pathogenesis. Gen. Dent. 46:491-497.
    • (1998) Gen. Dent. , vol.46 , pp. 491-497
    • Gustke, C.J.1
  • 14
    • 0031742046 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock
    • He, B., Y. H. Meng, and N. F. Mivechi. 1998. Glycogen synthase kinase 3 beta and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock. Mol. Cell. Biol. 18:6624-6633.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6624-6633
    • He, B.1    Meng, Y.H.2    Mivechi, N.F.3
  • 15
    • 0032007821 scopus 로고    scopus 로고
    • Cross-reactivity of specific antibodies directed to heat shock protein from periodonto-pathogenic bacteria and of human origin
    • Hinode, D., R. Nakamura, D. Grenier, and D. Mayrand. 1998. Cross-reactivity of specific antibodies directed to heat shock protein from periodonto-pathogenic bacteria and of human origin. Oral Microbiol. Immunol. 13:55-58.
    • (1998) Oral Microbiol. Immunol. , vol.13 , pp. 55-58
    • Hinode, D.1    Nakamura, R.2    Grenier, D.3    Mayrand, D.4
  • 16
    • 0033103768 scopus 로고    scopus 로고
    • Nitric oxide stimulates the stress-activated protein kinase p38 in rat renal mesangial cells
    • Huwiler, A., and J. Pfeilschifter. 1999. Nitric oxide stimulates the stress-activated protein kinase p38 in rat renal mesangial cells. J. Exp. Biol. 202:655-660.
    • (1999) J. Exp. Biol. , vol.202 , pp. 655-660
    • Huwiler, A.1    Pfeilschifter, J.2
  • 17
    • 0036007905 scopus 로고    scopus 로고
    • Interaction between arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins
    • Kim, B. H., and F. Schoff. 2002. Interaction between arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins. J. Exp. Bot. 53:371-375.
    • (2002) J. Exp. Bot. , vol.53 , pp. 371-375
    • Kim, B.H.1    Schoff, F.2
  • 18
    • 0030882907 scopus 로고    scopus 로고
    • Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members
    • Kim, J., A. Nueda, Y. H. Meng, W. S. Dynan, and N. F. Mivechi. 1997. Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members. J. Cell. Biochem. 67:43-54.
    • (1997) J. Cell. Biochem. , vol.67 , pp. 43-54
    • Kim, J.1    Nueda, A.2    Meng, Y.H.3    Dynan, W.S.4    Mivechi, N.F.5
  • 19
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor1 activity at control temperature by phosphorylation
    • Knauf, U., E. M. Newton, J. Kyriakis, and R. E. Kingston. 1996. Repression of human heat shock factor1 activity at control temperature by phosphorylation. Genes Dev. 10:2782-2793.
    • (1996) Genes Dev. , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 20
    • 0027282725 scopus 로고
    • Tumor necrosis factor-α induces interleukin-α and interkeukin-1 receptor antagonist production by cultured human keratinocytes
    • Kutsch, C. L., D. A. Norris, and W. P. Arend. 1993. Tumor necrosis factor-α induces interleukin-α and interkeukin-1 receptor antagonist production by cultured human keratinocytes. J. Investig. Dermatol. 101:79-85.
    • (1993) J. Investig. Dermatol. , vol.101 , pp. 79-85
    • Kutsch, C.L.1    Norris, D.A.2    Arend, W.P.3
  • 21
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44 MAPK and negatively by the p38/HOG MAPK pathway
    • Lavoie, J. N., G. L'Allemain, A. Brunet, R. Muller, and J. Pouyssegur. 1996. Cyclin D1 expression is regulated positively by the p42/p44 MAPK and negatively by the p38/HOG MAPK pathway. J. Biol. Chem. 271:20608-20616.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3    Muller, R.4    Pouyssegur, J.5
  • 22
    • 0027485803 scopus 로고
    • Corticosteroids differentially regulate secretion of IL-6, IL-8, and G-CSF by a human bronchial epithelial cell line
    • Levine, S. J., P. Larivee, C. Logun, C. W. Angus., and J. H. Shelhamer. 1993. Corticosteroids differentially regulate secretion of IL-6, IL-8, and G-CSF by a human bronchial epithelial cell line. Am. J. Physiol. 265:L360≥L368.
    • (1993) Am. J. Physiol. , vol.265
    • Levine, S.J.1    Larivee, P.2    Logun, C.3    Angus, C.W.4    Shelhamer, J.H.5
  • 23
    • 0034647525 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase is required for tumor necrosis factor-alpha-supported proliferation of leukemia and lymphoma cell lines
    • Liu, R. Y., C. Fan, G. Liu, N. E. Olashaw, and K. S. Zucherman. 2000. Activation of p38 mitogen-activated protein kinase is required for tumor necrosis factor-alpha-supported proliferation of leukemia and lymphoma cell lines. J. Biol. Chem. 275:21086-21093.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21086-21093
    • Liu, R.Y.1    Fan, C.2    Liu, G.3    Olashaw, N.E.4    Zucherman, K.S.5
  • 24
    • 0030894605 scopus 로고    scopus 로고
    • Differences in responses of interleukin-1 and tumor necrosis factor alpha production and secretion to cyclosporin-A and ultraviolet B-irradiation by normal transformed keratinocyte cultures
    • Marionnet, A. V., Y. Chardonnet, J. Viac, and D. Schmitt. 1997. Differences in responses of interleukin-1 and tumor necrosis factor alpha production and secretion to cyclosporin-A and ultraviolet B-irradiation by normal transformed keratinocyte cultures. Exp. Dermatol. 6:22-28.
    • (1997) Exp. Dermatol. , vol.6 , pp. 22-28
    • Marionnet, A.V.1    Chardonnet, Y.2    Viac, J.3    Schmitt, D.4
  • 25
    • 0035503696 scopus 로고    scopus 로고
    • Negative feedback regulation of ASK1 by protein phosphatase 5(PP5) in response to oxidative stress
    • Morita, K., M. Saitoh, K. Tobiume, H. Matsuura, S. Enomoto, H. Nishitoh, and H. Ichijo. 2001. Negative feedback regulation of ASK1 by protein phosphatase 5(PP5) in response to oxidative stress. EMBO J. 20:6028-6036.
    • (2001) EMBO J. , vol.20 , pp. 6028-6036
    • Morita, K.1    Saitoh, M.2    Tobiume, K.3    Matsuura, H.4    Enomoto, S.5    Nishitoh, H.6    Ichijo, H.7
  • 27
    • 0035322687 scopus 로고    scopus 로고
    • Microbiological characteristics of subgingival microbiota in adult periodontitis, localized juvenile periodontitis and rapidly progressive periodontitis subjects
    • Nonnenmacher, C., R. Mutters, and L. F. de Jacoby. 2001. Microbiological characteristics of subgingival microbiota in adult periodontitis, localized juvenile periodontitis and rapidly progressive periodontitis subjects. Clin. Microbiol. Infect. 7:213-217.
    • (2001) Clin. Microbiol. Infect. , vol.7 , pp. 213-217
    • Nonnenmacher, C.1    Mutters, R.2    De Jacoby, L.F.3
  • 28
    • 0035026658 scopus 로고    scopus 로고
    • p38 MAP kinase negatively regulates cyclin D1 expression in airway smooth muscle cells
    • Page, K., J. Li, and M. B. Hershenson. 2001. p38 MAP kinase negatively regulates cyclin D1 expression in airway smooth muscle cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 280:L955-L964.
    • (2001) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.280
    • Page, K.1    Li, J.2    Hershenson, M.B.3
  • 29
    • 0033730196 scopus 로고    scopus 로고
    • Sequential activation of ERK and repression of JNK by scatter factor/hepatocyte growth factor in madin-darby canine kidney epithelial cells
    • Paumelle, R., D. Tulasne, C. Leroy, J. Coll, B. Vandenbunder, and V. Fafeur. 2000. Sequential activation of ERK and repression of JNK by scatter factor/ hepatocyte growth factor in madin-darby canine kidney epithelial cells. Mol. Biol. Cell 11:3751-3763.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3751-3763
    • Paumelle, R.1    Tulasne, D.2    Leroy, C.3    Coll, J.4    Vandenbunder, B.5    Fafeur, V.6
  • 30
    • 0037258952 scopus 로고    scopus 로고
    • Kinetworks protein kinase multiblot analysis
    • Pelech, S., C. Sutter, and H. Zhang. 2003. Kinetworks protein kinase multiblot analysis. Methods Mol. Biol. 218:99-111.
    • (2003) Methods Mol. Biol. , vol.218 , pp. 99-111
    • Pelech, S.1    Sutter, C.2    Zhang, H.3
  • 31
    • 0031953590 scopus 로고    scopus 로고
    • Protein phosphatase-1 and insulin action
    • Ragolia, L., and N. Begum. 1998. Protein phosphatase-1 and insulin action. Mol. Cell. Biochem. 182:49-58.
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 49-58
    • Ragolia, L.1    Begum, N.2
  • 32
    • 0030088134 scopus 로고    scopus 로고
    • Comparison of the pro-inflammatory cytokine-stimulating activity of the surface-associated proteins of periodontopathic bacteria
    • Reddi, K., M. Wilson, S. Nair, and B. Henderson. 1996. Comparison of the pro-inflammatory cytokine-stimulating activity of the surface-associated proteins of periodontopathic bacteria. J. Periodontal Res. 31:120-130.
    • (1996) J. Periodontal Res. , vol.31 , pp. 120-130
    • Reddi, K.1    Wilson, M.2    Nair, S.3    Henderson, B.4
  • 33
    • 0033113724 scopus 로고    scopus 로고
    • The pathogenesis of periodontal diseases
    • Research, Science, and Therapy Committee of the American Academy of Periodontology. 1999. The pathogenesis of periodontal diseases. J. Periodontol. 70:457-470.
    • (1999) J. Periodontol. , vol.70 , pp. 457-470
  • 34
    • 0033950358 scopus 로고    scopus 로고
    • The role of protein kinase B and mitogen-activated protein kinase in epithermal growth factor and tumor necrosis factor alpha-mediated rat hepatocyte survival and apoptosis
    • Roberts, R. A., N. H. James, and S. C. Cosulich. 2000. The role of protein kinase B and mitogen-activated protein kinase in epithermal growth factor and tumor necrosis factor alpha-mediated rat hepatocyte survival and apoptosis. Hepatology 31:420-427.
    • (2000) Hepatology , vol.31 , pp. 420-427
    • Roberts, R.A.1    James, N.H.2    Cosulich, S.C.3
  • 35
    • 0034882639 scopus 로고    scopus 로고
    • Ceramide regulates cellular homeostasis via diverse stress signaling pathways
    • Ruvolo, P. P. 2001. Ceramide regulates cellular homeostasis via diverse stress signaling pathways. Leukemia 15:1153-1160.
    • (2001) Leukemia , vol.15 , pp. 1153-1160
    • Ruvolo, P.P.1
  • 37
    • 0032618702 scopus 로고    scopus 로고
    • Lipopolysaccharide from Actinobacillus actinomycetemcomitans stimulates production of interleukin-1beta, tumor necrosis factor-alpha, interleukin-6 and interleukin-1 receptor antagonist in human whole blood
    • Schytte Blix, I. J., K. Helgeland, E. Hyattum, and T. Lyberg. 1999. Lipopolysaccharide from Actinobacillus actinomycetemcomitans stimulates production of interleukin-1beta, tumor necrosis factor-alpha, interleukin-6 and interleukin-1 receptor antagonist in human whole blood. J. Periodontal Res. 34:34-40.
    • (1999) J. Periodontal Res. , vol.34 , pp. 34-40
    • Schytte Blix, I.J.1    Helgeland, K.2    Hyattum, E.3    Lyberg, T.4
  • 39
    • 0032884734 scopus 로고    scopus 로고
    • Tumor necrosis factor-α mediates antiapoptotic signals partially via p39 MAP kinase activation in human eosinophils
    • Tsukahara, K., A. Nakao, M. Hiraguri, S. Miike, M. Mamura, Y. Saito, and I. Iwamoto. 1999. Tumor necrosis factor-α mediates antiapoptotic signals partially via p39 MAP kinase activation in human eosinophils. Int. Arch. Allergy Immunol. 120:54-59.
    • (1999) Int. Arch. Allergy Immunol. , vol.120 , pp. 54-59
    • Tsukahara, K.1    Nakao, A.2    Hiraguri, M.3    Miike, S.4    Mamura, M.5    Saito, Y.6    Iwamoto, I.7
  • 40
    • 0036122481 scopus 로고    scopus 로고
    • Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling
    • Ugi, S., T. Imamura, W. Ricketts, and J. M. Olefsky. 2002. Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling. Mol. Cell. Biol. 22:2375-2387.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2375-2387
    • Ugi, S.1    Imamura, T.2    Ricketts, W.3    Olefsky, J.M.4
  • 41
    • 0034525293 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase mediates tumor necrosis factor-alpha-induced apoptosis in rat fetal brown adipocytes
    • Valladares, A., A. M. Alvarez, J. J. Ventura, C. Roncero, M. Benito, and A. Porras. 2000. p38 mitogen-activated protein kinase mediates tumor necrosis factor-alpha-induced apoptosis in rat fetal brown adipocytes. Endocrinology 141:4383-4395.
    • (2000) Endocrinology , vol.141 , pp. 4383-4395
    • Valladares, A.1    Alvarez, A.M.2    Ventura, J.J.3    Roncero, C.4    Benito, M.5    Porras, A.6
  • 42
    • 0030926673 scopus 로고    scopus 로고
    • Keratinocyte proinflammatory responses to adherent and nonadherent group A streptococci
    • Wang, B., N. Ruiz, A. Pentland, and M. Caparon. 1997. Keratinocyte proinflammatory responses to adherent and nonadherent group A streptococci. Infect. Immun. 65:2119-2126.
    • (1997) Infect. Immun. , vol.65 , pp. 2119-2126
    • Wang, B.1    Ruiz, N.2    Pentland, A.3    Caparon, M.4
  • 43
    • 0032724070 scopus 로고    scopus 로고
    • Induction of secretion of interlerkin-8 from human gastric epithelial cells by heat-shock protein 60 homologue of Helicobacter pylori
    • Yamaguchi, H., T. Osaki, N. Kurihara, M. Kitajima, M. Kai, M. Takahashi, and H. Taguchi. 1999. Induction of secretion of interlerkin-8 from human gastric epithelial cells by heat-shock protein 60 homologue of Helicobacter pylori. J. Med. Microbiol. 48:927-933.
    • (1999) J. Med. Microbiol. , vol.48 , pp. 927-933
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Kitajima, M.4    Kai, M.5    Takahashi, M.6    Taguchi, H.7
  • 44
    • 0033143121 scopus 로고    scopus 로고
    • The role of the cell-mediated immune response to Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in periodontitis
    • Zadeh, H. H., F. C. Nichols, and K. T. Miyasaki. 1999. The role of the cell-mediated immune response to Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in periodontitis. Periodontol. 2000 20:239-288.
    • (1999) Periodontol. 2000 , vol.20 , pp. 239-288
    • Zadeh, H.H.1    Nichols, F.C.2    Miyasaki, K.T.3
  • 45
    • 0035872251 scopus 로고    scopus 로고
    • Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinases
    • Zhang, L., S. L. Pelech, D. Mayrand, D. Grenier, J. Heino, and V. J. Uitto. 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
  • 46
    • 0035824547 scopus 로고    scopus 로고
    • An early growth response protein (Egr)1 cis element is required for gonadotropin-releasing hormone-induced mitogen-activated protein kinase phosphatase 2 gene expression
    • Zhang, T., M. W. Wolfe, and M. S. Roberson. 2001. An early growth response protein (Egr)1 cis element is required for gonadotropin-releasing hormone-induced mitogen-activated protein kinase phosphatase 2 gene expression. J. Biol. Chem. 276:45604-45613.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45604-45613
    • Zhang, T.1    Wolfe, M.W.2    Roberson, M.S.3
  • 47
    • 0037200054 scopus 로고    scopus 로고
    • The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases
    • Zhou, B., Z. X. Wang, Y. Zhao, D. L. Brautigan, and Z. Y. Zhang. 2002. The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases. J. Biol. Chem. 277:31818-31825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31818-31825
    • Zhou, B.1    Wang, Z.X.2    Zhao, Y.3    Brautigan, D.L.4    Zhang, Z.Y.5
  • 48
    • 0038737428 scopus 로고    scopus 로고
    • Role of heat shock proteins in protection from and pathogenesis of infectious diseases
    • Zügel, U., and S. H. Kaufmann. 1999. Role of heat shock proteins in protection from and pathogenesis of infectious diseases. Clin. Microbiol. Rev. 12:19-39.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 19-39
    • Zügel, U.1    Kaufmann, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.