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Volumn 292, Issue 1, 2004, Pages 231-240

Bacterial GroEL-like heat shock protein 60 protects epithelial cells from stress-induced death through activation of ERK and inhibition of caspase 3

Author keywords

Apoptosis; Bacterial heat shock protein; Caspase 3; Epithelial cells; Mitogen activated protein kinase; UV radiation

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; BACTERIAL PROTEIN; CASPASE 3; HEAT SHOCK PROTEIN 60; MITOGEN ACTIVATED PROTEIN KINASE 1; SYNAPTOPHYSIN;

EID: 0347356267     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2003.08.012     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0028827581 scopus 로고
    • Thermostability of lactate dehydrogenase LDH-A-4 isoenzyme: Effect of heat shock protein Dnak on the enzyme activity
    • Zietara M.S., Skorkowski E.F. Thermostability of lactate dehydrogenase LDH-A-4 isoenzyme: effect of heat shock protein Dnak on the enzyme activity. Int. J. Biochem. Cell Biol. 27:1995;1169-1174.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 1169-1174
    • Zietara, M.S.1    Skorkowski, E.F.2
  • 2
    • 0032438164 scopus 로고    scopus 로고
    • Subcellular localization 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. Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans. Infect. Immun. 66:1998;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
  • 3
    • 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. The GroEL-like protein from Campylobacter rectus: immunological characterization and interleukin-6 and -8 induction in human gingival fibroblast. FEMS Microbiol. Lett. 167:1998;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
  • 4
    • 0037435923 scopus 로고    scopus 로고
    • Immunopotentiating heat shock proteins: Negotiators between innate danger and control of autoimmunity
    • van Eden W., Koets A., van Kooten P., Prakken B., van der Zee R. Immunopotentiating heat shock proteins: negotiators between innate danger and control of autoimmunity. Vaccine. 21:2003;897-901.
    • (2003) Vaccine , vol.21 , pp. 897-901
    • Van Eden, W.1    Koets, A.2    Van Kooten, P.3    Prakken, B.4    Van Der Zee, R.5
  • 5
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduno R.A., Hoffman P.S., Garduno E. Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect. Immun. 66:1998;4602-4610.
    • (1998) Infect. Immun. , vol.66 , pp. 4602-4610
    • Garduno, R.A.1    Hoffman, P.S.2    Garduno, E.3
  • 7
    • 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 A.H., Finberg R.W., Libby P., Kurt-Jones E.A. 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. 164:2000;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
  • 8
    • 0037413845 scopus 로고    scopus 로고
    • Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages
    • Habich C., Kempe K., van der Zee R., Burkart V., Kolb H. Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages. FEBS Lett. 533:2003;105-109.
    • (2003) FEBS Lett. , vol.533 , pp. 105-109
    • Habich, C.1    Kempe, K.2    Van Der Zee, R.3    Burkart, V.4    Kolb, H.5
  • 9
    • 0037459033 scopus 로고    scopus 로고
    • Interleukin 15 induces the signals of epidermal proliferation through ERK and PI 3-kinase in a human epidermal keratinocyte cell line HaCaT
    • Yano S., Komine M., Fujimoto M., Okochi H., Tamaki K. Interleukin 15 induces the signals of epidermal proliferation through ERK and PI 3-kinase in a human epidermal keratinocyte cell line HaCaT. Biochem. Biophys. Res. Commun. 301:2003;841-847.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 841-847
    • Yano, S.1    Komine, M.2    Fujimoto, M.3    Okochi, H.4    Tamaki, K.5
  • 10
    • 0038660608 scopus 로고    scopus 로고
    • Calcium induces cell survival and proliferation through the activation of MAPK pathway in a human hormone-dependent leukaemia cell line (TF-1)
    • Apati A., Janossy J., Brozik A., Bauer P., Magocsi M. Calcium induces cell survival and proliferation through the activation of MAPK pathway in a human hormone-dependent leukaemia cell line (TF-1). J. Biol. Chem. 278:2003;9235-9243.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9235-9243
    • Apati, A.1    Janossy, J.2    Brozik, A.3    Bauer, P.4    Magocsi, M.5
  • 12
    • 0034097798 scopus 로고    scopus 로고
    • MAP kinase pathways activated by stress: The p38 MAPK pathway
    • Obata T., Brown G.E., Yaffe M.B. MAP kinase pathways activated by stress: the p38 MAPK pathway. Crit. Care Med. 28:2001;N67-N77.
    • (2001) Crit. Care Med. , vol.28
    • Obata, T.1    Brown, G.E.2    Yaffe, M.B.3
  • 13
    • 0033559508 scopus 로고    scopus 로고
    • 38 pathway during FTY720-induced apoptosis of T lymphocytes that is suppressed by the extracellular signal-regulated kinase pathway
    • 38 pathway during FTY720-induced apoptosis of T lymphocytes that is suppressed by the extracellular signal-regulated kinase pathway. J. Immunol. 162:1999;3321-3326.
    • (1999) J. Immunol. , vol.162 , pp. 3321-3326
    • Matsuda, S.1    Minowa, A.2    Suzuki, S.3    Koyasu, S.4
  • 14
    • 0032562682 scopus 로고    scopus 로고
    • The activation of p38 and apoptosis by the inhibition of ERK is antagonized by the phosphoinositide 3-kinase/Akt pathway
    • Berra E., Diaz-Meco M.T., Moscat J. The activation of p38 and apoptosis by the inhibition of ERK is antagonized by the phosphoinositide 3-kinase/Akt pathway. J. Biol. Chem. 273:1998;10792-10797.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10792-10797
    • Berra, E.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 15
    • 0037105386 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase/extracellular signal-regulated kinase signaling in activated T cells abrogates TRAIL-induced apoptosis upstream of the mitochondrial amplification loop and caspase-8
    • Soderstrom T.S., Poukkula M., Holmstrom T.H., Heiskanen K.M., Eriksson J.E. Mitogen-activated protein kinase/extracellular signal-regulated kinase signaling in activated T cells abrogates TRAIL-induced apoptosis upstream of the mitochondrial amplification loop and caspase-8. J. Immunol. 169:2002;2851-2860.
    • (2002) J. Immunol. , vol.169 , pp. 2851-2860
    • Soderstrom, T.S.1    Poukkula, M.2    Holmstrom, T.H.3    Heiskanen, K.M.4    Eriksson, J.E.5
  • 17
    • 0033724701 scopus 로고    scopus 로고
    • Chaperones in cell cycle regulation and mitogenic signal transduction: A review
    • Helmbrecht K., Zeise E., Rensing L. Chaperones in cell cycle regulation and mitogenic signal transduction: a review. Cell Prolif. 33:2000;341-365.
    • (2000) Cell Prolif. , vol.33 , pp. 341-365
    • Helmbrecht, K.1    Zeise, E.2    Rensing, L.3
  • 18
    • 0033610798 scopus 로고    scopus 로고
    • Differential activation of p38 mitogen-activated protein kinase and extracellular signal-regulated protein kinase confers cadmium-induced HSP70 expression in 9L rat brain tumor cells
    • Hung J.J., Cheng T.J., Lai Y.K., Chang M.D. Differential activation of p38 mitogen-activated protein kinase and extracellular signal-regulated protein kinase confers cadmium-induced HSP70 expression in 9L rat brain tumor cells. J. Biol. Chem. 273:1998;31924-31931.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31924-31931
    • Hung, J.J.1    Cheng, T.J.2    Lai, Y.K.3    Chang, M.D.4
  • 19
    • 0033635080 scopus 로고    scopus 로고
    • HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK
    • Volloch V., Gabai V.L., Rits S., Force T., Sherman M.Y. HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK. Cell Stress Chaperones. 5:2000;139-147.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 139-147
    • Volloch, V.1    Gabai, V.L.2    Rits, S.3    Force, T.4    Sherman, M.Y.5
  • 20
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • Park H.S., Lee J.S., Huh S.H., Seo J.S., Choi E.J. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J. 2001;446-456.
    • (2001) EMBO J. , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 21
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • Meriin A.B., Yaglom J.A., Gabai V.L., Zon L., Ganiatsas S., Mosser D.D., Zon L., Sherman M.Y. Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol. Cell. Biol. 19:1999;2547-2555.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.A.2    Gabai, V.L.3    Zon, L.4    Ganiatsas, S.5    Mosser, D.D.6    Zon, L.7    Sherman, M.Y.8
  • 22
    • 0034674061 scopus 로고    scopus 로고
    • 2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • 2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275:2000;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
  • 24
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase 3 Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells
    • Samali A., Cai J., Zhivotovsky B., Jones D.P., Orrenius S. Presence of a pre-apoptotic complex of pro-caspase 3 Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J. 18:1999;2040-2048.
    • (1999) EMBO J. , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 25
    • 0032007821 scopus 로고    scopus 로고
    • Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria of human origin
    • Hinode D., Nakamura R., Grenier D., Mayrand D. Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria of human origin. Oral Microbiol. Immunol. 13:1998;55-58.
    • (1998) Oral Microbiol. Immunol. , vol.13 , pp. 55-58
    • Hinode, D.1    Nakamura, R.2    Grenier, D.3    Mayrand, D.4
  • 26
    • 0032213048 scopus 로고    scopus 로고
    • Purified, characterization and immunochemical properties of novel 60-kDa of Vibrio anguillarum strains
    • Mutharia L.M., Klinck J., Yamaguchi H., Davey M. Purified, characterization and immunochemical properties of novel 60-kDa of Vibrio anguillarum strains. FEMS Microbiol. Lett. 168:1998;111-117.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 111-117
    • Mutharia, L.M.1    Klinck, J.2    Yamaguchi, H.3    Davey, M.4
  • 28
    • 0031053387 scopus 로고    scopus 로고
    • Ultraviolet B-radiation dose influences the induction of apoptosis and p53 in human keratinocytes
    • Cotton J., Spandau D.F. Ultraviolet B-radiation dose influences the induction of apoptosis and p53 in human keratinocytes. Radiat. Res. 147:1997;148-155.
    • (1997) Radiat. Res. , vol.147 , pp. 148-155
    • Cotton, J.1    Spandau, D.F.2
  • 29
    • 0344654820 scopus 로고    scopus 로고
    • Expression of the 72-kD heat shock protein is induced by ultraviolet a radiation in a human fibrosarcoma cell line
    • Trautinger F., Kokesch C., Klosner G., Knobler R.M., Kindas-Mugg I. Expression of the 72-kD heat shock protein is induced by ultraviolet A radiation in a human fibrosarcoma cell line. Exp. Dermatol. 8:1999;187-192.
    • (1999) Exp. Dermatol. , vol.8 , pp. 187-192
    • Trautinger, F.1    Kokesch, C.2    Klosner, G.3    Knobler, R.M.4    Kindas-Mugg, I.5
  • 30
    • 0032901153 scopus 로고    scopus 로고
    • UV-A-induced expression of GroEL in the UV-A-resistant marine cyanobacterium Oscillatoria sp. NKBG 091600
    • Yamazawa A., Takeyama H., Takeda D., Matsunaga T. UV-A-induced expression of GroEL in the UV-A-resistant marine cyanobacterium Oscillatoria sp. NKBG 091600. Microbiology. 145:1999;949-954.
    • (1999) Microbiology , vol.145 , pp. 949-954
    • Yamazawa, A.1    Takeyama, H.2    Takeda, D.3    Matsunaga, T.4
  • 31
    • 0035872251 scopus 로고    scopus 로고
    • Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinase
    • Zhang L., Pelech S.L., Mayrand D., Grenier D., Heino J., Uitto V.J. Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinase. Exp. Cell Res. 266:2001;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
  • 32
    • 0034736067 scopus 로고    scopus 로고
    • Cisplatin and UV radiation induce activation of the stress-activated protein kinase p38 gamma in human melanoma cells
    • Pillaire M.J., Nebreda A.R., Darbon J.M. Cisplatin and UV radiation induce activation of the stress-activated protein kinase p38 gamma in human melanoma cells. Biochem. Biophys. Res. Commun. 278:2000;724-728.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 724-728
    • Pillaire, M.J.1    Nebreda, A.R.2    Darbon, J.M.3
  • 33
    • 0035511842 scopus 로고    scopus 로고
    • Ultraviolet B irradiation induces apoptosis of keratinocytes by direct activation of Fas antigen
    • Takahashi H., Ishida-Yamamoto A., Iizuka H. Ultraviolet B irradiation induces apoptosis of keratinocytes by direct activation of Fas antigen. J. Investig. Dermatol. Symp. Proc. 6:2001;64-68.
    • (2001) J. Investig. Dermatol. Symp. Proc. , vol.6 , pp. 64-68
    • Takahashi, H.1    Ishida-Yamamoto, A.2    Iizuka, H.3
  • 34
    • 18344401788 scopus 로고    scopus 로고
    • Protein kinase C (PKC) inhibits fas receptor-induced apoptosis through modulation of the loss K+ and cell shrinkage. a role for PKC upstream of caspases
    • Gomez-Angelats M., Bortner C.D., Cidlowski J.A. Protein kinase C (PKC) inhibits fas receptor-induced apoptosis through modulation of the loss K+ and cell shrinkage. A role for PKC upstream of caspases. J. Biol. Chem. 275:2000;19609-19619.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19609-19619
    • Gomez-Angelats, M.1    Bortner, C.D.2    Cidlowski, J.A.3
  • 35
    • 0033603018 scopus 로고    scopus 로고
    • MEK1 activation rescues Jurkat T cells from Fas-induced apoptosis
    • Wilson D.J., Alessandrine A., Budd R.C. MEK1 activation rescues Jurkat T cells from Fas-induced apoptosis. Cell. Immunol. 194:1999;67-77.
    • (1999) Cell. Immunol. , vol.194 , pp. 67-77
    • Wilson, D.J.1    Alessandrine, A.2    Budd, R.C.3
  • 36
    • 0033933819 scopus 로고    scopus 로고
    • Phosphorylation-based signaling in Fas receptor-mediated apoptosis
    • Holmstrom T.H., Eriksson J.E. Phosphorylation-based signaling in Fas receptor-mediated apoptosis. Crit. Rev. Immunol. 20:2000;121-152.
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 121-152
    • Holmstrom, T.H.1    Eriksson, J.E.2
  • 37
    • 0033771527 scopus 로고    scopus 로고
    • 2-terminal kinase and p38 mitogen-activated protein kinase in human eosinophils
    • 2-terminal kinase and p38 mitogen-activated protein kinase in human eosinophils. Clin. Exp. Immunol. 122:2000;20-27.
    • (2000) Clin. Exp. Immunol. , vol.122 , pp. 20-27
    • Zhang, J.P.1    Wong, C.K.2    Lam, C.W.3
  • 38
    • 0033605366 scopus 로고    scopus 로고
    • 2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase 3-like proteases but is dispensable for cell death
    • 2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase 3-like proteases but is dispensable for cell death. J. Biol. Chem. 274:1999;5310-5317.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5310-5317
    • Ozaki, I.1    Tani, E.2    Ikemoto, H.3    Kitagawa, H.4    Fujikawa, H.5
  • 39
    • 18344399012 scopus 로고    scopus 로고
    • Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells
    • Galan A., Garcia-Bermejo M.L., Troyano A., Vilaboa N.E., de Blas E., Kazanietz M.G., Aller P. Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells. J. Biol. Chem. 275:2000;11418-11424.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11418-11424
    • Galan, A.1    Garcia-Bermejo, M.L.2    Troyano, A.3    Vilaboa, N.E.4    De Blas, E.5    Kazanietz, M.G.6    Aller, P.7
  • 40
    • 0032919249 scopus 로고    scopus 로고
    • An inhibitor of p38 and JNK MAP kinases prevents activation of caspase and apoptosis of cultured cerebellar granule neurons
    • Harada J., Sugimogo M. An inhibitor of p38 and JNK MAP kinases prevents activation of caspase and apoptosis of cultured cerebellar granule neurons. Jpn. J. Pharmacol. 79:1999;369-378.
    • (1999) Jpn. J. Pharmacol. , vol.79 , pp. 369-378
    • Harada, J.1    Sugimogo, M.2
  • 41
    • 0034647694 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase regulates a novel, caspase-independent pathway for the mitochondrial cytochrome c release in ultraviolet B radiation-induced apoptosis
    • Assefa Z., Vantieghem A., Garmyn M., Declereq W., Vandenabeele P., Vandenheede J.R., Bouillon R., Merlevede W., Agostinis P. p38 mitogen-activated protein kinase regulates a novel, caspase-independent pathway for the mitochondrial cytochrome c release in ultraviolet B radiation-induced apoptosis. J. Biol. Chem. 275:2000;21416-21421.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21416-21421
    • Assefa, Z.1    Vantieghem, A.2    Garmyn, M.3    Declereq, W.4    Vandenabeele, P.5    Vandenheede, J.R.6    Bouillon, R.7    Merlevede, W.8    Agostinis, P.9
  • 42
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin S.A., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta. 1366:1998;151-165.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 43
    • 0032897552 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase in UVB-induced apoptosis of human keratinocyte HaCaT cells
    • Shimizu H., Banno Y., Sumi N., Naganawa T., Kitajima Y., Nozawa Y. Activation of p38 mitogen-activated protein kinase in UVB-induced apoptosis of human keratinocyte HaCaT cells. J. Invest. Dermatol. 112:1999;769-774.
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 769-774
    • Shimizu, H.1    Banno, Y.2    Sumi, N.3    Naganawa, T.4    Kitajima, Y.5    Nozawa, Y.6
  • 44
    • 0033923816 scopus 로고    scopus 로고
    • Roles of JNK, p38 and ERK mitogen-activated protein kinase in the growth inhibition and apoptosis induced by cadmium
    • Chuang S.M., Wang I.C., Yang J.L. Roles of JNK, p38 and ERK mitogen-activated protein kinase in the growth inhibition and apoptosis induced by cadmium. Carcinogenesis. 21:2000;1423-1432.
    • (2000) Carcinogenesis , vol.21 , pp. 1423-1432
    • Chuang, S.M.1    Wang, I.C.2    Yang, J.L.3
  • 45
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase 3 activation
    • Li C.Y., Lee J.S., Ko Y.G., Kim J.I., Seo J.S. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase 3 activation. J. Biol. Chem. 275:2000;25665-25671.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3    Kim, J.I.4    Seo, J.S.5
  • 48
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins - Modulators of apoptosis in tumour cells
    • Creagh E.M., Sheehan D., Cotter T.G. Heat shock proteins - Modulators of apoptosis in tumour cells. Leukemia. 14:2000;1161-1173.
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3


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