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Volumn 6, Issue 10, 1999, Pages 689-698

The secondary fungal metabolite gliotoxin targets proteolytic activities of the proteasome

Author keywords

Gliotoxin; Inhibition; I B ; NF B; Proteasome

Indexed keywords


EID: 0033214494     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)80016-2     Document Type: Article
Times cited : (132)

References (65)
  • 1
    • 0023475466 scopus 로고
    • Favorable outcome of invasive aspergillosis in patients with acute leukemia
    • 1. Burch, P.A., Karp, J.E., Merz, W.G., Kuhlman, J.E. & Fishman, E.K. (1987). Favorable outcome of invasive aspergillosis in patients with acute leukemia. J. Clin. Oncol. 5, 1985-1993.
    • (1987) J. Clin. Oncol. , vol.5 , pp. 1985-1993
    • Burch, P.A.1    Karp, J.E.2    Merz, W.G.3    Kuhlman, J.E.4    Fishman, E.K.5
  • 2
    • 0028264950 scopus 로고
    • Investigation of the potential use of immunosuppressive agent gliotoxin in organ transplantation
    • 2. Sutton, P., Newcombe, W.R., Waring, P. & Müllbacher, A. (1994). Investigation of the potential use of immunosuppressive agent gliotoxin in organ transplantation. Infect. Immunol. 62, 1192-1198.
    • (1994) Infect. Immunol. , vol.62 , pp. 1192-1198
    • Sutton, P.1    Newcombe, W.R.2    Waring, P.3    Müllbacher, A.4
  • 3
    • 0023705905 scopus 로고
    • The chemistry and biology of the immunomodulating agent gliotoxin and related epipolythiodioxopiperazines
    • 3. Waring, P., Eichner, R.D. & Müllbacher, A. (1988).). The chemistry and biology of the immunomodulating agent gliotoxin and related epipolythiodioxopiperazines. Med. Res. Rev. 8, 499-524.
    • (1988) Med. Res. Rev. , vol.8 , pp. 499-524
    • Waring, P.1    Eichner, R.D.2    Müllbacher, A.3
  • 4
    • 0011925448 scopus 로고
    • Immunosuppression in vitro by a metabolite of a human pathogenic fungus
    • 4. Müllbacher, A. & Eichner, R.D. (1984). Immunosuppression in vitro by a metabolite of a human pathogenic fungus. Proc. Natl Acad. Sci. USA 81, 3835-3837.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3835-3837
    • Müllbacher, A.1    Eichner, R.D.2
  • 5
    • 0022658585 scopus 로고
    • Structural relationship of epipolythiodioxopiperazines and their immunomodulating activity
    • 5. Müllbacher, A., Waring, P., Palni, T. & Eichner, R.D. (1986). Structural relationship of epipolythiodioxopiperazines and their immunomodulating activity. Mol. Immunol. 23, 231-235.
    • (1986) Mol. Immunol. , vol.23 , pp. 231-235
    • Müllbacher, A.1    Waring, P.2    Palni, T.3    Eichner, R.D.4
  • 6
    • 0024259735 scopus 로고
    • Gliotoxin induces apoptosis in macrophages unrelated to its antiphagocytic properties
    • 6. Waring, P., Eichner, R.D., Müllbacher, A. & Sjaarda, A. (1988). Gliotoxin induces apoptosis in macrophages unrelated to its antiphagocytic properties. J. Biol. Chem. 263, 18493-18499.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18493-18499
    • Waring, P.1    Eichner, R.D.2    Müllbacher, A.3    Sjaarda, A.4
  • 7
    • 0000481359 scopus 로고
    • Fungal epipolythiodioxopiperazine toxins have therapeutic potential and roles in disease
    • 7. Jordan, T.W. & Cordiner, S.T. (1987). Fungal epipolythiodioxopiperazine toxins have therapeutic potential and roles in disease. Trends Plant Sci. 8, 144-149.
    • (1987) Trends Plant Sci. , vol.8 , pp. 144-149
    • Jordan, T.W.1    Cordiner, S.T.2
  • 8
    • 0022632638 scopus 로고
    • Studies of platelet activating factor (PAF) antagonists from microbial products. I. Bisdethiobis(methylthio)gliotoxin and its derivatives
    • 8. Okamoto, M., Yoshuda, K., Uchida, I., Nishikawa, M., Kohsaka, M. & Aoki, H. (1986). Studies of platelet activating factor (PAF) antagonists from microbial products. I. Bisdethiobis(methylthio)gliotoxin and its derivatives. Chem. Pharm. Bull. 34, 340-344.
    • (1986) Chem. Pharm. Bull. , vol.34 , pp. 340-344
    • Okamoto, M.1    Yoshuda, K.2    Uchida, I.3    Nishikawa, M.4    Kohsaka, M.5    Aoki, H.6
  • 9
    • 0020586709 scopus 로고
    • Fungal epipolythiodioxopiperazine toxins have therapeutic potential and roles in disease
    • 9. Cordiner, S.J. & Jordan, T.W. (1983). Fungal epipolythiodioxopiperazine toxins have therapeutic potential and roles in disease. Biochem. J. 212, 197-204.
    • (1983) Biochem. J. , vol.212 , pp. 197-204
    • Cordiner, S.J.1    Jordan, T.W.2
  • 10
    • 0022782512 scopus 로고
    • Sporidesmin and gliotoxin induce cell detachment and perturb microfilament structure in cultured liver cells
    • 10. Jordan, T.W. & Pedersen, J.S. (1986). Sporidesmin and gliotoxin induce cell detachment and perturb microfilament structure in cultured liver cells. J. Cell. Sci. 85, 33-46.
    • (1986) J. Cell. Sci. , vol.85 , pp. 33-46
    • Jordan, T.W.1    Pedersen, J.S.2
  • 11
    • 15844381960 scopus 로고    scopus 로고
    • The immunosuppressive fungal metabolite gliotoxin specifically inhibits transcription factor NF-kappaB
    • 11. Pahl, H.L., et al., & Baeuerle, P.A. (1996). The immunosuppressive fungal metabolite gliotoxin specifically inhibits transcription factor NF-kappaB. J. Exp. Med. 183, 1829-1840.
    • (1996) J. Exp. Med. , vol.183 , pp. 1829-1840
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 12
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • 12. Palombella, V., Rando, O., Goldberg, A. & Maniatis, T. (1994). The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.1    Rando, O.2    Goldberg, A.3    Maniatis, T.4
  • 13
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B
    • 13. Traenckner, E.B.M., Wilk, S. & Baeuerle, P.A. (1994). A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B. EMBO J. 13, 5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.M.1    Wilk, S.2    Baeuerle, P.A.3
  • 14
    • 0027520473 scopus 로고
    • Proteolytic degradation of MAD3 (I kappa B alpha) and enhanced processing of the NF-kappa B precursor p105 are obligatory steps in the activation of NF-kappa B
    • 14. Mellits, K., Hay, R. & Goodbourn, S. (1993). Proteolytic degradation of MAD3 (I kappa B alpha) and enhanced processing of the NF-kappa B precursor p105 are obligatory steps in the activation of NF-kappa B. Nucleic Acids Res. 21, 5059-5066.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5059-5066
    • Mellits, K.1    Hay, R.2    Goodbourn, S.3
  • 15
    • 0028978032 scopus 로고
    • Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli
    • 15. Traenckner, E.B.M., Pahl, H.L., Henkel, T., Schmidt, K.N., Wilk, S. & Baeuerle, P.A. (1995). Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J. 14, 2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.M.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 16
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • 16. Brown, K., Gerstberger, S., Carlson, L., Franzoso, G. & Siebenlist, U. (1995). Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 267, 1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 17
    • 0028929371 scopus 로고
    • Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation
    • 17. Brockman, J.A., et al., & Ballard, D.W. (1995). Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation. Mol. Cell. Biol. 15, 2809-2818.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2809-2818
    • Brockman, J.A.1    Ballard, D.W.2
  • 18
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation
    • 18. DiDonato, J.A., et al., & Karin, M. (1996).). Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16, 1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.A.1    Karin, M.2
  • 19
    • 0028972488 scopus 로고
    • Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination
    • 19. Scherer, D., Brockman, J., Chen, Z., Maniatis, T. & Ballard, D. (1995). Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination. Proc. Natl Acad. Sci. USA 92, 11259-11263.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11259-11263
    • Scherer, D.1    Brockman, J.2    Chen, Z.3    Maniatis, T.4    Ballard, D.5
  • 20
    • 0029896674 scopus 로고    scopus 로고
    • Identification of lysine residues required for signal-induced ubiquitination and degradation of I kappa B-alpha in vivo
    • 20. Rodriguez, M.S., et al., & Arenzana-Seisdedos, F. (1996). Identification of lysine residues required for signal-induced ubiquitination and degradation of I kappa B-alpha in vivo. Oncogens 12, 2425-2435.
    • (1996) Oncogene , vol.12 , pp. 2425-2435
    • Rodriguez, M.S.1    Arenzana-Seisdedos, F.2
  • 21
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha
    • 21. Baldi, L., Brown, K., Franzoso, G. & Siebenlist, U. (1996). Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha. J. Biol. Chem. 5, 376-379.
    • (1996) J. Biol. Chem. , vol.5 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 22
    • 0033591363 scopus 로고    scopus 로고
    • Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha
    • 22. Gonen, H., et al., & Ciechanover, A. (1999). Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. J. Biol. Chem. 274, 14823-14830.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14823-14830
    • Gonen, H.1    Ciechanover, A.2
  • 23
    • 0031594638 scopus 로고    scopus 로고
    • Proteolysis and the G1-S transition: The SCF connection
    • 23. Krek, W. (1998). Proteolysis and the G1-S transition: the SCF connection. Curr. Opin. Gen. Dev. 8, 36-42.
    • (1998) Curr. Opin. Gen. Dev. , vol.8 , pp. 36-42
    • Krek, W.1
  • 24
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IκBα-ubiquitin ligase
    • 24. Yaron, A., et al., & Ben-Neriah, Y. (1998).). Identification of the receptor component of the IκBα-ubiquitin ligase. Nature 396, 590-594.
    • (1998) Nature , vol.396 , pp. 590-594
    • Yaron, A.1    Ben-Neriah, Y.2
  • 25
    • 0033068154 scopus 로고    scopus 로고
    • The SCF(βTrCP)-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • 25. Winston, J.T., Strack, P., Beer-Romero, P., Chu, C.Y., Elledge, S.J. & Harper, J.W. (1999). The SCF(βTrCP)-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 13, 270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 26
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP
    • 26. Spencer, E., Jiang, J. & Chen, Z.J. (1999). Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP. Genes Dev. 13, 284-294.
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 27
    • 0033582821 scopus 로고    scopus 로고
    • Inducible degradation of IκBα by the proteasome requires interaction with the F-box protein h-βTrCP
    • 27. Kroll, M., et al., & Benarous, R. (1999). Inducible degradation of IκBα by the proteasome requires interaction with the F-box protein h-βTrCP. J. Biol. Chem. 274, 7941-7945.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7941-7945
    • Kroll, M.1    Benarous, R.2
  • 28
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • 28. Coux, O., Tanaka, K. & Goldberg, A.L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 29
    • 0023009780 scopus 로고
    • A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution
    • 29. Tanaka, K., Li, K., Ichihara, A., Waxman, L. and Goldberg, A.L. (1986). A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. J. Biol. Chem. 261, 15197-15202.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15197-15202
    • Tanaka, K.1    Li, K.2    Ichihara, A.3    Waxman, L.4    Goldberg, A.L.5
  • 31
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • 31. Rivett, J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, J.1
  • 32
    • 0024244675 scopus 로고
    • Electron microscopy and image analysis of the multicatalytic proteinase
    • 32. Baumeister, W., Dahlmann, B., Kopp, H.F., Kuehn, L. & Pfeifer, G. (1988). Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Lett. 241, 239-245.
    • (1988) FEBS Lett. , vol.241 , pp. 239-245
    • Baumeister, W.1    Dahlmann, B.2    Kopp, H.F.3    Kuehn, L.4    Pfeifer, G.5
  • 33
    • 0032476030 scopus 로고    scopus 로고
    • Contribution of proteasomal subunits to the cleavage of peptide substrates analyzed with yeast mutants
    • 33. Dick, T.P., et al., & Schild, H. (1998). Contribution of proteasomal subunits to the cleavage of peptide substrates analyzed with yeast mutants. J. Biol. Chem. 273, 25637-25646.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25637-25646
    • Dick, T.P.1    Schild, H.2
  • 34
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • 34. Groll, M., et al., & Huber, R. (1997). Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Huber, R.2
  • 35
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • 35. Orlowski, M., Cardozo, C. & Michaud, C. (1993). Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 32, 1563-1572.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 36
    • 9844226789 scopus 로고    scopus 로고
    • The carboxy-terminus of IκBα determines susceptibility to degradation by the catalytic core of the proteasome
    • 36. Kroll, M., et al., & Rodriguez, M.S. (1997). The carboxy-terminus of IκBα determines susceptibility to degradation by the catalytic core of the proteasome. Oncogene 15, 1841-1850.
    • (1997) Oncogene , vol.15 , pp. 1841-1850
    • Kroll, M.1    Rodriguez, M.S.2
  • 37
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • 37. Maki, C.G., Huibregtse, J.M. & Howley, P.M. (1996). In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res. 56, 2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 38
    • 0030978351 scopus 로고    scopus 로고
    • β-catenin is a target for the ubiquitin-proteasome pathway
    • 38. Aberle, H., Bauer, A., Stappert, J., Kispert, A. & Kemler, R. (1997). β-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16, 3797-3804.
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 39
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • 39. Johnston, J.A., Johnson, E.S., Waller, P.R. & Varshavsky, A. (1995). Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. J. Biol. Chem. 270, 8172-8178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
  • 40
    • 0029902764 scopus 로고    scopus 로고
    • Proteasome pathway operates for the degradation of ornithine decarboxylase in intact cells
    • 40. Murakami, Y., Tanahashi, N., Tanaka, K., Omura, S. & Hayashi, S. (1996). Proteasome pathway operates for the degradation of ornithine decarboxylase in intact cells. Biochem. J. 317, 77-80.
    • (1996) Biochem. J. , vol.317 , pp. 77-80
    • Murakami, Y.1    Tanahashi, N.2    Tanaka, K.3    Omura, S.4    Hayashi, S.5
  • 41
    • 0032947368 scopus 로고    scopus 로고
    • Stimulation of cystine uptake by nitric oxide: Regulation of endothelial cell glutathione levels
    • 41. Li, H., Marshall, Z.M. & Whorton, A.R. (1999). Stimulation of cystine uptake by nitric oxide: regulation of endothelial cell glutathione levels. Am. J. Physiol. 276, C803-C811.
    • (1999) Am. J. Physiol. , vol.276
    • Li, H.1    Marshall, Z.M.2    Whorton, A.R.3
  • 43
    • 0030014641 scopus 로고    scopus 로고
    • The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome
    • 43. Figueiredo-Pereira, M.E., Chen, W.E., Li, J. & Johdo, O. (1996). The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. J. Biol. Chem. 271, 16455-16459.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16455-16459
    • Figueiredo-Pereira, M.E.1    Chen, W.E.2    Li, J.3    Johdo, O.4
  • 44
    • 0030805604 scopus 로고    scopus 로고
    • Cyclosporine A is an uncompetitive inhibitor of proteasome activity and prevents NF-kappaB activation
    • 44. Meyer, S., Gail Kohler, N. & Joly, A. (1997). Cyclosporine A is an uncompetitive inhibitor of proteasome activity and prevents NF-kappaB activation. FEBS Lett. 413, 354-358.
    • (1997) FEBS Lett. , vol.413 , pp. 354-358
    • Meyer, S.1    Gail Kohler, N.2    Joly, A.3
  • 45
    • 0030962262 scopus 로고    scopus 로고
    • p53-dependent induction of apoptosis by proteasome inhibitors
    • 45. Gazos Lopes, U., Erhardt, P., Yao, R. & Cooper, G.M. (1997). p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem. 272, 12893-12896.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Gazos Lopes, U.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 46
    • 2342517449 scopus 로고    scopus 로고
    • Apoptosis induced in L1210 leukemia cells by an inhibitor of the chymotrypsin-like activity of the proteasome
    • 46. Wójcik, C., et al., & Jakóbisiak, M. (1997). Apoptosis induced in L1210 leukemia cells by an inhibitor of the chymotrypsin-like activity of the proteasome. Apoptosis 2, 455-462.
    • (1997) Apoptosis , vol.2 , pp. 455-462
    • Wójcik, C.1    Jakóbisiak, M.2
  • 47
    • 0025050661 scopus 로고
    • DNA fragmentation induced in macrophages by gliotoxin does not require protein synthesis and is preceded by raised inositol triphosphate levels
    • 47. Waring, P. (1990). DNA fragmentation induced in macrophages by gliotoxin does not require protein synthesis and is preceded by raised inositol triphosphate levels. J. Biol. Chem. 265, 14476-14480.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14476-14480
    • Waring, P.1
  • 49
    • 0028300808 scopus 로고
    • Gliotoxin induces apoptosis in mouse L929 fibroblast cells
    • 49. Piva, T.J. (1994). Gliotoxin induces apoptosis in mouse L929 fibroblast cells. Biochem. Mol. Biol. Int. 33, 411-419.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 411-419
    • Piva, T.J.1
  • 50
    • 0030871855 scopus 로고    scopus 로고
    • Apoptosis induced by gliotoxin is preceded by phosphorylation of Histone H3
    • 50. Waring, P., Khan, T. & Sjaarda, A. (1997). Apoptosis induced by gliotoxin is preceded by phosphorylation of Histone H3. J. Biol. Chem. 272, 17929-17936.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17929-17936
    • Waring, P.1    Khan, T.2    Sjaarda, A.3
  • 51
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • 51. Beg, A.A. & Baltimore, D. (1996). An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 274, 782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 52
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-kappaB
    • 52. Wang, C.Y., Mayo, M.W. & Baldwin, A.S., Jr (1996). TNF-and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB. Science 274, 784-786.
    • (1996) Science , vol.274 , pp. 784-786
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 54
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • 54. Wang, C.Y., Mayo, M.W., Korneluk, R.G., Goeddel, D.V. & Baldwin A.S., Jr, (1998). NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281, 1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin A.S., Jr.5
  • 55
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
    • 55. Chu, Z.-L., McKinsey, T.A., Liu, L., Gentry, J.J., Malim, M.H. & Ballard, D.W. (1997). Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc. Natl Acad. Sci. USA 94, 10057-10062.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10057-10062
    • Chu, Z.-L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 56
    • 0032516651 scopus 로고    scopus 로고
    • IEX-1L, an apoptosis inhibitor involved in NF-κB-mediated cell survival
    • 56. Wu, M.X., Ao, Z., Prasad, K.V.S., Wu, R. & Schlossman, S. (1998). IEX-1L, an apoptosis inhibitor involved in NF-κB-mediated cell survival. Science 281, 998-1001.
    • (1998) Science , vol.281 , pp. 998-1001
    • Wu, M.X.1    Ao, Z.2    Prasad, K.V.S.3    Wu, R.4    Schlossman, S.5
  • 57
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • 57. Heinemeyer, W., Kleinschmidt, J., Saidowsky, C.E. & Wolf, D.H. (1991). Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10, 555-562.
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.2    Saidowsky, C.E.3    Wolf, D.H.4
  • 58
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins
    • 58. Heinemeyer, W., Gruhler, A., Mohrle, V., Mahe, Y. & Wolf, D. H. (1993). PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268, 5115-5120.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Mohrle, V.3    Mahe, Y.4    Wolf, D.H.5
  • 59
    • 0032985374 scopus 로고    scopus 로고
    • Transient nuclear factor B (NF-B) activation stimulated by interleukin-1 may be partly dependent on proteasome activity, but not phosphorylation and ubiquitination of the IB molecule, in C6 glioma cells
    • 59. Uehara, T., et. al., & Nomura, Y. (1999). Transient nuclear factor B (NF-B) activation stimulated by interleukin-1 may be partly dependent on proteasome activity, but not phosphorylation and ubiquitination of the IB molecule, in C6 glioma cells. J. Biol. Chem. 274, 15875-15882.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15875-15882
    • Uehara, T.1    Nomura, Y.2
  • 61
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B
    • 61. Arenzana-Seisdedos, F., Thomson, J.A., Rodriguez, M.S., Bachelerie, F., Thomas, D. & Hay, R.T. (1995). Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol. Cell. Biol. 15, 2689-2696.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thomson, J.A.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5    Hay, R.T.6
  • 62
    • 0028884453 scopus 로고
    • Investigation of the potential use of immunosuppressive agent gliotoxin in organ transplantation
    • 62. Sutton, P., Moreland, A., Hutchinson, I.V. & Müllbacher, A. (1995). Investigation of the potential use of immunosuppressive agent gliotoxin in organ transplantation. Transplantation 60, 900-902.
    • (1995) Transplantation , vol.60 , pp. 900-902
    • Sutton, P.1    Moreland, A.2    Hutchinson, I.V.3    Müllbacher, A.4
  • 63
    • 0028986046 scopus 로고
    • Domain organization of I kappa B alpha and sites of interaction with NF-kappa B p65
    • 63. Jaffray, E., Wood, K. & Hay, R. (1995). Domain organization of I kappa B alpha and sites of interaction with NF-kappa B p65. Mol. Cell. Biol. 15, 2166-2172.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2166-2172
    • Jaffray, E.1    Wood, K.2    Hay, R.3
  • 64
    • 0014430011 scopus 로고
    • Dihydrofolate reductase of Streptococcus faicium. II. Purification and some properties of two dihydrofolate reductases from the amethopterin-resistant mutant Streptococcus faecium var. Durans strain A
    • 64. Nixon, P.F. & Blakley, R.L. (1968). Dihydrofolate reductase of Streptococcus faicium. II. Purification and some properties of two dihydrofolate reductases from the amethopterin-resistant mutant Streptococcus faecium var. Durans strain A. J. Biol. Chem. 243, 4722-4731.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4722-4731
    • Nixon, P.F.1    Blakley, R.L.2
  • 65
    • 0028340636 scopus 로고
    • Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease
    • 65. Friguet, B., Szweda, L.I. & Stadtman, E.R. (1994). Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease. Arch. Biochem. Biophys. 311, 168-173.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 168-173
    • Friguet, B.1    Szweda, L.I.2    Stadtman, E.R.3


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