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Volumn 20, Issue 7, 2000, Pages 2423-2435

c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells

Author keywords

[No Author keywords available]

Indexed keywords

MYC PROTEIN; PROTEASOME; UBIQUITIN;

EID: 0034059667     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.7.2423-2435.2000     Document Type: Article
Times cited : (383)

References (76)
  • 1
    • 0028055178 scopus 로고
    • Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines
    • Albert, T., B. Urlbauer, F. Kohlhuber, B. Hammerson, and D. Eick. 1994. Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines. Oncogene 9:759-763.
    • (1994) Oncogene , vol.9 , pp. 759-763
    • Albert, T.1    Urlbauer, B.2    Kohlhuber, F.3    Hammerson, B.4    Eick, D.5
  • 3
    • 0028895215 scopus 로고
    • Mouse and rat B-myc share amino acid sequence homology with the c-myc transcriptional activator domain and contain a B-myc specific carboxy terminal region
    • Asker, C. E., K. P. Magnusson, S. P. Piccoli, K. Andersson, G. Klein, M. D. Cole, and K. G. Wiman. 1995. Mouse and rat B-myc share amino acid sequence homology with the c-myc transcriptional activator domain and contain a B-myc specific carboxy terminal region. Oncogene 11:1963-1969.
    • (1995) Oncogene , vol.11 , pp. 1963-1969
    • Asker, C.E.1    Magnusson, K.P.2    Piccoli, S.P.3    Andersson, K.4    Klein, G.5    Cole, M.D.6    Wiman, K.G.7
  • 4
    • 0029176520 scopus 로고
    • The amino-terminal phosphorylation sites of C-MYC are frequently mutated in Burkitt's lymphoma lines hut not in mouse plasmacytomas and rat immunocytes
    • Axelson, H., M. Henriksson, Y. Wang, K. P. Magnusson, and G. Klein. 1995. The amino-terminal phosphorylation sites of C-MYC are frequently mutated in Burkitt's lymphoma lines hut not in mouse plasmacytomas and rat immunocytes. Eur. J. Cancer 31A:2099-2104.
    • (1995) Eur. J. Cancer , vol.31 A , pp. 2099-2104
    • Axelson, H.1    Henriksson, M.2    Wang, Y.3    Magnusson, K.P.4    Klein, G.5
  • 5
    • 0022995859 scopus 로고
    • Intranuclear degradation of the transformation-inducing protein encoded by avian MC29 virus
    • Bader, J. P., F. A. Hausman, and D. A. Ray. 1986. Intranuclear degradation of the transformation-inducing protein encoded by avian MC29 virus. J. Biol. Chem. 261:8303-8308.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8303-8308
    • Bader, J.P.1    Hausman, F.A.2    Ray, D.A.3
  • 6
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H, and L
    • Barrett, A. J., A. A. Kembhavi, M. A. Brown, H. Kirschke, C. G. Knight, M. Tamai, and K. Hanada. 1982. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H, and L. Biochem. J. 201:189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 7
    • 0027275755 scopus 로고
    • Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas
    • Bhatia, K., K. Huppi, G. Spangler, D. Siwarski, R. Iyer, and I. Magrath. 1993. Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas. Nat. Genet. 5:56-61.
    • (1993) Nat. Genet. , vol.5 , pp. 56-61
    • Bhatia, K.1    Huppi, K.2    Spangler, G.3    Siwarski, D.4    Iyer, R.5    Magrath, I.6
  • 8
    • 0031014535 scopus 로고    scopus 로고
    • Oncogenic activation of c-Myb by carboxyl-terminal truncation leads to decreased proteolysis by the ubiquitin-26S proteasome pathway
    • Bies, J., and L. Wolff. 1997. Oncogenic activation of c-Myb by carboxyl-terminal truncation leads to decreased proteolysis by the ubiquitin-26S proteasome pathway. Oncogene 14:203-212.
    • (1997) Oncogene , vol.14 , pp. 203-212
    • Bies, J.1    Wolff, L.2
  • 10
    • 0030903750 scopus 로고    scopus 로고
    • Regulation of E2F through ubiquitin-proteasome-dependent degradation: Stabilization by the pRB tumor suppressor protein
    • Campanero, M. R., and E. K. Flemington. 1997. Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by the pRB tumor suppressor protein. Proc. Natl. Acad. Sci. USA 94:2221-2226.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2221-2226
    • Campanero, M.R.1    Flemington, E.K.2
  • 11
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 12
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover, A. 1998. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 13
    • 0033551377 scopus 로고    scopus 로고
    • Myc-mediated transformation: The repression connection
    • Claassen, G. F., and S. R. Hann. 1999. Myc-mediated transformation: the repression connection. Oncogene 18:2925-2933.
    • (1999) Oncogene , vol.18 , pp. 2925-2933
    • Claassen, G.F.1    Hann, S.R.2
  • 14
    • 0028305664 scopus 로고
    • Mutations in the coding region of c-MYC in AIDS-associated and other aggressive lymphomas
    • Clark, H. M., T. Yano, T. Otsuki, E. S. Jaffe, D. Shibata, and M. Raffeld. 1994. Mutations in the coding region of c-MYC in AIDS-associated and other aggressive lymphomas. Cancer Res. 54:3383-3386.
    • (1994) Cancer Res. , vol.54 , pp. 3383-3386
    • Clark, H.M.1    Yano, T.2    Otsuki, T.3    Jaffe, E.S.4    Shibata, D.5    Raffeld, M.6
  • 16
    • 0033551390 scopus 로고    scopus 로고
    • The Myc oncoprotein: A critical evaluation of transactivation and target gene regulation
    • Cole, M. D., and S. B. McMahon. 1999. The Myc oncoprotein: a critical evaluation of transactivation and target gene regulation. Oncogene 18:2916-2924.
    • (1999) Oncogene , vol.18 , pp. 2916-2924
    • Cole, M.D.1    McMahon, S.B.2
  • 17
    • 0026099022 scopus 로고
    • The c-Myc protein activates transcription of the alpha prothymosin gene
    • Eilers, M., S. Schirm, and J. M. Bishop. 1991. The c-Myc protein activates transcription of the alpha prothymosin gene. EMBO J. 10:133-141.
    • (1991) EMBO J. , vol.10 , pp. 133-141
    • Eilers, M.1    Schirm, S.2    Bishop, J.M.3
  • 18
    • 0032540498 scopus 로고    scopus 로고
    • The role of protein stability in the cell cycle and cancer
    • Elledge, S. J., and J. W. Harper. 1998. The role of protein stability in the cell cycle and cancer. Biochim. Biophys. Acta 1377:M61-M70.
    • (1998) Biochim. Biophys. Acta , vol.1377
    • Elledge, S.J.1    Harper, J.W.2
  • 20
    • 0031806044 scopus 로고    scopus 로고
    • The molecular role of Myc in growth and transformation: Recent discoveries lead to new insights
    • Facchini, L. M., and L. Z. Penn. 1998. The molecular role of Myc in growth and transformation: recent discoveries lead to new insights. FASEB J. 12: 633-651.
    • (1998) FASEB J. , vol.12 , pp. 633-651
    • Facchini, L.M.1    Penn, L.Z.2
  • 21
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specitic amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specitic amino-terminal threonine modification by lactacystin. Science 258:726-731.
    • (1995) Science , vol.258 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 22
    • 3543060464 scopus 로고    scopus 로고
    • Myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome
    • Flinn, E. M., C. Magnus, C. Busch, and A. P. H. Wright. 1998. myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome. Mol. Cell. Biol. 18:5961-5969.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5961-5969
    • Flinn, E.M.1    Magnus, C.2    Busch, C.3    Wright, A.P.H.4
  • 25
    • 0020616953 scopus 로고
    • Proteins encoded by v-Myc and c-Myc oncogenes: Identification and localization in acute leukemia transformants and bursal lymphoma cell lines
    • Hann, S. R., H. D. Abrams, L. R. Rohrschneider, and R. N. Eisenman. 1983. Proteins encoded by v-Myc and c-Myc oncogenes: identification and localization in acute leukemia transformants and bursal lymphoma cell lines. Cell 34:789-798.
    • (1983) Cell , vol.34 , pp. 789-798
    • Hann, S.R.1    Abrams, H.D.2    Rohrschneider, L.R.3    Eisenman, R.N.4
  • 26
    • 0028004364 scopus 로고
    • The alternatively initiated c-Myc proteins differentially regulate transcription through a non-canonical DNA-binding site
    • Hann, S. R., M. Dixit, R. C. Sears, and L. Sealy. 1994. The alternatively initiated c-Myc proteins differentially regulate transcription through a non-canonical DNA-binding site. Genes Dev. 8:2441-2452.
    • (1994) Genes Dev. , vol.8 , pp. 2441-2452
    • Hann, S.R.1    Dixit, M.2    Sears, R.C.3    Sealy, L.4
  • 27
    • 0021688655 scopus 로고
    • Proteins encoded by the human c-myc oncogene: Differential expression in neoplastic cells
    • Hann, S. R., and R. N. Eisenman. 1984. Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells. Mol. Cell. Biol. 4:2486-2497.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2486-2497
    • Hann, S.R.1    Eisenman, R.N.2
  • 28
    • 0028263811 scopus 로고
    • C-Myc-induced apoptosis in fibroblasts is inhibited by specific cytokines
    • Harrington, E. A., M. R. Bennett, A. Fanidi, and G. I. Evan. 1994. c-Myc-induced apoptosis in fibroblasts is inhibited by specific cytokines. EMBO J. 13:3286-3295.
    • (1994) EMBO J. , vol.13 , pp. 3286-3295
    • Harrington, E.A.1    Bennett, M.R.2    Fanidi, A.3    Evan, G.I.4
  • 29
    • 0029797841 scopus 로고    scopus 로고
    • Degradation of E2F by the ubiquitin-proteasome pathway: Regulation by retinoblastoma family proteins and adenovirus transforming proteins
    • Hateboer, G., R. M. Kerkhoven, A. Shvarts, R. Bernards, and R. L. Beijersbergen. 1996. Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins. Genes Dev. 10:2960-2970.
    • (1996) Genes Dev. , vol.10 , pp. 2960-2970
    • Hateboer, G.1    Kerkhoven, R.M.2    Shvarts, A.3    Bernards, R.4    Beijersbergen, R.L.5
  • 30
    • 0027383378 scopus 로고
    • Phosphorylation sites mapping in the N-terminal domain of c-Myc modulate its transforming potential
    • Henriksson, M., A. Bakardjiev, G. Klein, and B. Luscher. 1993. Phosphorylation sites mapping in the N-terminal domain of c-Myc modulate its transforming potential. Oncogene 8:3199-3209.
    • (1993) Oncogene , vol.8 , pp. 3199-3209
    • Henriksson, M.1    Bakardjiev, A.2    Klein, G.3    Luscher, B.4
  • 31
    • 0029686266 scopus 로고    scopus 로고
    • Proteins of the Myc network: Essential regulators of cell growth and differentiation
    • Henriksson, M., and B. Luscher. 1996. Proteins of the Myc network: essential regulators of cell growth and differentiation. Adv. Cancer Res. 68:109-182.
    • (1996) Adv. Cancer Res. , vol.68 , pp. 109-182
    • Henriksson, M.1    Luscher, B.2
  • 32
    • 0029001787 scopus 로고
    • A link between increased transforming activity of lymphoma-derived MYC mutant alleles, their defective regulation by p107, and altered phosphorylation of the c-Myc transactivation domain
    • Hoang, A. T., B. Lutterbach, B. C. Lewis, T. Yano, T.-Y. Chou, J. F. Barrett, M. Raffeld, S. R. Hann, and C. V. Dang. 1995. A link between increased transforming activity of lymphoma-derived MYC mutant alleles, their defective regulation by p107, and altered phosphorylation of the c-Myc transactivation domain. Mol. Cell. Biol. 15:4031-4042.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4031-4042
    • Hoang, A.T.1    Lutterbach, B.2    Lewis, B.C.3    Yano, T.4    Chou, T.-Y.5    Barrett, J.F.6    Raffeld, M.7    Hann, S.R.8    Dang, C.V.9
  • 33
    • 0029820095 scopus 로고    scopus 로고
    • The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitin-proteasome pathway
    • Hofmann, F., F. Martelli, D. M. Livingston, and Z. Wang. 1996. The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitin-proteasome pathway. Genes Dev. 18:2949-2959.
    • (1996) Genes Dev. , vol.18 , pp. 2949-2959
    • Hofmann, F.1    Martelli, F.2    Livingston, D.M.3    Wang, Z.4
  • 34
    • 0033521876 scopus 로고    scopus 로고
    • Wild-type sequence of MYCN in neuroblastoma cell lines
    • Hogarty, M. D., and G. M. Brodeur. 1999. Wild-type sequence of MYCN in neuroblastoma cell lines. Int. J. Cancer 80:630-631.
    • (1999) Int. J. Cancer , vol.80 , pp. 630-631
    • Hogarty, M.D.1    Brodeur, G.M.2
  • 35
    • 0030575533 scopus 로고    scopus 로고
    • Ubiquitin in signal transduction and cell transformation
    • Isaksson, A., A. M. Musti, and D. Bohmann. 1996. Ubiquitin in signal transduction and cell transformation. Biochim. Biophys. Acta 1288:F21-F29.
    • (1996) Biochim. Biophys. Acta , vol.1288
    • Isaksson, A.1    Musti, A.M.2    Bohmann, D.3
  • 36
    • 0023000891 scopus 로고
    • Expression of the c-myc proto-oncogene during development of Xenopus laevis
    • King, M. W., J. M. Roberts, and R. N. Eisenman. 1986. Expression of the c-myc proto-oncogene during development of Xenopus laevis. Mol. Cell. Biol. 6:4499-4508.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4499-4508
    • King, M.W.1    Roberts, J.M.2    Eisenman, R.N.3
  • 37
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 38
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability
    • Lin, R., P. Beauparlant, C. Makris, S. Meloche, and J. Hiscott. 1996. Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. Mol. Cell. Biol. 16:1401-1409.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 39
    • 0031439931 scopus 로고    scopus 로고
    • A role for CKH phosphorylation of the cactus PEST domain in dorsoventral patterning of the Drosophila embryo
    • Liu, Z., R. L. Galindo, and S. A. Wasserman. 1997. A role for CKH phosphorylation of the cactus PEST domain in dorsoventral patterning of the Drosophila embryo. Genes Dev. 11:3413-3422.
    • (1997) Genes Dev. , vol.11 , pp. 3413-3422
    • Liu, Z.1    Galindo, R.L.2    Wasserman, S.A.3
  • 40
    • 0026657897 scopus 로고
    • Mitosis-specific phosphorylation of the nuclear oncoproteins Myc and Myb
    • Luscher, B., and R. N. Eisenman. 1992. Mitosis-specific phosphorylation of the nuclear oncoproteins Myc and Myb. J. Cell Biol. 118:775-784.
    • (1992) J. Cell Biol. , vol.118 , pp. 775-784
    • Luscher, B.1    Eisenman, R.N.2
  • 41
    • 0023919063 scopus 로고    scopus 로고
    • C-myc and c-myb protein degradation: Effect of metabolic inhibitors and heat shock
    • Luscher, B., and R. N. Eisenman. 1999. c-myc and c-myb protein degradation: effect of metabolic inhibitors and heat shock. Mol. Cell. Biol. 8:2504-2512.
    • (1999) Mol. Cell. Biol. , vol.8 , pp. 2504-2512
    • Luscher, B.1    Eisenman, R.N.2
  • 42
    • 0024446021 scopus 로고
    • Myc proteins are phosphorylated by casein kinase II
    • Luscher, B., E. A. Kuenzel, E. G. Krebs, and R. N. Eisenman. 1989. Myc proteins are phosphorylated by casein kinase II. EMBO J. 8:1111-1119.
    • (1989) EMBO J. , vol.8 , pp. 1111-1119
    • Luscher, B.1    Kuenzel, E.A.2    Krebs, E.G.3    Eisenman, R.N.4
  • 43
    • 0028023421 scopus 로고
    • Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis
    • Lutterbach, B., and S. R. Hann. 1994. Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis. Mol. Cell. Biol. 14:5510-5522.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5510-5522
    • Lutterbach, B.1    Hann, S.R.2
  • 44
    • 0025081901 scopus 로고
    • The pathogenesis of Burkitt's lymphoma
    • Magrath, I. 1990. The pathogenesis of Burkitt's lymphoma. Adv. Cancer Res. 55:133-270.
    • (1990) Adv. Cancer Res. , vol.55 , pp. 133-270
    • Magrath, I.1
  • 45
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • Maki, C. G., J. M. Huibregtse, and P. M. Howley. 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
  • 47
    • 0030849451 scopus 로고    scopus 로고
    • Phenotypes of c-Myc-defident rat fibroblasts isolated by targeted homologous recombination
    • Maleyak, M. K., A. J. Obaya, S. Adachi, and J. M. Sedivy. 1997. Phenotypes of c-Myc-defident rat fibroblasts isolated by targeted homologous recombination. Cell Growth Differ. 8:1039-1048.
    • (1997) Cell Growth Differ. , vol.8 , pp. 1039-1048
    • Maleyak, M.K.1    Obaya, A.J.2    Adachi, S.3    Sedivy, J.M.4
  • 48
    • 0030022860 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates IκBα at S-283, S-288, S-293, and T-291 and is required for its degradation
    • McElhinny, J. A., S. A. Trushin. G. D. Bren, N. Chester, and C. V. Paya. 1996. Casein kinase II phosphorylates IκBα at S-283, S-288, S-293, and T-291 and is required for its degradation. Mol. Cell. Biol. 16:899-906.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 899-906
    • McElhinny, J.A.1    Trushin, S.A.2    Bren, G.D.3    Chester, N.4    Paya, C.V.5
  • 49
    • 0028115718 scopus 로고
    • Site-specific modulation of c-Myc cotransformation by residues phosphorylated in vivo
    • Pulverer, B. J., K. Fischer, K. Vousden, T. Littlewood, G. Evan, and J. R. Woodgett. 1994. Site-specific modulation of c-Myc cotransformation by residues phosphorylated in vivo. Oncogene 9:59-70.
    • (1994) Oncogene , vol.9 , pp. 59-70
    • Pulverer, B.J.1    Fischer, K.2    Vousden, K.3    Littlewood, T.4    Evan, G.5    Woodgett, J.R.6
  • 50
    • 0021088187 scopus 로고
    • Altered nucleotide sequences of a translocated c-myc gene in Burkitt lymphoma
    • Rabbitts, T. H., P. H. Hamlyn, and R. Baer. 1983. Altered nucleotide sequences of a translocated c-myc gene in Burkitt lymphoma. Nature 306:760-765.
    • (1983) Nature , vol.306 , pp. 760-765
    • Rabbitts, T.H.1    Hamlyn, P.H.2    Baer, R.3
  • 51
    • 3142636201 scopus 로고
    • The protein encoded by the human proto-oncogene c-myc
    • Ramsay, G., G. I. Evan, and J. M. Bishop. 1984. The protein encoded by the human proto-oncogene c-myc. Proc. Natl. Acad. Sci. USA 81:7742-7746.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7742-7746
    • Ramsay, G.1    Evan, G.I.2    Bishop, J.M.3
  • 52
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 53
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Goldberg. 1994. Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 54
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 56
    • 0028171039 scopus 로고
    • 1 cyclin degradation: The PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover
    • 1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 14:7953-7966.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7953-7966
    • Salama, S.R.1    Hendricks, K.B.2    Thorner, J.3
  • 57
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti, S. E., S. Y. Kim, and W. P. Tansey. 1999. Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J. 18:717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 59
    • 0029665597 scopus 로고    scopus 로고
    • Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: Requirement for degradation of free IκBα
    • Schwarz, E. M., D. van Antwerp, and I. M. Verma. 1996. Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: requirement for degradation of free IκBα Mol. Cell. Biol. 16:3554-3559.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3554-3559
    • Schwarz, E.M.1    Van Antwerp, D.2    Verma, I.M.3
  • 62
    • 0021925123 scopus 로고
    • Cloning and sequencing of a c-myc oncogene in a Burkitt's lymphoma cell line that is translocated to a germ line alpha switch region
    • Showe, L. C., M. Ballantine, K. Nishikura, J. Erikson, H. Kaji, and C. M. Croce. 1985. Cloning and sequencing of a c-myc oncogene in a Burkitt's lymphoma cell line that is translocated to a germ line alpha switch region. Mol. Cell. Biol. 5:501-509.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 501-509
    • Showe, L.C.1    Ballantine, M.2    Nishikura, K.3    Erikson, J.4    Kaji, H.5    Croce, C.M.6
  • 63
    • 0026096540 scopus 로고
    • Control of c-Myc regulation in normal and neoplastic cells
    • Spencer, C. A., and M. Groudine. 1991. Control of c-Myc regulation in normal and neoplastic cells. Adv. Cancer Res. 56:1-48.
    • (1991) Adv. Cancer Res. , vol.56 , pp. 1-48
    • Spencer, C.A.1    Groudine, M.2
  • 64
    • 0025307435 scopus 로고
    • Enhanced translation and increased turnover of c-myc proteins occurs during differentiation of murine erythroleukemia cells
    • Spotts, G. D., and S. R. Hann. 1990. Enhanced translation and increased turnover of c-myc proteins occurs during differentiation of murine erythroleukemia cells. Mol. Cell. Biol. 10:3952-3964.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3952-3964
    • Spotts, G.D.1    Hann, S.R.2
  • 65
    • 0031037987 scopus 로고    scopus 로고
    • Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins
    • Spotts, G. D., S. V. Patel, Q. Xiao, and S. R. Hann. 1997. Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins. Mol. Cell. Biol. 17:1459-1468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1459-1468
    • Spotts, G.D.1    Patel, S.V.2    Xiao, Q.3    Hann, S.R.4
  • 66
    • 0028834782 scopus 로고
    • Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: Identification and characterization of the conjugating enzymes
    • Stancovski, I., H. Gonen, A. Orian, A. L. Schwartz, and A. Ciechanover. 1995. Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell. Biol. 15:7106-7116.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7106-7116
    • Stancovski, I.1    Gonen, H.2    Orian, A.3    Schwartz, A.L.4    Ciechanover, A.5
  • 67
    • 0023116071 scopus 로고
    • Definition of regions in human c-myc that are involved in transformation and nuclear localization
    • Stone, J., T. de Lange, G. Ramsay, E. Jakobovits, J. M. Bishop, H. Varmus, and W. Lee. 1987. Definition of regions in human c-myc that are involved in transformation and nuclear localization. Mol. Cell. Biol. 7:1697-1709.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1697-1709
    • Stone, J.1    De Lange, T.2    Ramsay, G.3    Jakobovits, E.4    Bishop, J.M.5    Varmus, H.6    W, L.7
  • 68
    • 0021278366 scopus 로고
    • Activation and somatic mutations of the translocated c-myc gene in Burkitt lymphoma cells
    • Taub, R., C. Moulding, J. Battey, W. Murphy, T. Vasicek, G. M. Lenoir, and P. Leder. 1984. Activation and somatic mutations of the translocated c-myc gene in Burkitt lymphoma cells. Cell 36:339-348.
    • (1984) Cell , vol.36 , pp. 339-348
    • Taub, R.1    Moulding, C.2    Battey, J.3    Murphy, W.4    Vasicek, T.5    Lenoir, G.M.6    Leder, P.7
  • 69
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the 8 domain
    • Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the 8 domain. Cell 78:787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 72
    • 0025255957 scopus 로고
    • Developing selective inhibitors of calpain
    • Wang, K. K. W. 1990. Developing selective inhibitors of calpain. Trends Pharmacol. Sci. 11:139-142.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 139-142
    • Wang, K.K.W.1
  • 75
    • 0032535253 scopus 로고    scopus 로고
    • Transactivation-detective c-MycS retains the ability to regulate proliferation and apoptosis
    • Xiao, Q., G. Claassen, J. Shi, S. Adachi, J. Sedivy, and S. R. Hann. 1998. Transactivation-detective c-MycS retains the ability to regulate proliferation and apoptosis. Genes Dev. 12:3803-3808.
    • (1998) Genes Dev. , vol.12 , pp. 3803-3808
    • Xiao, Q.1    Claassen, G.2    Shi, J.3    Adachi, S.4    Sedivy, J.5    Hann, S.R.6
  • 76
    • 0027220503 scopus 로고
    • Clustered mutations in the second exon of the MYC gene in sporadic Burkitt's lymphoma
    • Yano, T., C. A. Sander, H. M. Clark, M. V. Dolezal. E. S. Jaffe, and M. Raffeld. 1993. Clustered mutations in the second exon of the MYC gene in sporadic Burkitt's lymphoma. Oncogene 8:2741-2748.
    • (1993) Oncogene , vol.8 , pp. 2741-2748
    • Yano, T.1    Sander, C.A.2    Clark, H.M.3    Dolezal, M.V.4    Jaffe, E.S.5    Raffeld, M.6


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