메뉴 건너뛰기




Volumn 8, Issue 2, 2008, Pages 83-93

FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLIN E; NOTCH RECEPTOR; STEROL REGULATORY ELEMENT BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 38549086019     PISSN: 1474175X     EISSN: 14741768     Source Type: Journal    
DOI: 10.1038/nrc2290     Document Type: Review
Times cited : (914)

References (119)
  • 1
    • 0020804563 scopus 로고
    • Ubiquitin: Roles in protein modification and breakdown
    • Hershko, A. Ubiquitin: roles in protein modification and breakdown. Cell 34, 11-12 (1983).
    • (1983) Cell , vol.34 , pp. 11-12
    • Hershko, A.1
  • 2
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • An excellent up-to-date review of SCF and APC/C ubiquitin ligases
    • Nakayama, K. I. & Nakayama, K. Ubiquitin ligases: cell-cycle control and cancer. Nature Rev. Cancer 6, 369-381 (2006). An excellent up-to-date review of SCF and APC/C ubiquitin ligases.
    • (2006) Nature Rev. Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 3
    • 0015847513 scopus 로고
    • Genetic control of the cell division cycle in yeast: V. genetic analysis of cdc mutants
    • Hartwell, L. H., Mortimer, R. K., Culotti, J. & Culotti, M. Genetic control of the cell division cycle in yeast: V. genetic analysis of cdc mutants. Genetics 74, 267-286 (1973).
    • (1973) Genetics , vol.74 , pp. 267-286
    • Hartwell, L.H.1    Mortimer, R.K.2    Culotti, J.3    Culotti, M.4
  • 4
    • 0028114987 scopus 로고
    • The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae
    • Schwob, E., Bohm, T., Mendenhall, M. D. & Nasmyth, K. The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae. Cell 79, 233-244 (1994).
    • (1994) Cell , vol.79 , pp. 233-244
    • Schwob, E.1    Bohm, T.2    Mendenhall, M.D.3    Nasmyth, K.4
  • 5
    • 0030612012 scopus 로고    scopus 로고
    • Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
    • Verma, R. et al. Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase. Science 278, 455-460 (1997).
    • (1997) Science , vol.278 , pp. 455-460
    • Verma, R.1
  • 6
    • 0030929469 scopus 로고    scopus 로고
    • SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities
    • Verma, R., Feldman, R. M. & Deshaies, R. J. SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities. Mol. Biol. Cell 8, 1427-1437 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1427-1437
    • Verma, R.1    Feldman, R.M.2    Deshaies, R.J.3
  • 7
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J. & Harper, J. W. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91, 209-219 (1997).
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 8
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • References 4-8 and 28 were instrumental for discovering the function of SCF ubiquitin ligases
    • Feldman, R. M., Correll, C. C., Kaplan, K. B. & Deshaies, R. J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230 (1997). References 4-8 and 28 were instrumental for discovering the function of SCF ubiquitin ligases.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 9
    • 0030693702 scopus 로고    scopus 로고
    • Phosphorylation- and ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor Far1p in budding yeast
    • Henchoz, S. et al. Phosphorylation- and ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor Far1p in budding yeast. Genes Dev. 11, 3046-3060 (1997).
    • (1997) Genes Dev , vol.11 , pp. 3046-3060
    • Henchoz, S.1
  • 10
    • 0034017609 scopus 로고    scopus 로고
    • CDC4 ubiquitin-ligase complex
    • CDC4 ubiquitin-ligase complex. Mol. Biol. Cell 11, 915-927 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 915-927
    • Meimoun, A.1
  • 11
    • 0035801406 scopus 로고    scopus 로고
    • CDC4 recognition elements target Cdc6 for proteolysis in S phase and mitosis
    • CDC4 recognition elements target Cdc6 for proteolysis in S phase and mitosis. EMBO J. 20, 4836-4845 (2001).
    • (2001) EMBO J , vol.20 , pp. 4836-4845
    • Perkins, G.1    Drury, L.S.2    Diffley, J.F.3
  • 12
    • 0030868430 scopus 로고    scopus 로고
    • The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast
    • Drury, L. S., Perkins, G. & Diffley, J. F. The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast. EMBO J. 16, 5966-5976 (1997).
    • (1997) EMBO J , vol.16 , pp. 5966-5976
    • Drury, L.S.1    Perkins, G.2    Diffley, J.F.3
  • 13
    • 0032517963 scopus 로고    scopus 로고
    • Regulation of the G1 phase of the cell cycle by periodic stabilization and degradation of the p25rum1 CDK inhibitor
    • Benito, J., Martin-Castellanos, C. & Moreno, S. Regulation of the G1 phase of the cell cycle by periodic stabilization and degradation of the p25rum1 CDK inhibitor. EMBO J. 17, 482-497 (1998).
    • (1998) EMBO J , vol.17 , pp. 482-497
    • Benito, J.1    Martin-Castellanos, C.2    Moreno, S.3
  • 14
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • This paper defines the CPD
    • Nash, P. et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514-521 (2001). This paper defines the CPD.
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1
  • 15
    • 0035812709 scopus 로고    scopus 로고
    • Fbw7 ubiquitin ligase
    • Fbw7 ubiquitin ligase. Science 294, 173-177 (2001).
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1
  • 16
    • 0027435169 scopus 로고
    • Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans
    • Sundaram, M. & Greenwald, I. Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans. Genetics 135, 765-783 (1993).
    • (1993) Genetics , vol.135 , pp. 765-783
    • Sundaram, M.1    Greenwald, I.2
  • 17
    • 0030659821 scopus 로고    scopus 로고
    • sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins
    • References 16 and 17 identify Sel10/FBW7 as a Notch regulator in worms, and references 18-20 confirm that this pathway is also active in human cells
    • Hubbard, E. J., Wu, G., Kitajewski, J. & Greenwald, I. sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins. Genes Dev. 11, 3182-3193 (1997). References 16 and 17 identify Sel10/FBW7 as a Notch regulator in worms, and references 18-20 confirm that this pathway is also active in human cells.
    • (1997) Genes Dev , vol.11 , pp. 3182-3193
    • Hubbard, E.J.1    Wu, G.2    Kitajewski, J.3    Greenwald, I.4
  • 18
    • 0035929669 scopus 로고    scopus 로고
    • The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog
    • Oberg, C. et al. The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. J. Biol. Chem. 276, 35847-35853 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35847-35853
    • Oberg, C.1
  • 19
    • 0034791336 scopus 로고    scopus 로고
    • SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation
    • Wu, G. et al. SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation. Mol. Cell. Biol. 21, 7403-7415 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 7403-7415
    • Wu, G.1
  • 20
    • 0035860804 scopus 로고    scopus 로고
    • Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor
    • Gupta-Rossi, N. et al. Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. J. Biol. Chem. 276, 34371-34378 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 34371-34378
    • Gupta-Rossi, N.1
  • 21
    • 0035885864 scopus 로고    scopus 로고
    • Characterization of a mouse gene (Fbxw6) that encodes a homologue of Caenorhabditis elegans SEL-10
    • Maruyama, S. et al. Characterization of a mouse gene (Fbxw6) that encodes a homologue of Caenorhabditis elegans SEL-10. Genomics 78, 214-222 (2001).
    • (2001) Genomics , vol.78 , pp. 214-222
    • Maruyama, S.1
  • 22
    • 0035921928 scopus 로고    scopus 로고
    • Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines
    • Moberg, K. H., Bell, D. W., Wahrer, D. C., Haber, D. A. & Hariharan, I. K. Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature 413, 311-316 (2001).
    • (2001) Nature , vol.413 , pp. 311-316
    • Moberg, K.H.1    Bell, D.W.2    Wahrer, D.C.3    Haber, D.A.4    Hariharan, I.K.5
  • 23
    • 0035921849 scopus 로고    scopus 로고
    • Strohmaier, H. et al. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316-322 (2001). References 15, 22 and 23 identify FBW7 as a ubiquitin ligase for cyclin E and found that FBW7 is mutated in tumour cell lines (references 22 and 23) and downregulated in cancer (reference 15).
    • Strohmaier, H. et al. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316-322 (2001). References 15, 22 and 23 identify FBW7 as a ubiquitin ligase for cyclin E and found that FBW7 is mutated in tumour cell lines (references 22 and 23) and downregulated in cancer (reference 15).
  • 24
    • 0037102310 scopus 로고    scopus 로고
    • hCDC4 gene mutations in endometrial cancer
    • Spruck, C. H. et al. hCDC4 gene mutations in endometrial cancer. Cancer Res. 62, 4535-4539 (2002).
    • (2002) Cancer Res , vol.62 , pp. 4535-4539
    • Spruck, C.H.1
  • 25
    • 33749186359 scopus 로고    scopus 로고
    • Expression of mouse Fbxw7 isoforms is regulated in a cell cycle- or p53-dependent manner
    • Matsumoto, A., Onoyama, I. & Nakayama, K. I. Expression of mouse Fbxw7 isoforms is regulated in a cell cycle- or p53-dependent manner. Biochem. Biophys. Res. Commun. 350, 114-119 (2006).
    • (2006) Biochem. Biophys. Res. Commun , vol.350 , pp. 114-119
    • Matsumoto, A.1    Onoyama, I.2    Nakayama, K.I.3
  • 26
    • 0038420033 scopus 로고    scopus 로고
    • hCDC4b, a regulator of cyclin E, as a direct transcriptional target of p53
    • Kimura, T., Gotoh, M., Nakamura, Y. & Arakawa, H. hCDC4b, a regulator of cyclin E, as a direct transcriptional target of p53. Cancer Sci. 94, 431-436 (2003).
    • (2003) Cancer Sci , vol.94 , pp. 431-436
    • Kimura, T.1    Gotoh, M.2    Nakamura, Y.3    Arakawa, H.4
  • 27
    • 10644269326 scopus 로고    scopus 로고
    • Fbxw7/Cdc4 is a p53-dependent, haploinsufficient tumour suppressor gene
    • References 26 and 27 identify the FBW7β isoform as a p53-regulated transcript
    • Mao, J. H. et al. Fbxw7/Cdc4 is a p53-dependent, haploinsufficient tumour suppressor gene. Nature 432, 775-779 (2004). References 26 and 27 identify the FBW7β isoform as a p53-regulated transcript.
    • (2004) Nature , vol.432 , pp. 775-779
    • Mao, J.H.1
  • 28
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C. et al. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86, 263-274 (1996).
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1
  • 30
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin E complex: Multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • References 29 and 30 provide crystal structures of yeast Cdc4 and human FBW7, respectively, and define the contacts made with CPDs
    • Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W. & Pavletich, N. P. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol. Cell 26, 131-143 (2007). References 29 and 30 provide crystal structures of yeast Cdc4 and human FBW7, respectively, and define the contacts made with CPDs.
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 31
    • 34047255191 scopus 로고    scopus 로고
    • Fbw7/hCDC4 dimerization regulates its substrate interactions
    • Welcker, M. & Clurman, B. E. Fbw7/hCDC4 dimerization regulates its substrate interactions. Cell Div. 2, 7 (2007).
    • (2007) Cell Div , vol.2 , pp. 7
    • Welcker, M.1    Clurman, B.E.2
  • 32
    • 34250017680 scopus 로고    scopus 로고
    • Cdc4 dimer accommodates multiple geometries for substrate ubiquitination
    • Cdc4 dimer accommodates multiple geometries for substrate ubiquitination. Cell 129, 1165-1176 (2007).
    • (2007) Cell , vol.129 , pp. 1165-1176
    • Tang, X.1
  • 33
    • 33846266628 scopus 로고    scopus 로고
    • Fbw7 isoform interaction contributes to cyclin E proteolysis
    • Zhang, W. & Koepp, D. M. Fbw7 isoform interaction contributes to cyclin E proteolysis. Mol. Cancer Res. 4, 935-943 (2006).
    • (2006) Mol. Cancer Res , vol.4 , pp. 935-943
    • Zhang, W.1    Koepp, D.M.2
  • 34
    • 0034723296 scopus 로고    scopus 로고
    • Homodimer of two F-box proteins βTrCP1 or βTrCP2 binds to IκBα for signal-dependent ubiquitination
    • Suzuki, H. et al. Homodimer of two F-box proteins βTrCP1 or βTrCP2 binds to IκBα for signal-dependent ubiquitination. J. Biol. Chem. 275, 2877-2884 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 2877-2884
    • Suzuki, H.1
  • 35
    • 6944227551 scopus 로고    scopus 로고
    • A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size
    • Welcker, M., Orian, A., Grim, J. E., Eisenman, R. N. & Clurman, B. E. A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size. Curr. Biol. 14, 1852-1857 (2004).
    • (2004) Curr. Biol , vol.14 , pp. 1852-1857
    • Welcker, M.1    Orian, A.2    Grim, J.E.3    Eisenman, R.N.4    Clurman, B.E.5
  • 36
    • 0032440674 scopus 로고    scopus 로고
    • Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase
    • Kominami, K., Ochotorena, I. & Toda, T. Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase. Genes Cells 3, 721-735 (1998).
    • (1998) Genes Cells , vol.3 , pp. 721-735
    • Kominami, K.1    Ochotorena, I.2    Toda, T.3
  • 37
    • 0026649165 scopus 로고
    • Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle
    • Koff, A. et al. Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle. Science 257, 1689-1694 (1992).
    • (1992) Science , vol.257 , pp. 1689-1694
    • Koff, A.1
  • 38
    • 0026698263 scopus 로고
    • Association of human cyclin E with a periodic G1-S phase protein kinase
    • Dulic, V., Lees, E. & Reed, S. I. Association of human cyclin E with a periodic G1-S phase protein kinase. Science 257, 1958-1961 (1992).
    • (1992) Science , vol.257 , pp. 1958-1961
    • Dulic, V.1    Lees, E.2    Reed, S.I.3
  • 39
    • 18344381018 scopus 로고    scopus 로고
    • Cyclin E in normal and neoplastic cell cycles
    • Hwang, H. C. & Clurman, B. E. Cyclin E in normal and neoplastic cell cycles. Oncogene 24, 2776-2786 (2005).
    • (2005) Oncogene , vol.24 , pp. 2776-2786
    • Hwang, H.C.1    Clurman, B.E.2
  • 40
    • 33846018073 scopus 로고    scopus 로고
    • Kinase-independent function of cyclin E
    • Geng, Y. et al. Kinase-independent function of cyclin E. Mol. Cell 25, 127-139 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 127-139
    • Geng, Y.1
  • 41
    • 0029957947 scopus 로고    scopus 로고
    • Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation
    • Clurman, B. E., Sheaff, R. J., Thress, K., Groudine, M. & Roberts, J. M. Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Dev. 10, 1979-1990 (1996).
    • (1996) Genes Dev , vol.10 , pp. 1979-1990
    • Clurman, B.E.1    Sheaff, R.J.2    Thress, K.3    Groudine, M.4    Roberts, J.M.5
  • 42
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won, K. A. & Reed, S. I. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15, 4182-4193 (1996).
    • (1996) EMBO J , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.I.2
  • 43
    • 0141591688 scopus 로고    scopus 로고
    • Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation
    • This reference reports the identification of GSK3 as a CPD kinase and the identification of the, 4 negative charge in CPDs
    • Welcker, M. et al. Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation. Mol. Cell 12, 381-392 (2003). This reference reports the identification of GSK3 as a CPD kinase and the identification of the + 4 negative charge in CPDs.
    • (2003) Mol. Cell , vol.12 , pp. 381-392
    • Welcker, M.1
  • 44
    • 9644279589 scopus 로고    scopus 로고
    • Fbw7 ubiquitin ligase
    • Fbw7 ubiquitin ligase. J. Biol. Chem. 279, 50110-50119 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 50110-50119
    • Ye, X.1
  • 45
    • 33644850537 scopus 로고    scopus 로고
    • The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability
    • Yeh, E. S., Lew, B. O. & Means, A. R. The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability. J. Biol. Chem. 281, 241-251 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 241-251
    • Yeh, E.S.1    Lew, B.O.2    Means, A.R.3
  • 46
    • 33745508920 scopus 로고    scopus 로고
    • Ubiquitylation of cyclin E requires the sequential function of SCF complexes containing distinct hCdc4 isoforms
    • van Drogen, F. et al. Ubiquitylation of cyclin E requires the sequential function of SCF complexes containing distinct hCdc4 isoforms. Mol. Cell 23, 37-48 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 37-48
    • van Drogen, F.1
  • 47
  • 48
    • 2942693567 scopus 로고    scopus 로고
    • Myc degradation: Dancing with ubiquitin ligases
    • Amati, B. Myc degradation: dancing with ubiquitin ligases. Proc. Natl Acad. Sci. USA 101, 8843-8844 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8843-8844
    • Amati, B.1
  • 49
    • 2942614705 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7
    • Yada, M. et al. Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. EMBO J. 23, 2116-2125 (2004).
    • (2004) EMBO J , vol.23 , pp. 2116-2125
    • Yada, M.1
  • 50
    • 2942650133 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation
    • Welcker, M. et al. The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc. Natl Acad. Sci. USA 101, 9085-9090 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9085-9090
    • Welcker, M.1
  • 51
    • 33646843753 scopus 로고    scopus 로고
    • Activation by c-Myc of transcription by RNA polymerases I, II and III
    • Gomez-Roman, N. et al. Activation by c-Myc of transcription by RNA polymerases I, II and III. Biochem. Soc. Symp. 73, 141-154 (2006).
    • (2006) Biochem. Soc. Symp , vol.73 , pp. 141-154
    • Gomez-Roman, N.1
  • 52
    • 14744284578 scopus 로고    scopus 로고
    • c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I
    • Grandori, C. et al. c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I. Nature Cell Biol. 7, 311-318 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 311-318
    • Grandori, C.1
  • 53
    • 34347401998 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP28 is required for MYC stability
    • Popov, N. et al. The ubiquitin-specific protease USP28 is required for MYC stability. Nature Cell Biol. 9, 765-774 (2007).
    • (2007) Nature Cell Biol , vol.9 , pp. 765-774
    • Popov, N.1
  • 54
    • 0034306997 scopus 로고    scopus 로고
    • Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability
    • Sears, R. et al. Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes Dev. 14, 2501-2514 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2501-2514
    • Sears, R.1
  • 55
    • 2342526543 scopus 로고    scopus 로고
    • A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells
    • Yeh, E. et al. A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells. Nature Cell Biol. 6, 308-318 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 308-318
    • Yeh, E.1
  • 56
    • 0036098552 scopus 로고    scopus 로고
    • Shaulian, E. & Karin, M. AP-1 as a regulator of cell life and death. Nature Cell Biol. 4, 131-136 (2002).
    • Shaulian, E. & Karin, M. AP-1 as a regulator of cell life and death. Nature Cell Biol. 4, 131-136 (2002).
  • 58
    • 0031283180 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors
    • Fuchs, S. Y. et al. c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. J. Biol. Chem. 272, 32163-32168 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 32163-32168
    • Fuchs, S.Y.1
  • 59
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti, A. M., Treier, M. & Bohmann, D. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275, 400-402 (1997).
    • (1997) Science , vol.275 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 60
    • 22244476115 scopus 로고    scopus 로고
    • The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase
    • Wei, W., Jin, J., Schlisio, S., Harper, J. W. & Kaelin, W. G., Jr. The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell 8, 25-33 (2005).
    • (2005) Cancer Cell , vol.8 , pp. 25-33
    • Wei, W.1    Jin, J.2    Schlisio, S.3    Harper, J.W.4    Kaelin Jr., W.G.5
  • 61
    • 33847709027 scopus 로고    scopus 로고
    • SREBP in signal transduction: Cholesterol metabolism and beyond
    • Bengoechea-Alonso, M. T. & Ericsson, J. SREBP in signal transduction: cholesterol metabolism and beyond. Curr. Opin. Cell Biol. 19, 215-222 (2007).
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 215-222
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 63
    • 33748751591 scopus 로고    scopus 로고
    • Phosphorylation and ubiquitination of the transcription factor sterol regulatory element-binding protein-1 in response to DNA binding
    • Punga, T., Bengoechea-Alonso, M. T. & Ericsson, J. Phosphorylation and ubiquitination of the transcription factor sterol regulatory element-binding protein-1 in response to DNA binding. J. Biol. Chem. 281, 25278-25286 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 25278-25286
    • Punga, T.1    Bengoechea-Alonso, M.T.2    Ericsson, J.3
  • 64
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • Artavanis-Tsakonas, S., Rand, M. D. & Lake, R. J. Notch signaling: cell fate control and signal integration in development. Science 284, 770-776 (1999).
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 66
    • 34547780475 scopus 로고    scopus 로고
    • FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors
    • O'Neil, J. et al. FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors. J. Exp. Med. 204, 1813-1824 (2007).
    • (2007) J. Exp. Med , vol.204 , pp. 1813-1824
    • O'Neil, J.1
  • 67
    • 34547820257 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia. J. Exp. Med. 204, 1825-1835 (2007). References 66, 67, 80 and 93 identified a clear preference for missense mutations in FBW7 in T-ALL, indicating that FBW7 mutants might have dominant-negative effects.
    • FBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia. J. Exp. Med. 204, 1825-1835 (2007). References 66, 67, 80 and 93 identified a clear preference for missense mutations in FBW7 in T-ALL, indicating that FBW7 mutants might have dominant-negative effects.
  • 68
    • 33745131039 scopus 로고    scopus 로고
    • Myc is a Notch1 transcriptional target and a requisite for Notch1-induced mammary tumorigenesis in mice
    • Klinakis, A. et al. Myc is a Notch1 transcriptional target and a requisite for Notch1-induced mammary tumorigenesis in mice. Proc. Natl Acad. Sci. USA 103, 9262-9267 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9262-9267
    • Klinakis, A.1
  • 69
    • 33746546368 scopus 로고    scopus 로고
    • c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma
    • Weng, A. P. et al. c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia/lymphoma. Genes Dev. 20, 2096-2109 (2006).
    • (2006) Genes Dev , vol.20 , pp. 2096-2109
    • Weng, A.P.1
  • 70
    • 33845306813 scopus 로고    scopus 로고
    • NOTCH1 directly regulates c-MYC and activates a feed-forward-loop transcriptional network promoting leukemic cell growth
    • Palomero, T. et al. NOTCH1 directly regulates c-MYC and activates a feed-forward-loop transcriptional network promoting leukemic cell growth. Proc. Natl Acad. Sci. USA 103, 18261-18266 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18261-18266
    • Palomero, T.1
  • 71
    • 33750317437 scopus 로고    scopus 로고
    • Notch1 contributes to mouse T-cell leukemia by directly inducing the expression of c-myc
    • Sharma, V. M. et al. Notch1 contributes to mouse T-cell leukemia by directly inducing the expression of c-myc. Mol. Cell. Biol. 26, 8022-8031 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8022-8031
    • Sharma, V.M.1
  • 72
    • 0032416732 scopus 로고    scopus 로고
    • Evidence for functional and physical association between Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin
    • Wu, G., Hubbard, E. J., Kitajewski, J. K. & Greenwald, I. Evidence for functional and physical association between Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin. Proc. Natl Acad. Sci. USA 95, 15787-15791 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15787-15791
    • Wu, G.1    Hubbard, E.J.2    Kitajewski, J.K.3    Greenwald, I.4
  • 73
    • 0036736222 scopus 로고    scopus 로고
    • SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-β peptide production
    • Li, J. et al. SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-β peptide production. J. Neurochem. 82, 1540-1548 (2002).
    • (2002) J. Neurochem , vol.82 , pp. 1540-1548
    • Li, J.1
  • 75
    • 1642617693 scopus 로고    scopus 로고
    • PI3K/Akt signalling pathway and cancer
    • Fresno Vara, J. A. et al. PI3K/Akt signalling pathway and cancer. Cancer Treat. Rev. 30, 193-204 (2004).
    • (2004) Cancer Treat. Rev , vol.30 , pp. 193-204
    • Fresno Vara, J.A.1
  • 76
    • 1542364470 scopus 로고    scopus 로고
    • Mouse Fbw7/Sel-10/Cdc4 is required for notch degradation during vascular development
    • Tsunematsu, R. et al. Mouse Fbw7/Sel-10/Cdc4 is required for notch degradation during vascular development. J. Biol. Chem. 279, 9417-9423 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 9417-9423
    • Tsunematsu, R.1
  • 77
    • 1542409037 scopus 로고    scopus 로고
    • Defective cardiovascular development and elevated cyclin E and Notch proteins in mice lacking the Fbw7 F-box protein
    • Tetzlaff, M. T. et al. Defective cardiovascular development and elevated cyclin E and Notch proteins in mice lacking the Fbw7 F-box protein. Proc. Natl Acad. Sci. USA 101, 3338-3345 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3338-3345
    • Tetzlaff, M.T.1
  • 78
    • 36549071481 scopus 로고    scopus 로고
    • Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis
    • 5 Nov, doi:10.1084/jem.20062299
    • Onoyama, I. et al. Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis. J. Exp. Med. 5 Nov 2007 (doi:10.1084/jem.20062299).
    • (2007) J. Exp. Med
    • Onoyama, I.1
  • 80
    • 0032887168 scopus 로고    scopus 로고
    • DNA copy number losses in human neoplasms
    • Knuutila, S. et al. DNA copy number losses in human neoplasms. Am. J. Pathol. 155, 683-694 (1999).
    • (1999) Am. J. Pathol , vol.155 , pp. 683-694
    • Knuutila, S.1
  • 81
    • 34250863886 scopus 로고    scopus 로고
    • Chromosomally unstable mouse tumours have genomic alterations similar to diverse human cancers
    • Maser, R. S. et al. Chromosomally unstable mouse tumours have genomic alterations similar to diverse human cancers. Nature 447, 966-971 (2007).
    • (2007) Nature , vol.447 , pp. 966-971
    • Maser, R.S.1
  • 82
    • 33748097473 scopus 로고    scopus 로고
    • Mutational analysis of the hCDC4 gene in gastric carcinomas
    • Lee, J. W. et al. Mutational analysis of the hCDC4 gene in gastric carcinomas. Eur. J. Cancer 42, 2369-2373 (2006).
    • (2006) Eur. J. Cancer , vol.42 , pp. 2369-2373
    • Lee, J.W.1
  • 83
    • 29244460649 scopus 로고    scopus 로고
    • CDC4 mutations occur in a subset of colorectal cancers but are not predicted to cause loss of function and are not associated with chromosomal instability
    • Kemp, Z. et al. CDC4 mutations occur in a subset of colorectal cancers but are not predicted to cause loss of function and are not associated with chromosomal instability. Cancer Res. 65, 11361-11366 (2005).
    • (2005) Cancer Res , vol.65 , pp. 11361-11366
    • Kemp, Z.1
  • 84
    • 2942623550 scopus 로고    scopus 로고
    • Cyclin E dysregulation and chromosomal instability in endometrial cancer
    • Hubalek, M. M. et al. Cyclin E dysregulation and chromosomal instability in endometrial cancer. Oncogene 23, 4187-4192 (2004).
    • (2004) Oncogene , vol.23 , pp. 4187-4192
    • Hubalek, M.M.1
  • 85
    • 32544446008 scopus 로고    scopus 로고
    • CDC4 gene expression as potential biomarker for targeted therapy in prostate cancer
    • Koh, M. S., Ittmann, M., Kadmon, D., Thompson, T. C. & Leach, F. S. CDC4 gene expression as potential biomarker for targeted therapy in prostate cancer. Cancer Biol. Ther. 5, 78-83 (2006).
    • (2006) Cancer Biol. Ther , vol.5 , pp. 78-83
    • Koh, M.S.1    Ittmann, M.2    Kadmon, D.3    Thompson, T.C.4    Leach, F.S.5
  • 86
    • 0141425732 scopus 로고    scopus 로고
    • Calhoun, E. S. et al. BRAF and FBXW7 (CDC4, FBW7, AGO, SEL10) mutations in distinct subsets of pancreatic cancer: potential therapeutic targets. Am. J. Pathol. 163, 1255-1260 (2003).
    • Calhoun, E. S. et al. BRAF and FBXW7 (CDC4, FBW7, AGO, SEL10) mutations in distinct subsets of pancreatic cancer: potential therapeutic targets. Am. J. Pathol. 163, 1255-1260 (2003).
  • 87
    • 35148842479 scopus 로고    scopus 로고
    • Akhoondi, S. et al. FBXW7/hCDC4 is a general tumor suppressor in human cancer. Cancer Res. 67, 9006-9012 (2007). This paper documents an extensive genetic screen for mutations in FBW7 in over 1,500 diverse tumours.
    • Akhoondi, S. et al. FBXW7/hCDC4 is a general tumor suppressor in human cancer. Cancer Res. 67, 9006-9012 (2007). This paper documents an extensive genetic screen for mutations in FBW7 in over 1,500 diverse tumours.
  • 88
    • 33750444602 scopus 로고    scopus 로고
    • Mutation analysis of hCDC4 in AML cells identifies a new intronic polymorphism
    • Nowak, D. et al. Mutation analysis of hCDC4 in AML cells identifies a new intronic polymorphism. Int. J. Med. Sci. 3, 148-151 (2006).
    • (2006) Int. J. Med. Sci , vol.3 , pp. 148-151
    • Nowak, D.1
  • 89
    • 33745057420 scopus 로고    scopus 로고
    • Somatic mutation of hCDC4 gene is rare in lung adenocarcinomas
    • Woo Lee, J. et al. Somatic mutation of hCDC4 gene is rare in lung adenocarcinomas. Acta Oncol. 45, 487-488 (2006).
    • (2006) Acta Oncol , vol.45 , pp. 487-488
    • Woo Lee, J.1
  • 90
    • 20444481993 scopus 로고    scopus 로고
    • Infrequent mutations of Archipelago (hAGO, hCDC4, Fbw7) in primary ovarian cancer
    • Kwak, E. L. et al. Infrequent mutations of Archipelago (hAGO, hCDC4, Fbw7) in primary ovarian cancer. Gynecol. Oncol. 98, 124-128 (2005).
    • (2005) Gynecol. Oncol , vol.98 , pp. 124-128
    • Kwak, E.L.1
  • 91
    • 34247230300 scopus 로고    scopus 로고
    • Low frequency of hCDC4 mutations in human primary ovarian cancer
    • Sgambato, A. et al. Low frequency of hCDC4 mutations in human primary ovarian cancer. Gynecol. Oncol. 105, 553-555 (2007).
    • (2007) Gynecol. Oncol , vol.105 , pp. 553-555
    • Sgambato, A.1
  • 92
    • 33747837463 scopus 로고    scopus 로고
    • hCDC4 variation in osteosarcoma
    • Yan, T. et al. hCDC4 variation in osteosarcoma. Cancer Genet. Cytogenet. 169, 138-142 (2006).
    • (2006) Cancer Genet. Cytogenet , vol.169 , pp. 138-142
    • Yan, T.1
  • 93
    • 1542377277 scopus 로고    scopus 로고
    • Rajagopalan, H. et al. Inactivation of hCDC4 can cause chromosomal instability. Nature 428, 77-81 (2004). This paper shows that mutations in FBW7 can lead to genetic instability.
    • Rajagopalan, H. et al. Inactivation of hCDC4 can cause chromosomal instability. Nature 428, 77-81 (2004). This paper shows that mutations in FBW7 can lead to genetic instability.
  • 94
    • 34250837539 scopus 로고    scopus 로고
    • The tumor suppressor gene hCDC4 is frequently mutated in human T-cell acute lymphoblastic leukemia with functional consequences for Notch signaling
    • Malyukova, A. et al. The tumor suppressor gene hCDC4 is frequently mutated in human T-cell acute lymphoblastic leukemia with functional consequences for Notch signaling. Cancer Res. 67, 5611-5616 (2007).
    • (2007) Cancer Res , vol.67 , pp. 5611-5616
    • Malyukova, A.1
  • 95
    • 0022430244 scopus 로고
    • Sequence curiosity in v-myc oncogene
    • Papas, T. S. & Lautenberger, J. A. Sequence curiosity in v-myc oncogene. Nature 318, 237 (1985).
    • (1985) Nature , vol.318 , pp. 237
    • Papas, T.S.1    Lautenberger, J.A.2
  • 97
    • 0034059667 scopus 로고    scopus 로고
    • c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory, M. A. & Hann, S. R. c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells. Mol. Cell. Biol. 20, 2423-2335 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 2423-2335
    • Gregory, M.A.1    Hann, S.R.2
  • 98
    • 0034653998 scopus 로고    scopus 로고
    • c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover
    • Bahram, F., von der Lehr, N., Cetinkaya, C. & Larsson, L. G. c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover. Blood 95, 2104-2110 (2000).
    • (2000) Blood , vol.95 , pp. 2104-2110
    • Bahram, F.1    von der Lehr, N.2    Cetinkaya, C.3    Larsson, L.G.4
  • 99
    • 23844469503 scopus 로고    scopus 로고
    • Evasion of the p53 tumour surveillance network by tumour-derived MYC mutants
    • Hemann, M. T. et al. Evasion of the p53 tumour surveillance network by tumour-derived MYC mutants. Nature 436, 807-811 (2005).
    • (2005) Nature , vol.436 , pp. 807-811
    • Hemann, M.T.1
  • 100
    • 5044225888 scopus 로고    scopus 로고
    • Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia
    • Weng, A. P. et al. Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia. Science 306, 269-271 (2004).
    • (2004) Science , vol.306 , pp. 269-271
    • Weng, A.P.1
  • 101
    • 34248221516 scopus 로고    scopus 로고
    • FBXW7/hCDC4 controls glioma cell proliferation in vitro and is a prognostic marker for survival in glioblastoma patients
    • Hagedorn, M. et al. FBXW7/hCDC4 controls glioma cell proliferation in vitro and is a prognostic marker for survival in glioblastoma patients. Cell Div. 2, 9 (2007).
    • (2007) Cell Div , vol.2 , pp. 9
    • Hagedorn, M.1
  • 103
    • 22144457934 scopus 로고    scopus 로고
    • Ras activity regulates cyclin E degradation by the Fbw7 pathway
    • Minella, A. C., Welcker, M. & Clurman, B. E. Ras activity regulates cyclin E degradation by the Fbw7 pathway. Proc. Natl Acad. Sci. USA 102, 9649-54 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9649-9654
    • Minella, A.C.1    Welcker, M.2    Clurman, B.E.3
  • 104
    • 14844312051 scopus 로고    scopus 로고
    • The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4
    • Welcker, M. & Clurman, B. E. The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4. J. Biol. Chem. 280, 7654-7658 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 7654-7658
    • Welcker, M.1    Clurman, B.E.2
  • 105
    • 0031028246 scopus 로고    scopus 로고
    • Induction of mammary gland hyperplasia and carcinomas in transgenic mice expressing human cyclin E
    • Bortner, D. M. & Rosenberg, M. P. Induction of mammary gland hyperplasia and carcinomas in transgenic mice expressing human cyclin E. Mol. Cell. Biol. 17, 453-459 (1997).
    • (1997) Mol. Cell. Biol , vol.17 , pp. 453-459
    • Bortner, D.M.1    Rosenberg, M.P.2
  • 106
    • 0033575920 scopus 로고    scopus 로고
    • Deregulated cyclin E induces chromosome instability
    • Spruck, C. H., Won, K. A. & Reed, S. I. Deregulated cyclin E induces chromosome instability. Nature 401, 297-300 (1999).
    • (1999) Nature , vol.401 , pp. 297-300
    • Spruck, C.H.1    Won, K.A.2    Reed, S.I.3
  • 107
    • 0842325857 scopus 로고    scopus 로고
    • Mutation of hCDC4 leads to cell cycle deregulation of cyclin E in cancer
    • Ekholm-Reed, S. et al. Mutation of hCDC4 leads to cell cycle deregulation of cyclin E in cancer. Cancer Res 64, 795-800 (2004).
    • (2004) Cancer Res , vol.64 , pp. 795-800
    • Ekholm-Reed, S.1
  • 108
    • 0037195268 scopus 로고    scopus 로고
    • p53 and p21 form an inducible barrier that protects cells against cyclin E-cdk2 deregulation
    • Minella, A. C. et al. p53 and p21 form an inducible barrier that protects cells against cyclin E-cdk2 deregulation. Curr. Biol. 12, 1817-1827 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 1817-1827
    • Minella, A.C.1
  • 109
    • 22244492318 scopus 로고    scopus 로고
    • A mouse model for cyclin E-dependent genetic instability and tumorigenesis
    • Loeb, K. R. et al. A mouse model for cyclin E-dependent genetic instability and tumorigenesis. Cancer Cell 8, 35-47 (2005).
    • (2005) Cancer Cell , vol.8 , pp. 35-47
    • Loeb, K.R.1
  • 110
    • 33751329698 scopus 로고    scopus 로고
    • Deregulated cyclin E promotes p53 loss of heterozygosity and tumorigenesis in the mouse mammary gland
    • Smith, A. P. et al. Deregulated cyclin E promotes p53 loss of heterozygosity and tumorigenesis in the mouse mammary gland. Oncogene 25, 7245-7259 (2006).
    • (2006) Oncogene , vol.25 , pp. 7245-7259
    • Smith, A.P.1
  • 112
    • 0345255605 scopus 로고    scopus 로고
    • Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide
    • Issaeva, N. et al. Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide. Proc. Natl Acad. Sci. USA 100, 13303-13307 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13303-13307
    • Issaeva, N.1
  • 113
    • 0037025201 scopus 로고    scopus 로고
    • Sustained loss of a neoplastic phenotype by brief inactivation of MYC
    • Jain, M. et al. Sustained loss of a neoplastic phenotype by brief inactivation of MYC. Science 297, 102-104 (2002).
    • (2002) Science , vol.297 , pp. 102-104
    • Jain, M.1
  • 114
    • 33646366173 scopus 로고    scopus 로고
    • Notch 1 activation in the molecular pathogenesis of T-cell acute lymphoblastic leukaemia
    • Grabher, C., von Boehmer, H. & Look, A. T. Notch 1 activation in the molecular pathogenesis of T-cell acute lymphoblastic leukaemia. Nature Rev. Cancer 6, 347-359 (2006).
    • (2006) Nature Rev. Cancer , vol.6 , pp. 347-359
    • Grabher, C.1    von Boehmer, H.2    Look, A.T.3
  • 115
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B. A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386 (2000).
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1
  • 116
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F box-Skp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F box-Skp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 117
    • 7544234937 scopus 로고    scopus 로고
    • Systematic analysis and nomenclature of mammalian F-box proteins
    • Jin, J. et al. Systematic analysis and nomenclature of mammalian F-box proteins. Genes Dev. 18, 2573-2580 (2004).
    • (2004) Genes Dev , vol.18 , pp. 2573-2580
    • Jin, J.1
  • 118
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • A comprehensive review on ubiquitin ligases
    • Willems, A. R., Schwab, M. & Tyers, M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695, 133-170 (2004). A comprehensive review on ubiquitin ligases.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 119
    • 36849020875 scopus 로고    scopus 로고
    • Cdc4 ubiquitin ligase regulates calcineurin signaling through degradation of phosphorylated Rcn1, an inhibitor of calcineurin
    • Cdc4 ubiquitin ligase regulates calcineurin signaling through degradation of phosphorylated Rcn1, an inhibitor of calcineurin. Proc. Natl Acad. Sci. USA 104, 17418-17423 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17418-17423
    • Kishi, T.1    Ikeda, A.2    Nagao, R.3    Koyama, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.