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Volumn 21, Issue 9, 2010, Pages 936-943

E3 ubiquitin ligases in ErbB receptor quantity control

Author keywords

Cancer; Degradation; E3 ubiqutin ligase; ErbB receptor; Ubiquitination

Indexed keywords

AQUAPORIN; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; NEUREGULIN RECEPTOR DEGRADATION PROTEIN 1; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 78449296171     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2010.09.006     Document Type: Review
Times cited : (34)

References (113)
  • 1
    • 0030131175 scopus 로고    scopus 로고
    • Involvement of the neuregulins and their receptors in cardiac and neural development
    • Carraway K.L.3rd. Involvement of the neuregulins and their receptors in cardiac and neural development. Bioessays 1996, 18:263-266.
    • (1996) Bioessays , vol.18 , pp. 263-266
    • Carraway, K.1
  • 2
    • 0030919509 scopus 로고    scopus 로고
    • Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesis
    • Burden S., Yarden Y. Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesis. Neuron 1997, 18:847-855.
    • (1997) Neuron , vol.18 , pp. 847-855
    • Burden, S.1    Yarden, Y.2
  • 3
    • 34247863773 scopus 로고    scopus 로고
    • The neuregulin-I/ErbB signaling system in development and disease
    • Britsch S. The neuregulin-I/ErbB signaling system in development and disease. Adv Anat Embryol Cell Biol 2007, 190:1-65.
    • (2007) Adv Anat Embryol Cell Biol , vol.190 , pp. 1-65
    • Britsch, S.1
  • 5
    • 0037429725 scopus 로고    scopus 로고
    • The ErbB receptors and their role in cancer progression
    • Holbro T., Civenni G., Hynes N.E. The ErbB receptors and their role in cancer progression. Exp Cell Res 2003, 284:99-110.
    • (2003) Exp Cell Res , vol.284 , pp. 99-110
    • Holbro, T.1    Civenni, G.2    Hynes, N.E.3
  • 6
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: the complexity of targeted inhibitors
    • Hynes N.E., Lane H.A. ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer 2005, 5:341-354.
    • (2005) Nat Rev Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 7
    • 73949083511 scopus 로고    scopus 로고
    • Oncogenic EGFR signaling networks in glioma
    • Huang P.H., Xu A.M., White F.M. Oncogenic EGFR signaling networks in glioma. Sci Signal 2009, 2:re6.
    • (2009) Sci Signal , vol.2
    • Huang, P.H.1    Xu, A.M.2    White, F.M.3
  • 8
    • 33746485766 scopus 로고    scopus 로고
    • Epidermal growth factor receptor targeting in cancer
    • Mendelsohn J., Baselga J. Epidermal growth factor receptor targeting in cancer. Semin Oncol 2006, 33:369-385.
    • (2006) Semin Oncol , vol.33 , pp. 369-385
    • Mendelsohn, J.1    Baselga, J.2
  • 9
    • 76949087071 scopus 로고    scopus 로고
    • Colorectal cancer in review: the role of the EGFR pathway
    • Saif M.W. Colorectal cancer in review: the role of the EGFR pathway. Expert Opin Investig Drugs 2010, 19:357-369.
    • (2010) Expert Opin Investig Drugs , vol.19 , pp. 357-369
    • Saif, M.W.1
  • 10
    • 37049183697 scopus 로고
    • Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon D.J., Clark G.M., Wong S.G., Levin W.J., Ullrich A., McGuire W.L. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987, 235:177-182.
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 11
    • 0023857935 scopus 로고
    • Correlation of c-erbB-2 gene amplification and protein expression in human breast carcinoma with nodal status and nuclear grading
    • Berger M.S., Locher G.W., Saurer S., Gullick W.J., Waterfield M.D., Groner B., et al. Correlation of c-erbB-2 gene amplification and protein expression in human breast carcinoma with nodal status and nuclear grading. Cancer Res 1988, 48:1238-1243.
    • (1988) Cancer Res , vol.48 , pp. 1238-1243
    • Berger, M.S.1    Locher, G.W.2    Saurer, S.3    Gullick, W.J.4    Waterfield, M.D.5    Groner, B.6
  • 12
    • 0024337144 scopus 로고
    • Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer
    • Slamon D.J., Godolphin W., Jones L.A., Holt J.A., Wong S.G., Keith D.E., et al. Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer. Science 1989, 244:707-712.
    • (1989) Science , vol.244 , pp. 707-712
    • Slamon, D.J.1    Godolphin, W.2    Jones, L.A.3    Holt, J.A.4    Wong, S.G.5    Keith, D.E.6
  • 13
    • 0027012928 scopus 로고
    • C-erbB2 amplification and overexpression in human tumors
    • Lofts F.J., Gullick WJ. c-erbB2 amplification and overexpression in human tumors. Cancer Treat Res 1992, 61:161-179.
    • (1992) Cancer Treat Res , vol.61 , pp. 161-179
    • Lofts, F.J.1    Gullick, W.J.2
  • 14
    • 0026472124 scopus 로고
    • Expression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease
    • Guy C.T., Webster M.A., Schaller M., Parsons T.J., Cardiff R.D., Muller W.J. Expression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease. Proc Natl Acad Sci USA 1992, 89:10578-10582.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10578-10582
    • Guy, C.T.1    Webster, M.A.2    Schaller, M.3    Parsons, T.J.4    Cardiff, R.D.5    Muller, W.J.6
  • 15
    • 44149128380 scopus 로고    scopus 로고
    • The role of ErbB3 and its binding partners in breast cancer progression and resistance to hormone and tyrosine kinase directed therapies
    • Hamburger A.W. The role of ErbB3 and its binding partners in breast cancer progression and resistance to hormone and tyrosine kinase directed therapies. J Mammary Gland Biol Neoplasia 2008, 13:225-233.
    • (2008) J Mammary Gland Biol Neoplasia , vol.13 , pp. 225-233
    • Hamburger, A.W.1
  • 16
    • 67649472398 scopus 로고    scopus 로고
    • Novel anticancer targets: revisiting ERBB2 and discovering ERBB3
    • Baselga J., Swain S.M. Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nat Rev Cancer 2009, 9:463-475.
    • (2009) Nat Rev Cancer , vol.9 , pp. 463-475
    • Baselga, J.1    Swain, S.M.2
  • 17
    • 78449302931 scopus 로고    scopus 로고
    • HER3 comes of age: new insights into its functions and role in signaling, tumor biology, and cancer therapy
    • Campbell M.R., Amin D., Moasser M.M. HER3 comes of age: new insights into its functions and role in signaling, tumor biology, and cancer therapy. Clin Cancer Res 2010, 23:23.
    • (2010) Clin Cancer Res , vol.23 , pp. 23
    • Campbell, M.R.1    Amin, D.2    Moasser, M.M.3
  • 19
    • 0029053716 scopus 로고
    • Cooperative signaling of ErbB3 and ErbB2 in neoplastic transformation and human mammary carcinomas
    • Alimandi M., Romano A., Curia M.C., Muraro R., Fedi P., Aaronson S.A., et al. Cooperative signaling of ErbB3 and ErbB2 in neoplastic transformation and human mammary carcinomas. Oncogene 1995, 10:1813-1821.
    • (1995) Oncogene , vol.10 , pp. 1813-1821
    • Alimandi, M.1    Romano, A.2    Curia, M.C.3    Muraro, R.4    Fedi, P.5    Aaronson, S.A.6
  • 20
    • 0028358856 scopus 로고
    • Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin
    • Sliwkowski M.X., Schaefer G., Akita R.W., Lofgren J.A., Fitzpatrick V.D., Nuijens A., et al. Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J Biol Chem 1994, 269:14661-14665.
    • (1994) J Biol Chem , vol.269 , pp. 14661-14665
    • Sliwkowski, M.X.1    Schaefer, G.2    Akita, R.W.3    Lofgren, J.A.4    Fitzpatrick, V.D.5    Nuijens, A.6
  • 21
    • 0028176477 scopus 로고
    • A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling
    • Carraway K.L.3rd., Cantley L.C. A neu acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell 1994, 78:5-8.
    • (1994) Cell , vol.78 , pp. 5-8
    • Carraway, K.1    Cantley, L.C.2
  • 22
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: the biology of ErbB-2 and ErbB-3
    • Citri A., Skaria K.B., Yarden Y. The deaf and the dumb: the biology of ErbB-2 and ErbB-3. Exp Cell Res 2003, 284:54-65.
    • (2003) Exp Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 23
    • 0028302018 scopus 로고
    • ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor
    • Soltoff S.P., Carraway K.L., Prigent S.A., Gullick W.G., Cantley L.C. ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor. Mol Cell Biol 1994, 14:3550-3558.
    • (1994) Mol Cell Biol , vol.14 , pp. 3550-3558
    • Soltoff, S.P.1    Carraway, K.L.2    Prigent, S.A.3    Gullick, W.G.4    Cantley, L.C.5
  • 24
    • 0028077047 scopus 로고
    • Epidermal growth factor-dependent association of phosphatidylinositol 3-kinase with the erbB3 gene product
    • Kim H.H., Sierke S.L., Koland J.G. Epidermal growth factor-dependent association of phosphatidylinositol 3-kinase with the erbB3 gene product. J Biol Chem 1994, 269:24747-24755.
    • (1994) J Biol Chem , vol.269 , pp. 24747-24755
    • Kim, H.H.1    Sierke, S.L.2    Koland, J.G.3
  • 25
    • 0042307325 scopus 로고    scopus 로고
    • The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation
    • Holbro T., Beerli R.R., Maurer F., Koziczak M., Barbas C.F., Hynes N.E. The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation. Proc Natl Acad Sci USA 2003, 100:8933-8938.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8933-8938
    • Holbro, T.1    Beerli, R.R.2    Maurer, F.3    Koziczak, M.4    Barbas, C.F.5    Hynes, N.E.6
  • 26
    • 48649092620 scopus 로고    scopus 로고
    • A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy
    • Lee-Hoeflich S.T., Crocker L., Yao E., Pham T., Munroe X., Hoeflich K.P., et al. A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy. Cancer Res 2008, 68:5878-5887.
    • (2008) Cancer Res , vol.68 , pp. 5878-5887
    • Lee-Hoeflich, S.T.1    Crocker, L.2    Yao, E.3    Pham, T.4    Munroe, X.5    Hoeflich, K.P.6
  • 27
    • 33846552656 scopus 로고    scopus 로고
    • Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3
    • Sergina N.V., Rausch M., Wang D., Blair J., Hann B., Shokat K.M., et al. Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3. Nature 2007, 445:437-441.
    • (2007) Nature , vol.445 , pp. 437-441
    • Sergina, N.V.1    Rausch, M.2    Wang, D.3    Blair, J.4    Hann, B.5    Shokat, K.M.6
  • 28
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling
    • Engelman J.A., Zejnullahu K., Mitsudomi T., Song Y., Hyland C., Park J.O., et al. MET amplification leads to gefitinib resistance in lung cancer by activating ERBB3 signaling. Science 2007, 316:1039-1043.
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1    Zejnullahu, K.2    Mitsudomi, T.3    Song, Y.4    Hyland, C.5    Park, J.O.6
  • 29
    • 33947202858 scopus 로고    scopus 로고
    • Downregulation of erbB3 abrogates erbB2-mediated tamoxifen resistance in breast cancer cells
    • Liu B., Ordonez-Ercan D., Fan Z., Edgerton S.M., Yang X., Thor A.D. Downregulation of erbB3 abrogates erbB2-mediated tamoxifen resistance in breast cancer cells. Int J Cancer 2007, 120:1874-1882.
    • (2007) Int J Cancer , vol.120 , pp. 1874-1882
    • Liu, B.1    Ordonez-Ercan, D.2    Fan, Z.3    Edgerton, S.M.4    Yang, X.5    Thor, A.D.6
  • 30
    • 33845803144 scopus 로고    scopus 로고
    • Loss of Nrdp1 enhances ErbB2/ErbB3-dependent breast tumor cell growth
    • Yen L., Cao Z., Wu X., Ingalla E.R., Baron C., Young L.J., et al. Loss of Nrdp1 enhances ErbB2/ErbB3-dependent breast tumor cell growth. Cancer Res 2006, 66:11279-11286.
    • (2006) Cancer Res , vol.66 , pp. 11279-11286
    • Yen, L.1    Cao, Z.2    Wu, X.3    Ingalla, E.R.4    Baron, C.5    Young, L.J.6
  • 31
    • 0038575385 scopus 로고    scopus 로고
    • Expression of the HER1-4 family of receptor tyrosine kinases in breast cancer
    • Witton C.J., Reeves J.R., Going J.J., Cooke T.G., Bartlett J.M. Expression of the HER1-4 family of receptor tyrosine kinases in breast cancer. J Pathol 2003, 200:290-297.
    • (2003) J Pathol , vol.200 , pp. 290-297
    • Witton, C.J.1    Reeves, J.R.2    Going, J.J.3    Cooke, T.G.4    Bartlett, J.M.5
  • 33
    • 0031730476 scopus 로고    scopus 로고
    • Expression of c-erbB3 protein in primary breast carcinomas
    • Naidu R., Yadav M., Nair S., Kutty M.K. Expression of c-erbB3 protein in primary breast carcinomas. Br J Cancer 1998, 78:1385-1390.
    • (1998) Br J Cancer , vol.78 , pp. 1385-1390
    • Naidu, R.1    Yadav, M.2    Nair, S.3    Kutty, M.K.4
  • 34
    • 50349090450 scopus 로고    scopus 로고
    • Systems-level analysis of ErbB4 signaling in breast cancer: a laboratory to clinical perspective
    • Chuu C.P., Chen R.Y., Barkinge J.L., Ciaccio M.F., Jones R.B. Systems-level analysis of ErbB4 signaling in breast cancer: a laboratory to clinical perspective. Mol Cancer Res 2008, 6:885-891.
    • (2008) Mol Cancer Res , vol.6 , pp. 885-891
    • Chuu, C.P.1    Chen, R.Y.2    Barkinge, J.L.3    Ciaccio, M.F.4    Jones, R.B.5
  • 36
    • 77950628416 scopus 로고    scopus 로고
    • Mechanisms of resistance to HER family targeting antibodies
    • Kruser T.J., Wheeler D.L. Mechanisms of resistance to HER family targeting antibodies. Exp Cell Res 2010, 316:1083-1100.
    • (2010) Exp Cell Res , vol.316 , pp. 1083-1100
    • Kruser, T.J.1    Wheeler, D.L.2
  • 37
    • 62649175431 scopus 로고    scopus 로고
    • Mechanisms of ErbB receptor negative regulation and relevance in cancer
    • Fry W.H., Kotelawala L., Sweeney C., Carraway K.L. Mechanisms of ErbB receptor negative regulation and relevance in cancer. Exp Cell Res 2009, 315:697-706.
    • (2009) Exp Cell Res , vol.315 , pp. 697-706
    • Fry, W.H.1    Kotelawala, L.2    Sweeney, C.3    Carraway, K.L.4
  • 38
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L., Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 2003, 19:141-172.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 39
    • 54549102284 scopus 로고    scopus 로고
    • Derailed endocytosis: an emerging feature of cancer
    • Mosesson Y., Mills G.B., Yarden Y. Derailed endocytosis: an emerging feature of cancer. Nat Rev Cancer 2008, 8:835-850.
    • (2008) Nat Rev Cancer , vol.8 , pp. 835-850
    • Mosesson, Y.1    Mills, G.B.2    Yarden, Y.3
  • 40
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin A., Goh L.K. Endocytosis and intracellular trafficking of ErbBs. Exp Cell Res 2009, 315:683-696.
    • (2009) Exp Cell Res , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 41
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001, 70:503-533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 42
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies
    • Mogk A., Schmidt R., Bukau B. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol 2007, 17:165-172.
    • (2007) Trends Cell Biol , vol.17 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 43
    • 35548974677 scopus 로고    scopus 로고
    • The mammalian N-end rule pathway: new insights into its components and physiological roles
    • Tasaki T., Kwon Y.T. The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem Sci 2007, 32:520-528.
    • (2007) Trends Biochem Sci , vol.32 , pp. 520-528
    • Tasaki, T.1    Kwon, Y.T.2
  • 44
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell K., Coscoy L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 2005, 309:127-130.
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 45
    • 74049086778 scopus 로고    scopus 로고
    • Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates
    • Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H. Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates. J Cell Biol 2009, 187:655-668.
    • (2009) J Cell Biol , vol.187 , pp. 655-668
    • Wang, X.1    Herr, R.A.2    Rabelink, M.3    Hoeben, R.C.4    Wiertz, E.J.5    Hansen, T.H.6
  • 46
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson Y., Shtiegman K., Katz M., Zwang Y., Vereb G., Szollosi J., et al. Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J Biol Chem 2003, 278:21323-21326.
    • (2003) J Biol Chem , vol.278 , pp. 21323-21326
    • Mosesson, Y.1    Shtiegman, K.2    Katz, M.3    Zwang, Y.4    Vereb, G.5    Szollosi, J.6
  • 47
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund K., Dikic I. Ubiquitylation and cell signaling. EMBO J 2005, 24:3353-3359.
    • (2005) EMBO J , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 48
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs NF-kappaB activation, and TNFalpha-dependent apoptosis
    • Varfolomeev E., Blankenship J.W., Wayson S.M., Fedorova A.V., Kayagaki N., Garg P., et al. IAP antagonists induce autoubiquitination of c-IAPs NF-kappaB activation, and TNFalpha-dependent apoptosis. Cell 2007, 131:669-681.
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3    Fedorova, A.V.4    Kayagaki, N.5    Garg, P.6
  • 49
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • Canning M., Boutell C., Parkinson J., Everett R.D. A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J Biol Chem 2004, 279:38160-38168.
    • (2004) J Biol Chem , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 50
    • 4344646977 scopus 로고    scopus 로고
    • Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8
    • Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8. Mol Cell Biol 2004, 24:7748-7757.
    • (2004) Mol Cell Biol , vol.24 , pp. 7748-7757
    • Wu, X.1    Yen, L.2    Irwin, L.3    Sweeney, C.4    Carraway, K.L.5
  • 51
    • 74849138924 scopus 로고    scopus 로고
    • Regulation of protein stability by GSK3 mediated phosphorylation
    • Xu C., Kim N.G., Gumbiner B.M. Regulation of protein stability by GSK3 mediated phosphorylation. Cell Cycle 2009, 8:4032-4039.
    • (2009) Cell Cycle , vol.8 , pp. 4032-4039
    • Xu, C.1    Kim, N.G.2    Gumbiner, B.M.3
  • 52
    • 70349323592 scopus 로고    scopus 로고
    • Down-regulating destruction: phosphorylation regulates the E3 ubiquitin ligase Nedd4-2
    • Snyder P.M. Down-regulating destruction: phosphorylation regulates the E3 ubiquitin ligase Nedd4-2. Sci Signal 2009, 2.
    • (2009) Sci Signal , vol.2
    • Snyder, P.M.1
  • 53
    • 77952542570 scopus 로고    scopus 로고
    • The regulation of MDM2 by multisite phosphorylation - opportunities for molecular-based intervention to target tumours?
    • Meek D.W., Hupp T.R. The regulation of MDM2 by multisite phosphorylation - opportunities for molecular-based intervention to target tumours?. Semin Cancer Biol 2010, 20:19-28.
    • (2010) Semin Cancer Biol , vol.20 , pp. 19-28
    • Meek, D.W.1    Hupp, T.R.2
  • 54
    • 1342279417 scopus 로고    scopus 로고
    • Regulation of cullin-based ubiquitin ligases by the Nedd8/RUB ubiquitin-like proteins
    • Parry G., Estelle M. Regulation of cullin-based ubiquitin ligases by the Nedd8/RUB ubiquitin-like proteins. Semin Cell Dev Biol 2004, 15:221-229.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 221-229
    • Parry, G.1    Estelle, M.2
  • 55
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O., Felberbaum R., Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 2006, 22:159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 56
    • 44949242505 scopus 로고    scopus 로고
    • Regulation of cullin RING ligases
    • Hotton S.K., Callis J. Regulation of cullin RING ligases. Annu Rev Plant Biol 2008, 59:467-489.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 467-489
    • Hotton, S.K.1    Callis, J.2
  • 57
    • 33750354046 scopus 로고    scopus 로고
    • Parkin and defective ubiquitination in Parkinson's disease
    • Dawson T.M. Parkin and defective ubiquitination in Parkinson's disease. J Neural Transm Suppl 2006, 70:209-213.
    • (2006) J Neural Transm Suppl , vol.70 , pp. 209-213
    • Dawson, T.M.1
  • 58
    • 77953801296 scopus 로고    scopus 로고
    • Genetic determinants at the interface of cancer and neurodegenerative disease
    • Morris L.G., Veeriah S., Chan T.A. Genetic determinants at the interface of cancer and neurodegenerative disease. Oncogene 2010, 29:3453-3464.
    • (2010) Oncogene , vol.29 , pp. 3453-3464
    • Morris, L.G.1    Veeriah, S.2    Chan, T.A.3
  • 59
    • 77955871461 scopus 로고    scopus 로고
    • The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
    • Manfredi J.J. The Mdm2-p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor. Genes Dev 2010, 24:1580-1589.
    • (2010) Genes Dev , vol.24 , pp. 1580-1589
    • Manfredi, J.J.1
  • 60
    • 33751278712 scopus 로고    scopus 로고
    • Cellular functions of the BRCA tumour-suppressor proteins
    • Boulton S.J. Cellular functions of the BRCA tumour-suppressor proteins. Biochem Soc Trans 2006, 34:633-645.
    • (2006) Biochem Soc Trans , vol.34 , pp. 633-645
    • Boulton, S.J.1
  • 61
    • 33750590972 scopus 로고    scopus 로고
    • Genetic and expression aberrations of E3 ubiquitin ligases in human breast cancer
    • Chen C., Seth A.K., Aplin A.E. Genetic and expression aberrations of E3 ubiquitin ligases in human breast cancer. Mol Cancer Res 2006, 4:695-707.
    • (2006) Mol Cancer Res , vol.4 , pp. 695-707
    • Chen, C.1    Seth, A.K.2    Aplin, A.E.3
  • 62
    • 34250863911 scopus 로고    scopus 로고
    • FOXP3 is an X-linked breast cancer suppressor gene and an important repressor of the HER-2/ErbB2 oncogene
    • Zuo T., Wang L., Morrison C., Chang X., Zhang H., Li W., et al. FOXP3 is an X-linked breast cancer suppressor gene and an important repressor of the HER-2/ErbB2 oncogene. Cell 2007, 129:1275-1286.
    • (2007) Cell , vol.129 , pp. 1275-1286
    • Zuo, T.1    Wang, L.2    Morrison, C.3    Chang, X.4    Zhang, H.5    Li, W.6
  • 63
    • 78449287999 scopus 로고    scopus 로고
    • ZNF217, a candidate breast cancer oncogene amplified at 20q13, regulates expression of the ErbB3 receptor tyrosine kinase in breast cancer cells
    • Krig S.R., Miller J.K., Frietze S., Beckett L.A., Neve R.M., Farnham P.J., et al. ZNF217, a candidate breast cancer oncogene amplified at 20q13, regulates expression of the ErbB3 receptor tyrosine kinase in breast cancer cells. Oncogene 2010, 26:26.
    • (2010) Oncogene , vol.26 , pp. 26
    • Krig, S.R.1    Miller, J.K.2    Frietze, S.3    Beckett, L.A.4    Neve, R.M.5    Farnham, P.J.6
  • 66
    • 0027986757 scopus 로고
    • Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors
    • Siegel P.M., Dankort D.L., Hardy W.R., Muller W.J. Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors. Mol Cell Biol 1994, 14:7068-7077.
    • (1994) Mol Cell Biol , vol.14 , pp. 7068-7077
    • Siegel, P.M.1    Dankort, D.L.2    Hardy, W.R.3    Muller, W.J.4
  • 67
    • 0029838204 scopus 로고    scopus 로고
    • Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation
    • Siegel P.M., Muller W.J. Mutations affecting conserved cysteine residues within the extracellular domain of Neu promote receptor dimerization and activation. Proc Natl Acad Sci USA 1996, 93:8878-8883.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8878-8883
    • Siegel, P.M.1    Muller, W.J.2
  • 68
    • 0033561296 scopus 로고    scopus 로고
    • Elevated expression of activated forms of Neu/ErbB-2 and ErbB-3 are involved in the induction of mammary tumors in transgenic mice: implications for human breast cancer
    • Siegel P.M., Ryan E.D., Cardiff R.D., Muller W.J. Elevated expression of activated forms of Neu/ErbB-2 and ErbB-3 are involved in the induction of mammary tumors in transgenic mice: implications for human breast cancer. EMBO J 1999, 18:2149-2164.
    • (1999) EMBO J , vol.18 , pp. 2149-2164
    • Siegel, P.M.1    Ryan, E.D.2    Cardiff, R.D.3    Muller, W.J.4
  • 69
    • 54249104578 scopus 로고    scopus 로고
    • Suppression of the negative regulator LRIG1 contributes to ErbB2 overexpression in breast cancer
    • Miller J.K., Shattuck D.L., Ingalla E.Q., Yen L., Borowsky A.D., Young L.J., et al. Suppression of the negative regulator LRIG1 contributes to ErbB2 overexpression in breast cancer. Cancer Res 2008, 68:8286-8294.
    • (2008) Cancer Res , vol.68 , pp. 8286-8294
    • Miller, J.K.1    Shattuck, D.L.2    Ingalla, E.Q.3    Yen, L.4    Borowsky, A.D.5    Young, L.J.6
  • 70
    • 0035230358 scopus 로고    scopus 로고
    • Regulation of mouse mammary gland development and tumorigenesis by the ERBB signaling network
    • Troyer K.L., Lee D.C. Regulation of mouse mammary gland development and tumorigenesis by the ERBB signaling network. J Mammary Gland Biol Neoplasia 2001, 6:7-21.
    • (2001) J Mammary Gland Biol Neoplasia , vol.6 , pp. 7-21
    • Troyer, K.L.1    Lee, D.C.2
  • 71
    • 44149087535 scopus 로고    scopus 로고
    • ERBB2/HER2 duet in mammary development and breast cancer
    • ERBB3/HER3
    • Stern D.F., ERBB3/HER3 ERBB2/HER2 duet in mammary development and breast cancer. J Mammary Gland Biol Neoplasia 2008, 13:215-223.
    • (2008) J Mammary Gland Biol Neoplasia , vol.13 , pp. 215-223
    • Stern, D.F.1
  • 72
    • 44149120446 scopus 로고    scopus 로고
    • HER4 intracellular domain (4ICD) activity in the developing mammary gland and breast cancer
    • Jones F.E. HER4 intracellular domain (4ICD) activity in the developing mammary gland and breast cancer. J Mammary Gland Biol Neoplasia 2008, 13:247-258.
    • (2008) J Mammary Gland Biol Neoplasia , vol.13 , pp. 247-258
    • Jones, F.E.1
  • 73
    • 0031107224 scopus 로고    scopus 로고
    • Hormonal regulation of type I receptor tyrosine kinase expression in the mammary gland
    • De Bortoli M., Dati C. Hormonal regulation of type I receptor tyrosine kinase expression in the mammary gland. J Mammary Gland Biol Neoplasia 1997, 2:175-185.
    • (1997) J Mammary Gland Biol Neoplasia , vol.2 , pp. 175-185
    • De Bortoli, M.1    Dati, C.2
  • 75
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang F., Kirkpatrick D., Jiang X., Gygi S., Sorkin A. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell 2006, 21:737-748.
    • (2006) Mol Cell , vol.21 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 76
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: many adaptations to regulate protein tyrosine kinases
    • Thien C.B., Langdon W.Y. Cbl: many adaptations to regulate protein tyrosine kinases. Nat Rev Mol Cell Biol 2001, 2:294-307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 77
    • 0032217156 scopus 로고    scopus 로고
    • C-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz G., Waterman H., Zamir E., Kam Z., Oved S., Langdon W.Y., et al. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev 1998, 12:3663-3674.
    • (1998) Genes Dev , vol.12 , pp. 3663-3674
    • Levkowitz, G.1    Waterman, H.2    Zamir, E.3    Kam, Z.4    Oved, S.5    Langdon, W.Y.6
  • 78
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz G., Waterman H., Ettenberg S.A., Katz M., Tsygankov A.Y., Alroy I., et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 1999, 4:1029-1040.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1    Waterman, H.2    Ettenberg, S.A.3    Katz, M.4    Tsygankov, A.Y.5    Alroy, I.6
  • 79
    • 0034614652 scopus 로고    scopus 로고
    • The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor
    • Lill N.L., Douillard P., Awwad R.A., Ota S., Lupher M.L., Miyake S., et al. The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor. J Biol Chem 2000, 275:367-377.
    • (2000) J Biol Chem , vol.275 , pp. 367-377
    • Lill, N.L.1    Douillard, P.2    Awwad, R.A.3    Ota, S.4    Lupher, M.L.5    Miyake, S.6
  • 80
    • 0029917264 scopus 로고    scopus 로고
    • Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins
    • Levkowitz G., Klapper L.N., Tzahar E., Freywald A., Sela M., Yarden Y. Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins. Oncogene 1996, 12:1117-1125.
    • (1996) Oncogene , vol.12 , pp. 1117-1125
    • Levkowitz, G.1    Klapper, L.N.2    Tzahar, E.3    Freywald, A.4    Sela, M.5    Yarden, Y.6
  • 81
    • 0034234854 scopus 로고    scopus 로고
    • Tumor-inhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2
    • Klapper L.N., Waterman H., Sela M., Yarden Y. Tumor-inhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2. Cancer Res 2000, 60:3384-3388.
    • (2000) Cancer Res , vol.60 , pp. 3384-3388
    • Klapper, L.N.1    Waterman, H.2    Sela, M.3    Yarden, Y.4
  • 83
    • 34548759165 scopus 로고    scopus 로고
    • Degradation of HER2 by Cbl-based chimeric ubiquitin ligases
    • Li X., Shen L., Zhang J., Su J., Liu X., Han H., et al. Degradation of HER2 by Cbl-based chimeric ubiquitin ligases. Cancer Res 2007, 67:8716-8724.
    • (2007) Cancer Res , vol.67 , pp. 8716-8724
    • Li, X.1    Shen, L.2    Zhang, J.3    Su, J.4    Liu, X.5    Han, H.6
  • 85
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida J., Kraus M.H., Alimandi M., Di Fiore P.P., Carpenter G. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J Biol Chem 1996, 271:5251-5257.
    • (1996) J Biol Chem , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 86
    • 33947245587 scopus 로고    scopus 로고
    • 3rd. Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1
    • Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. 3rd. Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1. Mol Cell Biol 2007, 27:2180-2188.
    • (2007) Mol Cell Biol , vol.27 , pp. 2180-2188
    • Cao, Z.1    Wu, X.2    Yen, L.3    Sweeney, C.4    Carraway, K.L.5
  • 88
    • 30444452500 scopus 로고    scopus 로고
    • TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases
    • Meroni G., Diez-Roux G. TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases. Bioessays 2005, 27:1147-1157.
    • (2005) Bioessays , vol.27 , pp. 1147-1157
    • Meroni, G.1    Diez-Roux, G.2
  • 89
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov G.V., Walker J.R., Xue S., Finerty P.J., Mackenzie F., Newman E.M., et al. Amino-terminal dimerization NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J Biol Chem 2006, 281:38061-38070.
    • (2006) J Biol Chem , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6
  • 90
    • 33947723002 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3
    • Bouyain S., Leahy D.J. Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3. Protein Sci 2007, 16:654-661.
    • (2007) Protein Sci , vol.16 , pp. 654-661
    • Bouyain, S.1    Leahy, D.J.2
  • 91
    • 0037069388 scopus 로고    scopus 로고
    • Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3
    • Qiu X.B., Goldberg A.L. Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3. Proc Natl Acad Sci USA 2002, 99:14843-14848.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14843-14848
    • Qiu, X.B.1    Goldberg, A.L.2
  • 92
    • 77956508416 scopus 로고    scopus 로고
    • Post-transcriptional mechanisms contribute to the suppression of the ErbB3 negative regulator protein Nrdp1 in mammary tumors
    • Ingalla E.Q., Miller J.K., Wald J.H., Workman H.C., Kaur R.P., Yen L., et al. Post-transcriptional mechanisms contribute to the suppression of the ErbB3 negative regulator protein Nrdp1 in mammary tumors. J Biol Chem 2010, 285:28691-28697.
    • (2010) J Biol Chem , vol.285 , pp. 28691-28697
    • Ingalla, E.Q.1    Miller, J.K.2    Wald, J.H.3    Workman, H.C.4    Kaur, R.P.5    Yen, L.6
  • 94
    • 62649171270 scopus 로고    scopus 로고
    • The role of protease activity in ErbB biology
    • Blobel C.P., Carpenter G., Freeman M. The role of protease activity in ErbB biology. Exp Cell Res 2009, 315:671-682.
    • (2009) Exp Cell Res , vol.315 , pp. 671-682
    • Blobel, C.P.1    Carpenter, G.2    Freeman, M.3
  • 95
    • 0035824391 scopus 로고    scopus 로고
    • Gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni C.Y., Murphy M.P., Golde T.E., Carpenter G. gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 2001, 294:2179-2181.
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 97
    • 0034708598 scopus 로고    scopus 로고
    • A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis
    • Kainulainen V., Sundvall M., Maatta J.A., Santiestevan E., Klagsbrun M., Elenius K. A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis. J Biol Chem 2000, 275:8641-8649.
    • (2000) J Biol Chem , vol.275 , pp. 8641-8649
    • Kainulainen, V.1    Sundvall, M.2    Maatta, J.A.3    Santiestevan, E.4    Klagsbrun, M.5    Elenius, K.6
  • 98
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 2009, 10:398-409.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 100
    • 54249139553 scopus 로고    scopus 로고
    • Role of the UPS in Liddle syndrome
    • Rotin D. Role of the UPS in Liddle syndrome. BMC Biochem 2008, 21.
    • (2008) BMC Biochem , vol.21
    • Rotin, D.1
  • 102
    • 59249091294 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradation
    • Feng S.M., Muraoka-Cook R.S., Hunter D., Sandahl M.A., Caskey L.S., Miyazawa K., et al. The E3 ubiquitin ligase WWP1 selectively targets HER4 and its proteolytically derived signaling isoforms for degradation. Mol Cell Biol 2009, 29:892-906.
    • (2009) Mol Cell Biol , vol.29 , pp. 892-906
    • Feng, S.M.1    Muraoka-Cook, R.S.2    Hunter, D.3    Sandahl, M.A.4    Caskey, L.S.5    Miyazawa, K.6
  • 103
    • 69249218913 scopus 로고    scopus 로고
    • WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer
    • Li Y., Zhou Z., Alimandi M., Chen C. WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer. Oncogene 2009, 28:2948-2958.
    • (2009) Oncogene , vol.28 , pp. 2948-2958
    • Li, Y.1    Zhou, Z.2    Alimandi, M.3    Chen, C.4
  • 104
    • 67649311930 scopus 로고    scopus 로고
    • Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells
    • Zeng F., Xu J., Harris R.C. Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells. FASEB J 2009, 23:1935-1945.
    • (2009) FASEB J , vol.23 , pp. 1935-1945
    • Zeng, F.1    Xu, J.2    Harris, R.C.3
  • 105
    • 34547130074 scopus 로고    scopus 로고
    • HER4 D-box sequences regulate mitotic progression and degradation of the nuclear HER4 cleavage product s80HER4
    • Strunk K.E., Husted C., Miraglia L.C., Sandahl M., Rearick W.A., Hunter D.M., et al. HER4 D-box sequences regulate mitotic progression and degradation of the nuclear HER4 cleavage product s80HER4. Cancer Res 2007, 67:6582-6590.
    • (2007) Cancer Res , vol.67 , pp. 6582-6590
    • Strunk, K.E.1    Husted, C.2    Miraglia, L.C.3    Sandahl, M.4    Rearick, W.A.5    Hunter, D.M.6
  • 106
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: a specialized but essential protein-folding tool
    • Young J.C., Moarefi I., Hartl F.U. Hsp90: a specialized but essential protein-folding tool. J Cell Biol 2001, 154:267-273.
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 108
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L., Lindquist S.L. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005, 5:761-772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 109
    • 0028304022 scopus 로고
    • Accelerated degradation of 160kDa epidermal growth factor (EGF) receptor precursor by the tyrosine kinase inhibitor herbimycin A in the endoplasmic reticulum of A431 human epidermoid carcinoma cells
    • Murakami Y., Mizuno S., Uehara Y. Accelerated degradation of 160kDa epidermal growth factor (EGF) receptor precursor by the tyrosine kinase inhibitor herbimycin A in the endoplasmic reticulum of A431 human epidermoid carcinoma cells. Biochem J 1994, 301:63-68.
    • (1994) Biochem J , vol.301 , pp. 63-68
    • Murakami, Y.1    Mizuno, S.2    Uehara, Y.3
  • 110
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh E.G., Chavany C., Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996, 271:22796-22801.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 111
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu W., Marcu M., Yuan X., Mimnaugh E., Patterson C., Neckers L. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc Natl Acad Sci USA 2002, 99:12847-12852.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 112
    • 77955713474 scopus 로고    scopus 로고
    • Geldanamycin selectively targets the nascent form of ERBB3 for degradation
    • Gerbin C.S., Landgraf R. Geldanamycin selectively targets the nascent form of ERBB3 for degradation. Cell Stress Chaperones 2010, 15:529-544.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 529-544
    • Gerbin, C.S.1    Landgraf, R.2
  • 113


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