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Volumn 51, Issue 1, 2015, Pages 1-9

E3 ubiquitin ligases as drug targets and prognostic biomarkers in melanoma

Author keywords

F box proteins; Melanoma; RING proteins; SCF E3 ligases; Ubiquitin ligases

Indexed keywords

ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; F BOX PROTEIN; TUMOR MARKER; UBIQUITIN PROTEIN LIGASE;

EID: 84940041307     PISSN: 1010660X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.medici.2015.01.007     Document Type: Review
Times cited : (53)

References (84)
  • 2
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P., Duong D.M., Seyfried N.T., Cheng D., Xie Y., Robert J., et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009, 137:133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6
  • 3
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu Y., Okuda-Shimizu Y., Hendershot L.M. Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol Cell 2010, 40:917-926.
    • (2010) Mol Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 4
    • 84875523289 scopus 로고    scopus 로고
    • Ubiquitinations in the Notch signaling pathway
    • Moretti J., Brou Ch. Ubiquitinations in the Notch signaling pathway. Int J Mol Sci 2013, 14:6359-6381.
    • (2013) Int J Mol Sci , vol.14 , pp. 6359-6381
    • Moretti, J.1    Brou, C.2
  • 6
    • 77952571560 scopus 로고    scopus 로고
    • Growth and progression of melanoma and non-melanoma skin cancers regulated by ubiquitination
    • Nakayama K. Growth and progression of melanoma and non-melanoma skin cancers regulated by ubiquitination. Pigment Cell Melanoma Res 2010, 23:338-351.
    • (2010) Pigment Cell Melanoma Res , vol.23 , pp. 338-351
    • Nakayama, K.1
  • 7
    • 80052069445 scopus 로고    scopus 로고
    • RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis
    • Lipkowitz S., Weissman A.M. RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis. Nat Rev Cancer 2011, 11:629-644.
    • (2011) Nat Rev Cancer , vol.11 , pp. 629-644
    • Lipkowitz, S.1    Weissman, A.M.2
  • 8
    • 84874886341 scopus 로고    scopus 로고
    • Functional characterization of SAG/RBX2/ROC2/RNF7, an antioxidant protein and an E3 ubiquitin ligase
    • Sun Y., Li H. Functional characterization of SAG/RBX2/ROC2/RNF7, an antioxidant protein and an E3 ubiquitin ligase. Protein Cell 2013, 4(2):103-116.
    • (2013) Protein Cell , vol.4 , Issue.2 , pp. 103-116
    • Sun, Y.1    Li, H.2
  • 9
    • 84858135252 scopus 로고    scopus 로고
    • Following Ariadne's thread: a new perspective on RBR ubiquitin ligases
    • Wenzel D.M., Klevit R.E. Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol 2012, 10:24.
    • (2012) BMC Biol , vol.10 , pp. 24
    • Wenzel, D.M.1    Klevit, R.E.2
  • 10
    • 84879525973 scopus 로고    scopus 로고
    • Macromolecular juggling by ubiquitylation enzymes
    • Lorenz S., Cantor A.J., Rape M., Kuriyan J. Macromolecular juggling by ubiquitylation enzymes. BMC Biol 2013, 11:65.
    • (2013) BMC Biol , vol.11 , pp. 65
    • Lorenz, S.1    Cantor, A.J.2    Rape, M.3    Kuriyan, J.4
  • 12
    • 84875498138 scopus 로고    scopus 로고
    • Role of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases in skin cancer
    • Xie C., Wei W., Sun Y. Role of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases in skin cancer. J Genet Genomics 2013, 40:97e106.
    • (2013) J Genet Genomics , vol.40 , pp. 97e106
    • Xie, C.1    Wei, W.2    Sun, Y.3
  • 13
    • 1942502180 scopus 로고    scopus 로고
    • The many faces of beta-TrCP E3 ubiquitin ligases: reflections in the magic mirror of cancer
    • Fuchs S.Y., Spiegelman V.S., Kumar K.G. The many faces of beta-TrCP E3 ubiquitin ligases: reflections in the magic mirror of cancer. Oncogene 2004, 23:2028-2036.
    • (2004) Oncogene , vol.23 , pp. 2028-2036
    • Fuchs, S.Y.1    Spiegelman, V.S.2    Kumar, K.G.3
  • 14
    • 84886087051 scopus 로고    scopus 로고
    • Clinical characteristics and outcomes with specific BRAF and NRAS mutations in patients with metastatic melanoma
    • Bucheit A.D., Syklawer E., Jakob J.A., Bassett R.L., Curry J.L., Gershenwald J.E., et al. Clinical characteristics and outcomes with specific BRAF and NRAS mutations in patients with metastatic melanoma. Cancer 2013, 119(21):3821-3829.
    • (2013) Cancer , vol.119 , Issue.21 , pp. 3821-3829
    • Bucheit, A.D.1    Syklawer, E.2    Jakob, J.A.3    Bassett, R.L.4    Curry, J.L.5    Gershenwald, J.E.6
  • 15
    • 71549119163 scopus 로고    scopus 로고
    • P27-Associated G1 arrest induced by hinokitiol in human malignant melanoma cells is mediated via down-regulation of pRb, Skp2 ubiquitin ligase, and impairment of Cdk2 function
    • Liu S., Yamauchi H. p27-Associated G1 arrest induced by hinokitiol in human malignant melanoma cells is mediated via down-regulation of pRb, Skp2 ubiquitin ligase, and impairment of Cdk2 function. Cancer Lett 2009, 286:240-249.
    • (2009) Cancer Lett , vol.286 , pp. 240-249
    • Liu, S.1    Yamauchi, H.2
  • 16
    • 79960885211 scopus 로고    scopus 로고
    • Silymarin targets beta catenin signaling in blocking migration/invasion of human melanoma cells
    • Vaid M., Prasad R., Sun Q., Katiyar S.K. Silymarin targets beta catenin signaling in blocking migration/invasion of human melanoma cells. PLoS ONE 2011, 6:e23000.
    • (2011) PLoS ONE , vol.6 , pp. e23000
    • Vaid, M.1    Prasad, R.2    Sun, Q.3    Katiyar, S.K.4
  • 17
    • 41149141967 scopus 로고    scopus 로고
    • Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer
    • Hershko D.D. Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer. Cancer 2008, 112:1415-1424.
    • (2008) Cancer , vol.112 , pp. 1415-1424
    • Hershko, D.D.1
  • 18
    • 84871569969 scopus 로고    scopus 로고
    • Specific small molecule inhibitors of Skp2-mediated p27
    • Wu L., Grigoryan A., Li Y., Hao B., Pagano M., Cardozo T. Specific small molecule inhibitors of Skp2-mediated p27. Chem Biol 2012, 19(12):1515-1524.
    • (2012) Chem Biol , vol.19 , Issue.12 , pp. 1515-1524
    • Wu, L.1    Grigoryan, A.2    Li, Y.3    Hao, B.4    Pagano, M.5    Cardozo, T.6
  • 19
    • 79952229159 scopus 로고    scopus 로고
    • Cytoplasmic Skp2 expression is increased in human melanoma and correlated with patient survival
    • PMID: 21386910
    • Chen G., Cheng Y., Martinka M., Li G. Cytoplasmic Skp2 expression is increased in human melanoma and correlated with patient survival. PLoS ONE 2011, 6(2):e17578. PMID: 21386910.
    • (2011) PLoS ONE , vol.6 , Issue.2 , pp. e17578
    • Chen, G.1    Cheng, Y.2    Martinka, M.3    Li, G.4
  • 20
    • 7444234290 scopus 로고    scopus 로고
    • Skp2 and p27 kip1 expression in melanocytic nevi and melanoma: an inverse relationship
    • Li Q., Murphy M., Ross J., Sheehan C., Carlson J.A. Skp2 and p27 kip1 expression in melanocytic nevi and melanoma: an inverse relationship. J Cutan Pathol 2004, 31:633-642.
    • (2004) J Cutan Pathol , vol.31 , pp. 633-642
    • Li, Q.1    Murphy, M.2    Ross, J.3    Sheehan, C.4    Carlson, J.A.5
  • 22
    • 28844433551 scopus 로고    scopus 로고
    • Effective inhibition of cell growth and invasion of melanoma by combined suppression of BRAF (V599E) and Skp2 with lentiviral RNAi
    • Sumimoto H., Hirata K., Yamagata S., Miyoshi H., Miyagishi M., Taira K., et al. Effective inhibition of cell growth and invasion of melanoma by combined suppression of BRAF (V599E) and Skp2 with lentiviral RNAi. Int J Cancer 2006, 118:472-476.
    • (2006) Int J Cancer , vol.118 , pp. 472-476
    • Sumimoto, H.1    Hirata, K.2    Yamagata, S.3    Miyoshi, H.4    Miyagishi, M.5    Taira, K.6
  • 23
    • 78650383624 scopus 로고    scopus 로고
    • Chemical genetics approach to restoring p27Kip1 reveals novel compounds with antiproliferative activity in prostate cancer cells
    • Rico-Bautista E., Yang C.C., Lu L., Roth G.P., Wolf D.A. Chemical genetics approach to restoring p27Kip1 reveals novel compounds with antiproliferative activity in prostate cancer cells. BMC Biol 2010, 8:153.
    • (2010) BMC Biol , vol.8 , pp. 153
    • Rico-Bautista, E.1    Yang, C.C.2    Lu, L.3    Roth, G.P.4    Wolf, D.A.5
  • 24
    • 84891041882 scopus 로고    scopus 로고
    • A signal transduction pathway from TGF-β1 to SKP2 via Akt1 and c-Myc and its correlation with progression in human melanoma
    • Qu X., Shen L., Zheng Y., Cui Y., Feng Z., Liuand F., et al. A signal transduction pathway from TGF-β1 to SKP2 via Akt1 and c-Myc and its correlation with progression in human melanoma. J Invest Dermatol 2014, 134:159-167.
    • (2014) J Invest Dermatol , vol.134 , pp. 159-167
    • Qu, X.1    Shen, L.2    Zheng, Y.3    Cui, Y.4    Feng, Z.5    Liuand, F.6
  • 25
    • 85028121020 scopus 로고    scopus 로고
    • Role of the ubiquitin ligase Fbw7 in cancer progression
    • Cheng Y., Li G. Role of the ubiquitin ligase Fbw7 in cancer progression. Cancer Metastasis Rev 2012, 31:75-87.
    • (2012) Cancer Metastasis Rev , vol.31 , pp. 75-87
    • Cheng, Y.1    Li, G.2
  • 26
    • 84859430011 scopus 로고    scopus 로고
    • Fbxw7a- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma
    • Busino L., Millman S.E., Scotto L., Kyratsous C.A., Basrur V., O'Connor O., et al. Fbxw7a- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma. Nat Cell Biol 2012, 14(4):375-385.
    • (2012) Nat Cell Biol , vol.14 , Issue.4 , pp. 375-385
    • Busino, L.1    Millman, S.E.2    Scotto, L.3    Kyratsous, C.A.4    Basrur, V.5    O'Connor, O.6
  • 27
    • 84861189396 scopus 로고    scopus 로고
    • Tumor suppressor functions of FBW7 in cancer development and progression
    • Wang Z., Inuzuka H., Zhong J., Wan L., Fukushima H., Sarkar F., et al. Tumor suppressor functions of FBW7 in cancer development and progression. FEBS Lett 2012, 586:1409-1418.
    • (2012) FEBS Lett , vol.586 , pp. 1409-1418
    • Wang, Z.1    Inuzuka, H.2    Zhong, J.3    Wan, L.4    Fukushima, H.5    Sarkar, F.6
  • 28
    • 84877107994 scopus 로고    scopus 로고
    • Genetically engineered mouse models for functional studies
    • Zhou W., Wei W., Sun Y. Genetically engineered mouse models for functional studies. Cell Res 2013, 23:599-619.
    • (2013) Cell Res , vol.23 , pp. 599-619
    • Zhou, W.1    Wei, W.2    Sun, Y.3
  • 29
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase a tumour suppressor at the crossroads of cell division, growth and differentiation
    • Welcker M., Clurman B. FBW7 ubiquitin ligase a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat Rev Cancer 2008, 8:83-93.
    • (2008) Nat Rev Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.2
  • 30
    • 84871902443 scopus 로고    scopus 로고
    • Fbw7α and Fbw7γ collaborate to shuttle cyclin E1 into the nucleolus for multiubiquitylation
    • Bhaskaran N., van Drogen F., Ng H.F., Kumar R., Ekholm-Reed S., Peter M., et al. Fbw7α and Fbw7γ collaborate to shuttle cyclin E1 into the nucleolus for multiubiquitylation. Mol Cell Biol 2013, 33(1):85-97.
    • (2013) Mol Cell Biol , vol.33 , Issue.1 , pp. 85-97
    • Bhaskaran, N.1    van Drogen, F.2    Ng, H.F.3    Kumar, R.4    Ekholm-Reed, S.5    Peter, M.6
  • 32
    • 53049097854 scopus 로고    scopus 로고
    • The Fbxw7/hCdc4 tumor suppressor in human cancer
    • Tan Y., Sangfelt O., Spruck C. The Fbxw7/hCdc4 tumor suppressor in human cancer. Cancer Lett 2008, 271:1-12.
    • (2008) Cancer Lett , vol.271 , pp. 1-12
    • Tan, Y.1    Sangfelt, O.2    Spruck, C.3
  • 33
    • 84876157836 scopus 로고    scopus 로고
    • Opposing functions of Fbxw7 in keratinocyte growth, differentiation and skin tumorigenesis mediated through negative regulation of c-Myc and Notch
    • Ishikawa Y., Hosogane M., Okuyama R., Aoyama S., Onoyama I., Nakayama K.I., et al. Opposing functions of Fbxw7 in keratinocyte growth, differentiation and skin tumorigenesis mediated through negative regulation of c-Myc and Notch. Oncogene 2013, 32(15):1921-1932.
    • (2013) Oncogene , vol.32 , Issue.15 , pp. 1921-1932
    • Ishikawa, Y.1    Hosogane, M.2    Okuyama, R.3    Aoyama, S.4    Onoyama, I.5    Nakayama, K.I.6
  • 34
    • 34547780475 scopus 로고    scopus 로고
    • FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to γ-secretase inhibitors
    • O'Neil J., Grim J., Strack P., Rao S., Tibbitts D., Winter Ch., et al. FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to γ-secretase inhibitors. J Exp Med 2007, 204(8):1813-1824.
    • (2007) J Exp Med , vol.204 , Issue.8 , pp. 1813-1824
    • O'Neil, J.1    Grim, J.2    Strack, P.3    Rao, S.4    Tibbitts, D.5    Winter, C.6
  • 35
    • 79959923295 scopus 로고    scopus 로고
    • MiRNA-27a controls FBW7/hCDC4-dependent cyclin E degradation and cell cycle progression
    • Lerner M., Lundgren J., Akhoondi S., Jahn A., Ng H.F., Moqadam F.A., et al. MiRNA-27a controls FBW7/hCDC4-dependent cyclin E degradation and cell cycle progression. Cell Cycle 2011, 10:2172-2183.
    • (2011) Cell Cycle , vol.10 , pp. 2172-2183
    • Lerner, M.1    Lundgren, J.2    Akhoondi, S.3    Jahn, A.4    Ng, H.F.5    Moqadam, F.A.6
  • 36
    • 84879420289 scopus 로고    scopus 로고
    • Prognostic significance of Fbw7 in human melanoma and its role in cell migration
    • Cheng Y., Chen G., Martinka M., Ho V., Li G. Prognostic significance of Fbw7 in human melanoma and its role in cell migration. J Invest Dermatol 2013, 133(7):1794-1802.
    • (2013) J Invest Dermatol , vol.133 , Issue.7 , pp. 1794-1802
    • Cheng, Y.1    Chen, G.2    Martinka, M.3    Ho, V.4    Li, G.5
  • 37
    • 79952002262 scopus 로고    scopus 로고
    • Prognostic significance of BRMS1 expression in human melanoma and its role in tumor angiogenesis
    • Li J., Cheng Y., Tai D., Martinka M., Welch D.R., Li G. Prognostic significance of BRMS1 expression in human melanoma and its role in tumor angiogenesis. Oncogene 2011, 30:896-906.
    • (2011) Oncogene , vol.30 , pp. 896-906
    • Li, J.1    Cheng, Y.2    Tai, D.3    Martinka, M.4    Welch, D.R.5    Li, G.6
  • 38
    • 84862731787 scopus 로고    scopus 로고
    • Triggering Fbw7-mediated proteasomal degradation of c-Myc by oridonin induces cell growth inhibition and apoptosis
    • Huang H.L., Weng H.Y., Wang L.Q., Yu C.H., Huang Q.J., Zhao P.P., et al. Triggering Fbw7-mediated proteasomal degradation of c-Myc by oridonin induces cell growth inhibition and apoptosis. Mol Cancer Ther 2012, 11(5):1155-1165.
    • (2012) Mol Cancer Ther , vol.11 , Issue.5 , pp. 1155-1165
    • Huang, H.L.1    Weng, H.Y.2    Wang, L.Q.3    Yu, C.H.4    Huang, Q.J.5    Zhao, P.P.6
  • 39
    • 84869093164 scopus 로고    scopus 로고
    • Functional analysis and consequences of Mdm2 E3 ligase
    • Wade M., Li Y., Matani A., Braun S., Milanesi F., Rodewald L., et al. Functional analysis and consequences of Mdm2 E3 ligase. Oncogene 2012, 31(45):4789-4797.
    • (2012) Oncogene , vol.31 , Issue.45 , pp. 4789-4797
    • Wade, M.1    Li, Y.2    Matani, A.3    Braun, S.4    Milanesi, F.5    Rodewald, L.6
  • 40
    • 33845901313 scopus 로고    scopus 로고
    • MDM2 inhibitors for cancer therapy
    • Vassilev L.T. MDM2 inhibitors for cancer therapy. Trends Mol Med 2006, 13(1):23-30.
    • (2006) Trends Mol Med , vol.13 , Issue.1 , pp. 23-30
    • Vassilev, L.T.1
  • 41
    • 84873055344 scopus 로고    scopus 로고
    • MDM2, MDMX and p53 in oncogenesis and cancer therapy
    • Wade M., Li Y.-Ch., Wahl G.M. MDM2, MDMX and p53 in oncogenesis and cancer therapy. Nat Rev Cancer 2013, 13:83-96.
    • (2013) Nat Rev Cancer , vol.13 , pp. 83-96
    • Wade, M.1    Li, Y.-C.2    Wahl, G.M.3
  • 42
    • 84893274453 scopus 로고    scopus 로고
    • Targeting MDM2-p53 interaction for cancer therapy: are we there yet?
    • Nag S., Zhang X., Srivenugopal K.S., Wang M.H., Wang W., Zhang R. Targeting MDM2-p53 interaction for cancer therapy: are we there yet?. Curr Med Chem 2014, 21(5):553-574.
    • (2014) Curr Med Chem , vol.21 , Issue.5 , pp. 553-574
    • Nag, S.1    Zhang, X.2    Srivenugopal, K.S.3    Wang, M.H.4    Wang, W.5    Zhang, R.6
  • 43
    • 84891763776 scopus 로고    scopus 로고
    • Regulation of Mdm2 protein stability and the p53 response by NEDD4-1 E3 ligase
    • Xu C., Fan C.D., Wang X. Regulation of Mdm2 protein stability and the p53 response by NEDD4-1 E3 ligase. Oncogene 2015, 34(3):281-289.
    • (2015) Oncogene , vol.34 , Issue.3 , pp. 281-289
    • Xu, C.1    Fan, C.D.2    Wang, X.3
  • 44
    • 2642559887 scopus 로고    scopus 로고
    • Targeting E3 ubiquitin ligases for cancer therapy
    • Sun Y. Targeting E3 ubiquitin ligases for cancer therapy. Cancer Biol Ther 2003, 2(6):623-629.
    • (2003) Cancer Biol Ther , vol.2 , Issue.6 , pp. 623-629
    • Sun, Y.1
  • 45
    • 84855921054 scopus 로고    scopus 로고
    • P53 rescue through HDM2 antagonism suppresses melanoma growth and potentiates MEK inhibition
    • Ji Z., Njauw Ch.N., Taylor M., Neel V., Flaherty K.T., Tsao H. p53 rescue through HDM2 antagonism suppresses melanoma growth and potentiates MEK inhibition. J Invest Dermatol 2012, 132:356-364.
    • (2012) J Invest Dermatol , vol.132 , pp. 356-364
    • Ji, Z.1    Njauw, C.N.2    Taylor, M.3    Neel, V.4    Flaherty, K.T.5    Tsao, H.6
  • 46
    • 84874638103 scopus 로고    scopus 로고
    • Non-degradative ubiquitination of the Notch1 receptor by the E3 ligase MDM2 activates the Notch signaling pathway
    • Pettersson S., Sczaniecka M., McLaren L., Russel F., Gladstone K., Hupp T., et al. Non-degradative ubiquitination of the Notch1 receptor by the E3 ligase MDM2 activates the Notch signaling pathway. Biochem J 2013, 450(3):523-536.
    • (2013) Biochem J , vol.450 , Issue.3 , pp. 523-536
    • Pettersson, S.1    Sczaniecka, M.2    McLaren, L.3    Russel, F.4    Gladstone, K.5    Hupp, T.6
  • 49
    • 84859997937 scopus 로고    scopus 로고
    • MDM2 protein-mediated ubiquitination of NUMB protein identification of a second physiological substrate of MDM2 that employs a dual-site docking mechanism
    • Sczaniecka M., Gladstone K., Pettersson S., McLaren L., Huart A.S., Wallace M. MDM2 protein-mediated ubiquitination of NUMB protein identification of a second physiological substrate of MDM2 that employs a dual-site docking mechanism. Biol Chem 2012, 287(17):14052-14068.
    • (2012) Biol Chem , vol.287 , Issue.17 , pp. 14052-14068
    • Sczaniecka, M.1    Gladstone, K.2    Pettersson, S.3    McLaren, L.4    Huart, A.S.5    Wallace, M.6
  • 50
    • 84871980628 scopus 로고    scopus 로고
    • Molecular pathways: targeting Mdm2 and Mdm4 in cancer therapy
    • Li Q., Lozano G. Molecular pathways: targeting Mdm2 and Mdm4 in cancer therapy. Clin Cancer Res 2012, 19(1):1-8.
    • (2012) Clin Cancer Res , vol.19 , Issue.1 , pp. 1-8
    • Li, Q.1    Lozano, G.2
  • 52
    • 33748521536 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as cancer targets and biomarkers
    • Sun Y. E3 ubiquitin ligases as cancer targets and biomarkers. Neoplasia 2006, 8(8):645-654.
    • (2006) Neoplasia , vol.8 , Issue.8 , pp. 645-654
    • Sun, Y.1
  • 53
    • 84862665721 scopus 로고    scopus 로고
    • The relationship between MDM2 expression and tumor thickness and invasion in primary cutaneous malignant melanoma
    • Rajabi P., Karimian P., Heidarpour M. The relationship between MDM2 expression and tumor thickness and invasion in primary cutaneous malignant melanoma. J Res Med Sci 2012, 7(5):452-455.
    • (2012) J Res Med Sci , vol.7 , Issue.5 , pp. 452-455
    • Rajabi, P.1    Karimian, P.2    Heidarpour, M.3
  • 54
    • 84859506935 scopus 로고    scopus 로고
    • Notch signaling and malignant melanoma
    • Müller C.S. Notch signaling and malignant melanoma. Adv Exp Med Biol 2012, 727:258-264.
    • (2012) Adv Exp Med Biol , vol.727 , pp. 258-264
    • Müller, C.S.1
  • 55
    • 84874995996 scopus 로고    scopus 로고
    • Cullin-RING ligases as attractive anti-cancer targets
    • Zhao Y., Sun Y. Cullin-RING ligases as attractive anti-cancer targets. Curr Pharm Des 2013, 19(18):3215-3225.
    • (2013) Curr Pharm Des , vol.19 , Issue.18 , pp. 3215-3225
    • Zhao, Y.1    Sun, Y.2
  • 56
    • 32444449180 scopus 로고    scopus 로고
    • Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy
    • Tovar Ch., Rosinski J., Filipovic Z., Higgins B., Kolinsky K., Hilton H., et al. Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy. PNAS 2006, 103(6):1888-1893.
    • (2006) PNAS , vol.103 , Issue.6 , pp. 1888-1893
    • Tovar, C.1    Rosinski, J.2    Filipovic, Z.3    Higgins, B.4    Kolinsky, K.5    Hilton, H.6
  • 57
    • 20444369867 scopus 로고    scopus 로고
    • Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
    • Yang Y., Ludwig R.L., Jensen J.P., Pierre S.A., Medaglia M.V., Davydov I.V., et al. Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell 2005, 7:547-559.
    • (2005) Cancer Cell , vol.7 , pp. 547-559
    • Yang, Y.1    Ludwig, R.L.2    Jensen, J.P.3    Pierre, S.A.4    Medaglia, M.V.5    Davydov, I.V.6
  • 58
    • 78449232165 scopus 로고    scopus 로고
    • Targeting the MDM2-p53 interaction as a therapeutic strategy for the treatment of cancer
    • Peirce S.K., Findley H.W. Targeting the MDM2-p53 interaction as a therapeutic strategy for the treatment of cancer. Cell Health Cytoskeleton 2010, 2:49-58.
    • (2010) Cell Health Cytoskeleton , vol.2 , pp. 49-58
    • Peirce, S.K.1    Findley, H.W.2
  • 59
    • 84952061620 scopus 로고    scopus 로고
    • Selective inhibition of the p53-MDM2 interaction by nutlin drugs: a new therapeutic perspective for neuroblastoma
    • Maerken T.V., Rihani A., Goethem A.V., De Paepe A., Speleman F., Vandesompele J. Selective inhibition of the p53-MDM2 interaction by nutlin drugs: a new therapeutic perspective for neuroblastoma. Belg R Acad Med 2013, 2:198-207.
    • (2013) Belg R Acad Med , vol.2 , pp. 198-207
    • Maerken, T.V.1    Rihani, A.2    Goethem, A.V.3    De Paepe, A.4    Speleman, F.5    Vandesompele, J.6
  • 60
    • 79958811171 scopus 로고    scopus 로고
    • Targeting the p53 pathway in retinoblastoma with subconjunctival Nutlin-3a
    • Brennan R.C., Federico S., Bradley C., Zhang J., Flores-Otero J., Wilson M., et al. Targeting the p53 pathway in retinoblastoma with subconjunctival Nutlin-3a. Cancer Res 2011, 71(12):4205-4213.
    • (2011) Cancer Res , vol.71 , Issue.12 , pp. 4205-4213
    • Brennan, R.C.1    Federico, S.2    Bradley, C.3    Zhang, J.4    Flores-Otero, J.5    Wilson, M.6
  • 61
    • 66149108372 scopus 로고    scopus 로고
    • Nutlin-3 up-regulates the expression of Notch1 in both myeloid and lymphoid leukemic cells, as part of a negative feedback antiapoptotic mechanism
    • Secchiero P., Melloni E., di Iasio M.G., Tiribelli M., Rimondi E., Corallini F., et al. Nutlin-3 up-regulates the expression of Notch1 in both myeloid and lymphoid leukemic cells, as part of a negative feedback antiapoptotic mechanism. Blood 2009, 113:4300-4308.
    • (2009) Blood , vol.113 , pp. 4300-4308
    • Secchiero, P.1    Melloni, E.2    di Iasio, M.G.3    Tiribelli, M.4    Rimondi, E.5    Corallini, F.6
  • 62
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger M.B., Hristova V.A., Weissman A.M. HECT and RING finger families of E3 ubiquitin ligases at a glance. J Cell Sci 2012, 125:531-537.
    • (2012) J Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 63
    • 79961076734 scopus 로고    scopus 로고
    • The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
    • Huang L., Yan Z., Liao X., Li Y., Yang J., Wang Z.-G., et al. The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo. PNAS 2011, 108(29):12001-12006.
    • (2011) PNAS , vol.108 , Issue.29 , pp. 12001-12006
    • Huang, L.1    Yan, Z.2    Liao, X.3    Li, Y.4    Yang, J.5    Wang, Z.-G.6
  • 64
    • 79551474361 scopus 로고    scopus 로고
    • MDM2 and MDMX in cancer and development
    • Marine J.C. MDM2 and MDMX in cancer and development. Curr Top Dev Biol 2011, 94:45-75.
    • (2011) Curr Top Dev Biol , vol.94 , pp. 45-75
    • Marine, J.C.1
  • 65
    • 84865149674 scopus 로고    scopus 로고
    • Discovery of Mdm2-MdmX E3 ligase inhibitors using a cell-based ubiquitination assay
    • Herman A.G., Hayano M., Poyurovsky M.V., Shimada K., Skouta R., Prives C., et al. Discovery of Mdm2-MdmX E3 ligase inhibitors using a cell-based ubiquitination assay. Cancer Discov 2011, 1(4):312-325.
    • (2011) Cancer Discov , vol.1 , Issue.4 , pp. 312-325
    • Herman, A.G.1    Hayano, M.2    Poyurovsky, M.V.3    Shimada, K.4    Skouta, R.5    Prives, C.6
  • 66
    • 84903989817 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 2a stabilizes MDM4 and facilitates the p53-mediated intrinsic apoptotic pathway in glioblastoma
    • Wang Ch.-L., Wang J.Y., Liu Z.Y., Ma X.M., Wang X.W., Jin H., et al. Ubiquitin-specific protease 2a stabilizes MDM4 and facilitates the p53-mediated intrinsic apoptotic pathway in glioblastoma. Carcinogenesis 2014, 35(7):1500-1509.
    • (2014) Carcinogenesis , vol.35 , Issue.7 , pp. 1500-1509
    • Wang, C.-L.1    Wang, J.Y.2    Liu, Z.Y.3    Ma, X.M.4    Wang, X.W.5    Jin, H.6
  • 67
    • 84938531774 scopus 로고    scopus 로고
    • Mdmx promotes genomic instability independent of p53 and Mdm2
    • March
    • Carrillo A.M., Bouska A., Arrate M.P., Eischen C.M. Mdmx promotes genomic instability independent of p53 and Mdm2. Oncogene 2014, (March). 10.1038/onc.2014.27.
    • (2014) Oncogene
    • Carrillo, A.M.1    Bouska, A.2    Arrate, M.P.3    Eischen, C.M.4
  • 68
  • 69
    • 84951970268 scopus 로고    scopus 로고
    • Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy
    • Chang Y.S., Graves B., Guerlavais V., Tovar Ch., Packman K., To K.-H., et al. Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy. PNAS 2011, 108(29):12001-12006.
    • (2011) PNAS , vol.108 , Issue.29 , pp. 12001-12006
    • Chang, Y.S.1    Graves, B.2    Guerlavais, V.3    Tovar, C.4    Packman, K.5    To, K.-H.6
  • 71
    • 83555172630 scopus 로고    scopus 로고
    • SAG/RBX2/ROC2 E3 ubiquitin ligase is essential for vascular and neural development by targeting NF1 for degradation
    • Tan M., Zhao Y., Kim S.J., Liu M., Jia L., Saunders T.L., et al. SAG/RBX2/ROC2 E3 ubiquitin ligase is essential for vascular and neural development by targeting NF1 for degradation. Dev Cell 2011, 21:1062-1076.
    • (2011) Dev Cell , vol.21 , pp. 1062-1076
    • Tan, M.1    Zhao, Y.2    Kim, S.J.3    Liu, M.4    Jia, L.5    Saunders, T.L.6
  • 72
    • 34548846689 scopus 로고    scopus 로고
    • SAG/ROC2 E3 ligase regulates skin carcinogenesis by stage dependent targeting of c-Jun/AP1 and IkB/NF-kB
    • Gu Q., Bowden T.G., Normolle D., Sun Y. SAG/ROC2 E3 ligase regulates skin carcinogenesis by stage dependent targeting of c-Jun/AP1 and IkB/NF-kB. J Cell Biol 2007, 178:1009-1023.
    • (2007) J Cell Biol , vol.178 , pp. 1009-1023
    • Gu, Q.1    Bowden, T.G.2    Normolle, D.3    Sun, Y.4
  • 73
    • 76049102305 scopus 로고    scopus 로고
    • Validation of SAG/RBX2/ROC2 E3 ubiquitin ligase as an anticancer and radiosensitizing target
    • Jia L., Yang J., Hao X., Zheng M., He H., Xiong X., et al. Validation of SAG/RBX2/ROC2 E3 ubiquitin ligase as an anticancer and radiosensitizing target. Clin Cancer Res 2010, 16:814-824.
    • (2010) Clin Cancer Res , vol.16 , pp. 814-824
    • Jia, L.1    Yang, J.2    Hao, X.3    Zheng, M.4    He, H.5    Xiong, X.6
  • 74
    • 79952390921 scopus 로고    scopus 로고
    • Role of ROC1 protein in the control of cyclin D1 protein expression in skin melanomas
    • Nai G., Marques M. Role of ROC1 protein in the control of cyclin D1 protein expression in skin melanomas. Pathol Res Pract 2011, 207:174e181.
    • (2011) Pathol Res Pract , vol.207 , pp. 174e181
    • Nai, G.1    Marques, M.2
  • 75
    • 79951689476 scopus 로고    scopus 로고
    • SCF E3 ubiquitin ligases as anticancer targets
    • Jia L., Sun Y. SCF E3 ubiquitin ligases as anticancer targets. Curr Cancer Drug Targets 2011, 11(3):347-356.
    • (2011) Curr Cancer Drug Targets , vol.11 , Issue.3 , pp. 347-356
    • Jia, L.1    Sun, Y.2
  • 77
    • 72049101209 scopus 로고    scopus 로고
    • Diversification of the cullin family
    • Marin I. Diversification of the cullin family. BMC Evol Biol 2009, 9:267.
    • (2009) BMC Evol Biol , vol.9 , pp. 267
    • Marin, I.1
  • 78
    • 79551569897 scopus 로고    scopus 로고
    • Cullins and cancer
    • Lee J., Zhou P. Cullins and cancer. Genes Cancer 2010, 1(7):690-699.
    • (2010) Genes Cancer , vol.1 , Issue.7 , pp. 690-699
    • Lee, J.1    Zhou, P.2
  • 79
    • 58349123095 scopus 로고    scopus 로고
    • Restriction of Src activity by Cullin-5
    • Laszlo G.S., Cooper J.A. Restriction of Src activity by Cullin-5. Curr Biol 2009, 19(2):157-162.
    • (2009) Curr Biol , vol.19 , Issue.2 , pp. 157-162
    • Laszlo, G.S.1    Cooper, J.A.2
  • 80
    • 84866949680 scopus 로고    scopus 로고
    • Novel multiple markers to distinguish melanoma from dysplastic nevi
    • Zhang G., Li G. Novel multiple markers to distinguish melanoma from dysplastic nevi. PLoS ONE 2012, 7(9):e45037.
    • (2012) PLoS ONE , vol.7 , Issue.9 , pp. e45037
    • Zhang, G.1    Li, G.2
  • 81
    • 77957879187 scopus 로고    scopus 로고
    • Increased Cul1 expression promotes melanoma cell proliferation through regulating p27 expression
    • Chen G., Li G. Increased Cul1 expression promotes melanoma cell proliferation through regulating p27 expression. Int J Oncol 2010, 37:1339-1344.
    • (2010) Int J Oncol , vol.37 , pp. 1339-1344
    • Chen, G.1    Li, G.2
  • 82
    • 84896381855 scopus 로고    scopus 로고
    • Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation
    • Cheng F., He R., Zhang L., Li H., Zhang W., Ji X., et al. Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation. Oncol Lett 2014, 7:1645-1650.
    • (2014) Oncol Lett , vol.7 , pp. 1645-1650
    • Cheng, F.1    He, R.2    Zhang, L.3    Li, H.4    Zhang, W.5    Ji, X.6
  • 83
    • 70350359679 scopus 로고    scopus 로고
    • CRL4s: the CUL4-RING E3 ubiquitin ligases
    • Jackson S., Xiong Y. CRL4s: the CUL4-RING E3 ubiquitin ligases. Trends Biochem Sci 2009, 34(11):562-570.
    • (2009) Trends Biochem Sci , vol.34 , Issue.11 , pp. 562-570
    • Jackson, S.1    Xiong, Y.2
  • 84
    • 84873530887 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system, a new anti-tumor target
    • Du W., Mei Q. Ubiquitin-proteasome system, a new anti-tumor target. Acta Pharmacol Sin 2013, 34:187-188.
    • (2013) Acta Pharmacol Sin , vol.34 , pp. 187-188
    • Du, W.1    Mei, Q.2


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