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Volumn 14, Issue 6, 2014, Pages 549-556

NEDD4: A promising target for cancer therapy

Author keywords

Cancer; E3 ligase; NEDD4; Oncogene; Target; Therapy; Ubiquitination

Indexed keywords

NOTCH1 RECEPTOR; PHOSPHATIDYLINOSITOL 3, 4, 5 TRISPHOSPHATE 3 PHOSPHATASE; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; ESCRT PROTEIN; NEDD4 UBIQUITIN PROTEIN LIGASES; PROTEASOME; PROTEASOME INHIBITOR; UBIQUITIN PROTEIN LIGASE; BETA TRANSDUCIN REPEAT CONTAINING PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; UBIQUITIN PROTEIN LIGASE E3;

EID: 84907334131     PISSN: 15680096     EISSN: 18735576     Source Type: Journal    
DOI: 10.2174/1568009614666140725092430     Document Type: Review
Times cited : (58)

References (70)
  • 1
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: Tipping the scales of cancer
    • Frescas, D.; Pagano, M. Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat. Rev. Cancer, 2008, 8, 438-449.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 2
    • 44449158749 scopus 로고    scopus 로고
    • The tumour suppressor PTEN mediates a negative regulation of the E3 ubiquitin-protein ligase Nedd4
    • Ahn, Y.; Hwang, C.Y.; Lee, S.R.; Kwon, K.S.; Lee, C. The tumour suppressor PTEN mediates a negative regulation of the E3 ubiquitin-protein ligase Nedd4. Biochem. J., 2008, 412, 331-338.
    • (2008) Biochem. J , vol.412 , pp. 331-338
    • Ahn, Y.1    Hwang, C.Y.2    Lee, S.R.3    Kwon, K.S.4    Lee, C.5
  • 3
    • 33748991453 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
    • Hoeller, D.; Hecker, C.M.; Dikic, I. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat. Rev. Cancer, 2006, 6, 776-788.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 776-788
    • Hoeller, D.1    Hecker, C.M.2    Dikic, I.3
  • 4
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller, D.; Dikic, I. Targeting the ubiquitin system in cancer therapy. Nature, 2009, 458, 438-444.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 5
    • 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
  • 7
    • 84895984956 scopus 로고    scopus 로고
    • Functional characterization of anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis
    • Zhang, J.; Wan, L.; Dai, X.; Sun, Y.; Wei, W. Functional characterization of anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis. Biochim. Biophys. Acta., 2014, 1845, 277-293.
    • (2014) Biochim. Biophys. Acta , vol.1845 , pp. 277-293
    • Zhang, J.1    Wan, L.2    Dai, X.3    Sun, Y.4    Wei, W.5
  • 8
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • Nakayama, K.I.; Nakayama, K. Ubiquitin ligases: cell-cycle control and cancer. Nat. Rev. Cancer, 2006, 6, 369-381.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 9
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: Multiple players in cancer development
    • Bernassola, F.; Karin, M.; Ciechanover, A.; Melino, G. The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell., 2008, 14, 10-21.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 10
    • 84890136771 scopus 로고    scopus 로고
    • Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects
    • Scheffner, M.; Kumar, S. Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects. Biochim. Biophys Acta, 2014, 1843, 61-74.
    • (2014) Biochim. Biophys Acta , vol.1843 , pp. 61-74
    • Scheffner, M.1    Kumar, S.2
  • 11
    • 77449124047 scopus 로고    scopus 로고
    • Nedd4 and Nedd4-2: Closely related ubiquitinprotein ligases with distinct physiological functions
    • Yang, B.; Kumar, S. Nedd4 and Nedd4-2: closely related ubiquitinprotein ligases with distinct physiological functions. Cell Death Differ., 2010, 17, 68-77.
    • (2010) Cell Death Differ , vol.17 , pp. 68-77
    • Yang, B.1    Kumar, S.2
  • 12
    • 84873362507 scopus 로고    scopus 로고
    • Nedd4 and Nedd4-2: Ubiquitin ligases at work in the neuron
    • Donovan, P.; Poronnik, P. Nedd4 and Nedd4-2: ubiquitin ligases at work in the neuron. Int. J. Biochem. Cell Biol., 2013, 45, 706-710.
    • (2013) Int. J. Biochem. Cell Biol , vol.45 , pp. 706-710
    • Donovan, P.1    Poronnik, P.2
  • 13
    • 36248989248 scopus 로고    scopus 로고
    • The Nedd4-like family of E3 ubiquitin ligases and cancer
    • Chen, C.; Matesic, L.E. The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev., 2007, 26, 587-604.
    • (2007) Cancer Metastasis Rev , vol.26 , pp. 587-604
    • Chen, C.1    Matesic, L.E.2
  • 14
    • 33745089231 scopus 로고    scopus 로고
    • Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins
    • Shearwin-Whyatt, L.; Dalton, H.E.; Foot, N.; Kumar, S. Regulation of functional diversity within the Nedd4 family by accessory and adaptor proteins. Bioessays, 2006, 28, 617-628.
    • (2006) Bioessays , vol.28 , pp. 617-628
    • Shearwin-Whyatt, L.1    Dalton, H.E.2    Foot, N.3    Kumar, S.4
  • 15
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub, O.; Dho, S.; Henry, P.; Correa, J.; Ishikawa, T.; McGlade, J.; Rotin, D. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. Embo J., 1996, 15, 2371-2380.
    • (1996) Embo J , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Rotin, D.7
  • 16
    • 52049117442 scopus 로고    scopus 로고
    • Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2- adrenergic receptor
    • Shenoy, S.K.; Xiao, K.; Venkataramanan, V.; Snyder, P.M.; Freedman, N.J.; Weissman, A.M. Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2- adrenergic receptor. J. Biol. Chem., 2008, 283, 22166-22176.
    • (2008) J. Biol. Chem , vol.283 , pp. 22166-22176
    • Shenoy, S.K.1    Xiao, K.2    Venkataramanan, V.3    Snyder, P.M.4    Freedman, N.J.5    Weissman, A.M.6
  • 17
    • 78650070867 scopus 로고    scopus 로고
    • Activity-dependent ubiquitination of GluA1 mediates a distinct AMPA receptor endocytosis and sorting pathway
    • Schwarz, L.A.; Hall, B.J.; Patrick, G.N. Activity-dependent ubiquitination of GluA1 mediates a distinct AMPA receptor endocytosis and sorting pathway. J. Neurosci., 2010, 30, 16718-16729.
    • (2010) J. Neurosci , vol.30 , pp. 16718-16729
    • Schwarz, L.A.1    Hall, B.J.2    Patrick, G.N.3
  • 18
    • 80052690758 scopus 로고    scopus 로고
    • Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking
    • Lin, A.; Hou, Q.; Jarzylo, L.; Amato, S.; Gilbert, J.; Shang, F.; Man, H.Y. Nedd4-mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking. J. Neurochem., 2011, 119, 27-39.
    • (2011) J. Neurochem , vol.119 , pp. 27-39
    • Lin, A.1    Hou, Q.2    Jarzylo, L.3    Amato, S.4    Gilbert, J.5    Shang, F.6    Man, H.Y.7
  • 19
    • 11144350287 scopus 로고    scopus 로고
    • Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation
    • Sakata, T.; Sakaguchi, H.; Tsuda, L.; Higashitani, A.; Aigaki, T.; Matsuno, K.; Hayashi, S. Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation. Curr. Biol., 2004, 14, 2228-2236.
    • (2004) Curr. Biol , vol.14 , pp. 2228-2236
    • Sakata, T.1    Sakaguchi, H.2    Tsuda, L.3    Higashitani, A.4    Aigaki, T.5    Matsuno, K.6    Hayashi, S.7
  • 21
    • 84872736566 scopus 로고    scopus 로고
    • Ubiquitindependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response
    • Fan, C.D.; Lum, M.A.; Xu, C.; Black, J.D.; Wang, X. Ubiquitindependent regulation of phospho-AKT dynamics by the ubiquitin E3 ligase, NEDD4-1, in the insulin-like growth factor-1 response. J. Biol. Chem., 2013, 288, 1674-1684.
    • (2013) J. Biol. Chem , vol.288 , pp. 1674-1684
    • Fan, C.D.1    Lum, M.A.2    Xu, C.3    Black, J.D.4    Wang, X.5
  • 22
    • 0345381737 scopus 로고    scopus 로고
    • The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor
    • Vecchione, A.; Marchese, A.; Henry, P.; Rotin, D.; Morrione, A. The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor. Mol. Cell Biol., 2003, 23, 3363-3372.
    • (2003) Mol. Cell Biol , vol.23 , pp. 3363-3372
    • Vecchione, A.1    Marchese, A.2    Henry, P.3    Rotin, D.4    Morrione, A.5
  • 26
    • 59149105793 scopus 로고    scopus 로고
    • The cyclin-dependent kinase activator, Spy1A, is targeted for degradation by the ubiquitin ligase NEDD4
    • Al Sorkhy, M.; Craig, R.; Market, B.; Ard, R.; Porter, L.A. The cyclin-dependent kinase activator, Spy1A, is targeted for degradation by the ubiquitin ligase NEDD4. J. Biol. Chem., 2009, 284, 2617-2627.
    • (2009) J. Biol. Chem , vol.284 , pp. 2617-2627
    • Al Sorkhy, M.1    Craig, R.2    Market, B.3    Ard, R.4    Porter, L.A.5
  • 27
    • 84891706068 scopus 로고    scopus 로고
    • NEDD4 E3 ligase inhibits the activity of the Hippo pathway by targeting LATS1 for degradation
    • Salah, Z.; Cohen, S.; Itzhaki, E.; Aqeilan, R.I. NEDD4 E3 ligase inhibits the activity of the Hippo pathway by targeting LATS1 for degradation. Cell Cycle, 2013, 12.
    • (2013) Cell Cycle , vol.12
    • Salah, Z.1    Cohen, S.2    Itzhaki, E.3    Aqeilan, R.I.4
  • 29
    • 85019210425 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, 2014.
    • (2014) Oncogene
    • Xu, C.1    Fan, C.D.2    Wang, X.3
  • 30
    • 46049089636 scopus 로고    scopus 로고
    • Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization
    • Monami, G.; Emiliozzi, V.; Morrione, A. Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization. J. Cell Physiol., 2008, 216, 426-437.
    • (2008) J. Cell Physiol , vol.216 , pp. 426-437
    • Monami, G.1    Emiliozzi, V.2    Morrione, A.3
  • 31
    • 84055219407 scopus 로고    scopus 로고
    • Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1
    • Platta, H.W.; Abrahamsen, H.; Thoresen, S.B.; Stenmark, H. Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1. Biochem. J., 2012, 441, 399-406.
    • (2012) Biochem. J , vol.441 , pp. 399-406
    • Platta, H.W.1    Abrahamsen, H.2    Thoresen, S.B.3    Stenmark, H.4
  • 32
    • 84869102684 scopus 로고    scopus 로고
    • Identification of Nedd4 as a novel regulator in Hedgehog signaling
    • Luo, Q.F.; Chen, W.; Zhang, S.T. Identification of Nedd4 as a novel regulator in Hedgehog signaling. Chin. Med. J. (Engl)., 2012, 125, 3851-3855.
    • (2012) Chin. Med. J. (Engl) , vol.125 , pp. 3851-3855
    • Luo, Q.F.1    Chen, W.2    Zhang, S.T.3
  • 35
    • 77950844373 scopus 로고    scopus 로고
    • FoxM1B regulates NEDD4-1 expression, leading to cellular transformation and full malignant phenotype in immortalized human astrocytes
    • Dai, B.; Pieper, R.O.; Li, D.; Wei, P.; Liu, M.; Woo, S.Y.; Aldape, K.D.; Sawaya, R.; Xie, K.; Huang, S. FoxM1B regulates NEDD4-1 expression, leading to cellular transformation and full malignant phenotype in immortalized human astrocytes. Cancer Res., 2010, 70, 2951-2961.
    • (2010) Cancer Res , vol.70 , pp. 2951-2961
    • Dai, B.1    Pieper, R.O.2    Li, D.3    Wei, P.4    Liu, M.5    Woo, S.Y.6    Aldape, K.D.7    Sawaya, R.8    Xie, K.9    Huang, S.10
  • 37
    • 84873882079 scopus 로고    scopus 로고
    • The iron-regulated metastasis suppressor NDRG1 targets NEDD4L, PTEN, and SMAD4 and inhibits the PI3K and Ras signaling pathways
    • Kovacevic, Z.; Chikhani, S.; Lui, G.Y.; Sivagurunathan, S.; Richardson, D.R. The iron-regulated metastasis suppressor NDRG1 targets NEDD4L, PTEN, and SMAD4 and inhibits the PI3K and Ras signaling pathways. Antioxid. Redox. Signal., 2013, 18, 874-887.
    • (2013) Antioxid. Redox. Signal , vol.18 , pp. 874-887
    • Kovacevic, Z.1    Chikhani, S.2    Lui, G.Y.3    Sivagurunathan, S.4    Richardson, D.R.5
  • 38
    • 84897405021 scopus 로고    scopus 로고
    • Beta- TRCP-mediated degradation of NEDD4 inhibits tumorigenesis through modulating the PTEN/Akt signaling pathway
    • In Press
    • Liu, J. W.; L. Liu, P. Inuzuka, H.; Liu, J.; Wang, Z.; Wei, W. Beta- TRCP-mediated degradation of NEDD4 inhibits tumorigenesis through modulating the PTEN/Akt signaling pathway. Oncotarget., 2014, In Press.
    • (2014) Oncotarget
    • Liu, J.W.1    Liu, L.2    Inuzuka, H.P.3    Liu, J.4    Wang, Z.5    Wei, W.6
  • 41
    • 70450263302 scopus 로고    scopus 로고
    • Protein kinase Cdelta supports survival of MDA-MB-231 breast cancer cells by suppressing the ERK1/2 pathway
    • Lonne, G.K.; Masoumi, K.C.; Lennartsson, J.; Larsson, C. Protein kinase Cdelta supports survival of MDA-MB-231 breast cancer cells by suppressing the ERK1/2 pathway. J. Biol. Chem., 2009, 284, 33456-33465.
    • (2009) J. Biol. Chem , vol.284 , pp. 33456-33465
    • Lonne, G.K.1    Masoumi, K.C.2    Lennartsson, J.3    Larsson, C.4
  • 44
    • 67349270258 scopus 로고    scopus 로고
    • Abnormal development of the neuromuscular junction in Nedd4-deficient mice
    • Liu, Y.; Oppenheim, R.W.; Sugiura, Y.; Lin, W. Abnormal development of the neuromuscular junction in Nedd4-deficient mice. Dev. Biol., 2009, 330, 153-166.
    • (2009) Dev. Biol , vol.330 , pp. 153-166
    • Liu, Y.1    Oppenheim, R.W.2    Sugiura, Y.3    Lin, W.4
  • 48
    • 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
  • 51
    • 84896714532 scopus 로고    scopus 로고
    • NEDD4L is downregulated in colorectal cancer and inhibits canonical WNT signaling
    • Tanksley, J.P.; Chen, X.; Coffey, R.J. NEDD4L is downregulated in colorectal cancer and inhibits canonical WNT signaling. PLoS One, 2013, 8, e81514.
    • (2013) PLoS One , vol.8
    • Tanksley, J.P.1    Chen, X.2    Coffey, R.J.3
  • 52
    • 71449092100 scopus 로고    scopus 로고
    • Systems biology approach to identification of biomarkers for metastatic progression in gastric cancer
    • Wang, Y.Y.; Ye, Z.Y.; Zhao, Z.S.; Tao, H.Q.; Li, S.G. Systems biology approach to identification of biomarkers for metastatic progression in gastric cancer. J. Cancer Res. Clin. Oncol., 2010, 136, 135-141.
    • (2010) J. Cancer Res. Clin. Oncol , vol.136 , pp. 135-141
    • Wang, Y.Y.1    Ye, Z.Y.2    Zhao, Z.S.3    Tao, H.Q.4    Li, S.G.5
  • 53
    • 84873907094 scopus 로고    scopus 로고
    • Is NEDD4-1 a negative regulator of phosphatase and tensin homolog in gastric carcinogenesis?
    • Yang, Z.; Yuan, X.G.; Chen, J.; Lu, N.H. Is NEDD4-1 a negative regulator of phosphatase and tensin homolog in gastric carcinogenesis? World J. Gastroenterol., 2012, 18, 6345-6348.
    • (2012) World J. Gastroenterol , vol.18 , pp. 6345-6348
    • Yang, Z.1    Yuan, X.G.2    Chen, J.3    Lu, N.H.4
  • 54
    • 69949158818 scopus 로고    scopus 로고
    • Knockdown of ASIC1 and epithelial sodium channel subunits inhibits glioblastoma whole cell current and cell migration
    • Kapoor, N.; Bartoszewski, R.; Qadri, Y.J.; Bebok, Z.; Bubien, J. K.; Fuller, C.M.; Benos, D.J. Knockdown of ASIC1 and epithelial sodium channel subunits inhibits glioblastoma whole cell current and cell migration. J. Biol. Chem., 2009, 284, 24526-24541.
    • (2009) J. Biol. Chem , vol.284 , pp. 24526-24541
    • Kapoor, N.1    Bartoszewski, R.2    Qadri, Y.J.3    Bebok, Z.4    Bubien, J.K.5    Fuller, C.M.6    Benos, D.J.7
  • 56
    • 84855202017 scopus 로고    scopus 로고
    • Photodynamic therapy leads to death of C6 glioma cells partly through AMPAR
    • Du, P.; Hu, S.; Cheng, Y.; Li, F.; Li, M.; Li, J.; Yi, L.; Feng, H. Photodynamic therapy leads to death of C6 glioma cells partly through AMPAR. Brain Res., 2012, 1433, 153-159.
    • (2012) Brain Res , vol.1433 , pp. 153-159
    • Du, P.1    Hu, S.2    Cheng, Y.3    Li, F.4    Li, M.5    Li, J.6    Yi, L.7    Feng, H.8
  • 58
    • 84874598403 scopus 로고    scopus 로고
    • Beclin-1: Autophagic regulator and therapeutic target in cancer
    • Fu, L.L.; Cheng, Y.; Liu, B. Beclin-1: autophagic regulator and therapeutic target in cancer. Int. J. Biochem. Cell Biol., 2013, 45, 921-924.
    • (2013) Int. J. Biochem. Cell Biol , vol.45 , pp. 921-924
    • Fu, L.L.1    Cheng, Y.2    Liu, B.3
  • 60
    • 84874354425 scopus 로고    scopus 로고
    • Deltex-1 activates mitotic signaling and proliferation and increases the clonogenic and invasive potential of U373 and LN18 glioblastoma cells and correlates with patient survival
    • Huber, R.M.; Rajski, M.; Sivasankaran, B.; Moncayo, G.; Hemmings, B.A.; Merlo, A. Deltex-1 activates mitotic signaling and proliferation and increases the clonogenic and invasive potential of U373 and LN18 glioblastoma cells and correlates with patient survival. PLoS One, 2013, 8, e57793.
    • (2013) PLoS One , vol.8
    • Huber, R.M.1    Rajski, M.2    Sivasankaran, B.3    Moncayo, G.4    Hemmings, B.A.5    Merlo, A.6
  • 61
    • 84877313224 scopus 로고    scopus 로고
    • IGF-1R as an anti-cancer target--trials and tribulations
    • Chen, H.X.; Sharon, E. IGF-1R as an anti-cancer target--trials and tribulations. Chin. J. Cancer, 2013, 32, 242-252.
    • (2013) Chin. J. Cancer , vol.32 , pp. 242-252
    • Chen, H.X.1    Sharon, E.2
  • 62
    • 84883251999 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor type I as a target for cancer therapy
    • Corvaia, N.; Beck, A.; Caussanel, V.; Goetsch, L. Insulin-like growth factor receptor type I as a target for cancer therapy. Front. Biosci. (Schol. Ed)., 2013, 5, 439-450.
    • (2013) Front. Biosci. (Schol. Ed) , vol.5 , pp. 439-450
    • Corvaia, N.1    Beck, A.2    Caussanel, V.3    Goetsch, L.4
  • 63
    • 77958494807 scopus 로고    scopus 로고
    • LATS tumor suppressor: A new governor of cellular homeostasis
    • Visser, S.; Yang, X. LATS tumor suppressor: a new governor of cellular homeostasis. Cell Cycle, 2010, 9, 3892-3903.
    • (2010) Cell Cycle , vol.9 , pp. 3892-3903
    • Visser, S.1    Yang, X.2
  • 66
    • 84897710994 scopus 로고    scopus 로고
    • The regulation of MDM2 oncogene and its impact on human cancers
    • Zhao, Y.; Yu, H.; Hu, W. The regulation of MDM2 oncogene and its impact on human cancers. Acta Biochim. Biophys. Sin. (Shanghai), 2014, 46, 180-189.
    • (2014) Acta Biochim. Biophys. Sin. (Shanghai) , vol.46 , pp. 180-189
    • Zhao, Y.1    Yu, H.2    Hu, W.3
  • 70
    • 84888427862 scopus 로고    scopus 로고
    • Targeted inhibition of VEGF receptor 2: An update on ramucirumab
    • Clarke, J.M.; Hurwitz, H.I. Targeted inhibition of VEGF receptor 2: an update on ramucirumab. Expert. Opin. Biol. Ther., 2013, 13, 1187-1196.
    • (2013) Expert. Opin. Biol. Ther , vol.13 , pp. 1187-1196
    • Clarke, J.M.1    Hurwitz, H.I.2


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