메뉴 건너뛰기




Volumn 7, Issue 5, 2014, Pages 1645-1650

Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation

Author keywords

Apoptosis; Cell cycle; Melanoma; Neddylation; Ubiquitination

Indexed keywords

BORTEZOMIB; CYCLIN D; NEDD8 PROTEIN; SCAFFOLD PROTEIN; SMALL INTERFERING RNA;

EID: 84896381855     PISSN: 17921074     EISSN: 17921082     Source Type: Journal    
DOI: 10.3892/ol.2014.1953     Document Type: Article
Times cited : (7)

References (27)
  • 1
    • 84865468924 scopus 로고    scopus 로고
    • The role of PML ubiquitination in human malignancies
    • Chen RH, Lee YR and Yuan WC: The role of PML ubiquitination in human malignancies. J Biomed Sci 19: 81, 2012.
    • (2012) J Biomed Sci , vol.19 , pp. 81
    • Lee, Y.R.1    Yuan, W.C.2
  • 3
    • 43049154531 scopus 로고    scopus 로고
    • Alternative UPS drug targets upstream the 26S proteasome
    • Hjerpe R and Rodríguez MS: Alternative UPS drug targets upstream the 26S proteasome. Int J Biochem Cell Biol 40: 1126-1140, 2008.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1126-1140
    • Hjerpe, R.1    Rodríguez, M.S.2
  • 4
    • 77449127476 scopus 로고    scopus 로고
    • Ubiquitin-independent p53 proteasomal degradation
    • Tsvetkov P, Reuven N and Shaul Y: Ubiquitin-independent p53 proteasomal degradation. Cell Death Differ 17: 103-108, 2010.
    • (2010) Cell Death Differ , vol.17 , pp. 103-108
    • Tsvetkov, P.1    Reuven, N.2    Shaul, Y.3
  • 5
    • 77952548140 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy
    • Allende-Vega N and Saville MK: Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy. Semin Cancer Biol 20: 29-39, 2010.
    • (2010) Semin Cancer Biol , vol.20 , pp. 29-39
    • Allende-Vega, N.1    Saville, M.K.2
  • 6
    • 0032530151 scopus 로고    scopus 로고
    • Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21 (CIP1/WAF1) and cyclin D proteins
    • Yu ZK, Gervais JL and Zhang H: Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21 (CIP1/WAF1) and cyclin D proteins. Proc Natl Acad Sci USA 95: 11324-11329, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11324-11329
    • Yu, Z.K.1    Gervais, J.L.2    Zhang, H.3
  • 7
    • 0034255143 scopus 로고    scopus 로고
    • Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors
    • Dace A, Zhao L, Park KS, et al: Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors. Proc Natl Acad Sci USA 97: 8985-8990, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8985-8990
    • Dace, A.1    Zhao, L.2    Park, K.S.3
  • 8
    • 0034595849 scopus 로고    scopus 로고
    • A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo
    • Wada H, Yeh ET and Kamitani T: A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J Biol Chem 275: 17008-17015, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17008-17015
    • Wada, H.1    Yeh, E.T.2    Kamitani, T.3
  • 9
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation. 'Protein modifications: Beyond the usual suspects' review series
    • Rabut G and Peter M: Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 9: 969-976, 2008.
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 10
    • 0034644650 scopus 로고    scopus 로고
    • Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization
    • Wu K, Chen A and Pan ZQ: Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. J Biol Chem 275: 32317-32324, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 32317-32324
    • Wu, K.1    Chen, A.2    Pan, Z.Q.3
  • 11
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D and Dikic I: Targeting the ubiquitin system in cancer therapy. Nature 458: 438-444, 2009.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 12
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • Bergink S and Jentsch S: Principles of ubiquitin and SUMO modifications in DNA repair. Nature 458: 461-467, 2009.
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 13
    • 33645538920 scopus 로고    scopus 로고
    • Mechanistic rationale and clinical evidence for the efficacy of proteasome inhibitors against indolent and mantle cell lymphomas
    • Paoluzzi L and O'Connor OA: Mechanistic rationale and clinical evidence for the efficacy of proteasome inhibitors against indolent and mantle cell lymphomas. BioDrugs 20: 13-23, 2006.
    • (2006) BioDrugs , vol.20 , pp. 13-23
    • Paoluzzi, L.1    O'Connor, O.A.2
  • 14
    • 33644875054 scopus 로고    scopus 로고
    • Marked clinical activity of the proteasome inhibitor bortezomib in patients with follicular and mantle-cell lymphoma
    • O'Connor OA: Marked clinical activity of the proteasome inhibitor bortezomib in patients with follicular and mantle-cell lymphoma. Clin Lymphoma Myeloma 6: 191-199, 2005.
    • (2005) Clin Lymphoma Myeloma , vol.6 , pp. 191-199
    • O'Connor, O.A.1
  • 15
    • 35148886143 scopus 로고    scopus 로고
    • Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics
    • Yang Y, Kitagaki J, Dai RM, et al: Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics. Cancer Res 67: 9472-9481, 2007.
    • (2007) Cancer Res , vol.67 , pp. 9472-9481
    • Yang, Y.1    Kitagaki, J.2    Dai, R.M.3
  • 16
    • 67449119401 scopus 로고    scopus 로고
    • Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer
    • Soucy TA, Smith PG and Rolfe M: Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer. Clin Cancer Res 15: 3912-3916, 2009.
    • (2009) Clin Cancer Res , vol.15 , pp. 3912-3916
    • Soucy, T.A.1    Smith, P.G.2    Rolfe, M.3
  • 17
    • 35549000516 scopus 로고    scopus 로고
    • Control of cell proliferation via elevated NEDD8 conjugation in oral squamous cell carcinoma
    • Chairatvit K and Ngamkitidechakul C: Control of cell proliferation via elevated NEDD8 conjugation in oral squamous cell carcinoma. Mol Cell Biochem 306: 163-169, 2007.
    • (2007) Mol Cell Biochem , vol.306 , pp. 163-169
    • Chairatvit, K.1    Ngamkitidechakul, C.2
  • 18
    • 84864878953 scopus 로고    scopus 로고
    • Inhibition of the NEDD8 conjugation pathway by shRNA to UBA3, the subunit of the NEDD8-activating enzyme, suppresses the growth of melanoma cells
    • Cheng F, Chen H, Zhang L, Li RH, Liu Y and Sun JF: Inhibition of the NEDD8 conjugation pathway by shRNA to UBA3, the subunit of the NEDD8-activating enzyme, suppresses the growth of melanoma cells. Asian Pac J Cancer Prev 13: 57-62, 2012.
    • (2012) Asian Pac J Cancer Prev , vol.13 , pp. 57-62
    • Cheng, F.1    Chen, H.2    Zhang, L.3    Li, R.H.4    Liu, Y.5    Sun, J.F.6
  • 19
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, et al: An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 458: 732-736, 2009.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 20
    • 0034640373 scopus 로고    scopus 로고
    • Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins
    • Gong L, Kamitani T, Millas S and Yeh ET: Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins. J Biol Chem 275: 14212-14216, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 14212-14216
    • Gong, L.1    Kamitani, T.2    Millas, S.3    Yeh, E.T.4
  • 21
    • 10744227299 scopus 로고    scopus 로고
    • Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins
    • Hemelaar J, Borodovsky A, Kessler BM, et al: Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Mol Cell Biol 24: 84-95, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 84-95
    • Hemelaar, J.1    Borodovsky, A.2    Kessler, B.M.3
  • 22
    • 0031679192 scopus 로고    scopus 로고
    • Expression patterns of cyclin D1 and related proteins regulating G1-S phase transition in uveal melanoma and retinoblastoma
    • Coupland SE, Bechrakis N, Schüler A, Anagnostopoulos I, Hummel M, Bornfeld N and Stein H: Expression patterns of cyclin D1 and related proteins regulating G1-S phase transition in uveal melanoma and retinoblastoma. Br J Ophthalmol 82: 961-970, 1998.
    • (1998) Br J Ophthalmol , vol.82 , pp. 961-970
    • Coupland, S.E.1    Bechrakis, N.2    Schüler, A.3    Anagnostopoulos, I.4    Hummel, M.5    Bornfeld, N.6    Stein, H.7
  • 23
    • 47149085982 scopus 로고    scopus 로고
    • P21 and p27: Roles in carcinogenesis and drug resistance
    • Abukhdeir AM and Park BH: P21 and p27: roles in carcinogenesis and drug resistance. Expert Rev Mol Med 10: e19, 2008.
    • (2008) Expert Rev Mol Med , vol.e19 , pp. 10
    • Abukhdeir, A.M.1    Park, B.H.2
  • 24
    • 0036594890 scopus 로고    scopus 로고
    • The role of the cyclin-dependent kinase inhibitor p21 in apoptosis
    • Gartel AL and Tyner AL: The role of the cyclin-dependent kinase inhibitor p21 in apoptosis. Mol Cancer Ther 1: 639-649, 2002.
    • (2002) Mol Cancer Ther , vol.1 , pp. 639-649
    • Gartel, A.L.1    Tyner, A.L.2
  • 25
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane DM, Bossy-Wetzel E, Waterhouse NJ, Cotter TG and Green DR: Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J Biol Chem 274: 2225-2233, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 26
    • 84873648741 scopus 로고    scopus 로고
    • Ubiquitin family members in the regulation of the tumor suppressor p53
    • Xirodimas DP and Scheffner M: Ubiquitin family members in the regulation of the tumor suppressor p53. Subcell Biochem 54: 116-135, 2010.
    • (2010) Subcell Biochem , vol.54 , pp. 116-135
    • Xirodimas, D.P.1    Scheffner, M.2
  • 27
    • 84868486281 scopus 로고    scopus 로고
    • Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid Schiff base-copper complexes
    • Zuo J, Bi C, Fan Y, Buac D, Nardon C, Daniel KG and Dou QP: Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid Schiff base-copper complexes. J Inorg Biochem 118: 83-93, 2013.
    • (2013) J Inorg Biochem , vol.118 , pp. 83-93
    • Zuo, J.1    Bi, C.2    Fan, Y.3    Buac, D.4    Nardon, C.5    Daniel, K.G.6    Dou, Q.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.