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Volumn 19, Issue 6, 2012, Pages 324-328

Erratum to 2.6 Ubiquitin-Like Activity of shprh Protein and Ovarian Cancer (Curr Oncol, (2012), 19, (324-8), 10.3747/co.19.1175);Ubiquitin pathway and ovarian cancer

Author keywords

Gene expression; Ovarian cancer; Protein degradation; Therapy; Ubiquitin

Indexed keywords

CISPLATIN; CYCLINE; LACTACYSTIN; MITOGEN ACTIVATED PROTEIN KINASE; ONCOPROTEIN; PROTEASOME; PROTEIN P53; RPN13 PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 2; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84870753764     PISSN: None     EISSN: 17187729     Source Type: Journal    
DOI: 10.3747/co.20.1603     Document Type: Erratum
Times cited : (7)

References (32)
  • 2
    • 1842486790 scopus 로고    scopus 로고
    • Ubiquitin and breast cancer
    • Ohta T, Fukuda M. Ubiquitin and breast cancer. Oncogene 2004;23:2079-88.
    • (2004) Oncogene , vol.23 , pp. 2079-2088
    • Ohta, T.1    Fukuda, M.2
  • 3
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive brca1-directed ubiquitination
    • Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE. A UbcH5/ubiquitin noncovalent complex is required for processive brca1-directed ubiquitination. Mol Cell 2006;21:873-80.
    • (2006) Mol Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 4
    • 0035072535 scopus 로고    scopus 로고
    • Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors
    • Tenev T, Marani M, McNeish I, Lemoine NR. Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors. Cell Death Differ 2001;8:256-64.
    • (2001) Cell Death Differ , vol.8 , pp. 256-264
    • Tenev, T.1    Marani, M.2    McNeish, I.3    Lemoine, N.R.4
  • 5
    • 78149423097 scopus 로고    scopus 로고
    • Association of lipid metabolism with ovarian cancer
    • Tania M, Khan MA, Song Y. Association of lipid metabolism with ovarian cancer. Curr Oncol 2010;17:6-11.
    • (2010) Curr Oncol , vol.17 , pp. 6-11
    • Tania, M.1    Khan, M.A.2    Song, Y.3
  • 6
    • 34548415428 scopus 로고    scopus 로고
    • The brca1/2 pathway prevents hematologic cancers in addition to breast and ovarian cancers
    • Friedenson B. The brca1/2 pathway prevents hematologic cancers in addition to breast and ovarian cancers. BMC Cancer 2007;7:152.
    • (2007) BMC Cancer , vol.7 , pp. 152
    • Friedenson, B.1
  • 7
    • 0037684805 scopus 로고    scopus 로고
    • The multiple nuclear functions of brca1: Transcription, ubiquitination and dna repair
    • Starita LM, Parvin JD. The multiple nuclear functions of brca1: transcription, ubiquitination and dna repair. Curr Opin Cell Biol 2003;15:345-50.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 345-350
    • Starita, L.M.1    Parvin, J.D.2
  • 8
    • 34249950879 scopus 로고    scopus 로고
    • Ubiquitin-binding protein rap80 mediates brca1-dependent dna damage response
    • Kim H, Chen J, Yu X. Ubiquitin-binding protein rap80 mediates brca1-dependent dna damage response. Science 2007;316:1202-5.
    • (2007) Science , vol.316 , pp. 1202-1205
    • Kim, H.1    Chen, J.2    Yu, X.3
  • 9
    • 0035491589 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of brca1 protein in MCF-7 human breast cancer cells
    • Choi YH. Proteasome-mediated degradation of brca1 protein in MCF-7 human breast cancer cells. Int J Oncol 2001;19:687-93.
    • (2001) Int J Oncol , vol.19 , pp. 687-693
    • Choi, Y.H.1
  • 10
    • 11244267567 scopus 로고    scopus 로고
    • Down-regulation of brca1-bard1 ubiquitin ligase by cdk2
    • Hayami R, Sato K, Wu W, et al. Down-regulation of brca1-bard1 ubiquitin ligase by cdk2. Cancer Res 2005;65:6-10.
    • (2005) Cancer Res , vol.65 , pp. 6-10
    • Hayami, R.1    Sato, K.2    Wu, W.3
  • 11
    • 80055092789 scopus 로고    scopus 로고
    • BRCA1 tumor suppression depends on brct phosphoprotein binding, but not its E3 ligase activity
    • Shakya R, Reid LJ, Reczek CR, et al. BRCA1 tumor suppression depends on brct phosphoprotein binding, but not its E3 ligase activity. Science 2011;334:525-8.
    • (2011) Science , vol.334 , pp. 525-528
    • Shakya, R.1    Reid, L.J.2    Reczek, C.R.3
  • 12
    • 15144342687 scopus 로고    scopus 로고
    • Bap1: A novel ubiquitin hydrolase which binds to the brca1 ring finger and enhances brca1-mediated cell growth suppression
    • Jensen DE, Proctor M, Marquis ST, et al. Bap1: a novel ubiquitin hydrolase which binds to the brca1 ring finger and enhances brca1-mediated cell growth suppression. Oncogene 1998;16:1097-112.
    • (1998) Oncogene , vol.16 , pp. 1097-1112
    • Jensen, D.E.1    Proctor, M.2    Marquis, S.T.3
  • 13
    • 4344717012 scopus 로고    scopus 로고
    • BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to dna damage
    • Schoenfeld AR, Apgar S, Dolios G, Wang R, Aaronson SA. BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to dna damage. Mol Cell Biol 2004;24:7444-55.
    • (2004) Mol Cell Biol , vol.24 , pp. 7444-7455
    • Schoenfeld, A.R.1    Apgar, S.2    Dolios, G.3    Wang, R.4    Aaronson, S.A.5
  • 14
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature 2001;410:37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 15
    • 18044387648 scopus 로고    scopus 로고
    • Raf kinase as a target for anticancer therapeutics
    • Sridhar SS, Hedley D, Siu LL. Raf kinase as a target for anticancer therapeutics. Mol Cancer Ther 2005;4:677-85.
    • (2005) Mol Cancer Ther , vol.4 , pp. 677-685
    • Sridhar, S.S.1    Hedley, D.2    Siu, L.L.3
  • 16
    • 33646399160 scopus 로고    scopus 로고
    • Targeting the erk signaling pathway in cancer therapy
    • Kohno M, Pouyssegur J. Targeting the erk signaling pathway in cancer therapy. Ann Med 2006;38:200-11.
    • (2006) Ann Med , vol.38 , pp. 200-211
    • Kohno, M.1    Pouyssegur, J.2
  • 17
    • 5044228741 scopus 로고    scopus 로고
    • Mechanisms regulating the constitutive activation of the extracellular signalregulated kinase (erk) signaling pathway in ovarian cancer and the effect of ribonucleic acid interference for erk1/2 on cancer cell proliferation
    • Steinmetz R, Wagoner HA, Zeng P, et al. Mechanisms regulating the constitutive activation of the extracellular signalregulated kinase (erk) signaling pathway in ovarian cancer and the effect of ribonucleic acid interference for erk1/2 on cancer cell proliferation. Mol Endocrinol 2004;18:2570-82.
    • (2004) Mol Endocrinol , vol.18 , pp. 2570-2582
    • Steinmetz, R.1    Wagoner, H.A.2    Zeng, P.3
  • 18
    • 0036173032 scopus 로고    scopus 로고
    • Sef is a feedback-induced antagonist of Ras/mapk-mediated fgf signalling
    • Fürthauer M, Lin W, Ang SL, Thisse B, Thisse C. Sef is a feedback-induced antagonist of Ras/mapk-mediated fgf signalling. Nat Cell Biol 2002;4:170-4.
    • (2002) Nat Cell Biol , vol.4 , pp. 170-174
    • Fürthauer, M.1    Lin, W.2    Ang, S.L.3    Thisse, B.4    Thisse, C.5
  • 19
    • 10744224985 scopus 로고    scopus 로고
    • Negative feedback regulation of fgf signaling levels by Pyst1/mkp3 in chick embryos
    • Eblaghie MC, Lunn JS, Dickinson RJ, et al. Negative feedback regulation of fgf signaling levels by Pyst1/mkp3 in chick embryos. Curr Biol 2003;13:1009-18.
    • (2003) Curr Biol , vol.13 , pp. 1009-1018
    • Eblaghie, M.C.1    Lunn, J.S.2    Dickinson, R.J.3
  • 20
    • 51849123638 scopus 로고    scopus 로고
    • Loss of mkp3 mediated by oxidative stress enhances tumorigenicity and chemoresistance of ovarian cancer cells
    • Chan DW, Liu VW, Tsao GS, et al. Loss of mkp3 mediated by oxidative stress enhances tumorigenicity and chemoresistance of ovarian cancer cells. Carcinogenesis 2008;29:1742-50.
    • (2008) Carcinogenesis , vol.29 , pp. 1742-1750
    • Chan, D.W.1    Liu, V.W.2    Tsao, G.S.3
  • 21
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • Morgan DO. Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu Rev Cell Dev Biol 1997;13:261-91.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 22
    • 58149286563 scopus 로고    scopus 로고
    • Cyclin G2 is degraded through the ubiquitin-proteasome pathway and mediates the antiproliferative effect of activin receptor-like kinase 7
    • Xu G, Bernaudo S, Fu G, Lee DY, Yang BB, Peng C. Cyclin G2 is degraded through the ubiquitin-proteasome pathway and mediates the antiproliferative effect of activin receptor-like kinase 7. Mol Biol Cell 2008;19:4968-79.
    • (2008) Mol Biol Cell , vol.19 , pp. 4968-4979
    • Xu, G.1    Bernaudo, S.2    Fu, G.3    Lee, D.Y.4    Yang, B.B.5    Peng, C.6
  • 23
    • 79957621261 scopus 로고    scopus 로고
    • Developmental downregulation of Xenopus cyclin E is phosphorylation and nuclear import dependent and is mediated by ubiquitination
    • Brandt Y, Mitchell T, Wu Y, Hartley RS. Developmental downregulation of Xenopus cyclin E is phosphorylation and nuclear import dependent and is mediated by ubiquitination. Dev Biol 2011;355:65-76.
    • (2011) Dev Biol , vol.355 , pp. 65-76
    • Brandt, Y.1    Mitchell, T.2    Wu, Y.3    Hartley, R.S.4
  • 24
    • 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 U S A 2002;99:12847-52.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 25
    • 77952548140 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy
    • Allende-Vega N, Saville MK. Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy. Semin Cancer Biol 2010;20:29-39.
    • (2010) Semin Cancer Biol , vol.20 , pp. 29-39
    • Allende-Vega, N.1    Saville, M.K.2
  • 26
    • 77953001887 scopus 로고    scopus 로고
    • The ubiquitinproteasome system is inhibited by p53 protein expression in human ovarian cancer cells
    • Hwang IY, Baguley BC, Ching LM, Gilchrist CA. The ubiquitinproteasome system is inhibited by p53 protein expression in human ovarian cancer cells. Cancer Lett 2010;294:82-90.
    • (2010) Cancer Lett , vol.294 , pp. 82-90
    • Hwang, I.Y.1    Baguley, B.C.2    Ching, L.M.3    Gilchrist, C.A.4
  • 27
    • 33845309117 scopus 로고    scopus 로고
    • Human shprh is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen
    • Unk I, Hajdú I, Fátyol K, et al. Human shprh is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A 2006;103:18107-12.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18107-18112
    • Unk, I.1    Hajdú, I.2    Fátyol, K.3
  • 28
    • 0004920274 scopus 로고    scopus 로고
    • Lactacystin enhances cisplatin sensitivity in resistant human ovarian cancer cell lines via inhibition of DNA repair and ERCC-1 expression
    • Li QQ, Yunmbam MK, Zhong X, et al. Lactacystin enhances cisplatin sensitivity in resistant human ovarian cancer cell lines via inhibition of DNA repair and ERCC-1 expression. Cell Mol Biol (Noisy-le-grand) 2001;47:OL61-72.
    • (2001) Cell Mol Biol (Noisy-le-grand , vol.47
    • Li, Q.Q.1    Yunmbam, M.K.2    Zhong, X.3
  • 29
    • 13444310626 scopus 로고    scopus 로고
    • Inducible degradation of checkpoint kinase 2 links to cisplatin-induced resistance in ovarian cancer cells
    • Zhang P, Gao W, Li H, Reed E, Chen F. Inducible degradation of checkpoint kinase 2 links to cisplatin-induced resistance in ovarian cancer cells. Biochem Biophys Res Commun 2005;328:567-72.
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 567-572
    • Zhang, P.1    Gao, W.2    Li, H.3    Reed, E.4    Chen, F.5
  • 30
    • 58149330694 scopus 로고    scopus 로고
    • Ubiquitin proteasome system stress underlies synergistic killing of ovarian cancer cells by bortezomib and a novel HDAC6 inhibitor
    • Bazzaro M, Lin Z, Santillan A, et al. Ubiquitin proteasome system stress underlies synergistic killing of ovarian cancer cells by bortezomib and a novel HDAC6 inhibitor. Clin Cancer Res 2008;14:7340-7.
    • (2008) Clin Cancer Res , vol.14 , pp. 7340-7347
    • Bazzaro, M.1    Lin, Z.2    Santillan, A.3
  • 31
    • 70349559496 scopus 로고    scopus 로고
    • Bortezomib-mediated expression of p27Kip1 through S-phase kinase protein 2 degradation in epithelial ovarian cancer
    • Uddin S, Ahmed M, Hussain AR, et al. Bortezomib-mediated expression of p27Kip1 through S-phase kinase protein 2 degradation in epithelial ovarian cancer. Lab Invest 2009;89:1115-27.
    • (2009) Lab Invest , vol.89 , pp. 1115-1127
    • Uddin, S.1    Ahmed, M.2    Hussain, A.R.3
  • 32
    • 78149423680 scopus 로고    scopus 로고
    • Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development
    • Al-Shami A, Jhaver KG, Vogel P, et al. Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development. PLoS One 2010;5:e13654.
    • (2010) PLoS One , vol.5
    • Al-Shami, A.1    Jhaver, K.G.2    Vogel, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.