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Volumn 30, Issue 6, 2013, Pages 2871-2877

Lentivirus-mediated inhibition of USP39 suppresses the growth of breast cancer cells in vitro

Author keywords

Breast cancer; Deubiquitinating enzyme; Lentivirus; RNA interference; USP39

Indexed keywords

DEUBIQUITINASE; SHORT HAIRPIN RNA; UBIQUITIN SPECIFIC PROTEASE 39; UNCLASSIFIED DRUG; USP39;

EID: 84892421621     PISSN: 1021335X     EISSN: 17912431     Source Type: Journal    
DOI: 10.3892/or.2013.2798     Document Type: Article
Times cited : (40)

References (29)
  • 2
    • 84879297257 scopus 로고    scopus 로고
    • Chemopreventive and chemotherapeutic potential of curcumin in breast cancer
    • Sinha D, Biswas J, Sung B, Aggarwal BB and Bishayee A: Chemopreventive and chemotherapeutic potential of curcumin in breast cancer. Curr Drug Targets 13: 1799-1819, 2012.
    • (2012) Curr Drug Targets , vol.13 , pp. 1799-1819
    • Sinha, D.1    Biswas, J.2    Sung, B.3    Aggarwal, B.B.4    Bishayee, A.5
  • 3
    • 62249157059 scopus 로고    scopus 로고
    • An introduction to molecular targeted therapy of cancer
    • Allgayer H and Fulda S: An introduction to molecular targeted therapy of cancer. Adva Med Sci 53: 130-138, 2008.
    • (2008) Adva Med Sci , vol.53 , pp. 130-138
    • Allgayer, H.1    Fulda, S.2
  • 4
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM and Eddins MJ: Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695: 55-72, 2004.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 5
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart CM and Fushman D: Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 8: 610-616, 2004.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 6
    • 1842486790 scopus 로고    scopus 로고
    • Ubiquitin and breast cancer
    • Ohta T and Fukuda M: Ubiquitin and breast cancer. Oncogene 23: 2079-2088, 2004.
    • (2004) Oncogene , vol.23 , pp. 2079-2088
    • Ohta, T.1    Fukuda, M.2
  • 7
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson KD: Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J 11: 1245-1256, 1997.
    • (1997) FASEB J , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 8
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • Nijman SM, Luna-Vargas MP, Velds A, et al: A genomic and functional inventory of deubiquitinating enzymes. Cell 123: 773-786, 2005.
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.1    Luna-Vargas, M.P.2    Velds, A.3
  • 9
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu FE, Ventii KH and Wilkinson KD: Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78: 363-397, 2009.
    • (2009) Annu Rev Biochem , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 10
    • 0035873254 scopus 로고    scopus 로고
    • The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP are essential for the assembly of mature spliceosomes
    • Makarova OV, Makarov EM and Luhrmann R: The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP are essential for the assembly of mature spliceosomes. EMBO J 20: 2553-2563, 2001.
    • (2001) EMBO J , vol.20 , pp. 2553-2563
    • Makarova, O.V.1    Makarov, E.M.2    Luhrmann, R.3
  • 11
    • 50849116784 scopus 로고    scopus 로고
    • Usp39 is essential for mitotic spindle checkpoint integrity and controls mRNA-levels of aurora B
    • van Leuken RJ, Luna-Vargas MP, Sixma TK, Wolthuis RM and Medema RH: Usp39 is essential for mitotic spindle checkpoint integrity and controls mRNA-levels of aurora B. Cell Cycle 7: 2710-2719, 2008.
    • (2008) Cell Cycle , vol.7 , pp. 2710-2719
    • Van Leuken, R.J.1    Luna-Vargas, M.P.2    Sixma, T.K.3    Wolthuis, R.M.4    Medema, R.H.5
  • 12
    • 79851480297 scopus 로고    scopus 로고
    • Zebrafish usp39 mutation leads to rb1 mRNA splicing defect and pituitary lineage expansion
    • Rios Y, Melmed S, Lin S and Liu NA: Zebrafish usp39 mutation leads to rb1 mRNA splicing defect and pituitary lineage expansion. PLoS Genet 7: e1001271, 2011.
    • (2011) PLoS Genet , vol.7
    • Rios, Y.1    Melmed, S.2    Lin, S.3    Liu, N.A.4
  • 13
    • 14644435784 scopus 로고    scopus 로고
    • Short interfering RNAs as a tool for cancer gene therapy
    • Izquierdo M: Short interfering RNAs as a tool for cancer gene therapy. Cancer Gene Ther 12: 217-227, 2005.
    • (2005) Cancer Gene Ther , vol.12 , pp. 217-227
    • Izquierdo, M.1
  • 14
    • 0037422583 scopus 로고    scopus 로고
    • Inhibiting HIV-1 infection in human T cells by lentiviral-mediated delivery of small interfering RNA against CCR5
    • Qin XF, An DS, Chen IS and Baltimore D: Inhibiting HIV-1 infection in human T cells by lentiviral-mediated delivery of small interfering RNA against CCR5. Proc Natl Acad Sci USA 100: 183-188, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 183-188
    • Qin, X.F.1    An, D.S.2    Chen, I.S.3    Baltimore, D.4
  • 15
    • 0036468145 scopus 로고    scopus 로고
    • A specific protein substrate for a deubiquitinating enzyme: Liquid facets is the substrate of Fat facets
    • Chen X, Zhang B and Fischer JA: A specific protein substrate for a deubiquitinating enzyme: liquid facets is the substrate of Fat facets. Genes Dev 16: 289-294, 2002.
    • (2002) Genes Dev , vol.16 , pp. 289-294
    • Chen, X.1    Zhang, B.2    Fischer, J.A.3
  • 16
    • 31644448703 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase L1 regulates the morphology of neural progenitor cells and modulates their differentiation
    • Sakurai M, Ayukawa K, Setsuie R, et al: Ubiquitin C-terminal hydrolase L1 regulates the morphology of neural progenitor cells and modulates their differentiation. J Cell Sci 119: 162-171, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 162-171
    • Sakurai, M.1    Ayukawa, K.2    Setsuie, R.3
  • 17
    • 34548434688 scopus 로고    scopus 로고
    • Emerging roles of deubiquitinating enzymes in human cancer
    • Yang JM: Emerging roles of deubiquitinating enzymes in human cancer. Acta Pharmacologica Sin 28: 1325-1330, 2007.
    • (2007) Acta Pharmacologica Sin , vol.28 , pp. 1325-1330
    • Yang, J.M.1
  • 18
    • 31444449609 scopus 로고    scopus 로고
    • A novel and cytogenetically cryptic t(7;21)(p22;q22) in acute myeloid leukemia results in fusion of RUNX1 with the ubiquitin-specific protease gene USP42
    • Paulsson K, Békassy AN, Olofsson T, Mitelman F, Johansson B and Panagopoulos I: A novel and cytogenetically cryptic t(7;21)(p22;q22) in acute myeloid leukemia results in fusion of RUNX1 with the ubiquitin-specific protease gene USP42. Leukemia 20: 224-229, 2006.
    • (2006) Leukemia , vol.20 , pp. 224-229
    • Paulsson, K.1    Békassy, A.N.2    Olofsson, T.3    Mitelman, F.4    Johansson, B.5    Panagopoulos, I.6
  • 19
    • 84863356095 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP2a enhances tumor progression by targeting cyclin A1 in bladder cancer
    • Kim J, Kim WJ, Liu Z, Loda M and Freeman MR: The ubiquitin-specific protease USP2a enhances tumor progression by targeting cyclin A1 in bladder cancer. Cell Cycle 11: 1123-1130, 2012.
    • (2012) Cell Cycle , vol.11 , pp. 1123-1130
    • Kim, J.1    Kim, W.J.2    Liu, Z.3    Loda, M.4    Freeman, M.R.5
  • 21
    • 13244291457 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway
    • Nijman SM, Huang TT, Dirac AM, et al: The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway. Mol Cell 17: 331-339, 2005.
    • (2005) Mol Cell , vol.17 , pp. 331-339
    • Nijman, S.M.1    Huang, T.T.2    Dirac, A.M.3
  • 22
    • 33645708319 scopus 로고    scopus 로고
    • Regulation of monoubiquitinated PCNA by DUB autocleavage
    • Huang TT, Nijman SM, Mirchandani KD, et al: Regulation of monoubiquitinated PCNA by DUB autocleavage. Nat Cell Biol 8: 339-347, 2006.
    • (2006) Nat Cell Biol , vol.8 , pp. 339-347
    • Huang, T.T.1    Nijman, S.M.2    Mirchandani, K.D.3
  • 23
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang D, Zaugg K, Mak TW and Elledge SJ: A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 126: 529-542, 2006.
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 24
    • 35848942129 scopus 로고    scopus 로고
    • Fbw7 and Usp28 regulate myc protein stability in response to DNA damage
    • Popov N, Herold S, Llamazares M, Schulein C and Eilers M: Fbw7 and Usp28 regulate myc protein stability in response to DNA damage. Cell Cycle 6: 2327-2331, 2007.
    • (2007) Cell Cycle , vol.6 , pp. 2327-2331
    • Popov, N.1    Herold, S.2    Llamazares, M.3    Schulein, C.4    Eilers, M.5
  • 25
    • 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 and 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 24: 7444-7455, 2004.
    • (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
  • 26
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M, Chen D, Shiloh A, et al: Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416: 648-653, 2002.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3
  • 28
    • 75749132016 scopus 로고    scopus 로고
    • USP10 regulates p53 localization and stability by deubiquitinating p53
    • Yuan J, Luo K, Zhang L, Cheville JC and Lou Z: USP10 regulates p53 localization and stability by deubiquitinating p53. Cell 140: 384-396, 2010.
    • (2010) Cell , vol.140 , pp. 384-396
    • Yuan, J.1    Luo, K.2    Zhang, L.3    Cheville, J.C.4    Lou, Z.5
  • 29
    • 0033056024 scopus 로고    scopus 로고
    • A novel genetic screen for snRNP assembly factors in yeast identifies a conserved protein, Sad1p, also required for pre-mRNA splicing
    • Lygerou Z, Christophides G and Seraphin B: A novel genetic screen for snRNP assembly factors in yeast identifies a conserved protein, Sad1p, also required for pre-mRNA splicing. Mol Cell Biol 19: 2008-2020, 1999.
    • (1999) Mol Cell Biol , vol.19 , pp. 2008-2020
    • Lygerou, Z.1    Christophides, G.2    Seraphin, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.