메뉴 건너뛰기




Volumn 410, Issue 1, 2011, Pages 119-128

Interaction and co-localization of JC virus large T antigen and the F-box protein β-transducin-repeat containing protein

Author keywords

catenin; TrCP; JCV T antigen; Oncogenic potential; Proteasomal degradation

Indexed keywords

BETA CATENIN; BETA TRANSDUCIN REPEAT CONTAINING PROTEIN; BETA TRANSDUCIN REPEAT CONTAINING PROTEIN 1; BETA TRANSDUCIN REPEAT CONTAINING PROTEIN 2; F BOX PROTEIN; MUTANT PROTEIN; PROTEASOME; UNCLASSIFIED DRUG; VIRUS LARGE T ANTIGEN;

EID: 78650752833     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.10.038     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 1542317755 scopus 로고    scopus 로고
    • Cul7/p185/p193 binding to simian virus 40 large T antigen has a role in cellular transformation
    • Ali S.H., Kasper J.S., Arai T., DeCaprio J.A. Cul7/p185/p193 binding to simian virus 40 large T antigen has a role in cellular transformation. J. Virol. 2004, 78:2749-2757.
    • (2004) J. Virol. , vol.78 , pp. 2749-2757
    • Ali, S.H.1    Kasper, J.S.2    Arai, T.3    DeCaprio, J.A.4
  • 2
    • 33746676801 scopus 로고    scopus 로고
    • Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing 53 function
    • Andrews P., He Y.J., Xiong Y. Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing 53 function. Oncogene 2006, 25:4534-4548.
    • (2006) Oncogene , vol.25 , pp. 4534-4548
    • Andrews, P.1    He, Y.J.2    Xiong, Y.3
  • 3
    • 0345791500 scopus 로고    scopus 로고
    • HIV-1 Vpu sequesters beta-transducin repeat-containing protein (βTrCP) in the cytoplasm and provokes the accumulation of beta-catenin and other SCFβTrCP substrates
    • Besnard-Guerin C., Belaïdouni N., Lassot I., Segeral E., Jobart A., Marchal C., Benarous R. HIV-1 Vpu sequesters beta-transducin repeat-containing protein (βTrCP) in the cytoplasm and provokes the accumulation of beta-catenin and other SCFβTrCP substrates. J. Biol. Chem. 2004, 279:788-795.
    • (2004) J. Biol. Chem. , vol.279 , pp. 788-795
    • Besnard-Guerin, C.1    Belaïdouni, N.2    Lassot, I.3    Segeral, E.4    Jobart, A.5    Marchal, C.6    Benarous, R.7
  • 4
    • 36849066434 scopus 로고    scopus 로고
    • A novel role of Rac1 GTPase in JCV T-antigen-mediated β-catenin stabilization
    • Bhattacharyya R., Khalili K. A novel role of Rac1 GTPase in JCV T-antigen-mediated β-catenin stabilization. Oncogene 2007, 26:7628-7636.
    • (2007) Oncogene , vol.26 , pp. 7628-7636
    • Bhattacharyya, R.1    Khalili, K.2
  • 5
    • 0026755926 scopus 로고
    • PAb 2000 specifically recognizes the large T and small t proteins of JC virus
    • Bollag B., Frisque R.J. PAb 2000 specifically recognizes the large T and small t proteins of JC virus. Virus Res. 1992, 25:223-239.
    • (1992) Virus Res. , vol.25 , pp. 223-239
    • Bollag, B.1    Frisque, R.J.2
  • 6
    • 0034663285 scopus 로고    scopus 로고
    • Purified JC virus T and T' proteins differentially interact with the retinoblastoma family of tumor suppressor proteins
    • Bollag B., Prins C., Snyder E.L., Frisque R.J. Purified JC virus T and T' proteins differentially interact with the retinoblastoma family of tumor suppressor proteins. Virology 2000, 274:165-178.
    • (2000) Virology , vol.274 , pp. 165-178
    • Bollag, B.1    Prins, C.2    Snyder, E.L.3    Frisque, R.J.4
  • 7
    • 33845489472 scopus 로고    scopus 로고
    • JC virus T'135, T'136 and T'165 proteins interact with cellular p107 and p130 in vivo and influence viral transformation potential
    • Bollag B., Kilpatrick L.H., Tyagarajan S.K., Tevethia M.J., Frisque R.J. JC virus T'135, T'136 and T'165 proteins interact with cellular p107 and p130 in vivo and influence viral transformation potential. J. Neurovirol. 2006, 12:428-442.
    • (2006) J. Neurovirol. , vol.12 , pp. 428-442
    • Bollag, B.1    Kilpatrick, L.H.2    Tyagarajan, S.K.3    Tevethia, M.J.4    Frisque, R.J.5
  • 8
    • 77956500009 scopus 로고    scopus 로고
    • JC virus small t antigen binds phosphatase PP2A and Rb family proteins and is required for efficient viral DNA replication activity
    • Bollag B., Hofstetter C., Reviriego-Mendoza M.M., Frisque R.J. JC virus small t antigen binds phosphatase PP2A and Rb family proteins and is required for efficient viral DNA replication activity. PLoS ONE 2010, 5:e10606.
    • (2010) PLoS ONE , vol.5
    • Bollag, B.1    Hofstetter, C.2    Reviriego-Mendoza, M.M.3    Frisque, R.J.4
  • 9
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B
    • Bour S., Perrin C., Akari H., Strebel K. The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B. J. Biol. Chem. 2001, 276:15920-15928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 11
    • 41149094512 scopus 로고    scopus 로고
    • Regulation of DNA repair throughout the cell cycle
    • Branzei D., Foiani M. Regulation of DNA repair throughout the cell cycle. Nat. Rev. Mol. Cell Biol. 2008, 9:297-308.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 297-308
    • Branzei, D.1    Foiani, M.2
  • 13
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: insights into a molecular machine
    • Cardozo T., Pagano M. The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol. 2004, 5:739-751.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 15
    • 35548929728 scopus 로고    scopus 로고
    • G2/M cycle arrest in the life cycle of viruses
    • Davy C., Doorbar J. G2/M cycle arrest in the life cycle of viruses. Virology 2007, 368:219-226.
    • (2007) Virology , vol.368 , pp. 219-226
    • Davy, C.1    Doorbar, J.2
  • 17
    • 0036894604 scopus 로고    scopus 로고
    • Association of human polyomavirus JCV with colon cancer: evidence for interaction of viral T-antigen and beta-catenin
    • Enam S., Del Valle L., Lara C., Gan D.D., Ortiz-Hidalgo C., Palazzo J.P., Khalili K. Association of human polyomavirus JCV with colon cancer: evidence for interaction of viral T-antigen and beta-catenin. Cancer Res. 2002, 62:7093-7101.
    • (2002) Cancer Res. , vol.62 , pp. 7093-7101
    • Enam, S.1    Del Valle, L.2    Lara, C.3    Gan, D.D.4    Ortiz-Hidalgo, C.5    Palazzo, J.P.6    Khalili, K.7
  • 19
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP1: tipping the scales of cancer
    • Frescas D., Pagano M. Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP1: 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
  • 20
    • 0002551699 scopus 로고
    • The molecular biology of JC virus, causative agent of progressive multifocal leukoencephalopathy
    • Humana Press, Totowa NJ, R.P. Roos (Ed.)
    • Frisque R.J., White F.A.I.I.I. The molecular biology of JC virus, causative agent of progressive multifocal leukoencephalopathy. Molecular Neurovirology 1992, 25-158. Humana Press, Totowa NJ. R.P. Roos (Ed.).
    • (1992) Molecular Neurovirology , pp. 25-158
    • Frisque, R.J.1    White, F.A.I.I.I.2
  • 23
    • 0033602475 scopus 로고    scopus 로고
    • HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin
    • Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z. HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin. Oncogene 1999, 18:2039-2046.
    • (1999) Oncogene , vol.18 , pp. 2039-2046
    • Fuchs, S.Y.1    Chen, A.2    Xiong, Y.3    Pan, Z.Q.4    Ronai, Z.5
  • 24
    • 1942502180 scopus 로고    scopus 로고
    • The many faces of β-TrCP E3 ubiquitin ligases: reflections in the magic mirror of cancer
    • Fuchs S.Y., Spiegelman V.S., Kumar K.G. The many faces of β-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
  • 25
    • 0033781272 scopus 로고    scopus 로고
    • The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 nodification, and ubiquitin ligase activity of CUL1
    • Furukawa M., Zhang Y., McCarville Y., Ohta T., Xiong Y. The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 nodification, and ubiquitin ligase activity of CUL1. Mol. Cell. Biol. 2000, 20:8185-8197.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8185-8197
    • Furukawa, M.1    Zhang, Y.2    McCarville, Y.3    Ohta, T.4    Xiong, Y.5
  • 26
    • 0842265028 scopus 로고    scopus 로고
    • Interaction between JCV large T-antigen and beta-catenin
    • Gan D.D., Khalili K. Interaction between JCV large T-antigen and beta-catenin. Oncogene 2004, 23:483-490.
    • (2004) Oncogene , vol.23 , pp. 483-490
    • Gan, D.D.1    Khalili, K.2
  • 27
    • 0019351935 scopus 로고
    • SV40-transformed simian cells support the replication of early SV40 mutants
    • Gluzman Y. SV40-transformed simian cells support the replication of early SV40 mutants. Cell 1981, 23:175-182.
    • (1981) Cell , vol.23 , pp. 175-182
    • Gluzman, Y.1
  • 28
    • 0019401161 scopus 로고
    • Monoclonal antibodies specific for simian virus 40 tumor antigens
    • Harlow E., Crawford L.V., Pim D.C., Williamson N.M. Monoclonal antibodies specific for simian virus 40 tumor antigens. J. Virol. 1981, 39:861-869.
    • (1981) J. Virol. , vol.39 , pp. 861-869
    • Harlow, E.1    Crawford, L.V.2    Pim, D.C.3    Williamson, N.M.4
  • 29
    • 63449111028 scopus 로고    scopus 로고
    • Warts, cancer and ubiquitylation: lessons from the papillomaviruses
    • Howley P. Warts, cancer and ubiquitylation: lessons from the papillomaviruses. Trans. Am. Clin. Climatol. Assoc. 2006, 117:113-126.
    • (2006) Trans. Am. Clin. Climatol. Assoc. , vol.117 , pp. 113-126
    • Howley, P.1
  • 30
    • 18144413891 scopus 로고    scopus 로고
    • β-TrCP recognizes a previously undescribed nonphosphorylated destruction motif in Cdc25A and Cdc25B phosphatases
    • Kanemori Y., Uto K., Sagata N. β-TrCP recognizes a previously undescribed nonphosphorylated destruction motif in Cdc25A and Cdc25B phosphatases. Proc. Natl Acad. Sci. USA 2005, 102:6279-6284.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6279-6284
    • Kanemori, Y.1    Uto, K.2    Sagata, N.3
  • 31
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NFκB activity
    • Karin M., Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NFκB activity. Annu. Rev. Immunol. 2000, 18:621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 32
    • 24644525084 scopus 로고    scopus 로고
    • Simian virus 40 large T antigen's association with the CUL7 SCF complex contributes to cellular transformation
    • Kasper J.S., Kuwabara H., Arai T., Ali S.H., DeCaprio J.A. Simian virus 40 large T antigen's association with the CUL7 SCF complex contributes to cellular transformation. J. Virol. 2005, 79:11685-11692.
    • (2005) J. Virol. , vol.79 , pp. 11685-11692
    • Kasper, J.S.1    Kuwabara, H.2    Arai, T.3    Ali, S.H.4    DeCaprio, J.A.5
  • 34
    • 33745616856 scopus 로고    scopus 로고
    • The polyomavirus, JCV and its involvement in human disease
    • Khalili K., Gordon J., White M.K. The polyomavirus, JCV and its involvement in human disease. Adv. Exp. Med. Biol. 2006, 577:274-287.
    • (2006) Adv. Exp. Med. Biol. , vol.577 , pp. 274-287
    • Khalili, K.1    Gordon, J.2    White, M.K.3
  • 35
    • 33845351956 scopus 로고    scopus 로고
    • β-catenin destruction complex: insights and questions from a structural perspective
    • Kimelman D., Xu W. β-catenin destruction complex: insights and questions from a structural perspective. Oncogene 2006, 25:7482-7491.
    • (2006) Oncogene , vol.25 , pp. 7482-7491
    • Kimelman, D.1    Xu, W.2
  • 37
    • 0026576333 scopus 로고
    • Simian virus 40 large T antigen stably complexes with a 185-kilodalton host protein
    • Kohrman D.C., Imperiale M.J. Simian virus 40 large T antigen stably complexes with a 185-kilodalton host protein. J. Virol. 1992, 66:1752-1760.
    • (1992) J. Virol. , vol.66 , pp. 1752-1760
    • Kohrman, D.C.1    Imperiale, M.J.2
  • 39
    • 0142105396 scopus 로고    scopus 로고
    • SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor
    • Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y. SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor. EMBO J. 2003, 22:5480-5490.
    • (2003) EMBO J. , vol.22 , pp. 5480-5490
    • Kumar, K.G.1    Tang, W.2    Ravindranath, A.K.3    Clark, W.A.4    Croze, E.5    Fuchs, S.Y.6
  • 40
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting of the ubiquitin system
    • Laney J.D., Hochstrasser M. Substrate targeting of the ubiquitin system. Cell 1999, 97:427-430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 41
    • 59349107940 scopus 로고    scopus 로고
    • The common mechanisms of transformation by the small DNA tumor viruses: the inactivation of tumor suppressor gene products: p53
    • Levine A.J. The common mechanisms of transformation by the small DNA tumor viruses: the inactivation of tumor suppressor gene products: p53. Virology 2009, 384:285-293.
    • (2009) Virology , vol.384 , pp. 285-293
    • Levine, A.J.1
  • 42
    • 1942453784 scopus 로고    scopus 로고
    • Negative regulation of prolactin receptor stability and signaling mediated by SCF(beta-TrCP) E3 ubiquitin ligase
    • Li Y., Kumar K.G., Tang W., Spiegelman V.S., Fuchs S.Y. Negative regulation of prolactin receptor stability and signaling mediated by SCF(beta-TrCP) E3 ubiquitin ligase. Mol. Cell. Biol. 2004, 24:4038-4048.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4038-4048
    • Li, Y.1    Kumar, K.G.2    Tang, W.3    Spiegelman, V.S.4    Fuchs, S.Y.5
  • 43
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J., Pigue V. HIV-1 Vpu neutralizes the antiviral factor tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog. 2009, 5:e1000574.
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Pigue, V.6
  • 44
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin F., Bour S.P., Durand H., Selig L., Benichou S., Richard V., Thomas D., Strebel K., Benarous R. A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1998, 14:565-574.
    • (1998) Mol. Cell , vol.14 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 45
    • 70649102943 scopus 로고    scopus 로고
    • Destabilization of Rb by human papillomavirus E7 is cell cycle dependent: E2-25K is involved in the proteolysis
    • Oh K.J., Kalinina A., Bagchi S. Destabilization of Rb by human papillomavirus E7 is cell cycle dependent: E2-25K is involved in the proteolysis. Virology 2010, 396:118-124.
    • (2010) Virology , vol.396 , pp. 118-124
    • Oh, K.J.1    Kalinina, A.2    Bagchi, S.3
  • 46
    • 34047189884 scopus 로고    scopus 로고
    • A critical role for FBXW8 and MAPK in cyclin D1 degradation and cancer cell proliferation
    • Okabe H., Lee S.H., Phuchareon J., Albertson D.G., McCormick F., Tetsu O. A critical role for FBXW8 and MAPK in cyclin D1 degradation and cancer cell proliferation. PLoS ONE 2006, 1:e128.
    • (2006) PLoS ONE , vol.1
    • Okabe, H.1    Lee, S.H.2    Phuchareon, J.3    Albertson, D.G.4    McCormick, F.5    Tetsu, O.6
  • 47
    • 74049130966 scopus 로고    scopus 로고
    • Large T antigen promotes JC virus replication in G2-arrested cells by inducing ATM- and ATR-mediated G2 checkpoint signaling
    • Orba Y., Suzuki T., Makino Y., Kubota K., Tanaka S., Kimura T., Sawa H. Large T antigen promotes JC virus replication in G2-arrested cells by inducing ATM- and ATR-mediated G2 checkpoint signaling. J. Biol. Chem. 2010, 285:1544-1554.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1544-1554
    • Orba, Y.1    Suzuki, T.2    Makino, Y.3    Kubota, K.4    Tanaka, S.5    Kimura, T.6    Sawa, H.7
  • 48
    • 0035099918 scopus 로고    scopus 로고
    • Role of T antigen interactions with p53 in tumorigenesis
    • Pipas J., Levine A.J. Role of T antigen interactions with p53 in tumorigenesis. Semin. Cancer Biol. 2001, 11:23-30.
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 23-30
    • Pipas, J.1    Levine, A.J.2
  • 49
    • 0034643433 scopus 로고    scopus 로고
    • Differential interaction of palkoglobin and β-catenin with the ubiquitin-proteasome system
    • Sadot E., Simcha I., Iwai K., Ciechanover A., Geiger B., Ben-Ze'ev A. Differential interaction of palkoglobin and β-catenin with the ubiquitin-proteasome system. Oncogene 2000, 19:1992-2001.
    • (2000) Oncogene , vol.19 , pp. 1992-2001
    • Sadot, E.1    Simcha, I.2    Iwai, K.3    Ciechanover, A.4    Geiger, B.5    Ben-Ze'ev, A.6
  • 50
    • 42049096542 scopus 로고    scopus 로고
    • Plk1- and β-TrCP-dependent degradation of Bora controls mitotic progression
    • Seki A., Coppinger J.A., Du H., Jang C.-Y., Yates J.R., Fang G. Plk1- and β-TrCP-dependent degradation of Bora controls mitotic progression. J. Cell Biol. 2008, 181:65-78.
    • (2008) J. Cell Biol. , vol.181 , pp. 65-78
    • Seki, A.1    Coppinger, J.A.2    Du, H.3    Jang, C.-Y.4    Yates, J.R.5    Fang, G.6
  • 51
    • 2942629346 scopus 로고    scopus 로고
    • Tumor viruses and cell signaling pathways: deubiquitination versus ubiquitination
    • Shackelford J., Pagano J.S. Tumor viruses and cell signaling pathways: deubiquitination versus ubiquitination. Mol. Cell. Biol. 2004, 24:5089-5093.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5089-5093
    • Shackelford, J.1    Pagano, J.S.2
  • 52
    • 0018765428 scopus 로고
    • Subcellular localization of simian virus 40 large tumor antigen
    • Soule H.R., Butel J.S. Subcellular localization of simian virus 40 large tumor antigen. J. Virol. 1979, 30:523-532.
    • (1979) J. Virol. , vol.30 , pp. 523-532
    • Soule, H.R.1    Butel, J.S.2
  • 53
    • 0026801128 scopus 로고
    • Antibody response to human papovavirus JC (JCV) and simian virus-40 (SV40) T-antigens in SV40 T-antigen transgenic mice
    • Tevethia S.S., Epler M., Georgoff I., Teresky A., Marlow M., Levine A.J. Antibody response to human papovavirus JC (JCV) and simian virus-40 (SV40) T-antigens in SV40 T-antigen transgenic mice. Virology 1992, 190:195-206.
    • (1992) Virology , vol.190 , pp. 195-206
    • Tevethia, S.S.1    Epler, M.2    Georgoff, I.3    Teresky, A.4    Marlow, M.5    Levine, A.J.6
  • 55
    • 14844312051 scopus 로고    scopus 로고
    • The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4
    • Welcker M., Clurman B.E. The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4. J. Biol. Chem. 2005, 280:7654-7658.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7654-7658
    • Welcker, M.1    Clurman, B.E.2
  • 57
    • 0033068154 scopus 로고    scopus 로고
    • The SCFβ-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • Winston J.T., Strack P., Beer-Romero P., Chu C.Y., Elledge S.J., Harper J.W. The SCFβ-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 1999, 13:270-283.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.