메뉴 건너뛰기




Volumn 34, Issue 15, 2014, Pages 2800-2810

Autoactivation of the MDM2 E3 ligase by intramolecular interaction

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; CASPASE 3; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE E3;

EID: 84904307595     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00246-14     Document Type: Article
Times cited : (20)

References (61)
  • 1
  • 2
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN, Vousden KH. 1997. Regulation of p53 stability by Mdm2. Nature 387:299-303. http://dx.doi.org/10.1038/387299a0.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 3
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296-299. http://dx.doi.org/10.1038/387296a0.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 4
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano G. 1995. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378:203-206. http://dx.doi.org/10.1038/378203a0.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes de Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 5
    • 33644772395 scopus 로고    scopus 로고
    • Tissue-specific differences of p53 inhibition by Mdm2 and Mdm4
    • Grier JD, Xiong S, Elizondo-Fraire AC, Parant JM, Lozano G. 2006. Tissue-specific differences of p53 inhibition by Mdm2 and Mdm4. Mol. Cell. Biol. 26:192-198. http://dx.doi.org/10.1128/MCB.26.1.192-198.2006.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 192-198
    • Grier, J.D.1    Xiong, S.2    Elizondo-Fraire, A.C.3    Parant, J.M.4    Lozano, G.5
  • 6
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. 1995. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378:206- 208. http://dx.doi.org/10.1038/378206a0.
    • (1995) Nature , vol.378
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 10
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. 2000. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275:8945-8951. http://dx.doi.org/10.1074/jbc.275.12.8945.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 11
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. 1997. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420:25-27. http://dx.doi.org/10.1016/S0014-5793(97)01480-4.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 13
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, Prives C. 1997. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91:325-334. http://dx.doi.org/10.1016/S0092-8674(00)80416-X.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 14
    • 33745752959 scopus 로고    scopus 로고
    • Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression
    • Chao C, Herr D, Chun J, Xu Y. 2006. Ser18 and 23 phosphorylation is required for p53-dependent apoptosis and tumor suppression. EMBO J. 25:2615-2622. http://dx.doi.org/10.1038/sj.emboj.7601167.
    • (2006) EMBO J. , vol.25 , pp. 2615-2622
    • Chao, C.1    Herr, D.2    Chun, J.3    Xu, Y.4
  • 15
    • 72449125109 scopus 로고    scopus 로고
    • ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
    • Cheng Q, Chen L, Li Z, Lane WS, Chen J. 2009. ATM activates p53 by regulating MDM2 oligomerization and E3 processivity. EMBO J. 28: 3857-3867. http://dx.doi.org/10.1038/emboj.2009.294.
    • (2009) EMBO J. , vol.28 , pp. 3857-3867
    • Cheng, Q.1    Chen, L.2    Li, Z.3    Lane, W.S.4    Chen, J.5
  • 16
    • 83255162746 scopus 로고    scopus 로고
    • Regulation of MDM2 E3 ligase activity by phosphorylation after DNA damage
    • Cheng Q, Cross B, Li B, Chen L, Li Z, Chen J. 2011. Regulation of MDM2 E3 ligase activity by phosphorylation after DNA damage. Mol. Cell. Biol. 31:4951-4963. http://dx.doi.org/10.1128/MCB.05553-11.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4951-4963
    • Cheng, Q.1    Cross, B.2    Li, B.3    Chen, L.4    Li, Z.5    Chen, J.6
  • 18
    • 33747819484 scopus 로고    scopus 로고
    • Divorcing ARF and p53: an unsettled case
    • Sherr CJ. 2006. Divorcing ARF and p53: an unsettled case. Nat. Rev. Cancer 6:663-673. http://dx.doi.org/10.1038/nrc1954.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 663-673
    • Sherr, C.J.1
  • 19
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, Xiong Y. 2003. Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell. Biol. 23:8902-8912. http://dx.doi.org/10.1128/MCB.23.23.8902-8912.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 20
    • 0038724615 scopus 로고    scopus 로고
    • Regulation of HDM2 activity by the ribosomal protein L11
    • Lohrum MA, Ludwig RL, Kubbutat MH, Hanlon M, Vousden KH. 2003. Regulation of HDM2 activity by the ribosomal protein L11. Cancer Cell 3:577-587. http://dx.doi.org/10.1016/S1535-6108(03)00134-X.
    • (2003) Cancer Cell , vol.3 , pp. 577-587
    • Lohrum, M.A.1    Ludwig, R.L.2    Kubbutat, M.H.3    Hanlon, M.4    Vousden, K.H.5
  • 21
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • Deshaies RJ, Joazeiro CA. 2009. RING domain E3 ubiquitin ligases. Annu. Rev. Biochem. 78:399-434. http://dx.doi.org/10.1146/annurev.biochem.78.101807.093809.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 22
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation
    • Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. 2008. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134:995-1006. http://dx.doi.org/10.1016/j.cell.2008.07.022.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 24
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovova A, Jaffray EG, Tatham MH, Naismith JH, Hay RT. 2012. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489:115-120. http://dx.doi.org/10.1038/nature11376.
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovova, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 25
    • 0038788827 scopus 로고    scopus 로고
    • Critical contribution of the MDM2 acidic domain to p53 ubiquitination
    • Kawai H, Wiederschain D, Yuan ZM. 2003. Critical contribution of the MDM2 acidic domain to p53 ubiquitination. Mol. Cell. Biol. 23:4939- 4947. http://dx.doi.org/10.1128/MCB.23.14.4939-4947.2003.
    • (2003) Mol. Cell. Biol. , vol.23
    • Kawai, H.1    Wiederschain, D.2    Yuan, Z.M.3
  • 27
    • 25144496653 scopus 로고    scopus 로고
    • MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation
    • Wang C, Ivanov A, Chen L, Fredericks WJ, Seto E, Rauscher FJ, III, Chen J. 2005. MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation. EMBO J. 24:3279-3290. http://dx.doi.org/10.1038/sj.emboj.7600791.
    • (2005) EMBO J. , vol.24 , pp. 3279-3290
    • Wang, C.1    Ivanov, A.2    Chen, L.3    Fredericks, W.J.4    Seto, E.5    Rauscher, F.J.6    Chen, J.7
  • 30
    • 33244490784 scopus 로고    scopus 로고
    • Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway
    • Hu M, Gu L, Li M, Jeffrey PD, Gu W, Shi Y. 2006. Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. PLoS Biol. 4:e27. http://dx.doi.org/10.1371/journal.pbio.0040027.
    • (2006) PLoS Biol. , vol.4
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 31
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • Midgley CA, Desterro JM, Saville MK, Howard S, Sparks A, Hay RT, Lane DP. 2000. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19:2312- 2323. http://dx.doi.org/10.1038/sj.onc.1203593.
    • (2000) Oncogene , vol.19
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3    Howard, S.4    Sparks, A.5    Hay, R.T.6    Lane, D.P.7
  • 34
    • 0034697107 scopus 로고    scopus 로고
    • Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA
    • Burch LR, Midgley CA, Currie RA, Lane DP, Hupp TR. 2000. Mdm2 binding to a conformationally sensitive domain on p53 can be modulated by RNA. FEBS Lett. 472:93-98. http://dx.doi.org/10.1016/S0014-5793(00)01427-7.
    • (2000) FEBS Lett. , vol.472 , pp. 93-98
    • Burch, L.R.1    Midgley, C.A.2    Currie, R.A.3    Lane, D.P.4    Hupp, T.R.5
  • 35
    • 79955534071 scopus 로고    scopus 로고
    • Inhibition of p53 DNA binding function by the MDM2 protein acidic domain
    • Cross B, Chen L, Cheng Q, Li B, Yuan ZM, Chen J. 2011. Inhibition of p53 DNA binding function by the MDM2 protein acidic domain. J. Biol. Chem. 286:16018-16029. http://dx.doi.org/10.1074/jbc.M111.228981.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16018-16029
    • Cross, B.1    Chen, L.2    Cheng, Q.3    Li, B.4    Yuan, Z.M.5    Chen, J.6
  • 36
    • 34347205250 scopus 로고    scopus 로고
    • MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation
    • Sasaki M, Nie L, Maki CG. 2007. MDM2 binding induces a conformational change in p53 that is opposed by heat-shock protein 90 and precedes p53 proteasomal degradation. J. Biol. Chem. 282:14626-14634. http://dx.doi.org/10.1074/jbc.M610514200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14626-14634
    • Sasaki, M.1    Nie, L.2    Maki, C.G.3
  • 37
    • 57049095821 scopus 로고    scopus 로고
    • Function and structure of inherently disordered proteins
    • Dunker AK, Silman I, Uversky VN, Sussman JL. 2008. Function and structure of inherently disordered proteins. Curr. Opin. Struct. Biol. 18: 756-764. http://dx.doi.org/10.1016/j.sbi.2008.10.002.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 756-764
    • Dunker, A.K.1    Silman, I.2    Uversky, V.N.3    Sussman, J.L.4
  • 38
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6:197-208. http://dx.doi.org/10.1038/nrm1589.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 39
    • 0036340096 scopus 로고    scopus 로고
    • Hypophosphorylation of Mdm2 augments p53 stability
    • Blattner C, Hay T, Meek DW, Lane DP. 2002. Hypophosphorylation of Mdm2 augments p53 stability. Mol. Cell. Biol. 22:6170-6182. http://dx.doi.org/10.1128/MCB.22.17.6170-6182.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6170-6182
    • Blattner, C.1    Hay, T.2    Meek, D.W.3    Lane, D.P.4
  • 40
    • 11144328933 scopus 로고    scopus 로고
    • Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover
    • Winter M, Milne D, Dias S, Kulikov R, Knippschild U, Blattner C, Meek D. 2004. Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover. Biochemistry 43:16356-16364. http://dx.doi.org/10.1021/bi0489255.
    • (2004) Biochemistry , vol.43 , pp. 16356-16364
    • Winter, M.1    Milne, D.2    Dias, S.3    Kulikov, R.4    Knippschild, U.5    Blattner, C.6    Meek, D.7
  • 41
    • 23344447873 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance
    • Kulikov R, Boehme KA, Blattner C. 2005. Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance. Mol. Cell. Biol. 25:7170-7180. http://dx.doi.org/10.1128/MCB.25.16.7170-7180.2005.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7170-7180
    • Kulikov, R.1    Boehme, K.A.2    Blattner, C.3
  • 44
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ. 1993. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell. Biol. 13:4107-4114.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 47
    • 0030955170 scopus 로고    scopus 로고
    • Proteolytic cleavage of the mdm2 oncoprotein during apoptosis
    • Chen L, Marechal V, Moreau J, Levine AJ, Chen J. 1997. Proteolytic cleavage of the mdm2 oncoprotein during apoptosis. J. Biol. Chem. 272: 22966-22973. http://dx.doi.org/10.1074/jbc.272.36.22966.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22966-22973
    • Chen, L.1    Marechal, V.2    Moreau, J.3    Levine, A.J.4    Chen, J.5
  • 48
    • 56949108805 scopus 로고    scopus 로고
    • Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo
    • Sivakolundu SG, Nourse A, Moshiach S, Bothner B, Ashley C, Satumba J, Lahti J, Kriwacki RW. 2008. Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo. J. Mol. Biol. 384:240-254. http://dx.doi.org/10.1016/j.jmb.2008.09.019.
    • (2008) J. Mol. Biol. , vol.384 , pp. 240-254
    • Sivakolundu, S.G.1    Nourse, A.2    Moshiach, S.3    Bothner, B.4    Ashley, C.5    Satumba, J.6    Lahti, J.7    Kriwacki, R.W.8
  • 49
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: modular effectors of cellular regulation
    • Pufall MA, Graves BJ. 2002. Autoinhibitory domains: modular effectors of cellular regulation. Annu. Rev. Cell Dev. Biol. 18:421-462. http://dx.doi.org/10.1146/annurev.cellbio.18.031502.133614.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 50
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon TJ, Eck MJ. 2004. Structure and regulation of Src family kinases. Oncogene 23:7918-7927. http://dx.doi.org/10.1038/sj.onc.1208081.
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 51
    • 28944437358 scopus 로고    scopus 로고
    • Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation- induced E2F release
    • Rubin SM, Gall AL, Zheng N, Pavletich NP. 2005. Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation- induced E2F release. Cell 123:1093-1106. http://dx.doi.org/10.1016/j.cell.2005.09.044.
    • (2005) Cell , vol.123 , pp. 1093-1106
    • Rubin, S.M.1    Gall, A.L.2    Zheng, N.3    Pavletich, N.P.4
  • 52
    • 84871884749 scopus 로고    scopus 로고
    • Casein kinase 1alpha regulates an MDMX intramolecular interaction to stimulate p53 binding
    • Wu S, Chen L, Becker A, Schonbrunn E, Chen J. 2012. Casein kinase 1alpha regulates an MDMX intramolecular interaction to stimulate p53 binding. Mol. Cell. Biol. 32:4821-4832. http://dx.doi.org/10.1128/MCB.00851-12.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4821-4832
    • Wu, S.1    Chen, L.2    Becker, A.3    Schonbrunn, E.4    Chen, J.5
  • 53
    • 84887074375 scopus 로고    scopus 로고
    • MDMX contains an autoinhibitory sequence element
    • Bista M, Petrovich M, Fersht AR. 2013. MDMX contains an autoinhibitory sequence element. Proc. Natl. Acad. Sci. U. S. A. 110:17814-17819. http://dx.doi.org/10.1073/pnas.1317398110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 17814-17819
    • Bista, M.1    Petrovich, M.2    Fersht, A.R.3
  • 54
    • 84864279057 scopus 로고    scopus 로고
    • Mutational analysis reveals a dual role ofMdm2acidic domain in the regulation of p53 stability
    • Dolezelova P, Cetkovska K, Vousden KH, Uldrijan S. 2012. Mutational analysis reveals a dual role ofMdm2acidic domain in the regulation of p53 stability. FEBS Lett. 586:2225-2231. http://dx.doi.org/10.1016/j.febslet.2012.05.034.
    • (2012) FEBS Lett. , vol.586 , pp. 2225-2231
    • Dolezelova, P.1    Cetkovska, K.2    Vousden, K.H.3    Uldrijan, S.4
  • 55
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP. 1996. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274:948-953. http://dx.doi.org/10.1126/science.274.5289.948.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 56
    • 31344438433 scopus 로고    scopus 로고
    • Solution structure of the C4 zinc finger domain of HDM2
    • Yu GW, Allen MD, Andreeva A, Fersht AR, Bycroft M. 2006. Solution structure of the C4 zinc finger domain of HDM2. Protein Sci. 15:384-389. http://dx.doi.org/10.1110/ps.051927306.
    • (2006) Protein Sci. , vol.15 , pp. 384-389
    • Yu, G.W.1    Allen, M.D.2    Andreeva, A.3    Fersht, A.R.4    Bycroft, M.5
  • 57
    • 42149105590 scopus 로고    scopus 로고
    • Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
    • Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL. 2008. Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell Death Differ. 15:841-848. http://dx.doi.org/10.1038/sj.cdd.4402309.
    • (2008) Cell Death Differ. , vol.15 , pp. 841-848
    • Linke, K.1    Mace, P.D.2    Smith, C.A.3    Vaux, D.L.4    Silke, J.5    Day, C.L.6
  • 58
    • 84873055344 scopus 로고    scopus 로고
    • MDM2, MDMX and p53 in oncogenesis and cancer therapy
    • Wade M, Li YC, Wahl GM. 2013. MDM2, MDMX and p53 in oncogenesis and cancer therapy. Nat. Rev. Cancer 13:83-96. http://dx.doi.org/10.1038/nrc3430.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 83-96
    • Wade, M.1    Li, Y.C.2    Wahl, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.