메뉴 건너뛰기




Volumn 21, Issue 12, 2001, Pages 3974-3985

The corepressor mSin3a interacts with the proline-rich domain of p53 and protects p53 from proteasome-mediated degradation

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROLINE; PROTEASOME; PROTEIN P53; REPRESSOR PROTEIN;

EID: 0035021122     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.12.3974-3985.2001     Document Type: Article
Times cited : (103)

References (53)
  • 1
    • 0033592653 scopus 로고    scopus 로고
    • Down-regulation of the stathmin/Op18 and FKBP25 genes following p53 induction
    • Ahn, J., M. Murphy, S. Kratowicz, A. Wang, A. J. Levine, and D. L. George. 1999. Down-regulation of the stathmin/Op18 and FKBP25 genes following p53 induction. Oncogene 18:5954-5958.
    • (1999) Oncogene , vol.18 , pp. 5954-5958
    • Ahn, J.1    Murphy, M.2    Kratowicz, S.3    Wang, A.4    Levine, A.J.5    George, D.L.6
  • 2
    • 0033572417 scopus 로고    scopus 로고
    • Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation
    • Alarcon, R., C. Koumenis, R. K. Geyer, C. G. Maki, and A. J. Giaccia. 1999. Hypoxia induces p53 accumulation through MDM2 down-regulation and inhibition of E6-mediated degradation. Cancer Res. 59:6046-6051.
    • (1999) Cancer Res. , vol.59 , pp. 6046-6051
    • Alarcon, R.1    Koumenis, C.2    Geyer, R.K.3    Maki, C.G.4    Giaccia, A.J.5
  • 3
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylases: Transcriptional repression with SINers and NuRDs
    • Ayer, D. E. 1999. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9:193-198.
    • (1999) Trends Cell Biol. , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 4
    • 0025367297 scopus 로고
    • Genetic and immunochemical analysis of mutant p53 in human breast cancer cell lines
    • Bartek, J., R. Iggo, J. Gannon, and D. P. Lane. 1990. Genetic and immunochemical analysis of mutant p53 in human breast cancer cell lines. Oncogene 5:893-899.
    • (1990) Oncogene , vol.5 , pp. 893-899
    • Bartek, J.1    Iggo, R.2    Gannon, J.3    Lane, D.P.4
  • 5
    • 0031058283 scopus 로고    scopus 로고
    • Antisense targeting of E6AP elevates p53 in HPV-infected cells but not in normal cells
    • Beer-Romero, P., S. Glass, and M. Rolfe. 1997. Antisense targeting of E6AP elevates p53 in HPV-infected cells but not in normal cells. Oncogene 14: 595-602.
    • (1997) Oncogene , vol.14 , pp. 595-602
    • Beer-Romero, P.1    Glass, S.2    Rolfe, M.3
  • 6
    • 0031282325 scopus 로고    scopus 로고
    • Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo
    • Bottger, A., V. Bottger, A. Sparks, W. Liu, S. F. Howard, and D. P. Lane. 1997. Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr. Biol. 7:860-869.
    • (1997) Curr. Biol. , vol.7 , pp. 860-869
    • Bottger, A.1    Bottger, V.2    Sparks, A.3    Liu, W.4    Howard, S.F.5    Lane, D.P.6
  • 7
    • 0033598754 scopus 로고    scopus 로고
    • Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage
    • Chehab, N. H., A. Malikzay, E. S. Stavridi, and T. D. Halazonetis. 1999. Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage. Proc. Natl. Acad. Sci. USA 96:13777-13782.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13777-13782
    • Chehab, N.H.1    Malikzay, A.2    Stavridi, E.S.3    Halazonetis, T.D.4
  • 8
    • 0031939875 scopus 로고    scopus 로고
    • Synergistic activation of p53 by inhibition of MDM2 expression and DNA damage
    • Chen, L., S. Agrawal, W. Zhou, R. Zhang, and J. Chen. 1998. Synergistic activation of p53 by inhibition of MDM2 expression and DNA damage. Proc. Natl. Acad. Sci. USA 95:195-200.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 195-200
    • Chen, L.1    Agrawal, S.2    Zhou, W.3    Zhang, R.4    Chen, J.5
  • 9
    • 0029802591 scopus 로고    scopus 로고
    • p53 levels, functional domains, and DNA damage determine the extent of the apoptotic response of tumor cells
    • Chen, X., L. J. Ko, L. Jayaraman, and C. Prives. 1996. p53 levels, functional domains, and DNA damage determine the extent of the apoptotic response of tumor cells. Genes Dev. 10:2438-2451.
    • (1996) Genes Dev. , vol.10 , pp. 2438-2451
    • Chen, X.1    Ko, L.J.2    Jayaraman, L.3    Prives, C.4
  • 10
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary, D. R., J. J. Dermody, K. K. Jha, and H. L. Ozer. 1994. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell. Biol. 14:1997-2003.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 12
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDm2 and human papillomavirus E6
    • Freedman, D. A., and A. J. Levine. 1998. Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell. Biol. 18:7288-7293.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 14
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING finger is required to promote p53 nuclear export
    • Geyer, R. K., Z. K. Yu, and C. G. Maki. 2000. The MDM2 RING finger is required to promote p53 nuclear export. Nat. Cell Biol. 2:569-573.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 15
    • 0029980043 scopus 로고    scopus 로고
    • p53 in growth control and neoplasia
    • Gottlieb, T. M., and M. Oren. 1996. p53 in growth control and neoplasia. Biochem. Biophys. Acta 1287:77-102.
    • (1996) Biochem. Biophys. Acta , vol.1287 , pp. 77-102
    • Gottlieb, T.M.1    Oren, M.2
  • 17
    • 0033956689 scopus 로고    scopus 로고
    • Identification of a sequence element from p53 that signals for MDM2-targeted degradation
    • Gu, J., D. Chen, J. Rosenblum, R. M. Rubin, and Z.-M. Yuan. 2000. Identification of a sequence element from p53 that signals for MDM2-targeted degradation. Mol. Cell. Biol. 20:1243-1253.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1243-1253
    • Gu, J.1    Chen, D.2    Rosenblum, J.3    Rubin, R.M.4    Yuan, Z.-M.5
  • 18
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., R. Maya, A. Kazaz, and M. Oren. 1997. Mdm2 promotes the rapid degradation of p53. Nature 387:296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 19
    • 0032481111 scopus 로고    scopus 로고
    • Characterization of sequence elements involved in p53 stability regulation reveals cell type dependence for p53 degradation
    • Hengstermann, A., N. J. Whitaker, D. Zimmer, H. Zentgraf, and M. Scheffner. 1998. Characterization of sequence elements involved in p53 stability regulation reveals cell type dependence for p53 degradation. Oncogene 17:2933-2941.
    • (1998) Oncogene , vol.17 , pp. 2933-2941
    • Hengstermann, A.1    Whitaker, N.J.2    Zimmer, D.3    Zentgraf, H.4    Scheffner, M.5
  • 20
    • 0029820095 scopus 로고    scopus 로고
    • The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitinproteasome pathway
    • Hofmann, F., F. Martelli, D. M. Livingston, and Z. Wang. 1996 The retinoblastoma gene product protects E2F-1 from degradation by the ubiquitinproteasome pathway. Genes Dev. 10:2949-2959.
    • (1996) Genes Dev. , vol.10 , pp. 2949-2959
    • Hofmann, F.1    Martelli, F.2    Livingston, D.M.3    Wang, Z.4
  • 21
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda, R., H. Tanaka, and H. Yasuda. 1997. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420:25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 22
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19ARF with MDM2 inhibits ubiquitin ligase activity of MDM2 for tumor suppressor p53
    • Honda, R., and H. Yasuda. 1999. Association of p19ARF with MDM2 inhibits ubiquitin ligase activity of MDM2 for tumor suppressor p53. EMBO J. 18:22-27.
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 23
    • 0033082231 scopus 로고    scopus 로고
    • RB regulates the stability and the apoptotic function of p53 via MDM2
    • Hsieh, J., F. S. G. Chan, D. J. O'Connor, S. Mittnacht, S. Zhong, and X. Lu. 1999. RB regulates the stability and the apoptotic function of p53 via MDM2. Mol. Cell 3:181-193.
    • (1999) Mol. Cell , vol.3 , pp. 181-193
    • Hsieh, J.1    Chan, F.S.G.2    O'Connor, D.J.3    Mittnacht, S.4    Zhong, S.5    Lu, X.6
  • 24
    • 0032192481 scopus 로고    scopus 로고
    • Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation
    • Jiang, Y. H., D. Armstrong, U. Albrecht, C. M. Atkins, J. L. Noebels, G. Eichele, J. D. Sweatt, and A. L. Beaudet. 1998. Mutation of the Angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 21:799-811.
    • (1998) Neuron , vol.21 , pp. 799-811
    • Jiang, Y.H.1    Armstrong, D.2    Albrecht, U.3    Atkins, C.M.4    Noebels, J.L.5    Eichele, G.6    Sweatt, J.D.7    Beaudet, A.L.8
  • 26
    • 0033592868 scopus 로고    scopus 로고
    • Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
    • Khosravi, R., R. Maya, T. Gottlieb, M. Oren, Y. Shiloh, and D. Shkedy. 1999. Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage. Proc. Natl. Acad. Sci. USA 96:14973-14977.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14973-14977
    • Khosravi, R.1    Maya, R.2    Gottlieb, T.3    Oren, M.4    Shiloh, Y.5    Shkedy, D.6
  • 27
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko, L. J., and C. Prives. 1996. p53: puzzle and paradigm. Genes Dev. 10:1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 28
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of p53 stability
    • Kubbutat, M. H., and K. H. Vousden. 1997. Proteolytic cleavage of human p53 by calpain: a potential regulator of p53 stability. Mol. Cell. Biol. 17:460-468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 29
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutal, M. H., Jones, S. N., and K. H. Vousden. 1997. Regulation of p53 stability by Mdm2. Nature 387:299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutal, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 30
  • 31
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. 1997. p53, the cellular gatekeeper for growth and division. Cell 88:323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 32
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • Maki, C. G., J. M. Huibregtse, and P. M. Howley. 1996. In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res. 56:2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 33
    • 0033523015 scopus 로고    scopus 로고
    • Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2
    • Maki, C. G. 1999. Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2. J. Biol. Chem. 274:16531-16535.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16531-16535
    • Maki, C.G.1
  • 34
    • 0028821580 scopus 로고
    • The domain of p53 required for binding HPV 16 E6 is separable from the degradation domain
    • Mansur, C. P., B. Marcus, S. Dalal, and E. J. Androphy. 1995. The domain of p53 required for binding HPV 16 E6 is separable from the degradation domain. Oncogene 10:457-465.
    • (1995) Oncogene , vol.10 , pp. 457-465
    • Mansur, C.P.1    Marcus, B.2    Dalal, S.3    Androphy, E.J.4
  • 35
    • 0029803281 scopus 로고    scopus 로고
    • Wild-type p53 negatively regulates the expression of a microtubule associated protein
    • Murphy, M., A. Hinman, and A. J. Levine. 1996. Wild-type p53 negatively regulates the expression of a microtubule associated protein. Genes Dev. 10:2971-2980.
    • (1996) Genes Dev. , vol.10 , pp. 2971-2980
    • Murphy, M.1    Hinman, A.2    Levine, A.J.3
  • 36
    • 0033215387 scopus 로고    scopus 로고
    • Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a
    • Murphy, M., J. Ahn, K. K. Walker, W. H. Hoffman, R. M. Evans, A. J. Levine, and D. L. George. 1999. Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a. Genes Dev. 13:2490-2501.
    • (1999) Genes Dev. , vol.13 , pp. 2490-2501
    • Murphy, M.1    Ahn, J.2    Walker, K.K.3    Hoffman, W.H.4    Evans, R.M.5    Levine, A.J.6    George, D.L.7
  • 37
    • 0033579412 scopus 로고    scopus 로고
    • Regulation of the p53 tumor suppressor protein
    • Oren, M. 1999. Regulation of the p53 tumor suppressor protein. J. Biol. Chem. 274:36031-36034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36031-36034
    • Oren, M.1
  • 38
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the mdm2-p53 circuit
    • Prives, C. 1998. Signaling to p53: breaking the MDM2-p53 circuit. Cell 95:5-8.
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 39
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth, J., M. Dobbelstein, D. A. Freedman, T. Shenk, and A. J. Levine. 1998. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17:554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 40
    • 0030798557 scopus 로고    scopus 로고
    • The polyproline region of p53 is required to activate apoptosis but not growth arrest
    • Sakamuro, D., P. Sabbatini, E. White, and G. C. Prendergast. 1997. The polyproline region of p53 is required to activate apoptosis but not growth arrest. Oncogene 15:887-898.
    • (1997) Oncogene , vol.15 , pp. 887-898
    • Sakamuro, D.1    Sabbatini, P.2    White, E.3    Prendergast, G.C.4
  • 41
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti, S. E., S. Y. Kim, and W. P. Tansey. 1999. Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J. 18:717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 42
    • 0033621415 scopus 로고    scopus 로고
    • Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein
    • Sharp, D. A., S. A. Kratowicz, M. J. Sank, and D. L. George. 1999. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274:38189-38196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38189-38196
    • Sharp, D.A.1    Kratowicz, S.A.2    Sank, M.J.3    George, D.L.4
  • 43
    • 0033118933 scopus 로고    scopus 로고
    • DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization
    • Shieh, S. Y., Y. Taya, and C. Prives. 1999. DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization. EMBO J. 18:1815-1823.
    • (1999) EMBO J. , vol.18 , pp. 1815-1823
    • Shieh, S.Y.1    Taya, Y.2    Prives, C.3
  • 44
    • 0031973765 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cancer
    • Spataro, V., C. Norbury, and A. L. Harris. 1998. The ubiquitin-proteasome pathway in cancer. Br. J. Cancer 77:448-455.
    • (1998) Br. J. Cancer , vol.77 , pp. 448-455
    • Spataro, V.1    Norbury, C.2    Harris, A.L.3
  • 45
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel, J. M., N. D. Marchenko, G. S. Jimenez, U. M. Moll, T. J. Hope, and G. M. Wahl. 1999. A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18:1660-1672.
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 47
    • 0032513114 scopus 로고    scopus 로고
    • The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells
    • Talis, A. L., J. M. Huibregtse, and P. M. Howley. 1998. The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells. J. Biol. Chem. 273:6439-6445.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6439-6445
    • Talis, A.L.1    Huibregtse, J.M.2    Howley, P.M.3
  • 48
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao, W., and A. J. Levine. 1999. Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc. Natl. Acad. Sci. USA 96:3077-3080.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 49
    • 0032541325 scopus 로고    scopus 로고
    • The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific P1G3 gene transactivation and with transcriptional repression
    • Venot, C., M. Maratrat, C. Dureuil, E. Conseiller, L. Bracco, and L. Debussche. 1998. The requirement for the p53 proline-rich functional domain for mediation of apoptosis is correlated with specific P1G3 gene transactivation and with transcriptional repression. EMBO J. 17:4668-4679.
    • (1998) EMBO J. , vol.17 , pp. 4668-4679
    • Venot, C.1    Maratrat, M.2    Dureuil, C.3    Conseiller, E.4    Bracco, L.5    Debussche, L.6
  • 50
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker, K. K., and A. J. Levine. 1996. Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc. Natl. Acad. Sci. USA 93:15335-15340.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 51
    • 0030052598 scopus 로고    scopus 로고
    • An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants
    • Waterman, M. J. F., J. L. F. Waterman, and T. D. Halazonetis. 1996. An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants. Cancer Res. 56:158-163.
    • (1996) Cancer Res. , vol.56 , pp. 158-163
    • Waterman, M.J.F.1    Waterman, J.L.F.2    Halazonetis, T.D.3
  • 52
    • 0033000482 scopus 로고    scopus 로고
    • Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53
    • Zhang, Y., and Y. Xiong. 1999. Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. Mol. Cell 3:579-591.
    • (1999) Mol. Cell , vol.3 , pp. 579-591
    • Zhang, Y.1    Xiong, Y.2
  • 53
    • 0033602361 scopus 로고    scopus 로고
    • Differential regulation of cellular target genes by p53 devoid of the PXXP motifs with impaired apoptotic activity
    • Zhu, J., J. Jiang, W. Zhou, K. Zhu, and X. Chen. 1999. Differential regulation of cellular target genes by p53 devoid of the PXXP motifs with impaired apoptotic activity. Oncogene 18:2149-2155.
    • (1999) Oncogene , vol.18 , pp. 2149-2155
    • Zhu, J.1    Jiang, J.2    Zhou, W.3    K, Z.4    Chen, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.