메뉴 건너뛰기




Volumn 1, Issue 3, 2002, Pages 277-283

p53 antiproliferative function is enhanced by aspartate substitution at threonine 18 and serine 20

Author keywords

Fas APO 1; Growth regulation; Mdm 2; Mutagenesis; Protein conformation; Transactivation

Indexed keywords

ASPARTIC ACID; CALPAIN; CDKN1A PROTEIN, HUMAN; CYCLIN DEPENDENT KINASE INHIBITOR 1A; CYCLINE; FAS ANTIGEN; GLUTATHIONE TRANSFERASE; MDM2 PROTEIN, HUMAN; NUCLEAR PROTEIN; ONCOPROTEIN; PROTEIN MDM2; PROTEIN P53; SERINE; THREONINE;

EID: 0346455680     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.81     Document Type: Article
Times cited : (20)

References (64)
  • 1
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia AJ, Kastan MB. The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev 1998; 12:2973-83. (Pubitemid 28469299)
    • (1998) Genes and Development , vol.12 , Issue.19 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 2
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • DOI 10.1016/S0092-8674(00)81774-2
    • Prives C. Signaling to p53: breaking the MDM2-p53 circuit. Cell 1998; 95:5-8. (Pubitemid 28458016)
    • (1998) Cell , vol.95 , Issue.1 , pp. 5-8
    • Prives, C.1
  • 4
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin- Dependent kinases
    • DOI 10.1016/0092-8674(93)90499-G
    • Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ. The p21 cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 1993; 75:805-16. (Pubitemid 23346377)
    • (1993) Cell , vol.75 , Issue.4 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 5
    • 0026496885 scopus 로고
    • A mammalian cell-cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia
    • Kastan MB, Zhan Q, El-Deiry WS, Carrier F, Jacks T, Walsh WV, et al. A mammalian cell-cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia. Cell 1992; 71:587-97.
    • (1992) Cell , vol.71 , pp. 587-597
    • Kastan, M.B.1    Zhan, Q.2    El-Deiry, W.S.3    Carrier, F.4    Jacks, T.5    Walsh, W.V.6
  • 6
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 1995; 80:293-9.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 8
    • 0031987277 scopus 로고    scopus 로고
    • Regulation of p53 downstream genes
    • DOI 10.1006/scbi.1998.0097
    • El-Deiry WS. Regulation of p53 downstream genes. Semin Cancer Biol 1998; 8:345-57. (Pubitemid 29131356)
    • (1998) Seminars in Cancer Biology , vol.8 , Issue.5 , pp. 345-357
    • El-Deiry, W.S.1
  • 9
    • 0027459198 scopus 로고
    • Mdm2 Expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, Oren M. Mdm-2 expression is induced by wild-type p53 activity. EMBO J. 1993; 12:461-8. (Pubitemid 23073692)
    • (1993) EMBO Journal , vol.12 , Issue.2 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 10
    • 0027244853 scopus 로고
    • The p53/Mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D, Levine AJ. The p53/Mdm-2 autoregulatory feedback loop. Genes Dev. 1993; 7:1126-32.
    • (1993) Genes Dev. , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 11
    • 0028979005 scopus 로고
    • II31 is a transcriptional co-activator of the p53 protein
    • II31 is a transcriptional co-activator of the p53 protein. Proc Natl Acad Sci USA 1995; 92:5154-58.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5154-5158
    • Lu, H.1    Levine, A.J.2
  • 14
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • DOI 10.1038/42972
    • Gu W, Shi XL, Roeder RG. Synergistic activation of transcription by CBP and p53. Nature 1997; 387:819-23. (Pubitemid 27270909)
    • (1997) Nature , vol.387 , Issue.6635 , pp. 819-823
    • Gu, W.1    Shi, X.-L.2    Roeder, R.G.3
  • 16
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • DOI 10.1126/science.274.5289.948
    • Kussie PH, Gorina S, Marechal V et al. Structure of the Mdm-2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science. 1996; 274:948-53. (Pubitemid 26398409)
    • (1996) Science , vol.274 , Issue.5289 , 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
  • 18
    • 0027325132 scopus 로고
    • Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
    • DOI 10.1038/362857a0
    • Oliner JD, Pietenpol JA, Thiagalingam S, Gyuris J, Kinzler KW, Vogelstein B. Oncoprotein Mdm-2 conceals the activation domain of tumor suppressor p53. Nature. 1993; 362:857-60. (Pubitemid 23132165)
    • (1993) Nature , vol.362 , Issue.6423 , pp. 857-860
    • Oliner, J.D.1    Pietenpol, J.A.2    Thiagalingam, S.3    Gyuris, J.4    Kinzler, K.W.5    Vogelstein, B.6
  • 19
    • 0033553505 scopus 로고    scopus 로고
    • Murine double minute (Mdm-2) blocks p53 coactivator interaction, a new mechanism for inhibition of p53-dependent gene expression
    • Wadgaonkar R, Collins T. Murine double minute (Mdm-2) blocks p53 coactivator interaction, a new mechanism for inhibition of p53-dependent gene expression. J Biol Chem 1999; 274: 13760-7.
    • (1999) J Biol Chem , vol.274 , pp. 13760-13767
    • Wadgaonkar, R.1    Collins, T.2
  • 20
    • 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
    • DOI 10.1093/emboj/17.2.554
    • Roth J, Dobbelstein M, Freedman DA, Shenk T, Levine AJ. Nucleo-cytoplasmic shuttling of the Hdm-2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J 1998; 17:554-564. (Pubitemid 28045495)
    • (1998) EMBO Journal , vol.17 , Issue.2 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 21
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • DOI 10.1016/S0014-5793(97)01480-4, PII S0014579397014804
    • Honda R, Tanaka H, Yasuda H. Oncoprotein Mdm-2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 1997; 420: 25-27. (Pubitemid 28037193)
    • (1997) FEBS Letters , vol.420 , Issue.1 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 22
    • 0034708458 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of Mdm-2: Differential RING finger requirements for ubiquitination and proteasomal targeting of Mdm-2 and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. Ubiquitin protein ligase activity of Mdm-2: Differential RING finger requirements for ubiquitination and proteasomal targeting of Mdm-2 and p53. J Biol Chem 2000; 275:8945-51.
    • (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
  • 23
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • DOI 10.1038/387296a0
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm-2 promotes the rapid degradation of p53. Nature. 1997; 387:296-9. (Pubitemid 27220766)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 24
    • 0030965946 scopus 로고    scopus 로고
    • Analysis of the degradation function of Mdm-2
    • Kubbutat MHG, Jones SN, Vousden KH. Analysis of the degradation function of Mdm-2. Nature 1997; 387:299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 25
    • 0033429271 scopus 로고    scopus 로고
    • Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15
    • DOI 10.1016/S0014-5793(99)01647-6, PII S0014579399016476
    • Dumaz N, Milne DM, Meek DW. Protein kinase CK1 is a p53-threonine 18 kinase which requires prior phosphorylation of serine 15. FEBS Lett 1999; 463:312-16. (Pubitemid 30001941)
    • (1999) FEBS Letters , vol.463 , Issue.3 , pp. 312-316
    • Dumaz, N.1    Milne, D.M.2    Meek, D.W.3
  • 27
    • 0034737438 scopus 로고    scopus 로고
    • Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on MDM2 binding
    • DOI 10.1074/jbc.275.13.9278
    • Sakaguchi K, Saito S, Higashimoto Y, Roy S, Anderson CW, Appella E. Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a Casein 1-like Kinase. Effect on Mdm-2 binding. J Biol Chem 2000; 275:9278-83. (Pubitemid 30185148)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9278-9283
    • Sakaguchi, K.1    Saito, S.2    Higashimoto, Y.3    Roy, S.4    Anderson, C.W.5    Appella, E.6
  • 28
    • 0033598754 scopus 로고    scopus 로고
    • Phosphorylation of Ser20 mediates stabilization of human p53 in response to DNA damage
    • Chehab NH, Malikzay A, Stavridi ES, Halazonetis TD. Phosphorylation of Ser20 mediates stabilization of human p53 in response to DNA damage. Proc Natl Acad Sci USA 1999; 96:13777-82.
    • (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
  • 29
    • 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, Taya Y, Prives C. DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization. EMBO J 1999; 18:1815-23. (Pubitemid 29158525)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1815-1823
    • Shieh, S.-Y.1    Taya, Y.2    Prives, C.3
  • 31
    • 0034649511 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 at serine 20 correlates with p21 and Mdm-2 induction in vivo
    • Jabbur JR, Huang P, Zhang W. DNA damage-induced phosphorylation of p53 at serine 20 correlates with p21 and Mdm-2 induction in vivo. Oncogene 2000; 19:6203-9.
    • (2000) Oncogene , vol.19 , pp. 6203-6209
    • Jabbur, J.R.1    Huang, P.2    Zhang, W.3
  • 35
    • 0034142034 scopus 로고    scopus 로고
    • The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate, p53 at multiple DNA damage-inducible sites
    • Shieh SY, Ahn J, Tamai K, Taya Y, Prives C. The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites. Genes Dev 2000; 14:289-300. (Pubitemid 30106484)
    • (2000) Genes and Development , vol.14 , Issue.3 , pp. 289-300
    • Shieh, S.-Y.1    Ahn, J.2    Tamai, K.3    Taya, Y.4    Prives, C.5
  • 36
    • 0035258591 scopus 로고    scopus 로고
    • Enhancement of the antiproliferative function of p53 by phosphorylation at serine 20: An inference from site-directed mutagenesis studies
    • Jabbur JR, Huang P, Zhang W. Enhancement of the antiproliferative function of p53 by phosphorylation at serine 20: an inference from site-directed mutagenesis studies. Int J Mol Med 2001; 7:163-8.
    • (2001) Int J Mol Med , vol.7 , pp. 163-168
    • Jabbur, J.R.1    Huang, P.2    Zhang, W.3
  • 37
    • 0033572746 scopus 로고    scopus 로고
    • Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2
    • Dumaz N, Meek DW. Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with Hdm2. EMBO J 1999; 24:7002-10. (Pubitemid 30000453)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 7002-7010
    • Dumaz, N.1    Meek, D.W.2
  • 39
    • 0033609306 scopus 로고    scopus 로고
    • Mutations in serines 15 and 20 of human p53 impair its apoptotic activity
    • DOI 10.1038/sj.onc.1202656
    • Unger T, Sionov RV, Moallem E, Yee CL, Howley PM, Oren M, et al. Mutations in serines 15 and 20 of human p53 impair its apoptotic activity. Oncogene 1999; 18:3205-12. (Pubitemid 29286965)
    • (1999) Oncogene , vol.18 , Issue.21 , pp. 3205-3212
    • Unger, T.1    Vogt, S.R.2    Moallem, E.3    Yee, C.L.4    Howley, P.M.5    Oren, M.6    Haupt, Y.7
  • 41
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MHG, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997; 17:460-8. (Pubitemid 26425636)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.1 , pp. 460-468
    • Kubbutat, M.H.G.1    Vousden, K.H.2
  • 42
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • DOI 10.1016/S0092-8674(00)80416-X
    • Shieh SY, Ikeda M, Taya Y, Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM-2. Cell 1997; 91:325-34. (Pubitemid 27467963)
    • (1997) Cell , vol.91 , Issue.3 , pp. 325-334
    • Shieh, S.-Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 45
    • 0033567340 scopus 로고    scopus 로고
    • 18 that disrupt the binding of mdm2 (mouse double minute 2) protein are modified in human cancers
    • DOI 10.1042/0264-6021:3420133
    • Craig AL, Burch L, Vojtesek B, Mikutowska J, Thompson A, Hupp TR. Novel phosphorylation sites of human tumor suppressor protein p53 at Ser20 and Thr18 that disrupt the binding of Mdm-2 protein are modified in human cancers. British J Biochem 1999; 342:133-41. (Pubitemid 29410859)
    • (1999) Biochemical Journal , vol.342 , Issue.1 , pp. 133-141
    • Craig, A.L.1    Burch, L.2    Vojtesek, B.3    Mikutowska, J.4    Thompson, A.5    Hupp, T.R.6
  • 46
    • 0034664684 scopus 로고    scopus 로고
    • Thermodynamics of p53 binding to Hdm2 (1-126): Effects of phosphorylation and p53 peptide length
    • Lai Z, Auger KR, Manubay CM, Copeland RA. Thermodynamics of p53 binding to Hdm2 (1-126): effects of phosphorylation and p53 peptide length. Arch Biochem Biophys 2000; 381:278-84.
    • (2000) Arch Biochem Biophys , vol.381 , pp. 278-284
    • Lai, Z.1    Auger, K.R.2    Manubay, C.M.3    Copeland, R.A.4
  • 48
    • 0034704923 scopus 로고    scopus 로고
    • The loss of mdm-2 induces p53-mediated apoptosis
    • de Rozieres S, Maya R, Oren M, Lozano G. The loss of mdm-2 induces p53-mediated apoptosis. Oncogene 2000; 19:1691-7.
    • (2000) Oncogene , vol.19 , pp. 1691-1697
    • De Rozieres, S.1    Maya, R.2    Oren, M.3    Lozano, G.4
  • 49
    • 0034665461 scopus 로고    scopus 로고
    • p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage
    • Chao C, Saito S, Kang J, Anderson CW, Appella E, Xu Y. p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage. EMBO J. 2000; 19: 4967-4975.
    • (2000) EMBO J , vol.19 , pp. 4967-4975
    • Chao, C.1    Saito, S.2    Kang, J.3    Anderson, C.W.4    Appella, E.5    Xu, Y.6
  • 50
    • 0033821977 scopus 로고    scopus 로고
    • A transactivation-deficient mouse model provides insights into Trp53 regulation and function
    • Jimenez GS, Nister M, Stommel JM, Beeche M, Barcarse EA, Zhang XQ, et al. A transactivation-deficient mouse model provides insights into Trp53 regulation and function. Nat Gen 2000; 26:37-43.
    • (2000) Nat Gen , vol.26 , pp. 37-43
    • Jimenez, G.S.1    Nister, M.2    Stommel, J.M.3    Beeche, M.4    Barcarse, E.A.5    Zhang, X.Q.6
  • 51
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo LD, Turchi JJ, Berberich SJ. Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res 1997; 57:5013-16. (Pubitemid 27498111)
    • (1997) Cancer Research , vol.57 , Issue.22 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 53
    • 0034649503 scopus 로고    scopus 로고
    • ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation
    • DOI 10.1038/sj.onc.1204020
    • de Toledo SM, Azzam EI, Dahlberg WK, Gooding TB, Little JB. ATM complexes with Hdm-2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation. Oncogene 2000; 19:6185-93. (Pubitemid 32641831)
    • (2000) Oncogene , vol.19 , Issue.54 , pp. 6185-6193
    • De Toledo, S.M.1    Azzam, E.I.2    Dahlberg, W.K.3    Gooding, T.B.4    Little, J.B.5
  • 55
    • 0033486046 scopus 로고    scopus 로고
    • Identification of a CK2 phosphorylation site in Mdm-2
    • Gotz C, Kartarius S, Scholtes P et al. Identification of a CK2 phosphorylation site in Mdm-2. Eur J Biochem 1999; 266:493-501.
    • (1999) Eur J Biochem , vol.266 , pp. 493-501
    • Gotz, C.1    Kartarius, S.2    Scholtes, P.3
  • 56
    • 0035871222 scopus 로고    scopus 로고
    • Phosphorylation of murine double minute clone 2 (MDM2) protein at serine-267 by protein kinase CK2 in vitro and in cultured cells
    • DOI 10.1042/0264-6021:3550347
    • Hjerrild M, Milne D, Dumaz N, Hay T, Issinger OG, Meek D. Phosphorylation of Mdm-2 protein at serine 267 by protein kinase CK2 in vitro in cultured cells. Biochem J 2001; 355:347-56. (Pubitemid 32397793)
    • (2001) Biochemical Journal , vol.355 , Issue.2 , pp. 347-356
    • Hjerrild, M.1    Milne, D.2    Dumaz, N.3    Hay, T.4    Issinger, O.5    Meek, D.6
  • 57
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • DOI 10.1016/S0092-8674(00)80351-7
    • Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ. Activation mechanism of the MAP kinase ERK-2 by dual phosphorylation. Cell 1997; 90:859-69. (Pubitemid 27381625)
    • (1997) Cell , vol.90 , Issue.5 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 58
  • 60
    • 0035476793 scopus 로고    scopus 로고
    • Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest
    • Stavridi ES, Chehab NH, Malikzay A, Halazonetis TD. Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest. Cancer Res 2001; 61:7030-3. (Pubitemid 32946490)
    • (2001) Cancer Research , vol.61 , Issue.19 , pp. 7030-7033
    • Stavridi, E.S.1    Chehab, N.H.2    Malikzay, A.3    Halazonetis, T.D.4
  • 63
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • DOI 10.1038/sj.onc.1204362
    • Kwek SS, Derry J, Tyner AL et al. Functional analysis and intracellular localization of p53 modified by SUMO-1. Oncogene 2001; 20:2587-99. (Pubitemid 32531356)
    • (2001) Oncogene , vol.20 , Issue.20 , pp. 2587-2599
    • Kwek, S.S.S.1    Derry, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 64
    • 0035827335 scopus 로고    scopus 로고
    • A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation
    • DOI 10.1126/science.1058637
    • Zhang Y, Xiong Y. A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation. Science 2001; 292:1910-5. (Pubitemid 32538366)
    • (2001) Science , vol.292 , Issue.5523 , pp. 1910-1915
    • Zhang, Y.1    Xiong, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.