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Volumn 313, Issue 4, 2007, Pages 665-676

G2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization

Author keywords

CRM1; DNA damage; HECT; Leptomycin B; Nuclear export; Nucleolus; Ubiquitin ligase

Indexed keywords

CELL CYCLE PROTEIN; CELL DNA; EXPORTIN 1; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN; PROTEIN G2E3; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 33846698813     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.11.020     Document Type: Article
Times cited : (21)

References (53)
  • 1
    • 0035813136 scopus 로고    scopus 로고
    • The G(2) DNA damage checkpoint delays expression of genes encoding mitotic regulators
    • Crawford D.F., and Piwnica-Worms H. The G(2) DNA damage checkpoint delays expression of genes encoding mitotic regulators. J. Biol. Chem. 276 (2001) 37166-37177
    • (2001) J. Biol. Chem. , vol.276 , pp. 37166-37177
    • Crawford, D.F.1    Piwnica-Worms, H.2
  • 2
    • 0024427288 scopus 로고
    • Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2
    • Pines J., and Hunter T. Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. Cell 58 (1989) 833-846
    • (1989) Cell , vol.58 , pp. 833-846
    • Pines, J.1    Hunter, T.2
  • 3
    • 0028243084 scopus 로고
    • Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5
    • Golsteyn R.M., Schultz S.J., Bartek J., Ziemiecki A., Ried T., and Nigg E.A. Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. J. Cell Sci. 107 Pt. 6 (1994) 1509-1517
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 6 , pp. 1509-1517
    • Golsteyn, R.M.1    Schultz, S.J.2    Bartek, J.3    Ziemiecki, A.4    Ried, T.5    Nigg, E.A.6
  • 4
    • 0842281498 scopus 로고    scopus 로고
    • Aurora kinases link chromosome segregation and cell division to cancer susceptibility
    • Meraldi P., Honda R., and Nigg E.A. Aurora kinases link chromosome segregation and cell division to cancer susceptibility. Curr. Opin. Genet. Dev. 14 (2004) 29-36
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 29-36
    • Meraldi, P.1    Honda, R.2    Nigg, E.A.3
  • 6
    • 0037219218 scopus 로고    scopus 로고
    • Roles of DNA topoisomerases in chromosome segregation and mitosis
    • Cortes F., Pastor N., Mateos S., and Dominguez I. Roles of DNA topoisomerases in chromosome segregation and mitosis. Mutat. Res. 543 (2003) 59-66
    • (2003) Mutat. Res. , vol.543 , pp. 59-66
    • Cortes, F.1    Pastor, N.2    Mateos, S.3    Dominguez, I.4
  • 7
    • 0034331310 scopus 로고    scopus 로고
    • The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis
    • Hill E., Clarke M., and Barr F.A. The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis. EMBO J. 19 (2000) 5711-5719
    • (2000) EMBO J. , vol.19 , pp. 5711-5719
    • Hill, E.1    Clarke, M.2    Barr, F.A.3
  • 8
    • 12444311754 scopus 로고    scopus 로고
    • Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells
    • Wasch R., and Engelbert D. Anaphase-promoting complex-dependent proteolysis of cell cycle regulators and genomic instability of cancer cells. Oncogene 24 (2005) 1-10
    • (2005) Oncogene , vol.24 , pp. 1-10
    • Wasch, R.1    Engelbert, D.2
  • 9
    • 0038152755 scopus 로고    scopus 로고
    • Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase
    • Bornstein G., Bloom J., Sitry-D. Shevah K., Nakayama M., and Hershko A. Role of the SCFSkp2 ubiquitin ligase in the degradation of p21Cip1 in S phase. J. Biol. Chem. 278 (2003) 25752-25757
    • (2003) J. Biol. Chem. , vol.278 , pp. 25752-25757
    • Bornstein, G.1    Bloom, J.2    Sitry-D. Shevah, K.3    Nakayama, M.4    Hershko, A.5
  • 10
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15 (1999) 435-467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 11
    • 4544276433 scopus 로고    scopus 로고
    • APC/C and SCF: controlling each other and the cell cycle
    • Vodermaier H.C. APC/C and SCF: controlling each other and the cell cycle. Curr. Biol. 14 (2004) R787-R796
    • (2004) Curr. Biol. , vol.14
    • Vodermaier, H.C.1
  • 12
    • 0034721154 scopus 로고    scopus 로고
    • Chfr defines a mitotic stress checkpoint that delays entry into metaphase
    • Scolnick D.M., and Halazonetis T.D. Chfr defines a mitotic stress checkpoint that delays entry into metaphase. Nature 406 (2000) 430-435
    • (2000) Nature , vol.406 , pp. 430-435
    • Scolnick, D.M.1    Halazonetis, T.D.2
  • 13
    • 4143140977 scopus 로고    scopus 로고
    • Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
    • Matsusaka T., and Pines J. Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells. J. Cell Biol. 166 (2004) 507-516
    • (2004) J. Cell Biol. , vol.166 , pp. 507-516
    • Matsusaka, T.1    Pines, J.2
  • 14
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R., Tanaka H., and Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420 (1997) 25-27
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 15
    • 0035810050 scopus 로고    scopus 로고
    • Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding
    • Graves P.R., Lovly C.M., Uy G.L., and Piwnica-Worms H. Localization of human Cdc25C is regulated both by nuclear export and 14-3-3 protein binding. Oncogene 20 (2001) 1839-1851
    • (2001) Oncogene , vol.20 , pp. 1839-1851
    • Graves, P.R.1    Lovly, C.M.2    Uy, G.L.3    Piwnica-Worms, H.4
  • 16
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines J., and Hunter T. The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J. 13 (1994) 3772-3781
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 17
    • 0842269247 scopus 로고    scopus 로고
    • The importance of p53 location: nuclear or cytoplasmic zip code?
    • O'Brate A., and Giannakakou P. The importance of p53 location: nuclear or cytoplasmic zip code?. Drug Resist. Updat. 6 (2003) 313-322
    • (2003) Drug Resist. Updat. , vol.6 , pp. 313-322
    • O'Brate, A.1    Giannakakou, P.2
  • 18
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng C.Y., Graves P.R., Thoma R.S., Wu Z., Shaw A.S., and Piwnica-Worms H. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 277 (1997) 1501-1505
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 19
    • 0035793643 scopus 로고    scopus 로고
    • Combinatorial control of cyclin B1 nuclear trafficking through phosphorylation at multiple sites
    • Yang J., Song H., Walsh S., Bardes E.S., and Kornbluth S. Combinatorial control of cyclin B1 nuclear trafficking through phosphorylation at multiple sites. J. Biol. Chem. 276 (2001) 3604-3609
    • (2001) J. Biol. Chem. , vol.276 , pp. 3604-3609
    • Yang, J.1    Song, H.2    Walsh, S.3    Bardes, E.S.4    Kornbluth, S.5
  • 20
    • 0032755396 scopus 로고    scopus 로고
    • A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain
    • Liang S.H., and Clarke M.F. A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain. J. Biol. Chem. 274 (1999) 32699-32703
    • (1999) J. Biol. Chem. , vol.274 , pp. 32699-32703
    • Liang, S.H.1    Clarke, M.F.2
  • 21
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer R.K., Yu Z.K., and Maki C.G. The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat. Cell Biol. 2 (2000) 569-573
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 22
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M., Asano S., Nakamura T., Adachi M., Yoshida M., Yanagida M., and Nishida E. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390 (1997) 308-311
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 23
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., and Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90 (1997) 1051-1060
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 24
    • 33746561940 scopus 로고    scopus 로고
    • Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal
    • Sato H., Masuda M., Miura R., Yoneda M., and Kai C. Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal. Virology (2006)
    • (2006) Virology
    • Sato, H.1    Masuda, M.2    Miura, R.3    Yoneda, M.4    Kai, C.5
  • 25
    • 0037126617 scopus 로고    scopus 로고
    • A novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69
    • Lischka P., Rosorius O., Trommer E., and Stamminger T. A novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69. EMBO J. 20 (2001) 7271-7283
    • (2001) EMBO J. , vol.20 , pp. 7271-7283
    • Lischka, P.1    Rosorius, O.2    Trommer, E.3    Stamminger, T.4
  • 26
    • 0037033792 scopus 로고    scopus 로고
    • Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins
    • Brownawell A.M., and Macara I.G. Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins. J. Cell Biol. 156 (2002) 53-64
    • (2002) J. Cell Biol. , vol.156 , pp. 53-64
    • Brownawell, A.M.1    Macara, I.G.2
  • 28
    • 4444229456 scopus 로고    scopus 로고
    • Exportin 7 defines a novel general nuclear export pathway
    • Mingot J.M., Bohnsack M.T., Jakle U., and Gorlich D. Exportin 7 defines a novel general nuclear export pathway. EMBO J. 23 (2004) 3227-3236
    • (2004) EMBO J. , vol.23 , pp. 3227-3236
    • Mingot, J.M.1    Bohnsack, M.T.2    Jakle, U.3    Gorlich, D.4
  • 29
    • 33746277552 scopus 로고    scopus 로고
    • Structure and function of the nucleolus in the spotlight
    • Raska I., Shaw P.J., and Cmarko D. Structure and function of the nucleolus in the spotlight. Curr. Opin. Cell Biol. 18 (2006) 325-334
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 325-334
    • Raska, I.1    Shaw, P.J.2    Cmarko, D.3
  • 30
    • 0035986065 scopus 로고    scopus 로고
    • The promyelocytic leukemia nuclear body: sites of activity?
    • Eskiw C.H., and Bazett-Jones D.P. The promyelocytic leukemia nuclear body: sites of activity?. Biochem. Cell Biol. 80 (2002) 301-310
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 301-310
    • Eskiw, C.H.1    Bazett-Jones, D.P.2
  • 31
    • 0035969102 scopus 로고    scopus 로고
    • SUMO: of branched proteins and nuclear bodies
    • Seeler J.S., and Dejean A. SUMO: of branched proteins and nuclear bodies. Oncogene 20 (2001) 7243-7249
    • (2001) Oncogene , vol.20 , pp. 7243-7249
    • Seeler, J.S.1    Dejean, A.2
  • 32
    • 22744449772 scopus 로고    scopus 로고
    • The spliceosome: a novel multi-faceted target for therapy
    • Tazi J., Durand S., and Jeanteur P. The spliceosome: a novel multi-faceted target for therapy. Trends Biochem. Sci. 30 (2005) 469-478
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 469-478
    • Tazi, J.1    Durand, S.2    Jeanteur, P.3
  • 34
    • 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., Dobbelstein M., Freedman D.A., Shenk T., and Levine A.J. 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 (1998) 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
  • 35
    • 0142215639 scopus 로고    scopus 로고
    • The Wilms' tumour suppressor protein, WT1, undergoes CRM1-independent nucleocytoplasmic shuttling
    • Vajjhala P.R., Macmillan E., Gonda T., and Little M. The Wilms' tumour suppressor protein, WT1, undergoes CRM1-independent nucleocytoplasmic shuttling. FEBS Lett. 554 (2003) 143-148
    • (2003) FEBS Lett. , vol.554 , pp. 143-148
    • Vajjhala, P.R.1    Macmillan, E.2    Gonda, T.3    Little, M.4
  • 36
    • 0141706697 scopus 로고    scopus 로고
    • A novel nuclear export signal in Smad1 is essential for its signaling activity
    • Xiao Z., Brownawell A.M., Macara I.G., and Lodish H.F. A novel nuclear export signal in Smad1 is essential for its signaling activity. J. Biol. Chem. 278 (2003) 34245-34252
    • (2003) J. Biol. Chem. , vol.278 , pp. 34245-34252
    • Xiao, Z.1    Brownawell, A.M.2    Macara, I.G.3    Lodish, H.F.4
  • 37
  • 38
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson B.R., and Eleftheriou A. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256 (2000) 213-224
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 40
    • 32544439491 scopus 로고    scopus 로고
    • Intracellular localization and nucleocytoplasmic trafficking of steroid receptors: an overview
    • Kumar S., Saradhi M., Chaturvedi N.K., and Tyagi R.K. Intracellular localization and nucleocytoplasmic trafficking of steroid receptors: an overview. Mol. Cell. Endocrinol. 246 (2006) 147-156
    • (2006) Mol. Cell. Endocrinol. , vol.246 , pp. 147-156
    • Kumar, S.1    Saradhi, M.2    Chaturvedi, N.K.3    Tyagi, R.K.4
  • 41
    • 33646853354 scopus 로고    scopus 로고
    • Tanaka, J. Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25
    • Fujiwara T., Suzuki S., Kanno M., Sugiyama H., and Takahashi H. Tanaka, J. Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25. Exp. Cell Res. 312 (2006) 1703-1712
    • (2006) Exp. Cell Res. , vol.312 , pp. 1703-1712
    • Fujiwara, T.1    Suzuki, S.2    Kanno, M.3    Sugiyama, H.4    Takahashi, H.5
  • 42
    • 0037169534 scopus 로고    scopus 로고
    • Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein
    • Mo Y.Y., Yu Y., Shen Z., and Beck W.T. Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein. J. Biol. Chem. 277 (2002) 2958-2964
    • (2002) J. Biol. Chem. , vol.277 , pp. 2958-2964
    • Mo, Y.Y.1    Yu, Y.2    Shen, Z.3    Beck, W.T.4
  • 43
    • 0037185024 scopus 로고    scopus 로고
    • DNA damage-induced translocation of the Werner helicase is regulated by acetylation
    • Blander G., Zalle N., Daniely Y., Taplick J., Gray M.D., and Oren M. DNA damage-induced translocation of the Werner helicase is regulated by acetylation. J. Biol. Chem. 277 (2002) 50934-50940
    • (2002) J. Biol. Chem. , vol.277 , pp. 50934-50940
    • Blander, G.1    Zalle, N.2    Daniely, Y.3    Taplick, J.4    Gray, M.D.5    Oren, M.6
  • 44
    • 0036315747 scopus 로고    scopus 로고
    • Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation
    • Daniely Y., Dimitrova D.D., and Borowiec J.A. Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation. Mol. Cell. Biol. 22 (2002) 6014-6022
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6014-6022
    • Daniely, Y.1    Dimitrova, D.D.2    Borowiec, J.A.3
  • 45
    • 27544444006 scopus 로고    scopus 로고
    • DNA damage disrupts the p14ARF-B23(nucleophosmin) interaction and triggers a transient subnuclear redistribution of p14ARF
    • Lee C., Smith B.A., Bandyopadhyay K., and Gjerset R.A. DNA damage disrupts the p14ARF-B23(nucleophosmin) interaction and triggers a transient subnuclear redistribution of p14ARF. Cancer Res. 65 (2005) 9834-9842
    • (2005) Cancer Res. , vol.65 , pp. 9834-9842
    • Lee, C.1    Smith, B.A.2    Bandyopadhyay, K.3    Gjerset, R.A.4
  • 46
    • 0034102337 scopus 로고    scopus 로고
    • ATR disruption leads to chromosomal fragmentation and early embryonic lethality
    • Brown E.J., and Baltimore D. ATR disruption leads to chromosomal fragmentation and early embryonic lethality. Genes Dev. 14 (2000) 397-402
    • (2000) Genes Dev. , vol.14 , pp. 397-402
    • Brown, E.J.1    Baltimore, D.2
  • 47
    • 0029784528 scopus 로고    scopus 로고
    • Inactivation of the mouse Brca1 gene leads to failure in the morphogenesis of the egg cylinder in early postimplantation development
    • Liu C.Y., Flesken-Nikitin A., Li S., Zeng Y., and Lee W.H. Inactivation of the mouse Brca1 gene leads to failure in the morphogenesis of the egg cylinder in early postimplantation development. Genes Dev. 10 (1996) 1835-1843
    • (1996) Genes Dev. , vol.10 , pp. 1835-1843
    • Liu, C.Y.1    Flesken-Nikitin, A.2    Li, S.3    Zeng, Y.4    Lee, W.H.5
  • 48
    • 0030924656 scopus 로고    scopus 로고
    • Targeted mutations of breast cancer susceptibility gene homologs in mice: lethal phenotypes of Brca1, Brca2, Brca1/Brca2, Brca1/p53, and Brca2/p53 nullizygous embryos
    • Ludwig T., Chapman D.L., Papaioannou V.E., and Efstratiadis A. Targeted mutations of breast cancer susceptibility gene homologs in mice: lethal phenotypes of Brca1, Brca2, Brca1/Brca2, Brca1/p53, and Brca2/p53 nullizygous embryos. Genes Dev. 11 (1997) 1226-1241
    • (1997) Genes Dev. , vol.11 , pp. 1226-1241
    • Ludwig, T.1    Chapman, D.L.2    Papaioannou, V.E.3    Efstratiadis, A.4
  • 51
    • 0034863683 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53
    • Parant J., Chavez-Reyes A., Little N.A., Yan W., Reinke V., Jochemsen A.G., and Lozano G. Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat. Genet. 29 (2001) 92-95
    • (2001) Nat. Genet. , vol.29 , pp. 92-95
    • Parant, J.1    Chavez-Reyes, A.2    Little, N.A.3    Yan, W.4    Reinke, V.5    Jochemsen, A.G.6    Lozano, G.7
  • 52
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R., Wagner D.S., and Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378 (1995) 203-206
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes de Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 53
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones S.N., Roe A.E., Donehower L.A., and Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378 (1995) 206-208
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4


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