메뉴 건너뛰기




Volumn 26, Issue 26, 2007, Pages 3878-3891

Correction to: Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus (Oncogene, (2007), 26, 26, (3878-3891), 10.1038/sj.onc.1210162);Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus

Author keywords

DNA damage; NoLS; Nucleolus; p53

Indexed keywords

ADENOSINE TRIPHOSPHATE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; PROTEASOME INHIBITOR; PROTEIN P53;

EID: 34249935978     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/s41388-018-0321-1     Document Type: Erratum
Times cited : (26)

References (62)
  • 1
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E, Anderson CW. (2001). Post-translational modifications and activation of p53 by genotoxic stresses. Eur J Biochem 268: 2764-2772.
    • (2001) Eur J Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 2
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft M, Taya Y, Vousden KH. (2000). Stress signals utilize multiple pathways to stabilize p53. Mol Cell Biol 20: 3224-3233.
    • (2000) Mol Cell Biol , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 4
    • 0033611568 scopus 로고    scopus 로고
    • p53 represses ribosomal gene transcription
    • Budde A, Grummt I. (1999). p53 represses ribosomal gene transcription. Oncogene 18: 1119-1124.
    • (1999) Oncogene , vol.18 , pp. 1119-1124
    • Budde, A.1    Grummt, I.2
  • 5
    • 0036949663 scopus 로고    scopus 로고
    • Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: A statistical analysis of information in the National Cancer Institute database
    • Bykov VJ, Issaeva N, Selivanova G, Wiman KG. (2002a). Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database. Carcinogenesis 23: 2011-2018.
    • (2002) Carcinogenesis , vol.23 , pp. 2011-2018
    • Bykov, V.J.1    Issaeva, N.2    Selivanova, G.3    Wiman, K.G.4
  • 6
    • 0036128899 scopus 로고    scopus 로고
    • Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
    • Bykov VJ, Issaeva N, Shilov A, Hultcrantz M, Pugacheva E, Chumakov P et al. (2002b). Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound. Nat Med 8: 282-288.
    • (2002) Nat Med , vol.8 , pp. 282-288
    • Bykov, V.J.1    Issaeva, N.2    Shilov, A.3    Hultcrantz, M.4    Pugacheva, E.5    Chumakov, P.6
  • 9
    • 0030063697 scopus 로고    scopus 로고
    • Quantitation of the nucleophosmin/B23-translocation using imaging analysis
    • Chan PK, Qi Y, Amley J, Koller CA. (1996). Quantitation of the nucleophosmin/B23-translocation using imaging analysis. Cancer Lett 100: 191-197.
    • (1996) Cancer Lett , vol.100 , pp. 191-197
    • Chan, P.K.1    Qi, Y.2    Amley, J.3    Koller, C.A.4
  • 10
    • 0029802591 scopus 로고    scopus 로고
    • p53 levels, functional domains, and DNA damage determine the extent of the apoptotic response of tumor cells
    • Chen X, Ko LJ, Jayaraman L, Prives C. (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
  • 11
    • 0036302062 scopus 로고    scopus 로고
    • Nucleophosmin regulates the stability and transcriptional activity of p53
    • Colombo E, Marine JC, Danovi D, Falini B, Pelicci PG. (2002). Nucleophosmin regulates the stability and transcriptional activity of p53. Nat Cell Biol 4: 529-533.
    • (2002) Nat Cell Biol , vol.4 , pp. 529-533
    • Colombo, E.1    Marine, J.C.2    Danovi, D.3    Falini, B.4    Pelicci, P.G.5
  • 12
    • 0036315747 scopus 로고    scopus 로고
    • Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation
    • Daniely Y, Dimitrova DD, Borowiec JA. (2002). Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation. Mol Cell Biol 22: 6014-6022.
    • (2002) Mol Cell Biol , vol.22 , pp. 6014-6022
    • Daniely, Y.1    Dimitrova, D.D.2    Borowiec, J.A.3
  • 13
    • 0029160316 scopus 로고
    • The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein
    • Dundr M, Leno GH, Hammarskjold ML, Rekosh D, Helga-Maria C, Olson MO. (1995). The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein. J Cell Sci 108(Part 8): 2811-2823.
    • (1995) J Cell Sci , vol.108 , Issue.PART 8 , pp. 2811-2823
    • Dundr, M.1    Leno, G.H.2    Hammarskjold, M.L.3    Rekosh, D.4    Helga-Maria, C.5    Olson, M.O.6
  • 14
    • 16344368267 scopus 로고    scopus 로고
    • Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor
    • Fernandez-Fernandez MR, Veprintsev DB, Fersht AR. (2005). Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor. Proc Natl Acad Sci USA 102: 4735-4740.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4735-4740
    • Fernandez-Fernandez, M.R.1    Veprintsev, D.B.2    Fersht, A.R.3
  • 15
    • 0030570466 scopus 로고    scopus 로고
    • Nucleolin is a sequence-specific RNA-binding protein: Characterization of targets on pre-ribosomal RNA
    • Ghisolfi-Nieto L, Joseph G, Puvion-Dutilleul F, Amalric F, Bouvet P. (1996). Nucleolin is a sequence-specific RNA-binding protein: characterization of targets on pre-ribosomal RNA. J Mol Biol 260: 34-53.
    • (1996) J Mol Biol , vol.260 , pp. 34-53
    • Ghisolfi-Nieto, L.1    Joseph, G.2    Puvion-Dutilleul, F.3    Amalric, F.4    Bouvet, P.5
  • 16
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia AJ, Kastan MB. (1998). The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev 12: 2973-2983.
    • (1998) Genes Dev , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 18
    • 0030005052 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase II transcription causes chromatin decondensation, loss of nucleolar structure, and dispersion of chromosomal domains
    • Haaf T, Ward DC. (1996). Inhibition of RNA polymerase II transcription causes chromatin decondensation, loss of nucleolar structure, and dispersion of chromosomal domains. Exp Cell Res 224: 163-173.
    • (1996) Exp Cell Res , vol.224 , pp. 163-173
    • Haaf, T.1    Ward, D.C.2
  • 19
    • 0035081855 scopus 로고    scopus 로고
    • Segregation of nucleolar components coincides with caspase-3 activation in cisplatin-treated HeLa cells
    • Horky M, Wurzer G, Kotala V, Anton M, Vojtesek B, Vacha J et al. (2001). Segregation of nucleolar components coincides with caspase-3 activation in cisplatin-treated HeLa cells. J Cell Sci 114: 663-670.
    • (2001) J Cell Sci , vol.114 , pp. 663-670
    • Horky, M.1    Wurzer, G.2    Kotala, V.3    Anton, M.4    Vojtesek, B.5    Vacha, J.6
  • 21
    • 0029055808 scopus 로고
    • Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus
    • Jayaraman J, Prives C. (1995). Activation of p53 sequence-specific DNA binding by short single strands of DNA requires the p53 C-terminus. Cell 81: 1021-1029.
    • (1995) Cell , vol.81 , pp. 1021-1029
    • Jayaraman, J.1    Prives, C.2
  • 22
    • 0030877395 scopus 로고    scopus 로고
    • Functional dissection of p53 tumor suppressor protein
    • Jayaraman L, Freulich E, Prives C. (1997). Functional dissection of p53 tumor suppressor protein. Methods Enzymol 283: 245-256.
    • (1997) Methods Enzymol , vol.283 , pp. 245-256
    • Jayaraman, L.1    Freulich, E.2    Prives, C.3
  • 24
    • 0034993222 scopus 로고    scopus 로고
    • Accumulation of soluble and nucleolar-associated p53 proteins following cellular stress
    • Klibanov SA, O'Hagan HM, Ljungman M. (2001). Accumulation of soluble and nucleolar-associated p53 proteins following cellular stress. J Cell Sci 114: 1867-1873.
    • (2001) J Cell Sci , vol.114 , pp. 1867-1873
    • Klibanov, S.A.1    O'Hagan, H.M.2    Ljungman, M.3
  • 25
    • 2142650203 scopus 로고    scopus 로고
    • Nuclear substructure and dynamics
    • Lamond AI, Sleeman JE. (2003). Nuclear substructure and dynamics. Curr Biol 13: R825-R825.
    • (2003) Curr Biol , vol.13
    • Lamond, A.I.1    Sleeman, J.E.2
  • 26
    • 0037209627 scopus 로고    scopus 로고
    • p53 and MDM2 are regulated by PI-3-kinases on multiple levels under stress induced by UV radiation and proteasome dysfunction
    • Latonen L, Kurki S, Pitkanen K, Laiho M. (2003). p53 and MDM2 are regulated by PI-3-kinases on multiple levels under stress induced by UV radiation and proteasome dysfunction. Cell Signal 15: 95-102.
    • (2003) Cell Signal , vol.15 , pp. 95-102
    • Latonen, L.1    Kurki, S.2    Pitkanen, K.3    Laiho, M.4
  • 29
    • 0034823780 scopus 로고    scopus 로고
    • Regulation of p53 localization
    • Liang SH, Clarke MF. (2001). Regulation of p53 localization. Eur J Biochem 268: 2779-2783.
    • (2001) Eur J Biochem , vol.268 , pp. 2779-2783
    • Liang, S.H.1    Clarke, M.F.2
  • 30
    • 0037126392 scopus 로고    scopus 로고
    • The ferredoxin reductase gene is regulated by the p53 family and sensitizes cells to oxidative stress-induced apoptosis
    • Liu G, Chen X. (2002). The ferredoxin reductase gene is regulated by the p53 family and sensitizes cells to oxidative stress-induced apoptosis. Oncogene 21: 7195-7204.
    • (2002) Oncogene , vol.21 , pp. 7195-7204
    • Liu, G.1    Chen, X.2
  • 31
    • 0034744224 scopus 로고    scopus 로고
    • Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus
    • Llanos S, Clark PA, Rowe J, Peters G. (2001). Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus. Nat Cell Biol 3: 445-452.
    • (2001) Nat Cell Biol , vol.3 , pp. 445-452
    • Llanos, S.1    Clark, P.A.2    Rowe, J.3    Peters, G.4
  • 33
    • 0027999512 scopus 로고
    • The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes
    • Marechal V, Elenbaas B, Piette J, Nicolas JC, Levine AJ. (1994). The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes. Mol Cell Biol 14: 7414-7420.
    • (1994) Mol Cell Biol , vol.14 , pp. 7414-7420
    • Marechal, V.1    Elenbaas, B.2    Piette, J.3    Nicolas, J.C.4    Levine, A.J.5
  • 34
    • 25444473870 scopus 로고    scopus 로고
    • Cellular stress and nucleolar function
    • Mayer C, Grummt I. (2005). Cellular stress and nucleolar function. Cell Cycle 4: 1036-1038.
    • (2005) Cell Cycle , vol.4 , pp. 1036-1038
    • Mayer, C.1    Grummt, I.2
  • 35
    • 33644763294 scopus 로고    scopus 로고
    • The biological impact of the human master regulator p53 can be altered by mutations that change the spectrum and expression of its target genes
    • Menendez D, Inga A, Resnick MA. (2006). The biological impact of the human master regulator p53 can be altered by mutations that change the spectrum and expression of its target genes. Mol Cell Biol 26: 2297-2308.
    • (2006) Mol Cell Biol , vol.26 , pp. 2297-2308
    • Menendez, D.1    Inga, A.2    Resnick, M.A.3
  • 36
    • 0027724061 scopus 로고
    • Comparison of p53 protein expression and cellular localization in human and hamster pancreatic cancer cell lines
    • Mogaki M, Hirota M, Chaney WG, Pour PM. (1993). Comparison of p53 protein expression and cellular localization in human and hamster pancreatic cancer cell lines. Carcinogenesis 14: 2589-2594.
    • (1993) Carcinogenesis , vol.14 , pp. 2589-2594
    • Mogaki, M.1    Hirota, M.2    Chaney, W.G.3    Pour, P.M.4
  • 37
    • 18744364184 scopus 로고    scopus 로고
    • The moving parts of the nucleolus
    • Olson MO, Dundr M. (2005). The moving parts of the nucleolus. Histochem Cell Biol 123: 203-216.
    • (2005) Histochem Cell Biol , vol.123 , pp. 203-216
    • Olson, M.O.1    Dundr, M.2
  • 38
    • 0034193778 scopus 로고    scopus 로고
    • The nucleolus: An old factory with unexpected capabilities
    • Olson MO, Dundr M, Szebeni A. (2000). The nucleolus: an old factory with unexpected capabilities. Trends Cell Biol 10: 189-196.
    • (2000) Trends Cell Biol , vol.10 , pp. 189-196
    • Olson, M.O.1    Dundr, M.2    Szebeni, A.3
  • 39
    • 0035146502 scopus 로고    scopus 로고
    • Proteasome inhibitor induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5
    • Pokrovskaja K, Mattsson K, Kashuba E, Klein G, Szekely L. (2001). Proteasome inhibitor induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5. J Gen Virol 82: 345-358.
    • (2001) J Gen Virol , vol.82 , pp. 345-358
    • Pokrovskaja, K.1    Mattsson, K.2    Kashuba, E.3    Klein, G.4    Szekely, L.5
  • 40
    • 0242266896 scopus 로고    scopus 로고
    • Nucleotide binding by the Mdm2 RING domain facilitates Arf-independent Mdm2 nucleolar localization
    • Poyurovsky MV, Jacq X, Ma C, Karni-Schmidt O, Parker PJ, Chalfie M et al. (2003). Nucleotide binding by the Mdm2 RING domain facilitates Arf-independent Mdm2 nucleolar localization. Mol Cell 12: 875-887.
    • (2003) Mol Cell , vol.12 , pp. 875-887
    • Poyurovsky, M.V.1    Jacq, X.2    Ma, C.3    Karni-Schmidt, O.4    Parker, P.J.5    Chalfie, M.6
  • 41
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C, Hall PA. (1999). The p53 pathway. J Pathol 187: 112-126.
    • (1999) J Pathol , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 42
    • 0035966316 scopus 로고    scopus 로고
    • Why is p53 acetylated?
    • Prives C, Manley JL. (2001). Why is p53 acetylated? Cell 107: 815-818.
    • (2001) Cell , vol.107 , pp. 815-818
    • Prives, C.1    Manley, J.L.2
  • 43
    • 0028173667 scopus 로고
    • Acceleration of the G1/S phase transition by expression of cyclins D1 and E with an inducible system
    • Resnitzky D, Gossen M, Bujard H, Reed SI. (1994). Acceleration of the G1/S phase transition by expression of cyclins D1 and E with an inducible system. Mol Cell Biol 14: 1669-1679.
    • (1994) Mol Cell Biol , vol.14 , pp. 1669-1679
    • Resnitzky, D.1    Gossen, M.2    Bujard, H.3    Reed, S.I.4
  • 44
    • 34047109211 scopus 로고    scopus 로고
    • PRIMA-1(MET) induces nucleolar accumulation of mutant p53 and PML nuclear body-associated proteins
    • Epub ahead of print
    • Rokaeus N, Klein G, Wiman KG, Szekely L, Mattsson K. (2006). PRIMA-1(MET) induces nucleolar accumulation of mutant p53 and PML nuclear body-associated proteins. Oncogene [Epub ahead of print].
    • (2006) Oncogene
    • Rokaeus, N.1    Klein, G.2    Wiman, K.G.3    Szekely, L.4    Mattsson, K.5
  • 45
    • 0034610752 scopus 로고    scopus 로고
    • Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus
    • Rubbi CP, Milner J. (2000). Non-activated p53 co-localizes with sites of transcription within both the nucleoplasm and the nucleolus. Oncogene 19: 85-96.
    • (2000) Oncogene , vol.19 , pp. 85-96
    • Rubbi, C.P.1    Milner, J.2
  • 46
    • 0036517104 scopus 로고    scopus 로고
    • Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage
    • Shirangi TR, Zaika A, Moll UM. (2002). Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage. FASEB J 16: 420-422.
    • (2002) FASEB J , vol.16 , pp. 420-422
    • Shirangi, T.R.1    Zaika, A.2    Moll, U.M.3
  • 47
    • 0032518462 scopus 로고    scopus 로고
    • Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA
    • Stros M, Reich J. (1998). Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA. Eur J Biochem 251: 427-434.
    • (1998) Eur J Biochem , vol.251 , pp. 427-434
    • Stros, M.1    Reich, J.2
  • 48
    • 0033536063 scopus 로고    scopus 로고
    • P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • Tao W, Levine AJ. (1999). P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc Natl Acad Sci USA 96: 6937-6941.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 49
    • 0037716643 scopus 로고    scopus 로고
    • Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway
    • Thomas F, Kutay U. (2003). Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway. J Cell Sci 116: 2409-2419.
    • (2003) J Cell Sci , vol.116 , pp. 2409-2419
    • Thomas, F.1    Kutay, U.2
  • 50
    • 0036894648 scopus 로고    scopus 로고
    • A nucleolar mechanism controlling cell proliferation in stem cells and cancer cells
    • Tsai RY, McKay RD. (2002). A nucleolar mechanism controlling cell proliferation in stem cells and cancer cells. Genes Dev 16: 2991-3003.
    • (2002) Genes Dev , vol.16 , pp. 2991-3003
    • Tsai, R.Y.1    McKay, R.D.2
  • 51
    • 0033678851 scopus 로고    scopus 로고
    • The nucleolus: The magician's hat for cell cycle tricks
    • Visintin R, Amon A. (2000). The nucleolus: the magician's hat for cell cycle tricks. Curr Opin Cell Biol 12: 752.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 752
    • Visintin, R.1    Amon, A.2
  • 52
    • 0032254350 scopus 로고    scopus 로고
    • The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk- dependent phosphorylation
    • Visintin R, Craig K, Hwang ES, Prinz S, Tyers M, Amon A. (1998). The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk- dependent phosphorylation. Mol Cell 2: 709-718.
    • (1998) Mol Cell , vol.2 , pp. 709-718
    • Visintin, R.1    Craig, K.2    Hwang, E.S.3    Prinz, S.4    Tyers, M.5    Amon, A.6
  • 54
    • 0037056222 scopus 로고    scopus 로고
    • Escape of p53 protein from E6-mediated degradation in HeLa cells after cisplatin therapy
    • Wesierska-Gadek J, Schloffer D, Kotala V, Horky M. (2002). Escape of p53 protein from E6-mediated degradation in HeLa cells after cisplatin therapy. Int J Cancer 101: 128-136.
    • (2002) Int J Cancer , vol.101 , pp. 128-136
    • Wesierska-Gadek, J.1    Schloffer, D.2    Kotala, V.3    Horky, M.4
  • 55
    • 0036711651 scopus 로고    scopus 로고
    • Subnuclear shuttling of human telomerase induced by transformation and DNA damage
    • Wong JM, Kusdra L, Collins K. (2002). Subnuclear shuttling of human telomerase induced by transformation and DNA damage. Nat Cell Biol 4: 731-736.
    • (2002) Nat Cell Biol , vol.4 , pp. 731-736
    • Wong, J.M.1    Kusdra, L.2    Collins, K.3
  • 56
    • 0035887286 scopus 로고    scopus 로고
    • Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53
    • Xirodimas DP, Stephen CW, Lane DP. (2001). Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53. Exp Cell Res 270: 66-77.
    • (2001) Exp Cell Res , vol.270 , pp. 66-77
    • Xirodimas, D.P.1    Stephen, C.W.2    Lane, D.P.3
  • 57
    • 0037169562 scopus 로고    scopus 로고
    • A direct interaction between the survival motor neuron protein and p53 and its relationship to spinal muscular atrophy
    • Young PJ, Day PM, Zhou J, Androphy EJ, Morris GE, Lorson CL. (2002). A direct interaction between the survival motor neuron protein and p53 and its relationship to spinal muscular atrophy. J Biol Chem 277: 2852-2859.
    • (2002) J Biol Chem , vol.277 , pp. 2852-2859
    • Young, P.J.1    Day, P.M.2    Zhou, J.3    Androphy, E.J.4    Morris, G.E.5    Lorson, C.L.6
  • 58
    • 0024513462 scopus 로고
    • Ultrastructural changes in nucleoli and fibrillar centers under the effect of local ultraviolet microbeam irradiation of interphase culture cells
    • Zatsepina OV, Voronkova LN, Sakharov VN, Chentsov YS. (1989). Ultrastructural changes in nucleoli and fibrillar centers under the effect of local ultraviolet microbeam irradiation of interphase culture cells. Exp Cell Res 181: 94-104.
    • (1989) Exp Cell Res , vol.181 , pp. 94-104
    • Zatsepina, O.V.1    Voronkova, L.N.2    Sakharov, V.N.3    Chentsov, Y.S.4
  • 59
    • 0026703557 scopus 로고
    • Correlation between the conformational phenotype of p53 and its subcellular location
    • Zerrahn J, Deppert W, Weidemann D, Patschinsky T, Richards F, Milner J. (1992). Correlation between the conformational phenotype of p53 and its subcellular location. Oncogene 7: 1371-1381.
    • (1992) Oncogene , vol.7 , pp. 1371-1381
    • Zerrahn, J.1    Deppert, W.2    Weidemann, D.3    Patschinsky, T.4    Richards, F.5    Milner, J.6
  • 60
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang Y, Xiong Y, Yarbrough WG. (1998). ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92: 725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 61
    • 3142654673 scopus 로고    scopus 로고
    • Nuclear bodies and compartments: Functional roles and cellular signalling in health and disease
    • Zimber A, Nguyen QD, Gespach C. (2004). Nuclear bodies and compartments: functional roles and cellular signalling in health and disease. Cell Signal 16: 1085-1104.
    • (2004) Cell Signal , vol.16 , pp. 1085-1104
    • Zimber, A.1    Nguyen, Q.D.2    Gespach, C.3
  • 62
    • 0032888954 scopus 로고    scopus 로고
    • Zolotukhin AS, Felber BK. (1999). Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev. J Virol 73: 120-127.
    • Zolotukhin AS, Felber BK. (1999). Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev. J Virol 73: 120-127.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.