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Volumn 6, Issue 7, 2006, Pages 493-505

Nucleophosmin and cancer

Author keywords

[No Author keywords available]

Indexed keywords

ANAPLASTIC LYMPHOMA KINASE; ARF PROTEIN; CASPASE; CYCLIN A; CYCLIN DEPENDENT KINASE 2; CYCLIN E; CYCLINE; DEOXYRIBONUCLEASE; DNA; DNA DIRECTED DNA POLYMERASE ALPHA; DNA DIRECTED RNA POLYMERASE; HYBRID PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; INITIATION FACTOR 2ALPHA; INTERNAL TRANSCRIBED SPACER; MESSENGER RNA; NERVE GROWTH FACTOR; NUCLEOPHOSMIN; POLO LIKE KINASE 1; PROTEIN KINASE R; PROTEIN MDM2; PROTEIN P53; RETINOIC ACID RECEPTOR; RIBOSOME RNA; RNA POLYMERASE II; SHORT HAIRPIN RNA; SMALL NUCLEOLAR RIBONUCLEOPROTEIN; SUMO 1 PROTEIN; TUMOR MARKER; UNINDEXED DRUG;

EID: 33745534443     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1885     Document Type: Review
Times cited : (715)

References (146)
  • 1
    • 0023261706 scopus 로고
    • Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells
    • Feuerstein, N. & Mond, J. J. Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells. J. Immunol. 139, 1818-1822 (1987).
    • (1987) J. Immunol. , vol.139 , pp. 1818-1822
    • Feuerstein, N.1    Mond, J.J.2
  • 2
    • 0023369370 scopus 로고
    • A constitutive nucleolar protein identified as a member of the nucleoplasmin family
    • Schmidt-Zachmann, M. S., Hugle-Dorr, B. & Franke, W. W. A constitutive nucleolar protein identified as a member of the nucleoplasmin family. EMBO J. 6, 1881-1890 (1987).
    • (1987) EMBO J. , vol.6 , pp. 1881-1890
    • Schmidt-Zachmann, M.S.1    Hugle-Dorr, B.2    Franke, W.W.3
  • 3
    • 0023764934 scopus 로고
    • DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli. Correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23
    • Schmidt-Zachmann, M. S. & Franke, W. W. DNA cloning and amino acid sequence determination of a major constituent protein of mammalian nucleoli. Correspondence of the nucleoplasmin-related protein NO38 to mammalian protein B23. Chromosoma 96, 417-426 (1988).
    • (1988) Chromosoma , vol.96 , pp. 417-426
    • Schmidt-Zachmann, M.S.1    Franke, W.W.2
  • 4
    • 0016272411 scopus 로고
    • Phosphorylation of acid-soluble proteins in isolated nucleoli of Novikoff hepatoma ascites cells. Effects of divalent cations. Nucleolar phosphoproteins of normal rat liver and Novikoff hepatoma ascites cells
    • Kang, Y. J., Olson, M. O., Busch, H. & Jones, C. Phosphorylation of acid-soluble proteins in isolated nucleoli of Novikoff hepatoma ascites cells. Effects of divalent cations. Nucleolar phosphoproteins of normal rat liver and Novikoff hepatoma ascites cells. J. Biol. Chem. 249, 5580-5585 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 5580-5585
    • Kang, Y.J.1    Olson, M.O.2    Busch, H.3    Jones, C.4
  • 5
    • 0016823386 scopus 로고
    • Nucleolar phosphoproteins of normal rat liver and Novikoff hepatoma ascites cells
    • Kang, Y. J., Olson, M. O., Jones, C. & Busch, H. Nucleolar phosphoproteins of normal rat liver and Novikoff hepatoma ascites cells. Cancer Res. 35, 1470-1475 (1975).
    • (1975) Cancer Res. , vol.35 , pp. 1470-1475
    • Kang, Y.J.1    Olson, M.O.2    Jones, C.3    Busch, H.4
  • 6
    • 0023682002 scopus 로고
    • Identification of numatrin, the nuclear matrix protein associated with induction of mitogenesis, as the nucleolar protein B23. Implication for the role of the nucleolus in early transduction of mitogenic signals
    • Feuerstein, N., Chan, P. K. & Mond, J. J. Identification of numatrin, the nuclear matrix protein associated with induction of mitogenesis, as the nucleolar protein B23. Implication for the role of the nucleolus in early transduction of mitogenic signals. J. Biol. Chem. 263, 10608-10612 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 10608-10612
    • Feuerstein, N.1    Chan, P.K.2    Mond, J.J.3
  • 7
    • 0024595908 scopus 로고
    • Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth
    • Chan, W. Y. et al. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth. Biochemistry 28, 1033-1039 (1989).
    • (1989) Biochemistry , vol.28 , pp. 1033-1039
    • Chan, W.Y.1
  • 8
    • 24344437303 scopus 로고    scopus 로고
    • Role of nucleophosmin in embryonic development and tumorigenesis
    • Grisendi, S. et al. Role of nucleophosmin in embryonic development and tumorigenesis. Nature 437, 147-153 (2005). Shows for the first time that disruption of NPM expression in vivo leads to embryonic lethality at mid-gestation. The total or partial loss of Npm1 gene function leads to centrosome amplification, aneuploidy and cancer susceptibility.
    • (2005) Nature , vol.437 , pp. 147-153
    • Grisendi, S.1
  • 9
    • 26444561851 scopus 로고    scopus 로고
    • Nucleophosmin is required for DNA integrity and p19Arf protein stability
    • Colombo, E. et al. Nucleophosmin is required for DNA integrity and p19Arf protein stability. Mol. Cell. Biol. 25, 8874-86 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8874-8886
    • Colombo, E.1
  • 10
    • 19944427850 scopus 로고    scopus 로고
    • Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype
    • Falini, B. et al. Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype. N. Engl. J. Med. 352, 254-266 (2005). The first paper to identify the cytoplasmic dislocation of NPM and the mutation of exon 12 of the NPM1 gene as a hallmark of a large subgroup of AML (NPMc+ AML).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 254-266
    • Falini, B.1
  • 11
    • 0024966024 scopus 로고
    • Major nucleolar proteins shuttle between nucleus and cytoplasm
    • Borer, R. A., Lehner, C. F., Eppenberger, H. M. & Nigg, E. A. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56, 379-390 (1989).
    • (1989) Cell , vol.56 , pp. 379-390
    • Borer, R.A.1    Lehner, C.F.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 12
    • 0344309360 scopus 로고    scopus 로고
    • Nucleophosmin/B23 is a proliferate shuttle protein associated with nuclear matrix
    • Yun, J. P. et al. Nucleophosmin/B23 is a proliferate shuttle protein associated with nuclear matrix. J. Cell Biochem. 90, 1140-1148 (2003).
    • (2003) J. Cell Biochem. , vol.90 , pp. 1140-1148
    • Yun, J.P.1
  • 13
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • Hingorani, K., Szebeni, A. & Olson, M. O. Mapping the functional domains of nucleolar protein B23. J. Biol. Chem. 275, 24451-24457 (2000). In vitro analysis of the functional features of the different NPM molecular domains.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 14
    • 0032917157 scopus 로고    scopus 로고
    • Nucleolar protein B23 has molecular chaperone activities
    • Szebeni, A. & Olson, M. O. Nucleolar protein B23 has molecular chaperone activities. Protein Sci. 8, 905-912 (1999).
    • (1999) Protein Sci. , vol.8 , pp. 905-912
    • Szebeni, A.1    Olson, M.O.2
  • 15
    • 0035850837 scopus 로고    scopus 로고
    • Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone
    • Okuwaki, M., Matsumoto, K., Tsujimoto, M. & Nagata, K. Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone. FEBS Lett. 506, 272-276 (2001).
    • (2001) FEBS Lett. , vol.506 , pp. 272-276
    • Okuwaki, M.1    Matsumoto, K.2    Tsujimoto, M.3    Nagata, K.4
  • 16
    • 23844472662 scopus 로고    scopus 로고
    • Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription
    • Swaminathan, V., Kishore, A. H., Febitha, K. K. & Kundu, T. K. Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription. Mol. Cell. Biol. 25, 7534-7545 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7534-7545
    • Swaminathan, V.1    Kishore, A.H.2    Febitha, K.K.3    Kundu, T.K.4
  • 17
    • 0025147409 scopus 로고
    • Structure of the gene for rat nucleolar protein B23
    • Chang, J. H. & Olson, M. O. Structure of the gene for rat nucleolar protein B23. J. Biol. Chem. 265, 18227-18233 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 18227-18233
    • Chang, J.H.1    Olson, M.O.2
  • 18
    • 0027260688 scopus 로고
    • Expression and subcellular locations of two forms of nucleolar protein B23 in rat tissues and cells
    • Wang, D., Umekawa, H. & Olson, M. O. Expression and subcellular locations of two forms of nucleolar protein B23 in rat tissues and cells. Cell. Mol. Biol. Res. 39, 33-42 (1993).
    • (1993) Cell. Mol. Biol. Res. , vol.39 , pp. 33-42
    • Wang, D.1    Umekawa, H.2    Olson, M.O.3
  • 19
    • 0029914227 scopus 로고    scopus 로고
    • Sedimentation analyses of the salt- And divalent metal ion-induced oligomerization of nucleolar protein B23
    • Herrera, J. E., Correia, J. J., Jones, A. E. & Olson, M. O. Sedimentation analyses of the salt- and divalent metal ion-induced oligomerization of nucleolar protein B23. Biochemistry 35, 2668-2673 (1996).
    • (1996) Biochemistry , vol.35 , pp. 2668-2673
    • Herrera, J.E.1    Correia, J.J.2    Jones, A.E.3    Olson, M.O.4
  • 20
    • 9944245516 scopus 로고    scopus 로고
    • The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus
    • Namboodiri, V. M., Akey, I. V., Schmidt-Zachmann, M. S., Head, J. F. & Akey, C. W. The structure and function of Xenopus NO38-core, a histone chaperone in the nucleolus. Structure 12, 2149-2160 (2004).
    • (2004) Structure , vol.12 , pp. 2149-2160
    • Namboodiri, V.M.1    Akey, I.V.2    Schmidt-Zachmann, M.S.3    Head, J.F.4    Akey, C.W.5
  • 21
    • 0028135012 scopus 로고
    • The nucleic acid binding activity of nucleolar protein B23. 1 Resides in its carboxyl-terminal end. Interaction of nucleolar phosphoprotein B23 with nucleic acids
    • Wang, D. et al. The nucleic acid binding activity of nucleolar protein B23. 1 resides in its carboxyl-terminal end. Interaction of nucleolar phosphoprotein B23 with nucleic acids. J. Biol. Chem. 269, 30994-30998 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30994-30998
    • Wang, D.1
  • 22
    • 0035985191 scopus 로고    scopus 로고
    • The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype
    • Okuwaki, M., Tsujimoto, M. & Nagata, K. The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. Mol. Biol. Cell. 13, 2016-2030 (2002).
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 2016-2030
    • Okuwaki, M.1    Tsujimoto, M.2    Nagata, K.3
  • 23
    • 0032189707 scopus 로고    scopus 로고
    • Preferential cleavage in pre-ribosomal RNA byprotein B23 endoribonuclease
    • Savkur, R. S. & Olson, M. O. Preferential cleavage in pre-ribosomal RNA byprotein B23 endoribonuclease. Nucleic Acids Res. 26, 4508-4515 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4508-4515
    • Savkur, R.S.1    Olson, M.O.2
  • 24
    • 18944395803 scopus 로고    scopus 로고
    • Nucleophosmin/B23, a nuclear PI(3, 4, 5)P(3) receptor, mediates the antiapoptotic actions of NGF by inhibiting CAD
    • 3 receptor that mediates the anti-apoptotic effects of NGF by inhibiting the DNA fragmentation activity of CAD.
    • (2005) Mol. Cell , vol.18 , pp. 435-445
    • Ahn, J.Y.1
  • 25
    • 0026718967 scopus 로고
    • Genes preferentially expressed in embryo stomach are predominantly expressed in gastric cancer
    • Tanaka, M., Sasaki, H., Kino, I., Sugimura, T. & Terada, M. Genes preferentially expressed in embryo stomach are predominantly expressed in gastric cancer. Cancer Res. 52, 3372-3377 (1992).
    • (1992) Cancer Res. , vol.52 , pp. 3372-3377
    • Tanaka, M.1    Sasaki, H.2    Kino, I.3    Sugimura, T.4    Terada, M.5
  • 27
    • 0342437099 scopus 로고    scopus 로고
    • Induction of immune responses to ovarian tumor antigens by multiparity
    • Shields, L. B. et al. Induction of immune responses to ovarian tumor antigens by multiparity. J. Soc. Gynecol. Investig. 4, 298-304 (1997).
    • (1997) J. Soc. Gynecol. Investig. , vol.4 , pp. 298-304
    • Shields, L.B.1
  • 28
    • 0033151790 scopus 로고    scopus 로고
    • Monoclonal antibody to prostate cancer nuclear matrix protein (PRO:4-216) recognizes nucleophosmin/B23
    • Subong, E. N. et al. Monoclonal antibody to prostate cancer nuclear matrix protein (PRO:4-216) recognizes nucleophosmin/B23. Prostate 39, 298-304 (1999).
    • (1999) Prostate , vol.39 , pp. 298-304
    • Subong, E.N.1
  • 29
    • 7444253888 scopus 로고    scopus 로고
    • Association of nucleophosmin/B23 mRNA expression with clinical outcome in patients with bladder carcinoma
    • Tsui, K. H., Cheng, A. J., Chang, P. L., Pan, T. L. & Yung, B. Y. Association of nucleophosmin/B23 mRNA expression with clinical outcome in patients with bladder carcinoma. Urology 64, 839-844 (2004).
    • (2004) Urology , vol.64 , pp. 839-844
    • Tsui, K.H.1    Cheng, A.J.2    Chang, P.L.3    Pan, T.L.4    Yung, B.Y.5
  • 30
    • 0032457510 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis analyses identify nucleophosmin as an estrogen regulated protein associated with acquired estrogen-independence in human breast cancer cells
    • Skaar, T. C. et al. Two-dimensional gel electrophoresis analyses identify nucleophosmin as an estrogen regulated protein associated with acquired estrogen-independence in human breast cancer cells. J. Steroid Biochem. Mol. Biol. 67, 391-402 (1998).
    • (1998) J. Steroid Biochem. Mol. Biol. , vol.67 , pp. 391-402
    • Skaar, T.C.1
  • 31
    • 0030022316 scopus 로고    scopus 로고
    • The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion
    • Redner, R. L., Rush, E. A., Faas, S., Rudert, W. A. & Corey, S. J. The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion. Blood 87, 882-886 (1996).
    • (1996) Blood , vol.87 , pp. 882-886
    • Redner, R.L.1    Rush, E.A.2    Faas, S.3    Rudert, W.A.4    Corey, S.J.5
  • 32
    • 0028198206 scopus 로고
    • Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma
    • Morris, S. W. et al. Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma. Science 263, 1281-1284 (1994).
    • (1994) Science , vol.263 , pp. 1281-1284
    • Morris, S.W.1
  • 33
    • 0024502495 scopus 로고
    • Clinicopathologic manifestations and breakpoints of the t(3;5) in patients with acute nonlymphocytic leukemia
    • Raimondi, S. C. et al. Clinicopathologic manifestations and breakpoints of the t(3;5) in patients with acute nonlymphocytic leukemia. Leukemia 3, 42-47 (1989).
    • (1989) Leukemia , vol.3 , pp. 42-47
    • Raimondi, S.C.1
  • 34
    • 0030071926 scopus 로고    scopus 로고
    • The t(3;5)(q25. 1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1
    • Yoneda-Kato, N. et al. The t(3;5)(q25. 1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1. Oncogene 12, 265-275 (1996).
    • (1996) Oncogene , vol.12 , pp. 265-275
    • Yoneda-Kato, N.1
  • 37
    • 31444455542 scopus 로고    scopus 로고
    • Loss of the NPM1 gene in myeloid disorders with chromosome 5 rearrangements
    • Berger, R. et al. Loss of the NPM1 gene in myeloid disorders with chromosome 5 rearrangements. Leukemia 20, 319-321 (2006).
    • (2006) Leukemia , vol.20 , pp. 319-321
    • Berger, R.1
  • 38
    • 0030934862 scopus 로고    scopus 로고
    • Role of the nucleophosmin (NPM) portion of the non-Hodgkin's lymphoma-associated NPM-anaplastic lymphoma kinase fusion protein in oncogenesis
    • Bischof, D., Pulford, K., Mason, D. Y. & Morris, S. W. Role of the nucleophosmin (NPM) portion of the non-Hodgkin's lymphoma-associated NPM-anaplastic lymphoma kinase fusion protein in oncogenesis. Mol. Cell. Biol. 17, 2312-2325 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2312-2325
    • Bischof, D.1    Pulford, K.2    Mason, D.Y.3    Morris, S.W.4
  • 39
    • 0025907434 scopus 로고
    • In vivo and in vitro phosphorylation studies of numatrin, a cell cycle regulated nuclear protein, in insulin-stimulated NIH 3T3 HIR cells
    • Feuerstein, N. & Randazzo, P. A. In vivo and in vitro phosphorylation studies of numatrin, a cell cycle regulated nuclear protein, in insulin-stimulated NIH 3T3 HIR cells. Exp. Cell Res. 194, 289-296 (1991).
    • (1991) Exp. Cell Res. , vol.194 , pp. 289-296
    • Feuerstein, N.1    Randazzo, P.A.2
  • 40
    • 0033566141 scopus 로고    scopus 로고
    • Gene expression in proliferating human erythroid cells
    • Gubin, A. N., Njoroge, J. M., Bouffard, G. G. & Miller, J. L. Gene expression in proliferating human erythroid cells. Genomics 59, 168-177 (1999).
    • (1999) Genomics , vol.59 , pp. 168-177
    • Gubin, A.N.1    Njoroge, J.M.2    Bouffard, G.G.3    Miller, J.L.4
  • 41
    • 0036681061 scopus 로고    scopus 로고
    • A major nucleolar protein B23 as a marker of proliferation activity of human peripheral lymphocytes
    • Dergunova, N. N. et al. A major nucleolar protein B23 as a marker of proliferation activity of human peripheral lymphocytes. Immunol. Lett. 83, 67-72 (2002).
    • (2002) Immunol. Lett. , vol.83 , pp. 67-72
    • Dergunova, N.N.1
  • 42
    • 0035930544 scopus 로고    scopus 로고
    • Characterization of nucleophosmin (B23) as a Myc target by scanning chromatin immunoprecipitation
    • Zeller, K. I. et al. Characterization of nucleophosmin (B23) as a Myc target by scanning chromatin immunoprecipitation. J. Biol. Chem. 276, 48285-48291 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48285-48291
    • Zeller, K.I.1
  • 43
    • 17744400301 scopus 로고    scopus 로고
    • N-myc enhances the expression of a large set of genes functioning in ribosome biogenesis and protein synthesis
    • Boon, K. et al. N-myc enhances the expression of a large set of genes functioning in ribosome biogenesis and protein synthesis. EMBO J. 20, 1383-93 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1383-1393
    • Boon, K.1
  • 44
    • 0033019332 scopus 로고    scopus 로고
    • Nucleolar protein B23.1 binds to retinoblastoma protein and synergistically stimulates DNA polymerase α activity
    • Takemura, M. et al. Nucleolar protein B23.1 binds to retinoblastoma protein and synergistically stimulates DNA polymerase α activity. J. Biochem. (Tokyo) 125, 904-909 (1999).
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 904-909
    • Takemura, M.1
  • 45
    • 0032545978 scopus 로고    scopus 로고
    • Down-regulation of nucleophosmin/B23 during retinoic acid-induced differentiation of human promyelocytic leukemia HL-60 cells
    • Hsu, C. Y. & Yung, B. Y. Down-regulation of nucleophosmin/B23 during retinoic acid-induced differentiation of human promyelocytic leukemia HL-60 cells. Oncogene 16, 915-923 (1998).
    • (1998) Oncogene , vol.16 , pp. 915-923
    • Hsu, C.Y.1    Yung, B.Y.2
  • 46
    • 0033401328 scopus 로고    scopus 로고
    • Decrease in nucleophosmin/B23 mRNA and telomerase activity during indomethacin-induced apoptosis of gastric KATO-III cancer cells
    • You, B. J. et al. Decrease in nucleophosmin/B23 mRNA and telomerase activity during indomethacin-induced apoptosis of gastric KATO-III cancer cells. Naunyn Schmiedebergs Arch. Pharmacol. 360, 683-690 (1999).
    • (1999) Naunyn Schmiedebergs Arch. Pharmacol. , vol.360 , pp. 683-690
    • You, B.J.1
  • 47
    • 10044276927 scopus 로고    scopus 로고
    • c-Myc-mediated expression of nucleophosmin/B23 decreases during retinoic acid-induced differentiation of human leukemia HL-60 cells
    • Yung, B. Y. c-Myc-mediated expression of nucleophosmin/B23 decreases during retinoic acid-induced differentiation of human leukemia HL-60 cells. FEBS. Lett. 578, 211-216 (2004).
    • (2004) FEBS. Lett. , vol.578 , pp. 211-216
    • Yung, B.Y.1
  • 48
    • 0033590973 scopus 로고    scopus 로고
    • Down-regulation of nucleophosmin/B23 mRNA delays the entry of cells into mitosis
    • Jiang, P. S. & Yung, B. Y. Down-regulation of nucleophosmin/B23 mRNA delays the entry of cells into mitosis. Biochem. Biophys. Res. Commun. 257, 865-870 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 865-870
    • Jiang, P.S.1    Yung, B.Y.2
  • 49
    • 0033006804 scopus 로고    scopus 로고
    • Berberine-induced apoptosis of human leukemia HL-60 cells is associated with down-regulation of nucleophosmin/B23 and telomerase activity
    • Wu, H. L., Hsu, C. Y., Liu, W. H. & Yung, B. Y. Berberine-induced apoptosis of human leukemia HL-60 cells is associated with down-regulation of nucleophosmin/B23 and telomerase activity. Int. J. Cancer 81, 923-929 (1999).
    • (1999) Int. J. Cancer , vol.81 , pp. 923-929
    • Wu, H.L.1    Hsu, C.Y.2    Liu, W.H.3    Yung, B.Y.4
  • 50
    • 0033810002 scopus 로고    scopus 로고
    • Over-expression of nucleophosmin/B23 decreases the susceptibility of human leukemia HL-60 cells to retinoic acid-induced differentiation and apoptosis
    • Hsu, C. Y. & Yung, B. Y. Over-expression of nucleophosmin/B23 decreases the susceptibility of human leukemia HL-60 cells to retinoic acid-induced differentiation and apoptosis. Int. J. Cancer 88, 392-400 (2000).
    • (2000) Int. J. Cancer , vol.88 , pp. 392-400
    • Hsu, C.Y.1    Yung, B.Y.2
  • 51
    • 6344288701 scopus 로고    scopus 로고
    • ARF impedes NPM/B23 shuttling in an Mdm2-sensitive tumor suppressor pathway
    • Brady, S. N., Yu, Y., Maggi, L. B., Jr. & Weber, J. D. ARF impedes NPM/B23 shuttling in an Mdm2-sensitive tumor suppressor pathway. Mol. Cell. Biol. 24, 9327-9338 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9327-9338
    • Brady, S.N.1    Yu, Y.2    Maggi Jr., L.B.3    Weber, J.D.4
  • 52
    • 0024305925 scopus 로고
    • Interaction of nucleolar phosphoprotein B23 with nucleic acids
    • Dumbar, T. S., Gentry, G. A. & Olson, M. O. Interaction of nucleolar phosphoprotein B23 with nucleic acids. Biochemistry 28, 9495-9501 (1989).
    • (1989) Biochemistry , vol.28 , pp. 9495-9501
    • Dumbar, T.S.1    Gentry, G.A.2    Olson, M.O.3
  • 53
    • 0016255174 scopus 로고
    • Comparison of proteins of ribosomal subunits and nucleolar preribosomal particles from Novikoff hepatoma ascites cells by two-dimensional polyacrylamide gel electrophoresis
    • Prestayko, A. W., Klomp, G. R., Schmoll, D. J. & Busch, H. Comparison of proteins of ribosomal subunits and nucleolar preribosomal particles from Novikoff hepatoma ascites cells by two-dimensional polyacrylamide gel electrophoresis. Biochemistry 13, 1945-1951 (1974).
    • (1974) Biochemistry , vol.13 , pp. 1945-1951
    • Prestayko, A.W.1    Klomp, G.R.2    Schmoll, D.J.3    Busch, H.4
  • 54
    • 0022510230 scopus 로고
    • Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction
    • Olson, M. O., Wallace, M. O., Herrera, A. H., Marshall-Carlson, L. & Hunt, R. C. Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction. Biochemistry 25, 484-491 (1986).
    • (1986) Biochemistry , vol.25 , pp. 484-491
    • Olson, M.O.1    Wallace, M.O.2    Herrera, A.H.3    Marshall-Carlson, L.4    Hunt, R.C.5
  • 55
    • 0028786597 scopus 로고
    • The ribonuclease activity of nucleolar protein B23
    • Herrera, J. E., Savkur, R. & Olson, M. O. The ribonuclease activity of nucleolar protein B23. Nucleic Acids Res. 23, 3974-3979 (1995).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3974-3979
    • Herrera, J.E.1    Savkur, R.2    Olson, M.O.3
  • 56
    • 0345276485 scopus 로고    scopus 로고
    • Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation
    • Itahana, K. et al. Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation. Mol. Cell 12, 1151-1164 (2003). Downregulation of NPM expression affects the processing of pre-ribosomal RNA and induces cell death. ARF is proposed to promote the polyubiquitylation and degradation of NPM, a possible target of the ability of ARF to inhibit rRNA processing in a p53-independent manner.
    • (2003) Mol. Cell , vol.12 , pp. 1151-1164
    • Itahana, K.1
  • 57
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero, D. & Pandolfi, P. P. Does the ribosome translate cancer? Nature Rev. Cancer 3, 179-192 (2003).
    • (2003) Nature Rev. Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 58
    • 0035839844 scopus 로고    scopus 로고
    • Translocations involving c-myc and c-myc function
    • Boxer, L. M. & Dang, C. V. Translocations involving c-myc and c-myc function. Oncogene 20, 5595-5610 (2001).
    • (2001) Oncogene , vol.20 , pp. 5595-5610
    • Boxer, L.M.1    Dang, C.V.2
  • 59
    • 1642499357 scopus 로고    scopus 로고
    • Physical and functional interactions of the ARF tumor suppressor protein with nucleophosmin/B23
    • Bertwistle, D., Sugimoto, M. & Sherr, C. J. Physical and functional interactions of the ARF tumor suppressor protein with nucleophosmin/B23. Mol. Cell. Biol. 24, 985-996 (2004). Shows that a significant proportion of nucleolar ARF associates with NPM in high-molecular-weight complexes (2-5 MDa), where NPM regulates the ability of ARF to retard rRNA processing.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 985-996
    • Bertwistle, D.1    Sugimoto, M.2    Sherr, C.J.3
  • 60
    • 0037291204 scopus 로고    scopus 로고
    • Nucleolar ARF tumor suppressor inhibits ribosomal RNA processing
    • ARF. As ARF also prevents the proliferation of cells that lack p53, it is shown to be able to specifically retard the processing of ribosomal RNA precursors, an effect that requires neither p53 nor MDM2.
    • (2003) Mol. Cell , vol.11 , pp. 415-424
    • Sugimoto, M.1    Kuo, M.L.2    Roussel, M.F.3    Sherr, C.J.4
  • 61
    • 0037160082 scopus 로고    scopus 로고
    • Pescadillo is essential for nucleolar assembly, ribosome biogenesis, and mammalian cell proliferation
    • Lerch-Gaggl, A. et al. Pescadillo is essential for nucleolar assembly, ribosome biogenesis, and mammalian cell proliferation. J. Biol. Chem. 277, 45347-45355 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45347-45355
    • Lerch-Gaggl, A.1
  • 62
    • 27744578664 scopus 로고    scopus 로고
    • Nucleophosmin/B23, a multifunctional protein that can regulate apoptosis
    • Ye, K. Nucleophosmin/B23, a multifunctional protein that can regulate apoptosis. Cancer Biol. Ther. 4, 918-923 (2005).
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 918-923
    • Ye, K.1
  • 63
    • 0030930058 scopus 로고    scopus 로고
    • Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity
    • Kondo, T. et al. Identification and characterization of nucleophosmin/B23/numatrin which binds the anti-oncogenic transcription factor IRF-1 and manifests oncogenic activity. Oncogene 15, 1275-1281 (1997).
    • (1997) Oncogene , vol.15 , pp. 1275-1281
    • Kondo, T.1
  • 64
    • 0036198225 scopus 로고    scopus 로고
    • Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: Enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression
    • Wu, M. H., Chang, J. H. & Yung, B. Y. Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression. Carcinogenesis 23, 93-100 (2002).
    • (2002) Carcinogenesis , vol.23 , pp. 93-100
    • Wu, M.H.1    Chang, J.H.2    Yung, B.Y.3
  • 65
    • 0036182472 scopus 로고    scopus 로고
    • IRF-1 as a negative regulator of cell proliferation
    • Romeo, G. et al. IRF-1 as a negative regulator of cell proliferation. J. Interferon Cytokine Res. 22, 39-47 (2002).
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 39-47
    • Romeo, G.1
  • 66
    • 4744348300 scopus 로고    scopus 로고
    • Hypoxia-induced nucleophosmin protects cell death through inhibition of p53
    • Li, J., Zhang, X., Sejas, D. P., Bagby, G. C. & Pang, Q. Hypoxia-induced nucleophosmin protects cell death through inhibition of p53. J. Biol. Chem. 279, 41275-41279 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 41275-41279
    • Li, J.1    Zhang, X.2    Sejas, D.P.3    Bagby, G.C.4    Pang, Q.5
  • 67
    • 0035094982 scopus 로고    scopus 로고
    • Host defense, viruses and apoptosis
    • Barber, G. N. Host defense, viruses and apoptosis. Cell Death Differ. 8, 113-126 (2001).
    • (2001) Cell Death Differ. , vol.8 , pp. 113-126
    • Barber, G.N.1
  • 69
    • 0142149184 scopus 로고    scopus 로고
    • Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR
    • Pang, Q. et al. Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR. J. Biol. Chem. 278, 41709-41717 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 41709-41717
    • Pang, Q.1
  • 70
    • 27644583020 scopus 로고    scopus 로고
    • Negative regulation of p53 by nucleophosmin antagonizes stress-induced apoptosis in human normal and malignant hematopoietic cells
    • Li, J., Zhang, X., Sejas, D. P. & Pang, Q. Negative regulation of p53 by nucleophosmin antagonizes stress-induced apoptosis in human normal and malignant hematopoietic cells. Leuk. Res. (2005).
    • (2005) Leuk. Res.
    • Li, J.1    Zhang, X.2    Sejas, D.P.3    Pang, Q.4
  • 71
    • 0022428630 scopus 로고
    • Translocation of nucleolar phosphoprotein B23 (37 kDa/pl 5. 1) induced by selective inhibitors of ribosome synthesis
    • Yung, B. Y., Busch, H. & Chan, P. K. Translocation of nucleolar phosphoprotein B23 (37 kDa/pl 5. 1) induced by selective inhibitors of ribosome synthesis. Biochim. Biophys. Acta 826, 167-173 (1985).
    • (1985) Biochim. Biophys. Acta , vol.826 , pp. 167-173
    • Yung, B.Y.1    Busch, H.2    Chan, P.K.3
  • 72
    • 0025114362 scopus 로고
    • Short exposure to actinomycin D induces 'reversible' translocation of protein B23 as well as 'reversible' inhibition of cell growth and RNA synthesis in HeLa cells
    • Yung, B. Y., Bor, A. M. & Chan, P. K. Short exposure to actinomycin D induces 'reversible' translocation of protein B23 as well as 'reversible' inhibition of cell growth and RNA synthesis in HeLa cells. Cancer Res. 50, 5987-5991 (1990).
    • (1990) Cancer Res. , vol.50 , pp. 5987-5991
    • Yung, B.Y.1    Bor, A.M.2    Chan, P.K.3
  • 73
    • 0023274234 scopus 로고
    • Nucleolar protein B23 translocation after doxorubicin treatment in murine tumor cells
    • Chan, P. K., Aldrich, M. B. & Yung, B. Y. Nucleolar protein B23 translocation after doxorubicin treatment in murine tumor cells. Cancer Res. 47, 3798-3801 (1987).
    • (1987) Cancer Res. , vol.47 , pp. 3798-3801
    • Chan, P.K.1    Aldrich, M.B.2    Yung, B.Y.3
  • 74
    • 0026671702 scopus 로고
    • Phosphoprotein B23 translocation and modulation of actinomycin D and doxorubicin cytotoxicity by dipyridamole in HeLa cells
    • Bor, A. M., Chang, F. J. & Yung, B. Y. Phosphoprotein B23 translocation and modulation of actinomycin D and doxorubicin cytotoxicity by dipyridamole in HeLa cells. Int. J. Cancer 52, 658-663 (1992).
    • (1992) Int. J. Cancer , vol.52 , pp. 658-663
    • Bor, A.M.1    Chang, F.J.2    Yung, B.Y.3
  • 75
    • 0026443587 scopus 로고
    • Characterization and cellular localization of nucleophosmin/B23 in HeLa cells treated with selected cytotoxic agents (studies of B23-translocation mechanism)
    • Chan, P. K. Characterization and cellular localization of nucleophosmin/B23 in HeLa cells treated with selected cytotoxic agents (studies of B23-translocation mechanism). Exp. Cell Res. 203, 174-181 (1992).
    • (1992) Exp. Cell Res. , vol.203 , pp. 174-181
    • Chan, P.K.1
  • 76
    • 0037137873 scopus 로고    scopus 로고
    • Involvement of nucleophosmin/B23 in the response of HeLa cells to UV irradiation
    • Wu, M. H., Chang, J. H., Chou, C. C. & Yung, B. Y. Involvement of nucleophosmin/B23 in the response of HeLa cells to UV irradiation. Int. J. Cancer 97, 297-305 (2002).
    • (2002) Int. J. Cancer , vol.97 , pp. 297-305
    • Wu, M.H.1    Chang, J.H.2    Chou, C.C.3    Yung, B.Y.4
  • 77
    • 2342491487 scopus 로고    scopus 로고
    • Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation
    • Kurki, S. et al. Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation. Cancer Cell 5, 465-475 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 465-475
    • Kurki, S.1
  • 78
    • 0026352122 scopus 로고
    • Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: Dissociation by the Rev response element
    • Fankhauser, C., Izaurralde, E., Adachi, Y., Wingfield, P. & Laemmli, U. K. Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element. Mol. Cell. Biol. 11, 2567-2575 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2567-2575
    • Fankhauser, C.1    Izaurralde, E.2    Adachi, Y.3    Wingfield, P.4    Laemmli, U.K.5
  • 79
    • 0030956564 scopus 로고    scopus 로고
    • Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat
    • Li, Y. P. Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat. J. Virol. 71, 4098-4102 (1997).
    • (1997) J. Virol. , vol.71 , pp. 4098-4102
    • Li, Y.P.1
  • 80
    • 0029080215 scopus 로고
    • The cytotoxicity of human immunodeficiency virus type 1 Rev: Implications for its interaction with the nucleolar protein B23
    • Miyazaki, Y. et al. The cytotoxicity of human immunodeficiency virus type 1 Rev: implications for its interaction with the nucleolar protein B23. Exp. Cell Res. 219, 93-101 (1995).
    • (1995) Exp. Cell Res. , vol.219 , pp. 93-101
    • Miyazaki, Y.1
  • 81
    • 0035816633 scopus 로고    scopus 로고
    • The nucleolar phosphoprotein B23 interacts with hepatitis delta antigens and modulates the hepatitis delta virus RNA replication
    • Huang, W. H., Yung, B. Y., Syu, W. J. & Lee, Y. H. The nucleolar phosphoprotein B23 interacts with hepatitis delta antigens and modulates the hepatitis delta virus RNA replication. J. Biol. Chem. 276, 25166-25175 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 25166-25175
    • Huang, W.H.1    Yung, B.Y.2    Syu, W.J.3    Lee, Y.H.4
  • 82
    • 20544446874 scopus 로고    scopus 로고
    • Nucleophosmin/B23-binding peptide inhibits tumor growth and up-regulates transcriptional activity of p53
    • Chan, H. J., Weng, J. J. & Yung, B. Y. Nucleophosmin/ B23-binding peptide inhibits tumor growth and up-regulates transcriptional activity of p53. Biochem. Biophys. Res. Commun. 333, 396-403 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 396-403
    • Chan, H.J.1    Weng, J.J.2    Yung, B.Y.3
  • 84
    • 0030728468 scopus 로고    scopus 로고
    • Tumor suppression at the mouse INK4a locus mediated by the alternative reading frame product p19ARF
    • Kamijo, T. et al. Tumor suppression at the mouse INK4a locus mediated by the alternative reading frame product p19ARF. Cell 91, 649-659 (1997).
    • (1997) Cell , vol.91 , pp. 649-659
    • Kamijo, T.1
  • 85
    • 0035941033 scopus 로고    scopus 로고
    • Defining the molecular basis of Arf and Hdm2 interactions
    • Bothner, B. et al. Defining the molecular basis of Arf and Hdm2 interactions. J. Mol. Biol. 314, 263-277 (2001).
    • (2001) J. Mol. Biol. , vol.314 , pp. 263-277
    • Bothner, B.1
  • 86
    • 3543148255 scopus 로고    scopus 로고
    • N-terminal polyubiquitination and degradation of the Arf tumor suppressor
    • Kuo, M. L., den Besten, W., Bertwistle, D., Roussel, M. F. & Sherr, C. J. N-terminal polyubiquitination and degradation of the Arf tumor suppressor. Genes Dev. 18, 1862-1874 (2004). Shows that NPM, which binds to ARF with high stoichiometry, is able to retard ARF turnover. NPM is crucial for ARF stability, as ARF mutants that do not efficiently associate with NPM are unstable and functionally impaired.
    • (2004) Genes Dev. , vol.18 , pp. 1862-1874
    • Kuo, M.L.1    Den Besten, W.2    Bertwistle, D.3    Roussel, M.F.4    Sherr, C.J.5
  • 87
    • 0035487104 scopus 로고    scopus 로고
    • The INK4a/ARF network in tumour suppression
    • Sherr, C. J. The INK4a/ARF network in tumour suppression. Nature Rev. Mol. Cell Biol. 2, 731-737 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 731-737
    • Sherr, C.J.1
  • 88
    • 0032191393 scopus 로고    scopus 로고
    • Tumor surveillance via the ARF-p53 pathway
    • Sherr, C. J. Tumor surveillance via the ARF-p53 pathway. Genes Dev. 12, 2984-2991 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2984-2991
    • Sherr, C.J.1
  • 89
    • 13444287955 scopus 로고    scopus 로고
    • Nucleophosmin (B23) targets ARF to nucleoli and inhibits its function
    • Korgaonkar, C. et al. Nucleophosmin (B23) targets ARF to nucleoli and inhibits its function. Mol. Cell. Biol. 25, 1258-1271 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1258-1271
    • Korgaonkar, C.1
  • 90
    • 0034744224 scopus 로고    scopus 로고
    • Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus
    • Llanos, S., Clark, P. A., Rowe, J. & Peters, G. Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus. Nature Cell. Biol. 3, 445-452 (2001).
    • (2001) Nature Cell. Biol. , vol.3 , pp. 445-452
    • Llanos, S.1    Clark, P.A.2    Rowe, J.3    Peters, G.4
  • 91
    • 17644416385 scopus 로고    scopus 로고
    • Nucleophosmin in acute myelogenous leukemia
    • author reply 1819-1820
    • Nakagawa, M., Kameoka, Y. & Suzuki, R. Nucleophosmin in acute myelogenous leukemia. N. Engl. J. Med. 352, 1819-1820; author reply 1819-1820 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1819-1820
    • Nakagawa, M.1    Kameoka, Y.2    Suzuki, R.3
  • 92
    • 33645802652 scopus 로고    scopus 로고
    • Both carboxy-terminus NES motif and mutated tryptophan(s) are crucial for aberrant nuclear export of nucleophosmin leukemic mutants in NPMc + AML
    • Falini, B. et al. Both carboxy-terminus NES motif and mutated tryptophan(s) are crucial for aberrant nuclear export of nucleophosmin leukemic mutants in NPMc + AML. Blood 107, 4514-4523 (2006). Elucidates the molecular mechanism of altered traffic of NPM and its cytoplasmic accumulation in NPMc+ AML.
    • (2006) Blood , vol.107 , pp. 4514-4523
    • Falini, B.1
  • 93
    • 27744440147 scopus 로고    scopus 로고
    • Myeloid leukemia-associated nucleophosmin mutants perturb p53-dependent and independent activities of the Arf tumor suppressor protein
    • den Besten, W., Kuo, M. L., Williams, R. T. & Sherr, C. J. Myeloid leukemia-associated nucleophosmin mutants perturb p53-dependent and independent activities of the Arf tumor suppressor protein. Cell Cycle 4, 1593-1598 (2005).
    • (2005) Cell Cycle , vol.4 , pp. 1593-1598
    • Den Besten, W.1    Kuo, M.L.2    Williams, R.T.3    Sherr, C.J.4
  • 94
    • 33645526300 scopus 로고    scopus 로고
    • Delocalization and destabilization of the Arf tumor suppressor by the leukemia-associated NPM mutant
    • Colombo, E. et al. Delocalization and destabilization of the Arf tumor suppressor by the leukemia-associated NPM mutant. Cancer Res. 66, 3044-3050 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 3044-3050
    • Colombo, E.1
  • 95
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. p53, the cellular gatekeeper for growth and division. Cell 88, 323-331 (1997).
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 96
    • 0033579412 scopus 로고    scopus 로고
    • Regulation of the p53 tumor suppressor protein
    • Oren, M. Regulation of the p53 tumor suppressor protein. J. Biol. Chem. 274, 36031-36034 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36031-36034
    • Oren, M.1
  • 97
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi, C. P. & Milner, J. Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J. 22, 6068-6077 (2003). Shows that the nucleolus functions as a stress sensor that is responsible for the maintenance of low levels of p53 in proliferating cells.
    • (2003) EMBO J. , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 98
    • 0347717910 scopus 로고    scopus 로고
    • Cancer: Guarding the guardian?
    • Horn, H. F. & Vousden, K. H. Cancer: guarding the guardian? Nature 427, 110-111 (2004).
    • (2004) Nature , vol.427 , pp. 110-111
    • Horn, H.F.1    Vousden, K.H.2
  • 99
    • 0034977001 scopus 로고    scopus 로고
    • Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: Effects of nucleolar protein Bop1 on G(1)/S transition
    • Pestov, D. G., Strezoska, Z. & Lau, L. F. Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition. Mol. Cell. Biol. 21, 4246-4255 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4246-4255
    • Pestov, D.G.1    Strezoska, Z.2    Lau, L.F.3
  • 100
    • 0036302062 scopus 로고    scopus 로고
    • Nucleophosmin regulates the stability and transcriptional activity of p53
    • Colombo, E., Marine, J. C., Danovi, D., Falini, B. & Pelicci, P. G. Nucleophosmin regulates the stability and transcriptional activity of p53. Nature Cell. Biol. 4, 529-533 (2002).
    • (2002) Nature Cell. Biol. , vol.4 , pp. 529-533
    • Colombo, E.1    Marine, J.C.2    Danovi, D.3    Falini, B.4    Pelicci, P.G.5
  • 101
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D. & Lowe, S. W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88, 593-602 (1997).
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 102
    • 0033616501 scopus 로고    scopus 로고
    • GADD45 induction of a G2/M cell cycle checkpoint
    • Wang, X. W. et al. GADD45 induction of a G2/M cell cycle checkpoint. Proc. Natl Acad. Sci. USA 96, 3706-3711 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3706-3711
    • Wang, X.W.1
  • 103
    • 0344604528 scopus 로고    scopus 로고
    • Genomic instability in Gadd45a-deficient mice
    • Hollander, M. C. et al. Genomic instability in Gadd45a-deficient mice. Nature Genet. 23, 176-184 (1999).
    • (1999) Nature Genet. , vol.23 , pp. 176-184
    • Hollander, M.C.1
  • 104
    • 15744392470 scopus 로고    scopus 로고
    • B23 regulates GADD45a nuclear translocation and contributes to GADD45a-induced cell cycle G2-M arrest
    • Gao, H. et al. B23 regulates GADD45a nuclear translocation and contributes to GADD45a-induced cell cycle G2-M arrest. J. Biol. Chem. 280, 10988-10996 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 10988-10996
    • Gao, H.1
  • 105
    • 19544375560 scopus 로고    scopus 로고
    • A proteomics approach for the identification of nucleophosmin and heterogeneous nuclear ribonucleoprotein C1/C2 as chromatin-binding proteins in response to DNA double-strand breaks
    • Lee, S. Y. et al. A proteomics approach for the identification of nucleophosmin and heterogeneous nuclear ribonucleoprotein C1/C2 as chromatin-binding proteins in response to DNA double-strand breaks. Biochem. J. 388, 7-15 (2005).
    • (2005) Biochem. J. , vol.388 , pp. 7-15
    • Lee, S.Y.1
  • 106
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg, E. A. Mitotic kinases as regulators of cell division and its checkpoints. Nature Rev. Mol. Cell Biol. 2, 21-32 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 107
    • 0034729147 scopus 로고    scopus 로고
    • Different kinases phosphorylate nucleophosmin/B23 at different sites during G(2) and M phases of the cell cycle
    • Jiang, P. S., Chang, J. H. & Yung, B. Y. Different kinases phosphorylate nucleophosmin/B23 at different sites during G(2) and M phases of the cell cycle. Cancer Lett. 153, 151-160 (2000).
    • (2000) Cancer Lett. , vol.153 , pp. 151-160
    • Jiang, P.S.1    Chang, J.H.2    Yung, B.Y.3
  • 108
    • 0034730321 scopus 로고    scopus 로고
    • Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication
    • Okuda, M. et al. Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication. Cell 103, 127-140 (2000). Identifies NPM as a substrate of the CDK2-cyclin E complex, and implicates it in the regulation of centrosome duplication in a cell-cycle-dependent manner.
    • (2000) Cell , vol.103 , pp. 127-140
    • Okuda, M.1
  • 109
    • 0025045682 scopus 로고
    • The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II
    • Chan, P. K., Liu, Q. R. & Durban, E. The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II. Biochem. J. 270, 549-552 (1990).
    • (1990) Biochem. J. , vol.270 , pp. 549-552
    • Chan, P.K.1    Liu, Q.R.2    Durban, E.3
  • 110
    • 0025265082 scopus 로고
    • Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase
    • Peter, M., Nakagawa, J., Doree, M., Labbe, J. C. & Nigg, E. A. Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase. Cell 60, 791-801 (1990).
    • (1990) Cell , vol.60 , pp. 791-801
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 112
    • 0028384699 scopus 로고
    • The chromosome periphery during mitosis
    • Hernandez-Verdun, D. & Gautier, T. The chromosome periphery during mitosis. Bioessays 16, 179-185 (1994).
    • (1994) Bioessays , vol.16 , pp. 179-185
    • Hernandez-Verdun, D.1    Gautier, T.2
  • 113
    • 0034618074 scopus 로고    scopus 로고
    • The dynamics of postmitotic reassembly of the nucleolus
    • Dundr, M., Misteli, T. & Olson, M. O. The dynamics of postmitotic reassembly of the nucleolus. J. Cell Biol. 150, 433-446 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 433-446
    • Dundr, M.1    Misteli, T.2    Olson, M.O.3
  • 114
    • 0033046393 scopus 로고    scopus 로고
    • The nucleolar phosphoprotein B23 redistributes in part to the spindle poles during mitosis
    • Zatsepina, O. V. et al. The nucleolar phosphoprotein B23 redistributes in part to the spindle poles during mitosis. J. Cell Sci. 112 (Pt 4), 455-466 (1999).
    • (1999) J. Cell Sci. , vol.112 , Issue.4 PART , pp. 455-466
    • Zatsepina, O.V.1
  • 115
    • 0028239617 scopus 로고
    • NuMA, a nuclear protein involved in mitosis and nuclear reformation
    • Compton, D. A. & Cleveland, D. W. NuMA, a nuclear protein involved in mitosis and nuclear reformation. Curr. Opin. Cell Biol. 6, 343-346 (1994).
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 343-346
    • Compton, D.A.1    Cleveland, D.W.2
  • 116
    • 4544283606 scopus 로고    scopus 로고
    • Nek2A kinase regulates the localization of numatrin to centrosome in mitosis
    • Yao, J. et al. Nek2A kinase regulates the localization of numatrin to centrosome in mitosis. FEBS Lett. 575, 112-118 (2004).
    • (2004) FEBS Lett. , vol.575 , pp. 112-118
    • Yao, J.1
  • 117
    • 4143144444 scopus 로고    scopus 로고
    • B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1
    • Zhang, H. et al. B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1. J. Biol. Chem. 279, 35726-35734 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 35726-35734
    • Zhang, H.1
  • 118
    • 0037134898 scopus 로고    scopus 로고
    • The centrosome cycle
    • Meraldi, P. & Nigg, E. A. The centrosome cycle. FEBS Lett. 521, 9-13 (2002).
    • (2002) FEBS Lett. , vol.521 , pp. 9-13
    • Meraldi, P.1    Nigg, E.A.2
  • 119
    • 0033525007 scopus 로고    scopus 로고
    • Requirement of Cdk2-cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts
    • Hinchcliffe, E. H., Li, C., Thompson, E. A., Maller, J. L. & Sluder, G. Requirement of Cdk2-cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts. Science 283, 851-854 (1999).
    • (1999) Science , vol.283 , pp. 851-854
    • Hinchcliffe, E.H.1    Li, C.2    Thompson, E.A.3    Maller, J.L.4    Sluder, G.5
  • 120
    • 0029011885 scopus 로고
    • Substrate specificity and cell cycle regulation of the Nek2 protein kinase, a potential human homolog of the mitotic regulator NIMA of Aspergillus nidulans
    • Fry, A. M., Schultz, S. J., Bartek, J. & Nigg, E. A. Substrate specificity and cell cycle regulation of the Nek2 protein kinase, a potential human homolog of the mitotic regulator NIMA of Aspergillus nidulans. J. Biol. Chem. 270, 12899-12905 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12899-12905
    • Fry, A.M.1    Schultz, S.J.2    Bartek, J.3    Nigg, E.A.4
  • 121
    • 0037048312 scopus 로고    scopus 로고
    • The Nek2 protein kinase: A novel regulator of centrosome structure
    • Fry, A. M. The Nek2 protein kinase: a novel regulator of centrosome structure. Oncogene 21, 6184-6194 (2002).
    • (2002) Oncogene , vol.21 , pp. 6184-6194
    • Fry, A.M.1
  • 122
    • 0038739131 scopus 로고    scopus 로고
    • Never say never. The NIMA-related protein kinases in mitotic control
    • O'Connell, M. J., Krien, M. J. & Hunter, T. Never say never. The NIMA-related protein kinases in mitotic control. Trends Cell Biol. 13, 221-228 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 221-228
    • O'Connell, M.J.1    Krien, M.J.2    Hunter, T.3
  • 123
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen, J. S. et al. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426, 570-574 (2003).
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1
  • 124
    • 0035877719 scopus 로고    scopus 로고
    • Specific phosphorylation of nucleophosmin on Thr(199) by cyclin-dependent kinase 2-cyclin E and its role in centrosome duplication
    • Tokuyama, Y., Horn, H. F., Kawamura, K., Tarapore, P. & Fukasawa, K. Specific phosphorylation of nucleophosmin on Thr(199) by cyclin-dependent kinase 2-cyclin E and its role in centrosome duplication. J. Biol. Chem. 276, 21529-21537 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21529-21537
    • Tokuyama, Y.1    Horn, H.F.2    Kawamura, K.3    Tarapore, P.4    Fukasawa, K.5
  • 125
    • 0037048278 scopus 로고    scopus 로고
    • The role of nucleophosmin in centrosome duplication
    • Okuda, M. The role of nucleophosmin in centrosome duplication. Oncogene 21, 6170-6174 (2002).
    • (2002) Oncogene , vol.21 , pp. 6170-6174
    • Okuda, M.1
  • 126
    • 2342575033 scopus 로고    scopus 로고
    • Polo-like kinase 1 in the life and death of cancer cells
    • Liu, X. & Erikson, R. L. Polo-like kinase 1 in the life and death of cancer cells. Cell Cycle 2, 424-425 (2003).
    • (2003) Cell Cycle , vol.2 , pp. 424-425
    • Liu, X.1    Erikson, R.L.2
  • 127
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer, F., Lagrazon, K., Yuan, W. & Baer, R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278, 34743-34746 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 128
    • 1042278177 scopus 로고    scopus 로고
    • Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase
    • Nishikawa, H. et al. Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. J. Biol. Chem. 279, 3916-3924 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3916-3924
    • Nishikawa, H.1
  • 129
    • 3843059160 scopus 로고    scopus 로고
    • Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase
    • Sato, K. et al. Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase. J. Biol. Chem. 279, 30919-30922 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 30919-30922
    • Sato, K.1
  • 130
    • 0033106326 scopus 로고    scopus 로고
    • Centrosome amplification and a defective G2-M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells
    • Xu, X. et al. Centrosome amplification and a defective G2-M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells. Mol. Cell 3, 389-395 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 389-395
    • Xu, X.1
  • 131
    • 0042510099 scopus 로고    scopus 로고
    • Inactivation of E2F3 results in centrosome amplification
    • Saavedra, H. I. et al. Inactivation of E2F3 results in centrosome amplification. Cancer Cell 3, 333-346 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 333-346
    • Saavedra, H.I.1
  • 132
    • 0142219891 scopus 로고    scopus 로고
    • Functional proteomic analysis of melanoma progression
    • Bernard, K. et al. Functional proteomic analysis of melanoma progression. Cancer Res. 63, 6716-6725 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 6716-6725
    • Bernard, K.1
  • 133
    • 4143086570 scopus 로고    scopus 로고
    • Mitotic functions of the Ran GTPase network: The importance of being in the right place at the right time
    • Di Fiore, B., Ciciarello, M. & Lavia, P. Mitotic functions of the Ran GTPase network: the importance of being in the right place at the right time. Cell Cycle 3, 305-313 (2004).
    • (2004) Cell Cycle , vol.3 , pp. 305-313
    • Di Fiore, B.1    Ciciarello, M.2    Lavia, P.3
  • 134
    • 0035830499 scopus 로고    scopus 로고
    • Running on Ran: Nuclear transport and the mitotic spindle
    • Dasso, M. Running on Ran: nuclear transport and the mitotic spindle. Cell 104, 321-324 (2001).
    • (2001) Cell , vol.104 , pp. 321-324
    • Dasso, M.1
  • 135
    • 0042091978 scopus 로고    scopus 로고
    • Involvement of Crm1 in hepatitis B virus X protein-induced aberrant centriole replication and abnormal mitotic spindles
    • Forgues, M. et al. Involvement of Crm1 in hepatitis B virus X protein-induced aberrant centriole replication and abnormal mitotic spindles. Mol. Cell. Biol. 23, 5282-5292 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5282-5292
    • Forgues, M.1
  • 136
    • 0041954978 scopus 로고    scopus 로고
    • Part of Ran is associated with AKAP450 at the centrosome: Involvement in microtubule-organizing activity
    • Keryer, G. et al. Part of Ran is associated with AKAP450 at the centrosome: involvement in microtubule-organizing activity. Mol. Biol. Cell 14, 4260-4271 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4260-4271
    • Keryer, G.1
  • 137
    • 23144449790 scopus 로고    scopus 로고
    • Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication
    • Wang, W., Budhu, A., Forgues, M. & Wang, X. W. Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication. Nature Cell Biol. 7, 823-830 (2005). The RAN-CRM1 network is involved in the regulation of centrosome duplication and proper formation of a bipolar spindle. NPM is proposed to be a RAN-CRM1 substrate in the control of centrosome duplication.
    • (2005) Nature Cell Biol. , vol.7 , pp. 823-830
    • Wang, W.1    Budhu, A.2    Forgues, M.3    Wang, X.W.4
  • 138
    • 27944478938 scopus 로고    scopus 로고
    • Characterization of centrosomal association of nucleophosmin/B23 linked to Crm1 activity
    • Shinmura, K., Tarapore, P., Tokuyama, Y., George, K. R. & Fukasawa, K. Characterization of centrosomal association of nucleophosmin/B23 linked to Crm1 activity. FEBS Lett. 579, 6621-6634 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 6621-6634
    • Shinmura, K.1    Tarapore, P.2    Tokuyama, Y.3    George, K.R.4    Fukasawa, K.5
  • 139
    • 27744569412 scopus 로고    scopus 로고
    • Loading and unloading: Orchestrating centrosome duplication and spindle assembly by Ran/Crm1
    • Budhu, A. S. & Wang, X. W. Loading and unloading: orchestrating centrosome duplication and spindle assembly by Ran/Crm1. Cell Cycle 4, 1508-1512 (2005).
    • (2005) Cell Cycle , vol.4 , pp. 1508-1512
    • Budhu, A.S.1    Wang, X.W.2
  • 141
    • 1842858997 scopus 로고    scopus 로고
    • Tryptophans 286 and 288 in the C-terminal region of protein B23.1 are important for its nucleolar localization
    • Nishimura, Y., Ohkubo, T., Furuichi, Y. & Umekawa, H. Tryptophans 286 and 288 in the C-terminal region of protein B23.1 are important for its nucleolar localization. Biosci. Biotechnol. Biochem. 66, 2239-2242 (2002).
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2239-2242
    • Nishimura, Y.1    Ohkubo, T.2    Furuichi, Y.3    Umekawa, H.4
  • 142
    • 0035839867 scopus 로고    scopus 로고
    • Translocations involving anaplastic lymphoma kinase (ALK)
    • Duyster, J., Bai, R. Y. & Morris, S. W. Translocations involving anaplastic lymphoma kinase (ALK). Oncogene 20, 5623-5637 (2001).
    • (2001) Oncogene , vol.20 , pp. 5623-5637
    • Duyster, J.1    Bai, R.Y.2    Morris, S.W.3
  • 143
    • 0034796741 scopus 로고    scopus 로고
    • Anaplastic large cell lymphoma: Pathological, molecular and clinical features
    • Falini, B. Anaplastic large cell lymphoma: pathological, molecular and clinical features. Br. J. Haematol. 114, 741-760 (2001).
    • (2001) Br. J. Haematol. , vol.114 , pp. 741-760
    • Falini, B.1
  • 144
    • 0034663029 scopus 로고    scopus 로고
    • Characterization of acute promyelocytic leukemia cases lacking the classic t(15;17): Results of the European Working Party
    • Groupe Francais de Cytogenetique Hematologique, Groupe de Francais d'Hematologie Cellulaire, UK Cancer Cytogenetics Group and BIOMED 1 European Community-Concerted Action 'Molecular Cytogenetic Diagnosis in Haematological Malignancies'
    • Grimwade, D. et al. Characterization of acute promyelocytic leukemia cases lacking the classic t(15;17): results of the European Working Party. Groupe Francais de Cytogenetique Hematologique, Groupe de Francais d'Hematologie Cellulaire, UK Cancer Cytogenetics Group and BIOMED 1 European Community-Concerted Action 'Molecular Cytogenetic Diagnosis in Haematological Malignancies'. Blood 96, 1297-1308 (2000).
    • (2000) Blood , vol.96 , pp. 1297-1308
    • Grimwade, D.1
  • 145
    • 0036798277 scopus 로고    scopus 로고
    • Variations on a theme: The alternate translocations in APL
    • Redner, R. L. Variations on a theme: the alternate translocations in APL. Leukemia 16, 1927-1932 (2002).
    • (2002) Leukemia , vol.16 , pp. 1927-1932
    • Redner, R.L.1
  • 146
    • 23744479178 scopus 로고    scopus 로고
    • Nucleophosmin mutations in childhood acute myelogenous leukemia with normal karyotype
    • Cazzaniga, G. et al. Nucleophosmin mutations in childhood acute myelogenous leukemia with normal karyotype. Blood 106, 1419-1422 (2005).
    • (2005) Blood , vol.106 , pp. 1419-1422
    • Cazzaniga, G.1


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