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Volumn 116, Issue 3, 2003, Pages 513-524

Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently

Author keywords

Daxx; Heat shock; Heavy metal; ND10; Nuclear depot; PML; Stress; Transcriptional regulation

Indexed keywords

CADMIUM CHLORIDE; CD2 ANTIGEN; DAXX PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 25; HEAT SHOCK PROTEIN 70; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; NUCLEAR PROTEIN; PROTEIN ND10; PROTEIN SP100; SUMO PROTEIN; SYNAPTOPHYSIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; CADMIUM; CARRIER PROTEIN; DAXX PROTEIN, MOUSE; ENZYME INHIBITOR; HSPB1 PROTEIN, MOUSE; PML PROTEIN, MOUSE; PROTEINASE; SENP1 PROTEIN, HUMAN; SIGNAL PEPTIDE; SUMO 1 PROTEIN; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 0037327059     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00253     Document Type: Review
Times cited : (67)

References (53)
  • 1
    • 0028881770 scopus 로고
    • UV irradiation and heat shock mediate JNK activation via alternate pathways
    • Adler, V., Schaffer, A., Kim, J., Dolan, L. and Ronai, Z. (1995). UV irradiation and heat shock mediate JNK activation via alternate pathways. J. Biol. Chem. 270, 26071-26077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26071-26077
    • Adler, V.1    Schaffer, A.2    Kim, J.3    Dolan, L.4    Ronai, Z.5
  • 2
    • 0025871767 scopus 로고
    • Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-Myc and c-Jun proteins by an epidermal growth factor receptor threonine 669 protein kinase
    • Alvarez, E., Northwood, I. C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T. and Davis, R. J. (1991). Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-Myc and c-Jun proteins by an epidermal growth factor receptor threonine 669 protein kinase. J. Biol. Chem. 266, 15277-15285.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15277-15285
    • Alvarez, E.1    Northwood, I.C.2    Gonzalez, F.A.3    Latour, D.A.4    Seth, A.5    Abate, C.6    Curran, T.7    Davis, R.J.8
  • 3
    • 0026019835 scopus 로고
    • Identification of a novel nuclear domain
    • Ascoli, C. A. and Maul, G. G. (1991). Identification of a novel nuclear domain. J. Cell Biol. 112, 785-795.
    • (1991) J. Cell Biol. , vol.112 , pp. 785-795
    • Ascoli, C.A.1    Maul, G.G.2
  • 5
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Chelbi-Alix, M. K., Quignon, F., Pelicano, L., Koken, M. H. and de The, H. (1998). Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J. Virol. 72, 1043-1051.
    • (1998) J. Virol. , vol.72 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.4    de The, H.5
  • 6
    • 0035881526 scopus 로고    scopus 로고
    • PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA
    • Cohen, N., Sharma, M., Kentsis, A., Perez, J. M., Strudwick, S. and Borden, K. L. (2001). PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. EMBO J. 20, 4547-4559.
    • (2001) EMBO J. , vol.20 , pp. 4547-4559
    • Cohen, N.1    Sharma, M.2    Kentsis, A.3    Perez, J.M.4    Strudwick, S.5    Borden, K.L.6
  • 7
    • 0031467707 scopus 로고    scopus 로고
    • HSF1 granules: A novel stress-induced nuclear compartment of human cells
    • Cotto, J., Fox, S. and Morimoto, R. (1997). HSF1 granules: a novel stress-induced nuclear compartment of human cells. J. Cell Sci. 110, 2925-2934.
    • (1997) J. Cell Sci. , vol.110 , pp. 2925-2934
    • Cotto, J.1    Fox, S.2    Morimoto, R.3
  • 8
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda, A., Rouse, J., Doza, Y. N., Meier, R., Cohen, P., Gallagher, T. F., Young, P. R. and Lee, J. C. (1995). SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1 FFBS Lett. 364, 229-233.
    • (1995) FFBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 9
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000). Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 11
    • 0028039189 scopus 로고
    • HSV-1 IE protein Vmw110 causes redistribution of PML
    • Everett, R. D. and Maul, G. G. (1994). HSV-1 IE protein Vmw110 causes redistribution of PML. EMBO J. 13, 5062-5069.
    • (1994) EMBO J. , vol.13 , pp. 5062-5069
    • Everett, R.D.1    Maul, G.G.2
  • 12
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D., Freemont, P., Saitoh, H., Dasso, M., Orr, A., Kathoria, M. and Parkinson, J. (1998). The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72, 6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 13
    • 0035147230 scopus 로고    scopus 로고
    • Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies
    • Fabunmi, R. P., Wigley, W. C., Thomas, P. J. and DeMartino, G. N. (2001). Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies. J. Cell Sci. 114, 29-36.
    • (2001) J. Cell Sci. , vol.114 , pp. 29-36
    • Fabunmi, R.P.1    Wigley, W.C.2    Thomas, P.J.3    DeMartino, G.N.4
  • 14
    • 0027443128 scopus 로고
    • Induction of reactivation of herpes simplex virus in murine sensory ganglia in vivo by cadmium
    • Fawl, R. L. and Roizman, B. (1993). Induction of reactivation of herpes simplex virus in murine sensory ganglia in vivo by cadmium. J. Virol. 67, 7025-7031.
    • (1993) J. Virol. , vol.67 , pp. 7025-7031
    • Fawl, R.L.1    Roizman, B.2
  • 15
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin-specific protease
    • Gong, L., Millas, S., Maul, G. G. and Yeh, E. T. (2000). Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J. Biol. Chem. 275, 3355-3359.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.4
  • 17
    • 0029894340 scopus 로고    scopus 로고
    • Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML)
    • Grotzinger, T., Sternsdorf, T., Jensen, K. and Will, H. (1996). Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238, 554-560.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 554-560
    • Grotzinger, T.1    Sternsdorf, T.2    Jensen, K.3    Will, H.4
  • 18
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov, A. M. and Maul, G. G. (1996). The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 134, 815-826.
    • (1996) J. Cell Biol. , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 19
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M., Sotnikov, A. G., Negorev, D., Vladimirova, O. V., Neff, N., Kamitani, T., Yeh, E. T., Strauss, J. F., 3rd and Maul, G. G. (1999). PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147, 221-234.
    • (1999) J. Cell Biol. , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6    Yeh, E.T.7    Strauss J.F. III8    Maul, G.G.9
  • 20
    • 0036310441 scopus 로고    scopus 로고
    • Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains
    • Ishov, A. M., Vladimirova, O. V. and Maul, G. G. (2002). Daxx-mediated accumulation of human cytomegalovirus tegument protein pp71 at ND10 facilitates initiation of viral infection at these nuclear domains. J. Virol. 76, 7705-7712.
    • (2002) J. Virol. , vol.76 , pp. 7705-7712
    • Ishov, A.M.1    Vladimirova, O.V.2    Maul, G.G.3
  • 21
    • 0033536006 scopus 로고    scopus 로고
    • Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules
    • Jolly, C., Usson, Y. and Morimoto, R. I. (1999). Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules. Proc. Natl. Acad. Sci. USA 96, 6769-6774.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6769-6774
    • Jolly, C.1    Usson, Y.2    Morimoto, R.I.3
  • 23
    • 0032738332 scopus 로고    scopus 로고
    • SUMO/sentrin: Protein modifiers regulating important cellular functions
    • Kretz-Remy, C. and Tanguay, R. M. (1999). SUMO/sentrin: protein modifiers regulating important cellular functions. Biochem. Cell. Biol. 77, 299-309.
    • (1999) Biochem. Cell. Biol. , vol.77 , pp. 299-309
    • Kretz-Remy, C.1    Tanguay, R.M.2
  • 25
    • 0025727532 scopus 로고
    • Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells
    • Landry, J., Chretien, P., Laszlo, A. and Lambert, H. (1991). Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells. J. Cell. Physiol. 147, 93-101.
    • (1991) J. Cell. Physiol. , vol.147 , pp. 93-101
    • Landry, J.1    Chretien, P.2    Laszlo, A.3    Lambert, H.4
  • 27
    • 0029844746 scopus 로고    scopus 로고
    • Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export
    • Liu, Y., Liang, S. and Tartakoff, A. M. (1996). Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export. EMBO J. 15, 6750-6757.
    • (1996) EMBO J. , vol.15 , pp. 6750-6757
    • Liu, Y.1    Liang, S.2    Tartakoff, A.M.3
  • 28
    • 0031892538 scopus 로고    scopus 로고
    • The stress inducer arsenite activates mitogen-activated protein kinases extracellular signal-regulated kinases 1 and 2 via a MAPK kinase 6/p38-dependent pathway
    • Ludwig, S., Hoffmeyer, A., Goebeler, M., Kilian, K., Hafner, H., Neufeld, B., Han, J. and Rapp, U. R. (1998). The stress inducer arsenite activates mitogen-activated protein kinases extracellular signal-regulated kinases 1 and 2 via a MAPK kinase 6/p38-dependent pathway. J. Biol. Chem. 273, 1917-1922.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1917-1922
    • Ludwig, S.1    Hoffmeyer, A.2    Goebeler, M.3    Kilian, K.4    Hafner, H.5    Neufeld, B.6    Han, J.7    Rapp, U.R.8
  • 29
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., Coutavas, E. and Blobel, G. (1996). A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135, 1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 30
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul, G. G. (1998). Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays 20, 660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 31
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul, G. G. and Everett, R. D. (1994). The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 75, 1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 32
    • 0023212912 scopus 로고
    • Detection of nuclear lamins B epitopes in oocyte nuclei from mice, sea urchins, and clams using a human autoimmune serum
    • Maul, G. G., Schatten, G., Jimenez, S. A. and Carrera, A. E. (1987). Detection of nuclear lamins B epitopes in oocyte nuclei from mice, sea urchins, and clams using a human autoimmune serum. Dev. Biol. 121, 368-375.
    • (1987) Dev. Biol. , vol.121 , pp. 368-375
    • Maul, G.G.1    Schatten, G.2    Jimenez, S.A.3    Carrera, A.E.4
  • 33
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)
    • Maul, G. G., Guldner, H. H. and Spivack, J. G. (1993). Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J. Gen. Virol. 74, 2679-2690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 34
    • 0029583591 scopus 로고
    • Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress
    • Maul, G. G., Yu, E., Ishov, A. M. and Epstein, A. L. (1995). Nuclear domain 10 (ND10) associated proteins are also present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J. Cell. Biochem. 59, 498-513.
    • (1995) J. Cell. Biochem. , vol.59 , pp. 498-513
    • Maul, G.G.1    Yu, E.2    Ishov, A.M.3    Epstein, A.L.4
  • 35
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • Maul, G. G., Ishov, A. M. and Everett, R. D. (1996). Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology 217, 67-75.
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 36
    • 0033179775 scopus 로고    scopus 로고
    • Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development
    • Michaelson, J. S., Bader, D., Kuo, F., Kozak, C. and Leder, P. (1999). Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development. Genes Dev. 13, 1918-1923.
    • (1999) Genes Dev. , vol.13 , pp. 1918-1923
    • Michaelson, J.S.1    Bader, D.2    Kuo, F.3    Kozak, C.4    Leder, P.5
  • 37
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R. I. and Santoro, M. G. (1998). Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat. Biotechnol. 16, 833-838.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 38
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M. J. and Dejean, A. (1998). Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 39
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Negorev, D. and Maul, G. G. (2001). Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20, 7234-7242.
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 40
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S. W. (1996). PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 41
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse, J., Cohen, P., Trigon, S., Morange, M., Alonso-Llamazares, A., Zamanillo, D., Hunt, T. and Nebreda, A. R. (1994). A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78, 1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 42
    • 0026608638 scopus 로고
    • Rapid in vivo reactivation of herpes simplex virus in latently infected murine ganglionic neurons after transient hyperthermia
    • Sawtell, N. M. and Thompson, R. L. (1992). Rapid in vivo reactivation of herpes simplex virus in latently infected murine ganglionic neurons after transient hyperthermia. J. Virol. 66, 2150-2156.
    • (1992) J. Virol. , vol.66 , pp. 2150-2156
    • Sawtell, N.M.1    Thompson, R.L.2
  • 43
    • 0033152703 scopus 로고    scopus 로고
    • The PML nuclear bodies: Actors or extras?
    • Seeler, J. S. and Dejean, A. (1999). The PML nuclear bodies: actors or extras? Curr. Opin. Genet. Dev. 9, 362-367.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 362-367
    • Seeler, J.S.1    Dejean, A.2
  • 44
    • 0035756707 scopus 로고    scopus 로고
    • Monoclonal antibodies against protein Daxx and its localization in nuclear domains 10
    • Sotnikov, A. G., Negorev, D., Ishov, A. M. and Maul, G. G. (2001). Monoclonal antibodies against protein Daxx and its localization in nuclear domains 10. Tsitologiia 43, 1123-1129.
    • (2001) Tsitologiia , vol.43 , pp. 1123-1129
    • Sotnikov, A.G.1    Negorev, D.2    Ishov, A.M.3    Maul, G.G.4
  • 46
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein SP100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T., Jensen, K., Reich, B. and Will, H. (1999). The nuclear dot protein SP100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274, 12555-12566.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 48
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • Szostecki, C., Guldner, H. H., Netter, H. J. and Will, H. (1990). Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 145, 4338-4347.
    • (1990) J. Immunol. , vol.145 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 49
    • 0027207956 scopus 로고
    • Tissue-specific expression of heat shock proteins of the mouse in the absence of stress
    • Tanguay, R. M., Wu, Y. and Khandjian, E. W. (1993). Tissue-specific expression of heat shock proteins of the mouse in the absence of stress. Dev. Genet. 14, 112-118.
    • (1993) Dev. Genet. , vol.14 , pp. 112-118
    • Tanguay, R.M.1    Wu, Y.2    Khandjian, E.W.3
  • 50
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz, A. J., Flynn, A., Proud, C. G. and Cooper, J. A. (1997). Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16, 1909-1920.
    • (1997) EMBO J. , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 51
    • 0025376211 scopus 로고
    • A nucleolar auto-antigen is part of a major chromosomal surface component
    • Yasuda, Y. and Maul, G. G. (1990). A nucleolar auto-antigen is part of a major chromosomal surface component. Chromosoma 99, 152-160.
    • (1990) Chromosoma , vol.99 , pp. 152-160
    • Yasuda, Y.1    Maul, G.G.2
  • 53
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P. and Pandolfi, P. P. (2000b). The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2, E85-E90.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3


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