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Volumn 287, Issue 36, 2012, Pages 30729-30742

Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation

Author keywords

[No Author keywords available]

Indexed keywords

ASSEMBLY MECHANISM; C TERMINUS; C-TERMINAL DOMAINS; C-TERMINAL REGIONS; COILED COIL; ISOFORMS; N-TERMINALS; NUCLEAR BODIES; NUCLEAR PROTEIN COMPLEXES; PROMYELOCYTIC LEUKEMIA PROTEINS; STRONG INTERACTION; STRUCTURAL COMPONENT; TUMOR SUPPRESSION;

EID: 84865749807     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.374769     Document Type: Article
Times cited : (33)

References (59)
  • 1
    • 0033380850 scopus 로고    scopus 로고
    • Cell cycle regulation of PML modification and ND10 composition
    • Everett, R. D., Lomonte, P., Sternsdorf, T., van Driel, R., and Orr, A. (1999) Cell cycle regulation of PML modification and ND10 composition. J. Cell Sci. 112, 4581-4588
    • (1999) J. Cell Sci. , vol.112 , pp. 4581-4588
    • Everett, R.D.1    Lomonte, P.2    Sternsdorf, T.3    Van Driel, R.4    Orr, A.5
  • 2
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni, P., and Pandolfi, P. P. (2002) The role of PML in tumor suppression. Cell 108, 165-170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 3
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P., and Pandolfi, P. P. (2000) 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
  • 5
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • Regad, T., and Chelbi-Alix, M. K. (2001) Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20, 7274-7286
    • (2001) Oncogene , vol.20 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 7
    • 25444517110 scopus 로고    scopus 로고
    • Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies
    • Tang, J., Xie, W., and Yang, X. (2005) Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies. Cancer Biol. Ther. 4, 645-649
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 645-649
    • Tang, J.1    Xie, W.2    Yang, X.3
  • 8
    • 0025875679 scopus 로고
    • The PML-RAR α fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de Thé, H., Lavau, C., Marchio, A., Chomienne, C., Degos, L., and Dejean, A. (1991) The PML-RAR α fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675-684
    • (1991) Cell , vol.66 , pp. 675-684
    • De Thé, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 9
    • 0035839892 scopus 로고    scopus 로고
    • In vivo analysis of the molecular genetics of acute promyelocytic leukemia
    • Pandolfi, P. P. (2001) In vivo analysis of the molecular genetics of acute promyelocytic leukemia. Oncogene 20, 5726-5735
    • (2001) Oncogene , vol.20 , pp. 5726-5735
    • Pandolfi, P.P.1
  • 10
    • 33744908280 scopus 로고    scopus 로고
    • Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication
    • Cantrell, S. R., and Bresnahan, W. A. (2006) Human cytomegalovirus (HCMV) UL82 gene product (pp71) relieves hDaxx-mediated repression of HCMV replication. J. Virol. 80, 6188-6191
    • (2006) J. Virol. , vol.80 , pp. 6188-6191
    • Cantrell, S.R.1    Bresnahan, W.A.2
  • 11
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett, R. D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T., and Orr, A. (2006) PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80, 7995-8005
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 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
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee, H. R., Kim, D. J., Lee, J. M., Choi, C. Y., Ahn, B. Y., Hayward, G. S., and Ahn, J. H. (2004) Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J. Virol. 78, 6527-6542
    • (2004) J. Virol. , vol.78 , pp. 6527-6542
    • Lee, H.R.1    Kim, D.J.2    Lee, J.M.3    Choi, C.Y.4    Ahn, B.Y.5    Hayward, G.S.6    Ahn, J.H.7
  • 14
  • 15
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen, K., Shiels, C., and Freemont, P. S. (2001) PML protein isoforms and the RBCC/TRIM motif. Oncogene 20, 7223-7233
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 16
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukemia proto-oncoprotein PML
    • Borden, K. L., Boddy, M. N., Lally, J., O'Reilly, N. J., Martin, S., Howe, K., Solomon, E., and Freemont, P. S. (1995) The solution structure of the RING finger domain from the acute promyelocytic leukemia proto-oncoprotein PML. EMBO J. 14, 1532-1541
    • (1995) EMBO J. , vol.14 , pp. 1532-1541
    • Borden, K.L.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5    Howe, K.6    Solomon, E.7    Freemont, P.S.8
  • 18
    • 1242272073 scopus 로고    scopus 로고
    • The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome
    • Fanelli, M., Fantozzi, A., De Luca, P., Caprodossi, S., Matsuzawa, S., Lazar, M. A., Pelicci, P. G., and Minucci, S. (2004) The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome. J. Biol. Chem. 279, 5374-5379
    • (2004) J. Biol. Chem. , vol.279 , pp. 5374-5379
    • Fanelli, M.1    Fantozzi, A.2    De Luca, P.3    Caprodossi, S.4    Matsuzawa, S.5    Lazar, M.A.6    Pelicci, P.G.7    Minucci, S.8
  • 19
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11 S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor α degradation
    • Lallemand-Breitenbach, V., Zhu, J., Puvion, F., Koken, M., Honoré, N., Doubeikovsky, A., Duprez, E., Pandolfi, P. P., Puvion, E., Freemont, P., and de Thé, H. (2001) Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11 S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor α degradation. J. Exp. Med. 193, 1361-1371
    • (2001) J. Exp. Med. , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honoré, N.5    Doubeikovsky, A.6    Duprez, E.7    Pandolfi, P.P.8    Puvion, E.9    Freemont, P.10    De Thé, H.11
  • 22
    • 0033925534 scopus 로고    scopus 로고
    • Review. Properties and assembly mechanisms of ND10, PML bodies, or PODs
    • Maul, G. G., Negorev, D., Bell, P., and Ishov, A. M. (2000) Review. Properties and assembly mechanisms of ND10, PML bodies, or PODs. J. Struct. Biol. 129, 278-287
    • (2000) J. Struct. Biol. , vol.129 , pp. 278-287
    • Maul, G.G.1    Negorev, D.2    Bell, P.3    Ishov, A.M.4
  • 24
    • 79952280117 scopus 로고    scopus 로고
    • Dynamic as well as stable protein interactions contribute to genome function and maintenance
    • Hemmerich, P., Schmiedeberg, L., and Diekmann, S. (2011) Dynamic as well as stable protein interactions contribute to genome function and maintenance. Chromosome Res. 19, 131-151
    • (2011) Chromosome Res. , vol.19 , pp. 131-151
    • Hemmerich, P.1    Schmiedeberg, L.2    Diekmann, S.3
  • 25
    • 81355161213 scopus 로고    scopus 로고
    • De novo assembly of a PML nuclear subcompartment occurs through multiple pathways and induces telomere elongation
    • Chung, I., Leonhardt, H., and Rippe, K. (2011) De novo assembly of a PML nuclear subcompartment occurs through multiple pathways and induces telomere elongation. J. Cell Sci. 124, 3603-3618
    • (2011) J. Cell Sci. , vol.124 , pp. 3603-3618
    • Chung, I.1    Leonhardt, H.2    Rippe, K.3
  • 29
    • 2942711737 scopus 로고    scopus 로고
    • HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures
    • Guccione, E., Lethbridge, K. J., Killick, N., Leppard, K. N., and Banks, L. (2004) HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures. Oncogene 23, 4662-4672
    • (2004) Oncogene , vol.23 , pp. 4662-4672
    • Guccione, E.1    Lethbridge, K.J.2    Killick, N.3    Leppard, K.N.4    Banks, L.5
  • 30
    • 0031743484 scopus 로고    scopus 로고
    • ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase
    • Burkham, J., Coen, D. M., and Weller, S. K. (1998) ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase. J. Virol. 72, 10100-10107
    • (1998) J. Virol. , vol.72 , pp. 10100-10107
    • Burkham, J.1    Coen, D.M.2    Weller, S.K.3
  • 31
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AML1 and PML
    • Nguyen, L. A., Pandolfi, P. P., Aikawa, Y., Tagata, Y., Ohki, M., and Kitabayashi, I. (2005) Physical and functional link of the leukemia-associated factors AML1 and PML. Blood 105, 292-300
    • (2005) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1    Pandolfi, P.P.2    Aikawa, Y.3    Tagata, Y.4    Ohki, M.5    Kitabayashi, I.6
  • 32
    • 59849108860 scopus 로고    scopus 로고
    • Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis
    • Leppard, K. N., Emmott, E., Cortese, M. S., and Rich, T. (2009) Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis. J. Gen. Virol. 90, 95-104
    • (2009) J. Gen. Virol. , vol.90 , pp. 95-104
    • Leppard, K.N.1    Emmott, E.2    Cortese, M.S.3    Rich, T.4
  • 33
    • 33644768122 scopus 로고    scopus 로고
    • Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption
    • Hoppe, A., Beech, S. J., Dimmock, J., and Leppard, K. N. (2006) Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption. J. Virol. 80, 3042-3049
    • (2006) J. Virol. , vol.80 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3    Leppard, K.N.4
  • 34
    • 14644394332 scopus 로고    scopus 로고
    • A role for PML3 in centrosome duplication and genome stability
    • Xu, Z. X., Zou, W. X., Lin, P., and Chang, K. S. (2005) A role for PML3 in centrosome duplication and genome stability. Mol. Cell 17, 721-732
    • (2005) Mol. Cell , vol.17 , pp. 721-732
    • Xu, Z.X.1    Zou, W.X.2    Lin, P.3    Chang, K.S.4
  • 35
    • 0033598931 scopus 로고    scopus 로고
    • A role for PML and the nuclear body in genomic stability
    • Zhong, S., Hu, P., Ye, T. Z., Stan, R., Ellis, N. A., and Pandolfi, P. P. (1999) A role for PML and the nuclear body in genomic stability. Oncogene 18, 7941-7947
    • (1999) Oncogene , vol.18 , pp. 7941-7947
    • Zhong, S.1    Hu, P.2    Ye, T.Z.3    Stan, R.4    Ellis, N.A.5    Pandolfi, P.P.6
  • 36
    • 79551649719 scopus 로고    scopus 로고
    • The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies
    • Sarkari, F., Wang, X., Nguyen, T., and Frappier, L. (2011) The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies. PLoS One 6, e16598
    • (2011) PLoS One , vol.6
    • Sarkari, F.1    Wang, X.2    Nguyen, T.3    Frappier, L.4
  • 39
    • 69549138485 scopus 로고    scopus 로고
    • PML-IV functions as a negative regulator of telomerase by interacting with TERT
    • Oh, W., Ghim, J., Lee, E. W., Yang, M. R., Kim, E. T., Ahn, J. H., and Song, J. (2009) PML-IV functions as a negative regulator of telomerase by interacting with TERT. J. Cell Sci. 122, 2613-2622
    • (2009) J. Cell Sci. , vol.122 , pp. 2613-2622
    • Oh, W.1    Ghim, J.2    Lee, E.W.3    Yang, M.R.4    Kim, E.T.5    Ahn, J.H.6    Song, J.7
  • 41
    • 19544380887 scopus 로고    scopus 로고
    • Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization
    • Beech, S. J., Lethbridge, K. J., Killick, N., McGlincy, N., and Leppard, K. N. (2005) Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp. Cell Res. 307, 109-117
    • (2005) Exp. Cell Res. , vol.307 , pp. 109-117
    • Beech, S.J.1    Lethbridge, K.J.2    Killick, N.3    McGlincy, N.4    Leppard, K.N.5
  • 42
    • 78449241862 scopus 로고    scopus 로고
    • Subcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia protein
    • Jul-Larsen, A., Grudic, A., Bjerkvig, R., and Bøe, S. O. (2010) Subcellular distribution of nuclear import-defective isoforms of the promyelocytic leukemia protein. BMC Mol. Biol. 11, 89
    • (2010) BMC Mol. Biol. , vol.11 , pp. 89
    • Jul-Larsen, A.1    Grudic, A.2    Bjerkvig, R.3    Bøe, S.O.4
  • 43
  • 44
    • 35548950835 scopus 로고    scopus 로고
    • A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells
    • Condemine, W., Takahashi, Y., Le Bras, M., and de Thé, H. (2007) A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells. J. Cell Sci. 120, 3219-3227
    • (2007) J. Cell Sci. , vol.120 , pp. 3219-3227
    • Condemine, W.1    Takahashi, Y.2    Le Bras, M.3    De Thé, H.4
  • 45
    • 77956202370 scopus 로고    scopus 로고
    • Assembly dynamics of PML nuclear bodies in living cells
    • Brand, P., Lenser, T., and Hemmerich, P. (2010) Assembly dynamics of PML nuclear bodies in living cells. PMC Biophys. 3, 3
    • (2010) PMC Biophys. , vol.3 , pp. 3
    • Brand, P.1    Lenser, T.2    Hemmerich, P.3
  • 46
    • 0034746551 scopus 로고    scopus 로고
    • Evidence for separate ND10 binding and homo-oligomerization domains of Sp100
    • Negorev, D., Ishov, A. M., and Maul, G. G. (2001) Evidence for separate ND10 binding and homo-oligomerization domains of Sp100. J. Cell Sci. 114, 59-68
    • (2001) J. Cell Sci. , vol.114 , pp. 59-68
    • Negorev, D.1    Ishov, A.M.2    Maul, G.G.3
  • 47
    • 2442590725 scopus 로고    scopus 로고
    • A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein
    • Tang, J., Wu, S., Liu, H., Stratt, R., Barak, O. G., Shiekhattar, R., Picketts, D. J., and Yang, X. (2004) A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein. J. Biol. Chem. 279, 20369-20377
    • (2004) J. Biol. Chem. , vol.279 , pp. 20369-20377
    • Tang, J.1    Wu, S.2    Liu, H.3    Stratt, R.4    Barak, O.G.5    Shiekhattar, R.6    Picketts, D.J.7    Yang, X.8
  • 48
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier, P., and Muller, S. (2009) Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol. Cell 33, 400-409
    • (2009) Mol. Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 49
    • 23244441649 scopus 로고    scopus 로고
    • Measuring fast dynamics in solutions and cells with a laser scanning microscope
    • Digman, M. A., Brown, C. M., Sengupta, P., Wiseman, P. W., Horwitz, A. R., and Gratton, E. (2005) Measuring fast dynamics in solutions and cells with a laser scanning microscope. Biophys. J. 89, 1317-1327
    • (2005) Biophys. J. , vol.89 , pp. 1317-1327
    • Digman, M.A.1    Brown, C.M.2    Sengupta, P.3    Wiseman, P.W.4    Horwitz, A.R.5    Gratton, E.6
  • 50
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1 dependence of different nuclear export signals
    • Henderson, B. R., and Eleftheriou, A. (2000) A comparison of the activity, sequence specificity, and CRM1 dependence of different nuclear export signals. Exp. Cell Res. 256, 213-224
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 51
    • 33751229633 scopus 로고    scopus 로고
    • Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs
    • Pack, C., Saito, K., Tamura, M., and Kinjo, M. (2006) Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91, 3921-3936
    • (2006) Biophys. J. , vol.91 , pp. 3921-3936
    • Pack, C.1    Saito, K.2    Tamura, M.3    Kinjo, M.4
  • 52
    • 17844394185 scopus 로고    scopus 로고
    • Fluctuation correlation spectroscopy with a laser-scanning microscope. Exploiting the hidden time structure
    • Digman, M. A., Sengupta, P., Wiseman, P. W., Brown, C. M., Horwitz, A. R., and Gratton, E. (2005) Fluctuation correlation spectroscopy with a laser-scanning microscope. Exploiting the hidden time structure. Biophys. J. 88, L33-L36
    • (2005) Biophys. J. , vol.88
    • Digman, M.A.1    Sengupta, P.2    Wiseman, P.W.3    Brown, C.M.4    Horwitz, A.R.5    Gratton, E.6
  • 55
    • 80053607423 scopus 로고    scopus 로고
    • Functional connection between Rad51 and PML in homology-directed repair
    • Boichuk, S., Hu, L., Makielski, K., Pandolfi, P. P., and Gjoerup, O. V. (2011) Functional connection between Rad51 and PML in homology-directed repair. PLoS One 6, e25814
    • (2011) PLoS One , vol.6
    • Boichuk, S.1    Hu, L.2    Makielski, K.3    Pandolfi, P.P.4    Gjoerup, O.V.5
  • 56
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies. Dynamic sensors of DNA damage and cellular stress
    • Dellaire, G., and Bazett-Jones, D. P. (2004) PML nuclear bodies. Dynamic sensors of DNA damage and cellular stress. Bioessays 26, 963-977
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 57
    • 33748794780 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA
    • Bøe, S. O., Haave, M., Jul-Larsen, A., Grudic, A., Bjerkvig, R., and Lønning, P. E. (2006) Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA. J. Cell Sci. 119, 3284-3295
    • (2006) J. Cell Sci. , vol.119 , pp. 3284-3295
    • Bøe, S.O.1    Haave, M.2    Jul-Larsen, A.3    Grudic, A.4    Bjerkvig, R.5    Lønning, P.E.6
  • 58
    • 33845871732 scopus 로고    scopus 로고
    • Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus
    • Kumar, P. P., Bischof, O., Purbey, P. K., Notani, D., Urlaub, H., Dejean, A., and Galande, S. (2007) Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus. Nat. Cell Biol. 9, 45-56
    • (2007) Nat. Cell Biol. , vol.9 , pp. 45-56
    • Kumar, P.P.1    Bischof, O.2    Purbey, P.K.3    Notani, D.4    Urlaub, H.5    Dejean, A.6    Galande, S.7
  • 59
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions
    • Wang, J., Shiels, C., Sasieni, P., Wu, P. J., Islam, S. A., Freemont, P. S., and Sheer, D. (2004) Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions. J. Cell Biol. 164, 515-526
    • (2004) J. Cell Biol. , vol.164 , pp. 515-526
    • Wang, J.1    Shiels, C.2    Sasieni, P.3    Wu, P.J.4    Islam, S.A.5    Freemont, P.S.6    Sheer, D.7


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