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Alcalay, M., Tomassoni, L., Colombo, E., Stoldt, S., Grignani, F., Fagioli, M., Szekely, L., Helin, K. and Pelicci, P. G (1998). The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein. Mol. Cell Biol 18, 1084-1093.[Abstract/Free Full Text]

Ascoli, C. A. and Maul, G. G (1991). Identification of a novel nuclear domain. J. Cell Biol 112, 785-795.[Abstract/Free Full Text]

Baxevanis, A. D. and Landsman, D (1995). The HMG-1 box protein family: classification and functional relationships. Nucl. Acids Res 23, 1604-1613.[Abstract/Free Full Text]

Bloch, D. B., de la Monte, S. M., Guigaouri, P., Filippov, A. and Bloch, K. D (1996). Identification and characterization of a leukocyte-specific component of the nuclear body. J. Biol. Chem 271, 29198-29204.[Abstract/Free Full Text]

Boddy, M. N., Howe, K., Etkin, L. D., Solomon, E. and Freemont, P. S (1996). PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13, 971-982.[Medline]

Boshart, M., Weber, F., Jahn, G., Dorsch, H. K., Fleckenstein, B. and Schaffner, W (1985). A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus. Cell 41, 521-530.[Medline]

Brasch, K. and Ochs, R. L (1992). Nuclear bodies (NBs): A newly \324rediscovered' organelle. Exp. Cell Res 202, 211-223.[Medline]

Bustin, M., Lehn, D. A. and Landsman, D (1990). Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049, 231-243.[Medline]

Buwitt, U., Flohr, T. and Bottger, E. C (1992). Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. EMBO J 11, 489-496.[Medline]

Cao, T., Duprez, E., Borden, K. L., Freemont, P. S. and Etkin, L. D (1998). Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. J. Cell Sci 111, 1319-1329.[Abstract]

Carvalho, T., Seeler, J. S., \205hman, K., Jordan, P., Pettersson, U., Akusj\212rvi, G., Carmo-Fonseca, M. and Dejean, A (1995). Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies. J. Cell Biol 131, 45-56.[Abstract/Free Full Text]

Chan, J. Y., Li, L., Fan, Y. H., Mu, Z. M., Zhang, W. W. and Chang, K. S (1997). Cell-cycle regulation of DNA damage-induced expression ofthe suppressor gene PML. Biochem. Biophys. Res. Commun 240, 640-646.[Medline]

Chelbi-Alix, M. K., Pelicano, L., Quignon, F., Koken, M. H. M., Venturini, L., Stadler, M., Pavlovic, J., Degos, L. and de The, H (1995). Inductionof the PML protein by interferons in normal and APL cells. Leukemia 9, 2027-2033.[Medline]

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.[Abstract/Free Full Text]

Dang, C. V. and Lee, W. M (1989). Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins. J. Biol. Chem 264, 18019-18023.[Abstract/Free Full Text]

Daniel, M. T., Koken, M. H. M., Romagne, O., Barbey, S., Bazarbachi, A., Stadler, M., Guillemin, M. C., Degos, L., Chomienne, C. and de The, H (1993). PML protein expression in hematopoietic and acute promyelocytic leukemia cells. Blood 82, 1858-1867.[Abstract/Free Full Text]

de The, H., Riviere, M. and Bernhard, W (1960). Examen au microscope electronique de la tumeur VX2 du lapin domestique derivee du papillome de shope. Bull. Cancer 47, 569-584.

de The, H., Chomienne, C., Lanotte, M., Degos, L. and Dejean, A (1990). The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus. Nature 347, 558-561.[Medline]

Dent, A. L., Yewdell, J., Puviondutilleul, F., Koken, M. H. M., de The, H. and Staudt, L. M (1996). LYSP100-associated nuclear domains (LANDs): Description of a new class of subnuclear structures and their relationship to PML nuclear bodies. Blood 88, 1423-1436.[Abstract/Free Full Text]

Dingwall, C. and Laskey, R. A (1991). Nuclear targeting sequences\321a consensus?. Trends Biochem. Sci 16, 478-481.[Medline]

Doucas, V. and Evans, R. M (1996). The PML nuclear compartment and cancer. Biochim. Biophys. Acta 1288, 25-.

Dyck, J. A., Maul, G. G., Miller, W. J., Chen, J. D., Kakizuka, A. and Evans, R. M (1994). A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343.[Medline]

Fagioli, M., Alcalay, M., Pandolfi, P. P., Venturini, L., Mencarelli, A., Simeone, A., Acampora, D., Grignani, F. and Pelicci, P. G (1992). Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms. Oncogene 7, 1083-1091.[Medline]

Gariglio, M., Ying, G. G., Hertel, L., Gaboli, M., Clerc, R. G. and Landolfo, S (1997). The high-mobility group protein T160 binds to both linear and cruciform DNA and mediates DNA bending as determined by ring closure. Exp. Cell Res 236, 472-481.[Medline]

Giese, K., Cox, J. and Grosschedl, R (1992). The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures. Cell 69, 185-195.[Medline]

Goddard, A. D., Borrow, J., Freemont, P. S. and Solomon, E (1991). Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia. Science 254, 1371-1374.[Abstract/Free Full Text]

Gongora, C., David, G., Pintard, L., Tissot, C., Hua, T. D., Dejean, A. and Mechti, N (1997). Molecular cloning of a new interferon-induced PML nuclear body-associated protein. J. Biol. Chem 272, 19457-19463.[Abstract/Free Full Text]

Grande, M. A., van der Kraan, I., van Steensel, B., Schul, W., de The, H., van der Voort, H. T., de Jong, L. and van Driel, R (1996). PML-containing nuclear bodies: their spatial distribution in relation to other nuclear components. J. Cell Biochem 63, 280-291.[Medline]

Gross, C. T. and McGinnis, W (1996). DEAF-1, a novel protein that binds an essential region in a Deformed response element. EMBO J 15, 1961-1970.[Medline]

Grosschedl, R. K., Giese, K. and Pagel, J (1994). HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet 10, 94-100.[Medline]

Gr\232tzinger, T., Jensen, K., Guldner, H. H., Sternsdorf, T., Szostecki, C., Schwab, M., Savelyeva, L., Reich, B. and Will, H (1996). A highly amplified mouse gene is homologous to the human interferon-responsive Sp100 gene encoding an autoantigen associated with nuclear dots. Mol. Cell Biol 16, 1150-1156.[Abstract]

Gr\232tzinger, T., Jensen, K. and Will, H (1996). The interferon (IFN)-stimulated gene Sp100 promoter contains an IFN gamma activation site and an imperfect IFN-stimulated response element which mediate type I IFN inducibility. J. Biol. Chem 271, 25253-25260.[Abstract/Free Full Text]

Gr\232tzinger, 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.[Medline]

Guldner, H. H., Lakomek, H. J. and Bautz, F. A (1986). Anti-(U1)RNP and anti-Sm autoantibody profiles in patients with systemic rheumatic diseases: differential detection of immunoglobulin G and M by immunoblotting. Clin. Immunol. Immunopathol 40, 532-538.[Medline]

Guldner, H. H., Netter, H. J., Szostecki, C., Jaeger, E. and Will, H (1990). Human anti-p68 autoantibodies recognize a common epitope of U1 RNA containing small nuclear ribonucleoprotein and influenza B virus. J. Exp. Med 171, 819-829.[Abstract/Free Full Text]

Guldner, H. H., Szostecki, C., Gr\232tzinger, T. and Will, H (1992). IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol 149, 4067-4073.[Abstract]

Hartl, P. and Lipp, M (1987). Generation of a variant t(2;8) translocation of Burkitt's lymphoma by site-specific recombination via the kappa light-chain joining signals. Mol. Cell Biol 7, 2037-2045.[Abstract/Free Full Text]

Jantzen, H. M., Admon, A., Bell, S. P. and Tjian, R (1990). Nucleolar transcription factor hUBF contains a DNA-binding motif with homology to HMG proteins. Nature 344, 830-836.[Medline]

Kadereit, S., Gewert, D. R., Galabru, J., Hovanessian, A. G. and Meurs, E. F (1993). Molecular cloning of two new interferon-induced, highly related nuclear phosphoproteins. J. Biol. Chem 268, 24432-24441.[Abstract/Free Full Text]

Kakizuka, A., Miller, W. J., Umesono, K., Warrell, R. J., Frankel, S. R., Murty, V. V., Dmitrovsky, E. and Evans, R. M (1991). Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66, 663-674.[Medline]

Kamei, H (1997). Cystine starvation induces reversible large-body formation from nuclear bodies in T24 cells. Exp. Cell Res 237, 207-216.[Medline]

Kamitani, T., Kito, K., Nguyen, H. P., Wada, H., Fukuda-Kamitani, T. and Yeh, E. T. H (1998). Identification of three major sentrinization sites in PML. J. Biol. Chem 273, 26675-26682.[Abstract/Free Full Text]

Koken, M. H., Reid, A., Quignon, F., Chelbi-Alix, M. K., Davies, J. M., Kabarowski, J. H., Zhu, J., Dong, S., Chen, S., Chen, Z. et al (1997). Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies. Proc. Nat. Acad. Sci. USA 94, 10255-10260.[Abstract/Free Full Text]

Koken, M. H. M., Linares-Cruz, G., Quignon, F., Viron, A., Chelbi-Alix, M. K., Sobczak-Thepot, J., Juhlin, L., Degos, L., Calvo, F. and de The, H (1995). The PML growth-suppressor has an altered expression in human oncogenesis. Oncogene 10, 1315-1324.[Medline]

Koken, M. H. M., Puvion, D. F., Guillemin, M. C., Viron, A., Linares-Cruz, G., Stuurman, N., de Jong, L., Szostecki, C., Calvo, F., Chomienne, C. et al (1994). The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO J 13, 1073-1083.[Medline]

Korioth, F., Gieffers, C., Maul, G. G. and Frey, J (1995). Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment. J. Cell Biol 130, 1-13.[Abstract/Free Full Text]

Lamond, A. I. and Earnshaw, W. C (1998). Structure and function in the nucleus. Science 280, 547-553.[Abstract/Free Full Text]

LaMorte, V. J., Dyck, J. A., Ochs, R. L. and Evans, R. M (1998). Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Nat. Acad. Sci. USA 95, 4991-4996.[Abstract/Free Full Text]

Laudet, V., Stehelin, D. and Clevers, H (1993). Ancestry and diversity of the HMG box superfamily. Nucl. Acids Res 21, 2493-2501.[Abstract/Free Full Text]

Lavau, C., Marchio, A., Fagioli, M., Jansen, J., Falini, B., Lebon, P., Grosveld, F., Pandolfi, P. P., Pelicci, P. G. and Dejean, A (1995). The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene 11, 871-878.[Medline]

LeBoeuf, R. D., Ban, E. M. H., Green, M. M., Stone, A. S., Probst, S. M., Blalock, E. J. and Tauber, J. D (1998). Molecular cloning, sequence analysis, expression, and tissue distribution of Suppressin, a novel suppressor of cell cycle entry. J. Biol. Chem 273, 361-368.[Abstract/Free Full Text]

LeBoeuf, R. D., Burns, J. N., Bost, K. L. and Blalock, J. E (1990). Isolation, purification, and partial characterization of suppressin, a novel inhibitor of cell proliferation. J. Biol. Chem 265, 158-165.[Abstract/Free Full Text]

Lehming, N., Le Saux, A., Schuller, J. and Ptashne, M (1998). Chromatin components as part of a putative transcriptional repressing complex. Proc. Nat. Acad. Sci. USA 95, 7322-7326.[Abstract/Free Full Text]

Lovell-Badge, R (1995). Developmental genetics. Living with bad architecture. Nature 376, 725-726.[Medline]

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.[Medline]

Mu, Z. M., Chin, K. V., Liu, J. H., Lozano, G. and Chang, K. S (1994). PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell Biol 14, 6858-6867.[Abstract/Free Full Text]

Mu, Z. M., Le, X. F., Glassman, A. B. and Chang, K. S (1996). The biologic function of PML and its role in acute promyelocytic leukemia. Leuk. Lymphoma 23, 277-285.[Medline]

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.[Medline]

Ohndorf, U. M., Whitehead, J. P., Raju, N. L. and Lippard, S. J (1997). Binding of tsHMG, a mouse testis-specific HMG-domain protein, to cisplatin-DNA adducts. Biochemistry 36, 14807-14815.[Medline]

Plass, C., Weichenhan, D., Kunze, B., Hellwig, T., Schneider, C., Bautz, F. A., Grzeschik, K. H., Traut, W. and Winking, H (1995). A member of the mouse LRR transcript family with homology to the human Sp100 gene. Hereditas 122, 245-256.[Medline]

P\232hler, J. R., Norman, D. G., Bramham, J., Bianchi, M. E. and Lilley, D. M (1998). HMG box proteins bind to four-way DNA junctions in their open conformation. EMBO J 17, 817-826.[Medline]

Quignon, F., De Bels, F., Koken, M., Feunteun, J., Ameisen, J. C. and de The, H (1998). PML induces a novel caspase-independent death process. Nat. Genet 20, 259-265.[Medline]

Reyes, J. C., Muchardt, C. and Yaniv, M (1997). Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J. Cell Biol 137, 263-274.[Abstract/Free Full Text]

Ross, J (1995). mRNA stability in mammalian cells. Microbiol. Rev 59, 423-450.[Abstract/Free Full Text]

Saitoh, H., Pu, R. T. and Dasso, M (1997). SUMO-1: wrestling with a new ubiquitin-related modifier. Trends Biochem. Sci 22, 374-376.[Medline]

Seeler, J. S., Marchio, A., Sitterlin, D., Transy, C. and Dejean, A (1998). Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. Proc. Nat. Acad. Sci. USA 95, 7316-7321.[Abstract/Free Full Text]

Shirakawa, H. and Yoshida, M (1992). Structure of a gene coding for human HMG2 protein. J. Biol. Chem 267, 6641-6645.[Abstract/Free Full Text]

Skinner, P. J., Koshy, B. T., Cummings, C. J., Klement, I. A., Helin, K., Servadio, A., Zoghbi, H. Y. and Orr, H. T (1997). Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures. Nature 389, 971-974.[Medline]

Stadler, M., Chelbi-Alix, M. K., Koken, M. H. M., Venturini, L., Lee, C., Saib, A., Quignon, F., Pelicano, L., Guillemin, M. C., Schindler, C. and de The, H (1995). Transcriptional induction of the PML growth suppressor gene by interferons is mediated through an ISRE and a GAS element. Oncogene 11, 2565-2573.[Medline]

Stemler, M., Weimer, T., Tu, Z. X., Wan, D. F., Levrero, M., Jung, C., Pape, G. R. and Will, H (1990). Mapping of B-cell epitopes of the human hepatitis B virus X protein. J. Virol 64, 2802-2809.[Abstract/Free Full Text]

Sternsdorf, T., Gr\232tzinger, T., Jensen, K. and Will, H (1997). Nuclear dots: Actors on many stages. Immunobiology 198, 307-331.[Medline]

Sternsdorf, T., Jensen, K. and Will, H (1997). Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J. Cell Biol 139, 1621-1634.[Abstract/Free Full Text]

Sternsdorf, T., Jensen, K., Zuchner, D. and Will, H (1997). Cellularlocalization, expression, and structure of the nuclear dot protein 52. J. Cell Biol 138, 435-448.[Abstract/Free Full Text]

Stros, M. and Dixon, G. H (1993). A retropseudogene for non-histone chromosomal protein HMG-1. Biochim. Biophys. Acta 1172, 231-235.[Medline]

Szostecki, C., Krippner, H., Penner, E. and Bautz, F. A (1987). Autoimmune sera recognize a 100 kD nuclear protein antigen (Sp100). Clin. Exp. Immunol 68, 108-116.[Medline]

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.[Abstract]

Szostecki, C., Will, H., Netter, H. J. and Guldner, H. H (1992). Autoantibodies to the nuclear Sp100 protein in primary biliary cirrhosis and associated diseases: epitope specificity and immunoglobulin class distribution. Scand. J. Immunol 36, 555-564.[Medline]

Terris, B., Baldin, V., Dubois, S., Degott, C., Flejou, J. F., Henin, D. and Dejean, A (1995). PML nuclear bodies are general targets for inflammation and cell proliferation. Cancer Res 55, 1590-1597.[Abstract/Free Full Text]

Tjian, R. and Maniatis, T (1994). Transcriptional activation: a complex puzzle with few easy pieces. Cell 77, 5-8.[Medline]

Vallian, S., Gaken, J. A., Trayner, I. D., Gingold, E. B., Kouzarides, T., Chang, K. S. and Farzaneh, F (1997). Transcriptional repression by the promyelocytic leukemia protein, PML. Exp. Cell Res 237, 371-382.[Medline]

Wang, J. F., Bashir, M., Engelsberg, B. N., Witmer, C., Rozmiarek, H. and Billings, P. C (1997). High mobility group proteins 1 and 2 recognize chromium-damaged DNA. Carcinogenesis 18, 371-375.[Abstract/Free Full Text]

Wang, W., Chi, T., Xue, Y., Zhou, S., Kuo, A. and Crabtree, G. R (1998). Architectural DNA binding by a high-mobility-group/kinesin-like subunit in mammalian SWI/SNF-related complexes. Proc. Nat. Acad. Sci. USA 95, 492-498.[Abstract/Free Full Text]

Wang, Z. G., Ruggero, D., Ronchetti, S., Zhong, S., Gaboli, M., Rivi, R. and Pandolfi, P. P (1998). PML is essential for multiple apoptotic pathways. Nat. Genet 20, 266-272.[Medline]

Weichenhan, D., Kunze, B., Zacker, S., Traut, W. and Winking, H (1997). Structure and expression of the murine Sp100 nuclear dot gene. Genomics 43, 298-306.[Medline]

Weis, K., Rambaud, S., Lavau, C., Jansen, J., Carvalho, T., Carmo-Fonseca, M., Lamond, A. and Dejean, A (1994). Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76, 345-356.[Medline]

Wen, L., Huang, J. K., Johnson, B. H. and Reeck, G. R (1989). A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1. Nucl. Acids Res 17, 1197-1214.[Abstract/Free Full Text]

Wolffe, A. P (1994). Architectural transcription factors. Science 264, 1100-1111.[Free Full Text]

Xie, K., Lambie, E. J. and Snyder, M (1993). Nuclear dot antigens may specify transcriptional domains in the nucleus. Mol. Cell Biol 13, 6170-6179.[Abstract/Free Full Text]

Zheng, P., Guo, Y., Niu, Q., Levy, D. E., Dyck, J. A., Lu, S., Sheiman, L. A. and Liu, Y (1998). Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature 396, 373-376.[Medline]




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