Review: Properties and Assembly Mechanisms of ND10, PML Bodies, or PODs

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., & Blobel, G. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.6.1457 · Cited by 1,197

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. H., Strauss, J. F., & Maul, G. G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.221 · Cited by 832

Daxx, a Novel Fas-Binding Protein That Activates JNK and Apoptosis

Yang, X., Khosravi-Far, R., Chang, H. Y., & Baltimore, D. (1997) · Cell · doi:10.1016/s0092-8674(00)80294-9 · Cited by 828

A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein

Dyck, J. A., Maul, G. G., Miller, W. H., Chen, J. D., Kakizuka, A., & Evans, R. M. (1994) · Cell · doi:10.1016/0092-8674(94)90340-9 · Cited by 785

A novel nuclear structure containing the survival of motor neurons protein.

Liu, Q., & Dreyfuss, G. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00725.x · Cited by 780

Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus

Muller, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.1.61 · Cited by 674

Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells

Weis, K., Rambaud, S., Lavau, C., Jansen, J., Carvalho, T., Carmo-Fonseca, M., Lamond, A., & Dejean, A. (1994) · Cell · doi:10.1016/0092-8674(94)90341-7 · Cited by 652

Pml is essential for multiple apoptotic pathways

Wang, Z.-G., Ruggero, D., Ronchetti, S., Zhong, S., Gaboli, M., Rivi, R., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/3073 · Cited by 558

The Cell Nucleus

BUSCH, H. (1966) · Nature · doi:10.1038/2111347a0 · Cited by 515

The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion.

Koken, M. H., Puvion-Dutilleul, F., Guillemin, M. C., Viron, A., Linares-Cruz, G., Stuurman, N., de Jong, L., Szostecki, C., Calvo, F., & Chomienne, C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06356.x · Cited by 499

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., & Parkinson, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.8.6581-6591.1998 · Cited by 402

PML induces a novel caspase-independent death process

Quignon, F., De Bels, F., Koken, M., Feunteun, J., Ameisen, J.-C., & de Thé, H. (1998) · Nature Genetics · doi:10.1038/3068 · Cited by 374

HSV-1 IE protein Vmw110 causes redistribution of PML.

Everett, R. D., & Maul, G. G. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06835.x · Cited by 351

Differential SMN2 expression associated with SMA severity

Gavrilov, D. K., Shi, X., Das, K., Gilliam, T. C., & Wang, C. H. (1998) · Nature Genetics · doi:10.1038/3030 · Cited by 338

Evidence for Covalent Modification of the Nuclear Dot–associated Proteins PML and Sp100 by PIC1/SUMO-1

Sternsdorf, T., Jensen, K., & Will, H. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1621 · Cited by 331

Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)

Maul, G. G., Guldner, H. H., & Spivack, J. G. (1993) · Journal of General Virology · doi:10.1099/0022-1317-74-12-2679 · Cited by 315

SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation

Duprez, E., Saurin, A. J., Desterro, J. M., Lallemand-Breitenbach, V., Howe, K., Boddy, M. N., Solomon, E., Thé, H. D., Hay, R. T., & Freemont, P. S. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.3.381 · Cited by 312

Identification of Three Major Sentrinization Sites in PML

Kamitani, T., Kito, K., Nguyen, H. P., Wada, H., Fukuda-Kamitani, T., & Yeh, E. T. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26675 · Cited by 310

Identification of a novel nuclear domain.

Ascoli, C. A., & Maul, G. G. (1991) · The Journal of cell biology · doi:10.1083/jcb.112.5.785 · Cited by 285

Differential Regulation of Sentrinized Proteins by a Novel Sentrin-specific Protease

Gong, L., Millas, S., Maul, G. G., & Yeh, E. T. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3355 · Cited by 279

Interaction of SP100 with HP1 proteins: A link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment

Seeler, J.-S., Marchio, A., Sitterlin, D., Transy, C., & Dejean, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7316 · Cited by 274

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., & Will, H. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.145.12.4338 · Cited by 269

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., & Will, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12555 · Cited by 264

A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies

Stuurman, N., Graaf, A. D., Floore, A., Josso, A., Humbel, B., Jong, L. D., & Driel, R. V. (1992) · Journal of Cell Science · doi:10.1242/jcs.101.4.773 · Cited by 256

Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body

LaMorte, V. J., Dyck, J. A., Ochs, R. L., & Evans, R. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4991 · Cited by 239

The acute promyelocytic leukaemia-associated PML gene is induced by interferon.

Lavau, C., Marchio, A., Fagioli, M., Jansen, J. H., Falini, B., Lebon, P., Grosveld, F. G., Pandolfi, P. P., Pelicci, P. G., & Dejean, A. (1995) · PubMed · Cited by 228

Induction of the PML protein by interferons in normal and APL cells.

Chelbi‐Alix, M. K., Pelicano, L., Quignon, F., Koken, M. H. M., Venturini, L., Stadler, M., Pavlovic, J., Degos, L., & de Thé, H. (1995) · PubMed · Cited by 216

Intracellular Localization of Proteasomal Degradation of a Viral Antigen

Antón, L. C., Schubert, U., Bacík, I., Princiotta, M. F., Wearsch, P. A., Gibbs, J., Day, P. M., Realini, C., Rechsteiner, M. C., Bennink, J. R., et al. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.1.113 · Cited by 215

The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx

Hollenbach, A. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3702 · Cited by 203

Disruption of PML Subnuclear Domains by the Acidic IE1 Protein of Human Cytomegalovirus Is Mediated through Interaction with PML and May Modulate a RING Finger-Dependent Cryptic Transactivator Function of PML

Ahn, J.-H., Brignole, E. J., & Hayward, G. S. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4899 · Cited by 175

Chromatin components as part of a putative transcriptional repressing complex

Lehming, N., Le Saux, A., Schüller, J., & Ptashne, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7322 · Cited by 175

Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling

Doucas, V., Tini, M., Egan, D. A., & Evans, R. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2627 · Cited by 170

PML nuclear bodies are general targets for inflammation and cell proliferation.

Terris, B., Baldin, V., Dubois, S., Degott, C., Fléjou, J., Hénin, D., & Dejean, A. (1995) · PubMed · Cited by 163

Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment.

Korioth, F., Gieffers, C., Maul, G. G., & Frey, J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.1.1 · Cited by 161

The Promyelocytic Leukemia Gene Product (PML) Forms Stable Complexes with the Retinoblastoma Protein

Alcalay, M., Tomassoni, L., Colombo, E., Stoldt, S., Grignani, F., Fagioli, M., Szekely, L., Helin, K., & Pelicci, P. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.1084 · Cited by 161

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., & Epstein, A. L. (1995) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240590410 · Cited by 143

Exclusion of Int-6 from PML Nuclear Bodies by Binding to the HTLV-I Tax Oncoprotein

Morris, C., Rousset, R., Bantignies, F., & Jalinot, P. (1996) · Science · doi:10.1126/science.273.5277.951 · Cited by 131

Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death

Pluta, A. F., Earnshaw, W. C., & Goldberg, I. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.14.2029 · Cited by 124

Localization of Nuclear Functions as Revealed by Ultrastructural Autoradiography and Cytochemistry

Bouteille, M., Laval, M., & Dupuy-Coin, A. M. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-147601-4.50009-9 · Cited by 119

Diversity of autoantibodies in primary biliary cirrhosis and chronic active hepatitis.

Bernstein, R. M., Neuberger, J., Bunn, C., Callender, M. E., Hughes, G. R. V., & Williams, R. L. (1984) · PubMed Central · Cited by 110

Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin

Bridger, J. M., Herrmann, H. O., Münkel, C., & Lichter, P. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.9.1241 · Cited by 85

Cloning and Expression of Primate Daxx cDNAs and Mapping of the Human Gene to Chromosome 6p21.3 in the MHC Region

Kiriakidou, M., Driscoll, D. A., López-Guisa, J. M., & Strauss, J. F. (1997) · DNA and Cell Biology · doi:10.1089/dna.1997.16.1289 · Cited by 58

Nuclear redistribution of BRCA1 during viral infection.

Maul, G. G., Jensen, D. E., Ishov, A. M., Herlyn, M., & Rauscher, F. J. (1998) · PubMed · Cited by 42

A gene amplified in a transformed mouse cell line undergoes complex transcriptional processing and encodes a nuclear protein.

Snyder, L. C., Trusko, S. P., Freeman, N., et al. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37511-2 · Cited by 17

ANTINUCLEAR ANTIBODIES IN PRIMARY BILIARY CIRRHOSIS

Bernstein, R. (1984) · The Lancet · doi:10.1016/s0140-6736(84)92869-1 · Cited by 12

Molecular Biology of Pseudorabies Virus: Impact on Neurovirology and Veterinary Medicine

Pomeranz, L. E., Reynolds, A. E., & Hengartner, C. J. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.3.462-500.2005 · Cited by 869

Defying death after DNA damage

Rich, T., Allen, R. L., & Wyllie, A. H. (2000) · Nature · doi:10.1038/35037717 · Cited by 724

A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins

Rothbauer, U., Zolghadr, K., Muyldermans, S., Schepers, A., Cardoso, M. C., & Leonhardt, H. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700342-mcp200 · Cited by 677

Alternative lengthening of telomeres in mammalian cells

Henson, J. D., Neumann, A. A., Yeager, T. R., & Reddel, R. R. (2002) · Oncogene · doi:10.1038/sj.onc.1205058 · Cited by 664

Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2

Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L. (2002) · Nature Cell Biology · doi:10.1038/ncb715 · Cited by 592