Science 29 November 1991: Vol. 254. no. 5036, pp. 1371 - 1374 DOI: 10.1126/science.1720570

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Articles

PML Activates Transcription by Protecting HIPK2 and p300 from SCFFbx3-Mediated Degradation.

Y. Shima, T. Shima, T. Chiba, T. Irimura, P. P. Pandolfi, and I. Kitabayashi (2008)
Mol. Cell. Biol. 28, 7126-7138
 |  Abstract »  |  Full Text »  |  PDF »

Dynamics of component exchange at PML nuclear bodies.

S. Weidtkamp-Peters, T. Lenser, D. Negorev, N. Gerstner, T. G. Hofmann, G. Schwanitz, C. Hoischen, G. Maul, P. Dittrich, and P. Hemmerich (2008)
J. Cell Sci. 121, 2731-2743
 |  Abstract »  |  Full Text »  |  PDF »

Aberrant Association of Promyelocytic Leukemia Protein-Retinoic Acid Receptor-{alpha} with Coactivators Contributes to Its Ability to Regulate Gene Expression.

E. L. Reineke, H. Liu, M. Lam, Y. Liu, and H.-Y. Kao (2007)
J. Biol. Chem. 282, 18584-18596
 |  Abstract »  |  Full Text »  |  PDF »

Interferon Regulatory Factor-8 Is Indispensable for the Expression of Promyelocytic Leukemia and the Formation of Nuclear Bodies in Myeloid Cells.

N. Dror, N. Rave-Harel, A. Burchert, A. Azriel, T. Tamura, P. Tailor, A. Neubauer, K. Ozato, and B.-Z. Levi (2007)
J. Biol. Chem. 282, 5633-5640
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The promyelocytic leukemia protein functions as a negative regulator of IFN-{gamma} signaling.

Y.-H. Choi, R. Bernardi, P. P. Pandolfi, and E. N. Benveniste (2006)
PNAS 103, 18715-18720
 |  Abstract »  |  Full Text »  |  PDF »

Promyelocytic Leukemia Activates Chk2 by Mediating Chk2 Autophosphorylation.

S. Yang, J.-H. Jeong, A. L. Brown, C.-H. Lee, P. P. Pandolfi, J. H. Chung, and M. K. Kim (2006)
J. Biol. Chem. 281, 26645-26654
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The Interaction of Piasy with Trim32, an E3-Ubiquitin Ligase Mutated in Limb-girdle Muscular Dystrophy Type 2H, Promotes Piasy Degradation and Regulates UVB-induced Keratinocyte Apoptosis through NF{kappa}B.

A. Albor, S. El-Hizawi, E. J. Horn, M. Laederich, P. Frosk, K. Wrogemann, and M. Kulesz-Martin (2006)
J. Biol. Chem. 281, 25850-25866
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Evidence for a Role of the Cellular ND10 Protein PML in Mediating Intrinsic Immunity against Human Cytomegalovirus Infections..

N. Tavalai, P. Papior, S. Rechter, M. Leis, and T. Stamminger (2006)
J. Virol. 80, 8006-8018
 |  Abstract »  |  Full Text »  |  PDF »

The ProMiscuousLy (PML) exciting nuclear protein has another partner.

K. Jensen, C. Shiels, and P. S. Freemont (2005)
Blood 105, 3393-3394
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The promyelocytic leukemia protein PML regulates c-Jun function in response to DNA damage.

P. Salomoni, R. Bernardi, S. Bergmann, A. Changou, S. Tuttle, and P. P. Pandolfi (2005)
Blood 105, 3686-3690
 |  Abstract »  |  Full Text »  |  PDF »

PML bodies: a meeting place for genomic loci?.

R. W. Ching, G. Dellaire, C. H. Eskiw, and D. P. Bazett-Jones (2005)
J. Cell Sci. 118, 847-854
 |  Abstract »  |  Full Text »  |  PDF »

Physical and functional link of the leukemia-associated factors AML1 and PML.

L. A. Nguyen, P. P. Pandolfi, Y. Aikawa, Y. Tagata, M. Ohki, and I. Kitabayashi (2005)
Blood 105, 292-300
 |  Abstract »  |  Full Text »  |  PDF »

HLS5, a Novel RBCC (Ring Finger, B Box, Coiled-coil) Family Member Isolated from a Hemopoietic Lineage Switch, Is a Candidate Tumor Suppressor.

J.-P. Lalonde, R. Lim, E. Ingley, P. A. Tilbrook, M. J. Thompson, R. McCulloch, J. G Beaumont, C. Wicking, H. J. Eyre, G. R. Sutherland, et al. (2004)
J. Biol. Chem. 279, 8181-8189
 |  Abstract »  |  Full Text »  |  PDF »

Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions.

J. Wang, C. Shiels, P. Sasieni, P. J. Wu, S. A. Islam, P. S. Freemont, and D. Sheer (2004)
J. Cell Biol. 164, 515-526
 |  Abstract »  |  Full Text »  |  PDF »

JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells.

C. Moog-Lutz, F. Cave-Riant, F. C. Guibal, M. A. Breau, Y. Di Gioia, P. O. Couraud, Y. E. Cayre, S. Bourdoulous, and P. G. Lutz (2003)
Blood 102, 3371-3378
 |  Abstract »  |  Full Text »  |  PDF »

Physical and Functional Interactions between PML and MDM2.

X. Wei, Z. K. Yu, A. Ramalingam, S. R. Grossman, J. H. Yu, D. B. Bloch, and C. G. Maki (2003)
J. Biol. Chem. 278, 29288-29297
 |  Abstract »  |  Full Text »  |  PDF »

The Promyelocytic Leukemia Protein Does Not Mediate Foamy Virus Latency In Vitro.

C. D. Meiering and M. L. Linial (2003)
J. Virol. 77, 2207-2213
 |  Abstract »  |  Full Text »  |  PDF »

Arsenic Trioxide Promotes Histone H3 Phosphoacetylation at the Chromatin of CASPASE-10 in Acute Promyelocytic Leukemia Cells.

J. Li, P. Chen, N. Sinogeeva, M. Gorospe, R. P. Wersto, F. J. Chrest, J. Barnes, and Y. Liu (2002)
J. Biol. Chem. 277, 49504-49510
 |  Abstract »  |  Full Text »  |  PDF »

The Retinoic Acid Receptor {alpha} (RAR{alpha}) Chimeric Proteins PML-, PLZF-, NPM-, and NuMA-RAR{alpha} Have Distinct Intracellular Localization Patterns.

J. L. Hummel, T. Zhang, R. A. Wells, and S. Kamel-Reid (2002)
Cell Growth Differ. 13, 173-183
 |  Abstract »  |  Full Text »  |  PDF »

Effects of Promyelocytic Leukemia Protein on Virus-Host Balance.

W. V. Bonilla, D. D. Pinschewer, P. Klenerman, V. Rousson, M. Gaboli, P. P. Pandolfi, R. M. Zinkernagel, M. S. Salvato, and H. Hengartner (2002)
J. Virol. 76, 3810-3818
 |  Abstract »  |  Full Text »  |  PDF »

PML bodies associate specifically with the MHC gene cluster in interphase nuclei.

C. Shiels, S. A. Islam, R. Vatcheva, P. Sasieni, M. J. E. Sternberg, P. S. Freemont, and D. Sheer (2002)
J. Cell Sci. 114, 3705-3716
 |  Abstract »  |  Full Text »  |  PDF »

SUMO-1 Modification of Human Cytomegalovirus IE1/IE72.

M. L. Spengler, K. Kurapatwinski, A. R. Black, and J. Azizkhan-Clifford (2002)
J. Virol. 76, 2990-2996
 |  Abstract »  |  Full Text »  |  PDF »

Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk.

Q. Zhu, J.-W. Zhang, H.-Q. Zhu, Y.-L. Shen, M. Flexor, P.-M. Jia, Y. Yu, X. Cai, S. Waxman, M. Lanotte, et al. (2002)
Blood 99, 1014-1022
 |  Abstract »  |  Full Text »  |  PDF »

Oncogenes and tumor suppressors in the molecular pathogenesis of acute promyelocytic leukemia.

P. P. Pandolfi (2001)
Hum. Mol. Genet. 10, 769-775
 |  Abstract »  |  Full Text »  |  PDF »

Human RERE Is Localized to Nuclear Promyelocytic Leukemia Oncogenic Domains and Enhances Apoptosis.

T. Waerner, P. Gardellin, K. Pfizenmaier, A. Weith, and N. Kraut (2001)
Cell Growth Differ. 12, 201-210
 |  Abstract »  |  Full Text »

Epstein-Barr Virus Immediate-Early Protein BZLF1 Is SUMO-1 Modified and Disrupts Promyelocytic Leukemia Bodies.

A. L. Adamson and S. Kenney (2001)
J. Virol. 75, 2388-2399
 |  Abstract »  |  Full Text »

Evidence for separate ND10-binding and homo-oligomerization domains of Sp100.

D Negorev, A. Ishov, and G. Maul (2001)
J. Cell Sci. 114, 59-68
 |  Abstract »  |  PDF »

PAX8-PPARgamma 1 Fusion in Oncogene Human Thyroid Carcinoma.

T. G. Kroll, P. Sarraf, L. Pecciarini, C.-J. Chen, E. Mueller, B. M. Spiegelman, and J. A. Fletcher (2000)
Science 289, 1357-1360
 |  Abstract »  |  Full Text »

PML is induced by oncogenic ras and promotes premature senescence.

G. Ferbeyre, E. de Stanchina, E. Querido, N. Baptiste, C. Prives, and S. W. Lowe (2000)
Genes & Dev. 14, 2015-2027
 |  Abstract »  |  Full Text »

Leukemia initiated by PMLRARalpha : the PML domain plays a critical role while retinoic acid-mediated transactivation is dispensable.

S. C. Kogan, S.-h. Hong, D. B. Shultz, M. L. Privalsky, and J. M. Bishop (2000)
Blood 95, 1541-1550
 |  Abstract »  |  Full Text »  |  PDF »

Promyelocytic Leukemia Protein (PML) and Daxx Participate in a Novel Nuclear Pathway for Apoptosis.

S. Zhong, P. Salomoni, S. Ronchetti, A. Guo, D. Ruggero, and P. P. Pandolfi (2000)
J. Exp. Med. 191, 631-640
 |  Abstract »  |  Full Text »  |  PDF »

PML Is Critical for ND10 Formation and Recruits the PML-interacting Protein Daxx to this Nuclear Structure When Modified by SUMO-1.

A. M. Ishov, A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T.H. Yeh, J. F. Strauss , III, and G. G. Maul (1999)
J. Cell Biol. 147, 221-234
 |  Abstract »  |  Full Text »  |  PDF »

Underdeveloped uterus and reduced estrogen responsiveness in mice with disruption of the estrogen-responsive finger protein gene, which is a direct target of estrogen receptor alpha.

A. Orimo, S. Inoue, O. Minowa, N. Tominaga, Y. Tomioka, M. Sato, J. Kuno, H. Hiroi, Y. Shimizu, M. Suzuki, et al. (1999)
PNAS 96, 12027-12032
 |  Abstract »  |  Full Text »  |  PDF »

Complete Remission of t(11;17) Positive Acute Promyelocytic Leukemia Induced by All-trans Retinoic Acid and Granulocyte Colony-Stimulating Factor.

J.H. Jansen, M.C. de Ridder, W.M.C. Geertsma, C.A.J. Erpelinck, K. van Lom, E.M.E. Smit, R. Slater, B.A. v. Reijden, G.E. de Greef, P. Sonneveld, et al. (1999)
Blood 94, 39-45
 |  Abstract »  |  Full Text »  |  PDF »

Viral Immediate-Early Proteins Abrogate the Modification by SUMO-1 of PML and Sp100 Proteins, Correlating with Nuclear Body Disruption.

S. Müller and A. Dejean (1999)
J. Virol. 73, 5137-5143
 |  Abstract »  |  Full Text »

Deconstructing a Disease: RAR{alpha}, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia.

A. Melnick and J. D. Licht (1999)
Blood 93, 3167-3215
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Seed Versus Soil: The Importance of the Target Cell for Transgenic Models of Human Leukemias.

P. Westervelt and T. J. Ley (1999)
Blood 93, 2143-2148
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Splice variants of the nuclear dot-associated Sp100 protein contain homologies to HMG-1 and a human nuclear phosphoprotein-box motif.

H. Guldner, C Szostecki, P Schroder, U Matschl, K Jensen, C Luders, H Will, and T Sternsdorf (1999)
J. Cell Sci. 112, 733-747
 |  Abstract »  |  PDF »

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

E Duprez, A. Saurin, J. Desterro, V Lallemand-Breitenbach, K Howe, M. Boddy, E Solomon, H de The, R. Hay, and P. Freemont (1999)
J. Cell Sci. 112, 381-393
 |  Abstract »  |  PDF »

The Promyelocytic Leukemia Protein Interacts with Sp1 and Inhibits Its Transactivation of the Epidermal Growth Factor Receptor Promoter.

S. Vallian, K.-V. Chin, and K.-S. Chang (1998)
Mol. Cell. Biol. 18, 7147-7156
 |  Abstract »  |  Full Text »

Trivalent Antimonials Induce Degradation of the PML-RARalpha Oncoprotein and Reorganization of the Promyelocytic Leukemia Nuclear Bodies in Acute Promyelocytic Leukemia NB4 Cells.

S. Muller, W. H. Miller Jr, and A. Dejean (1998)
Blood 92, 4308-4316
 |  Abstract »  |  Full Text »  |  PDF »

The Novel Estrogen-Responsive B Box Protein (EBBP) Gene Is Tamoxifen Regulated in Cells Expressing an Estrogen Receptor DNA-Binding Domain Mutant.

H.-L. C. Liu, E. Golder-Novoselsky, M. H. Seto, L. Webster, J. McClary, and D. A. Zajchowski (1998)
Mol. Endocrinol. 12, 1733-1748
 |  Abstract »  |  Full Text »

Identification of Three Major Sentrinization Sites in PML.

T. Kamitani, K. Kito, H. P. Nguyen, H. Wada, T. Fukuda-Kamitani, and E. T. H. Yeh (1998)
J. Biol. Chem. 273, 26675-26682
 |  Abstract »  |  Full Text »  |  PDF »

Coactivator TIF1beta Interacts with Transcription Factor C/EBPbeta and Glucocorticoid Receptor To Induce alpha 1-Acid Glycoprotein Gene Expression.

C.-J. Chang, Y.-L. Chen, and S.-C. Lee (1998)
Mol. Cell. Biol. 18, 5880-5887
 |  Abstract »  |  Full Text »

The Promyelocytic Leukemia Zinc Finger Protein Affects Myeloid Cell Growth, Differentiation, and Apoptosis.

R. Shaknovich, P. L. Yeyati, S. Ivins, A. Melnick, C. Lempert, S. Waxman, A. Zelent, and J. D. Licht (1998)
Mol. Cell. Biol. 18, 5533-5545
 |  Abstract »  |  Full Text »

The Disruption of ND10 during Herpes Simplex Virus Infection Correlates with the Vmw110- and Proteasome-Dependent Loss of Several PML Isoforms.

R. D. Everett, P. Freemont, H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson (1998)
J. Virol. 72, 6581-6591
 |  Abstract »  |  Full Text »  |  PDF »

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.

J.-H. Ahn, E. J. Brignole III, and G. S. Hayward (1998)
Mol. Cell. Biol. 18, 4899-4913
 |  Abstract »  |  Full Text »

Two RING Finger Proteins, the Oncoprotein PML and the Arenavirus Z Protein, Colocalize with the Nuclear Fraction of the Ribosomal P Proteins.

K. L. B. Borden, E. J. CampbellDwyer, G. W. Carlile, M. Djavani, and M. S. Salvato (1998)
J. Virol. 72, 3819-3826
 |  Abstract »  |  Full Text »  |  PDF »

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

V. J. LaMorte, J. A. Dyck, R. L. Ochs, and R. M. Evans (1998)
PNAS 95, 4991-4996
 |  Abstract »  |  Full Text »  |  PDF »

Structure and Function in the Nucleus.

A. I. Lamond and W. C. Earnshaw (1998)
Science 280, 547-553
 |  Abstract »  |  Full Text »

Reduced Retinoic Acid-Sensitivities of Nuclear Receptor Corepressor Binding to PML- and PLZF-RARalpha Underlie Molecular Pathogenesis and Treatment of Acute Promyelocytic Leukemia.

F. Guidez, S. Ivins, J. Zhu, M. Soderstrom, S. Waxman, and A. Zelent (1998)
Blood 91, 2634-2642
 |  Abstract »  |  Full Text »  |  PDF »

Role of PML in Cell Growth and the Retinoic Acid Pathway.

Z. Gang Wang, L. Delva, M. Gaboli, R. Rivi, M. Giorgio, C. Cordon-Cardo, F. Grosveld, and P. Paolo Pandolfi (1998)
Science 279, 1547-1551
 |  Abstract »  |  Full Text »

An Arenavirus RING (Zinc-Binding) Protein Binds the Oncoprotein Promyelocyte Leukemia Protein (PML) and Relocates PML Nuclear Bodies to the Cytoplasm.

K. L. B. Borden, E. J. Campbell Dwyer, and M. S. Salvato (1998)
J. Virol. 72, 758-766
 |  Abstract »  |  Full Text »  |  PDF »

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

T. Sternsdorf, K. Jensen, and H. Will (1997)
J. Cell Biol. 139, 1621-1634
 |  Abstract »  |  Full Text »  |  PDF »

Characterization of Cryptic Rearrangements and Variant Translocations in Acute Promyelocytic Leukemia.

D. Grimwade, P. Gorman, E. Duprez, K. Howe, S. Langabeer, F. Oliver, H. Walker, D. Culligan, J. Waters, M. Pomfret, et al. (1997)
Blood 90, 4876-4885
 |  Abstract »  |  Full Text »  |  PDF »

Leukemia-associated retinoic acid receptor alpha  fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies.

M. H. M. Koken, A. Reid, F. Quignon, M. K. Chelbi-Alix, J. M. Davies, J. H. S. Kabarowski, J. Zhu, S. Dong, S.-J. Chen, Z. Chen, et al. (1997)
PNAS 94, 10255-10260
 |  Abstract »  |  Full Text »  |  PDF »

Characterization of the Retinoid Binding Properties of the Major Fusion Products Present in Acute Promyelocytic Leukemia Cells.

L. Benedetti, A. A. Levin, B. M. Scicchitano, F. Grignani, G. Allenby, D. Diverio, F. Lo Coco, G. Avvisati, M. Ruthardt, S. Adamo, et al. (1997)
Blood 90, 1175-1185
 |  Abstract »  |  Full Text »  |  PDF »

Transcription Factors, Normal Myeloid Development, and Leukemia.

D. G. Tenen, R. Hromas, J. D. Licht, and D.-E. Zhang (1997)
Blood 90, 489-519
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Use of Arsenic Trioxide (As2O3 ) in the Treatment of Acute Promyelocytic Leukemia (APL): I. As2O3 Exerts Dose-Dependent Dual Effects on APL Cells.

G.-Q. Chen, X.-G. Shi, W. Tang, S.-M. Xiong, J. Zhu, X. Cai, Z.-G. Han, J.-H. Ni, G.-Y. Shi, P.-M. Jia, et al. (1997)
Blood 89, 3345-3353
 |  Abstract »  |  Full Text »  |  PDF »

Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia.

J. Zhu, M. H. M. Koken, F. Quignon, M. K. Chelbi-Alix, L. Degos, Z. Y. Wang, Z. Chen, and H. de The (1997)
PNAS 94, 3978-3983
 |  Abstract »  |  Full Text »  |  PDF »

Altered Myeloid Development and Acute Leukemia in Transgenic Mice Expressing PML-RARalpha Under Control of Cathepsin G Regulatory Sequences.

J. L. Grisolano, R. L. Wesselschmidt, P. G. Pelicci, and T. J. Ley (1997)
Blood 89, 376-387
 |  Abstract »  |  Full Text »  |  PDF »

All-Trans-Retinoic Acid Pharmacology and Its Impact on the Treatment of Acute Promyelocytic Leukemia.

P. C. Adamson (1996)
Oncologist 1, 305-314
 |  Abstract »  |  Full Text »  |  PDF »

Analysis of the Growth and Transformation Suppressor Domains of Promyelocytic Leukemia Gene, PML.

X.-F. Le, P. Yang, and K.-S. Chang (1996)
J. Biol. Chem. 271, 130-135
 |  Abstract »  |  Full Text »  |  PDF »

Molecular Cloning, Structure, and Expression of Mouse Estrogen-responsive Finger Protein Efp.

A. Orimo, S. Inoue, K. Ikeda, S. Noji, and M. Muramatsu (1995)
J. Biol. Chem. 270, 24406-24413
 |  Abstract »  |  Full Text »  |  PDF »

Acute Promyelocytic Leukemia.

R. P. Warrell, H. de The, Z.-Y. Wang, and L. Degos (1993)
N. Engl. J. Med. 329, 177-189
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LYAR, a novel nucleolar protein with zinc finger DNA-binding motifs, is involved in cell growth regulation..

L Su, R J Hershberger, and I L Weissman (1993)
Genes & Dev. 7, 735-748
 |  Abstract »  |  PDF »

Xenopus nuclear factor 7 (xnf7) possesses an NLS that functions efficiently in both oocytes and embryos.

X Li and L. Etkin (1993)
J. Cell Sci. 105, 389-395
 |  Abstract »  |  PDF »

Cloning and Characterization of LUN, a Novel RING Finger Protein That Is Highly Expressed in Lung and Specifically Binds to a Palindromic Sequence.

D. Chu, N. Kakazu, M. J. Gorrin-Rivas, H.-P. Lu, M. Kawata, T. Abe, K. Ueda, and Y. Adachi (2001)
J. Biol. Chem. 276, 14004-14013
 |  Abstract »  |  Full Text »  |  PDF »

PRAM-1 Is a Novel Adaptor Protein Regulated by Retinoic Acid (RA) and Promyelocytic Leukemia (PML)-RA Receptor alpha in Acute Promyelocytic Leukemia Cells.

C. Moog-Lutz, E. J. Peterson, P. G. Lutz, S. Eliason, F. Cave-Riant, A. Singer, Y. Di Gioia, S. Dmowski, J. Kamens, Y. E. Cayre, et al. (2001)
J. Biol. Chem. 276, 22375-22381
 |  Abstract »  |  Full Text »  |  PDF »

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