“High-density genetic map of the BRCA1 region of chromosome 17q12-q21”. Genomics17 (3): 618–23. (September 1993). doi:10.1006/geno.1993.1381. PMID8244378.
“Acute promyelocytic leukemia: new issues on pathogenesis and treatment response”. The International Journal of Biochemistry & Cell Biology39 (6): 1063–70. (2007). doi:10.1016/j.biocel.2007.01.028. PMID17468032.
“Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells”. The Journal of Biological Chemistry273 (27): 16985–92. (July 1998). doi:10.1074/jbc.273.27.16985. PMID9642262.
“Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock”. Cell105 (7): 877–89. (June 2001). doi:10.1016/S0092-8674(01)00401-9. PMID11439184.
“Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II”. The Journal of Biological Chemistry278 (8): 6355–62. (February 2003). doi:10.1074/jbc.M210697200. PMID12482873.
“Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2”. Molecular Endocrinology15 (2): 241–54. (February 2001). doi:10.1210/mend.15.2.0595. PMID11158331.
“A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo”. The Journal of Biological Chemistry274 (48): 34283–93. (November 1999). doi:10.1074/jbc.274.48.34283. PMID10567404.
“Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein”. The Journal of Biological Chemistry274 (22): 15901–7. (May 1999). doi:10.1074/jbc.274.22.15901. PMID10336495.
“Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia”. Blood91 (8): 2634–42. (April 1998). doi:10.1182/blood.V91.8.2634.2634_2634_2642. PMID9531570.
“Interactions of STAT5b-RARalpha, a novel acute promyelocytic leukemia fusion protein, with retinoic acid receptor and STAT3 signaling pathways”. Blood99 (8): 2637–46. (April 2002). doi:10.1182/blood.V99.8.2637. PMID11929748.
“Suppressive effect of receptor-interacting protein 140 on coregulator binding to retinoic acid receptor complexes, histone-modifying enzyme activity, and gene activation”. The Journal of Biological Chemistry279 (1): 319–25. (January 2004). doi:10.1074/jbc.M307621200. PMID14581481.
“Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity”. Biochemistry42 (4): 971–9. (February 2003). doi:10.1021/bi020497k. PMID12549917.
“Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner)”. Molecular Endocrinology12 (10): 1551–7. (October 1998). doi:10.1210/mend.12.10.0184. PMID9773978.
“A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1”. Genes & Development9 (7): 769–82. (April 1995). doi:10.1101/gad.9.7.769. PMID7705655.
“A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins”. Nature Genetics23 (3): 287–95. (November 1999). doi:10.1038/15463. PMID10610177.
“High-density genetic map of the BRCA1 region of chromosome 17q12-q21”. Genomics17 (3): 618–23. (September 1993). doi:10.1006/geno.1993.1381. PMID8244378.
“Acute promyelocytic leukemia: new issues on pathogenesis and treatment response”. The International Journal of Biochemistry & Cell Biology39 (6): 1063–70. (2007). doi:10.1016/j.biocel.2007.01.028. PMID17468032.
“Interaction of BAG-1 with retinoic acid receptor and its inhibition of retinoic acid-induced apoptosis in cancer cells”. The Journal of Biological Chemistry273 (27): 16985–92. (July 1998). doi:10.1074/jbc.273.27.16985. PMID9642262.
“Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock”. Cell105 (7): 877–89. (June 2001). doi:10.1016/S0092-8674(01)00401-9. PMID11439184.
“Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II”. The Journal of Biological Chemistry278 (8): 6355–62. (February 2003). doi:10.1074/jbc.M210697200. PMID12482873.
“Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2”. Molecular Endocrinology15 (2): 241–54. (February 2001). doi:10.1210/mend.15.2.0595. PMID11158331.
“A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo”. The Journal of Biological Chemistry274 (48): 34283–93. (November 1999). doi:10.1074/jbc.274.48.34283. PMID10567404.
“Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein”. The Journal of Biological Chemistry274 (22): 15901–7. (May 1999). doi:10.1074/jbc.274.22.15901. PMID10336495.
“Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia”. Blood91 (8): 2634–42. (April 1998). doi:10.1182/blood.V91.8.2634.2634_2634_2642. PMID9531570.
“Interactions of STAT5b-RARalpha, a novel acute promyelocytic leukemia fusion protein, with retinoic acid receptor and STAT3 signaling pathways”. Blood99 (8): 2637–46. (April 2002). doi:10.1182/blood.V99.8.2637. PMID11929748.
“Suppressive effect of receptor-interacting protein 140 on coregulator binding to retinoic acid receptor complexes, histone-modifying enzyme activity, and gene activation”. The Journal of Biological Chemistry279 (1): 319–25. (January 2004). doi:10.1074/jbc.M307621200. PMID14581481.
“Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity”. Biochemistry42 (4): 971–9. (February 2003). doi:10.1021/bi020497k. PMID12549917.
“Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner)”. Molecular Endocrinology12 (10): 1551–7. (October 1998). doi:10.1210/mend.12.10.0184. PMID9773978.
“A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1”. Genes & Development9 (7): 769–82. (April 1995). doi:10.1101/gad.9.7.769. PMID7705655.
“A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins”. Nature Genetics23 (3): 287–95. (November 1999). doi:10.1038/15463. PMID10610177.