1. Ligand-dependent enhancer activation regulated by topoisomerase-I activity.

    Cell 160(3):367 (2015) PMID 25619691

    The discovery that enhancers are regulated transcription units, encoding eRNAs, has raised new questions about the mechanisms of their activation. Here, we report an unexpected molecular mechanism that underlies ligand-dependent enhancer activation, based on DNA nicking to relieve torsional stre...
  2. Ligand-dependent enhancer activation regulated by topoisomerase-I activity.

    Cell 160(3):367 (2015) PMID 25619691

    The discovery that enhancers are regulated transcription units, encoding eRNAs, has raised new questions about the mechanisms of their activation. Here, we report an unexpected molecular mechanism that underlies ligand-dependent enhancer activation, based on DNA nicking to relieve torsional stre...
  3. Ligand-Dependent Enhancer Activation Regulated by Topoisomerase-I Activity

    Cell 160(3):367 (2015) PMID 25619691

    The discovery that enhancers are regulated transcription units, encoding eRNAs, has raised new questions about the mechanisms of their activation. Here, we report an unexpected molecular mechanism that underlies ligand-dependent enhancer activation, based on DNA nicking to relieve tors...
  4. Ligand-dependent enhancer activation regulated by topoisomerase-I activity.

    Cell 160(3):367 (2015) PMID 25619691

    The discovery that enhancers are regulated transcription units, encoding eRNAs, has raised new questions about the mechanisms of their activation. Here, we report an unexpected molecular mechanism that underlies ligand-dependent enhancer activation, based on DNA nicking to relieve torsional stre...
  5. Ligand-dependent Enhancer Activation Regulated by Topoisomerase-I Activity

    Cell (2014)

    The discovery that enhancers are regulated transcription units, encoding eRNAs, has raised new questions about the mechanisms of their activation. Here, we report an unexpected molecular mechanism that underlies ligand-dependent enhancer activation, based on DNA nicking to relieve tors...
  6. SOX2 and CHD7 cooperatively regulate human disease genes.

    Nature Genetics 43(6):505 (2011) PMID 21614087

  7. SOX2 and CHD7 cooperatively regulate human disease genes.

    Nature Genetics 43(6):505 (2011) PMID 21614087

  8. Cell cycle checkpoint defects contribute to genomic instability in PTEN deficient cells independent of DNA DSB repair.

    Cell Cycle 8(14):2198 (2009) PMID 19502790

    Chromosomes in PTEN deficient cells display both numerical as well as structural alterations including regional amplification. We found that PTEN deficient cells displayed a normal DNA damage response (DDR) as evidenced by the ionizing radiation (IR)-induced phosphorylation of Ataxia Telangiecta...
  9. Cell cycle checkpoint defects contribute to genomic instability in PTEN deficient cells independent of DNA DSB repair.

    Cell Cycle 8(14):2198 (2009) PMID 19502790

    Chromosomes in PTEN deficient cells display both numerical as well as structural alterations including regional amplification. We found that PTEN deficient cells displayed a normal DNA damage response (DDR) as evidenced by the ionizing radiation (IR)-induced phosphorylation of Ataxia Telangiecta...
  10. A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation.

    Molecular Cell 27(4):609 (2007) PMID 17707232 PMCID PMC2709280

    Deciphering the epigenetic "code" remains a central issue in transcriptional regulation. Here, we report the identification of a JAMM/MPN(+) domain-containing histone H2A deubiquitinase (2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A) that has permitted delineation of a stra...
  11. A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation.

    Molecular Cell 27(4):609 (2007) PMID 17707232 PMCID PMC2709280

    Deciphering the epigenetic "code" remains a central issue in transcriptional regulation. Here, we report the identification of a JAMM/MPN(+) domain-containing histone H2A deubiquitinase (2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A) that has permitted delineation of a stra...
  12. A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation and H1 Dissociation in Transcriptional Regulation

    Molecular Cell 27(4):609 (2007)

    Deciphering the epigenetic “code” remains a central issue in transcriptional regulation. Here, we report the identification of a JAMM/MPN + domain-containing histone H 2A de ubiquitinase (2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A) that has permitt...
  13. A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation and H1 Dissociation in Transcriptional Regulation

    Molecular Cell 27(4):609 (2007)

    Deciphering the epigenetic “code” remains a central issue in transcriptional regulation. Here, we report the identification of a JAMM/MPN + domain-containing histone H 2A de ubiquitinase (2A-DUB, or KIAA1915/MYSM1) specific for monoubiquitinated H2A (uH2A) that has permitt...
  14. Analysis of PTEN mutation in non-familial pheochromocytoma.

    Annals of the New York Academy of Sciences 1073:317 (2006) PMID 17102102

    PTEN, a tumor suppressor gene, is frequently mutated in a variety of human tumors. In mice, monoallelic inactivation of this gene predisposes animals to neoplasia of multiple organs. Interestingly, Pten heterozygous mice develop bilateral hyperplasia of the adrenal medulla. In this report we dem...
  15. Analysis of PTEN mutation in non-familial pheochromocytoma.

    Annals of the New York Academy of Sciences 1073:317 (2006) PMID 17102102

    PTEN, a tumor suppressor gene, is frequently mutated in a variety of human tumors. In mice, monoallelic inactivation of this gene predisposes animals to neoplasia of multiple organs. Interestingly, Pten heterozygous mice develop bilateral hyperplasia of the adrenal medulla. In this report we dem...
  16. PTEN loss inhibits CHK1 to cause double stranded-DNA breaks in cells.

    Cell Cycle 4(7):927 (2005) PMID 15970699

    CHK1 is an essential kinase involved in the regulation of the cell cycle progression and preservation of genomic integrity. Inhibition of CHK1 leads to the accumulation of double-stranded DNA breaks. Loss of PTEN impairs CHK1-mediated checkpoint activation due to cytoplasmic sequestration of ubi...
  17. PTEN loss inhibits CHK1 to cause double stranded-DNA breaks in cells.

    Cell Cycle 4(7):927 (2005) PMID 15970699

    CHK1 is an essential kinase involved in the regulation of the cell cycle progression and preservation of genomic integrity. Inhibition of CHK1 leads to the accumulation of double-stranded DNA breaks. Loss of PTEN impairs CHK1-mediated checkpoint activation due to cytoplasmic sequestration of ubi...
  18. Lack of PTEN sequesters CHK1 and initiates genetic instability.

    Cancer Cell 7(2):193 (2005) PMID 15710331

    Pten-/- cells display a partially defective checkpoint in response to ionizing radiation (IR). The checkpoint defect was traced to the ability of AKT to phosphorylate CHK1 at serine 280, since a nonphosphorylated mutant of CHK1 (S280A) complemented the checkpoint defect and restored CDC25A degra...
  19. Lack of PTEN sequesters CHK1 and initiates genetic instability

    Cancer Cell 7(2):193 (2005) PMID 15710331

    Pten −/− cells display a partially defective checkpoint in response to ionizing radiation (IR). The checkpoint defect was traced to the ability of AKT to phosphorylate CHK1 at serine 280, since a nonphosphorylated mutant of CHK1 (S280A) complemented the checkpoint defect and re...
  20. Lack of PTEN sequesters CHK1 and initiates genetic instability

    Cancer Cell 7(2):193 (2005) PMID 15710331

    Pten −/− cells display a partially defective checkpoint in response to ionizing radiation (IR). The checkpoint defect was traced to the ability of AKT to phosphorylate CHK1 at serine 280, since a nonphosphorylated mutant of CHK1 (S280A) complemented the checkpoint defect and re...