1. Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.

    Nano Letters 14(10):5920 (2014) PMID 25204359 PMCID PMC4189620

    We report a dual illumination, single-molecule imaging strategy to dissect directly and in real-time the correlation between nanometer-scale domain motion of a DNA repair protein and its interaction with individual DNA substrates. The strategy was applied to XPD, an FeS cluster-containing DNA re...
  2. Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.

    Nano Letters 14(10):5920 (2014) PMID 25204359 PMCID PMC4189620

    We report a dual illumination, single-molecule imaging strategy to dissect directly and in real-time the correlation between nanometer-scale domain motion of a DNA repair protein and its interaction with individual DNA substrates. The strategy was applied to XPD, an FeS cluster-containing DNA re...
  3. Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.

    Nano Letters 14(10):5920 (2014) PMID 25204359 PMCID PMC4189620

    We report a dual illumination, single-molecule imaging strategy to dissect directly and in real-time the correlation between nanometer-scale domain motion of a DNA repair protein and its interaction with individual DNA substrates. The strategy was applied to XPD, an FeS cluster-containing DNA re...
  4. Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.

    DNA Repair 20:58 (2014) PMID 24560558

    XPD-like helicases constitute a prominent DNA helicase family critical for many aspects of genome maintenance. These enzymes share a unique structural feature, an auxiliary domain stabilized by an iron-sulphur (FeS) cluster, and a 5'-3' polarity of DNA translocation and duplex unwinding. Biochem...
  5. Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.

    DNA Repair 20:58 (2014) PMID 24560558

    XPD-like helicases constitute a prominent DNA helicase family critical for many aspects of genome maintenance. These enzymes share a unique structural feature, an auxiliary domain stabilized by an iron-sulphur (FeS) cluster, and a 5'-3' polarity of DNA translocation and duplex unwinding. Biochem...
  6. Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.

    DNA Repair 20:58 (2014) PMID 24560558 PMCID PMC4295835

    XPD-like helicases constitute a prominent DNA helicase family critical for many aspects of genome maintenance. These enzymes share a unique structural feature, an auxiliary domain stabilized by an iron-sulphur (FeS) cluster, and a 5'-3' polarity of DNA translocation and duplex unwinding. Biochem...
  7. Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.

    DNA Repair 20:58 (2014) PMID 24560558 PMCID PMC4295835

    XPD-like helicases constitute a prominent DNA helicase family critical for many aspects of genome maintenance. These enzymes share a unique structural feature, an auxiliary domain stabilized by an iron-sulphur (FeS) cluster, and a 5'-3' polarity of DNA translocation and duplex unwinding. Biochem...
  8. Two steps forward, one step back: determining XPD helicase mechanism by single-molecule fluorescence and high-resolution optical tweezers.

    DNA Repair 20:58 (2014) PMID 24560558

    XPD-like helicases constitute a prominent DNA helicase family critical for many aspects of genome maintenance. These enzymes share a unique structural feature, an auxiliary domain stabilized by an iron-sulphur (FeS) cluster, and a 5'-3' polarity of DNA translocation and duplex unwinding. Biochem...
  9. Fulfilling the dream of a perfect genome editing tool.

    PNAS 111(28):10029 (2014) PMID 24989506 PMCID PMC4104902

  10. Fulfilling the dream of a perfect genome editing tool.

    PNAS 111(28):10029 (2014) PMID 24989506 PMCID PMC4104902

  11. Fulfilling the dream of a perfect genome editing tool.

    PNAS 111(28):10029 (2014) PMID 24989506 PMCID PMC4104902

  12. Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.

    PNAS 111(3):E316 (2014) PMID 24395779 PMCID PMC3903253

    High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2-hMSH6 heterodimer is the first responder in postreplicative MMR and also pl...
  13. Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.

    PNAS 111(3):E316 (2014) PMID 24395779 PMCID PMC3903253

    High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2-hMSH6 heterodimer is the first responder in postreplicative MMR and also pl...
  14. Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.

    PNAS 111(3):E316 (2014) PMID 24395779 PMCID PMC3903253

    High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2-hMSH6 heterodimer is the first responder in postreplicative MMR and also pl...
  15. Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.

    PNAS 111(3):E316 (2014) PMID 24395779 PMCID PMC3903253

    High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2-hMSH6 heterodimer is the first responder in postreplicative MMR and also pl...
  16. Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate.

    PNAS 111(3):E316 (2014) PMID 24395779 PMCID PMC3903253

    High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2-hMSH6 heterodimer is the first responder in postreplicative MMR and also pl...
  17. Contributions of the RAD51 N-terminal domain to BRCA2-RAD51 interaction.

    Nucleic Acids Research 41(19):9020 (2013) PMID 23935068 PMCID PMC3799448

    RAD51 DNA strand exchange protein catalyzes the central step in homologous recombination, a cellular process fundamentally important for accurate repair of damaged chromosomes, preservation of the genetic integrity, restart of collapsed replication forks and telomere maintenance. BRCA2 protein, ...
  18. Survival of the replication checkpoint deficient cells requires MUS81-RAD52 function.

    PLoS Genetics 9(10):e1003910 (2013) PMID 24204313 PMCID PMC3814295

    In checkpoint-deficient cells, DNA double-strand breaks (DSBs) are produced during replication by the structure-specific endonuclease MUS81. The mechanism underlying MUS81-dependent cleavage, and the effect on chromosome integrity and viability of checkpoint deficient cells is only partly unders...
  19. Survival of the replication checkpoint deficient cells requires MUS81-RAD52 function.

    PLoS Genetics 9(10):e1003910 (2013) PMID 24204313 PMCID PMC3814295

    In checkpoint-deficient cells, DNA double-strand breaks (DSBs) are produced during replication by the structure-specific endonuclease MUS81. The mechanism underlying MUS81-dependent cleavage, and the effect on chromosome integrity and viability of checkpoint deficient cells is only partly unders...
  20. Survival of the replication checkpoint deficient cells requires MUS81-RAD52 function.

    PLoS Genetics 9(10):e1003910 (2013) PMID 24204313 PMCID PMC3814295

    In checkpoint-deficient cells, DNA double-strand breaks (DSBs) are produced during replication by the structure-specific endonuclease MUS81. The mechanism underlying MUS81-dependent cleavage, and the effect on chromosome integrity and viability of checkpoint deficient cells is only partly unders...