Ed Luk

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. ncbi request reprint Chz1, a nuclear chaperone for histone H2AZ
    Ed Luk
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Mol Cell 25:357-68. 2007
  2. doi request reprint Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome
    Ed Luk
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 143:725-36. 2010
  3. pmc Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement
    Anand Ranjan
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA Electronic address
    Cell 154:1232-45. 2013
  4. pmc N terminus of Swr1 binds to histone H2AZ and provides a platform for subunit assembly in the chromatin remodeling complex
    Wei Hua Wu
    Laboratory of Biochemistry and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 284:6200-7. 2009
  5. pmc NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B
    Zheng Zhou
    Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 15:868-9. 2008

Collaborators

  • Yawen Bai
  • Anand Ranjan
  • Carl Wu
  • Gaku Mizuguchi
  • Debbie Wei
  • Wei Hua Wu
  • Zheng Zhou
  • Peter C FitzGerald
  • Christopher L Woodcock
  • Feng Wang
  • Yingzi Huang
  • Hua Xiao
  • Andreas Ladurner
  • Chwen Huey Wu
  • Lewis E Kay
  • D Flemming Hansen
  • DARON I FREEDBERG
  • Hidenori Kato
  • Hanqiao Feng

Detail Information

Publications5

  1. ncbi request reprint Chz1, a nuclear chaperone for histone H2AZ
    Ed Luk
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Mol Cell 25:357-68. 2007
    ..The presence of this motif in other metazoan proteins suggests that H2AZ-specific chaperones may be widely conserved...
  2. doi request reprint Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome
    Ed Luk
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Cell 143:725-36. 2010
    ..Z-H2B. These results suggest that the combination of H2A-containing nucleosome and free H2A.Z-H2B dimer acting as both effector and substrate for SWR1 governs the specificity and outcome of the replacement reaction...
  3. pmc Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement
    Anand Ranjan
    Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA Electronic address
    Cell 154:1232-45. 2013
    ....
  4. pmc N terminus of Swr1 binds to histone H2AZ and provides a platform for subunit assembly in the chromatin remodeling complex
    Wei Hua Wu
    Laboratory of Biochemistry and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 284:6200-7. 2009
    ..These findings suggest that one SWR1 enzyme might be capable of binding two H2AZ-H2B dimers, and provide further insight on the hierarchy and interdependency of molecular interactions within the SWR1 complex...
  5. pmc NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B
    Zheng Zhou
    Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nat Struct Mol Biol 15:868-9. 2008
    ..A molecular model that docks Chz1 onto the nucleosome has implications for its potential functions...