Alexander J Ruthenburg

Summary

Affiliation: The Rockefeller University
Country: USA

Publications

  1. ncbi request reprint Multivalent engagement of chromatin modifications by linked binding modules
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10065, USA
    Nat Rev Mol Cell Biol 8:983-94. 2007
  2. ncbi request reprint How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    Sean D Taverna
    Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA
    Nat Struct Mol Biol 14:1025-40. 2007
  3. pmc Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA
    Cell 145:692-706. 2011
  4. pmc Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis
    Thomas A Milne
    Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065, USA
    Mol Cell 38:853-63. 2010
  5. ncbi request reprint Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10021, USA
    Mol Cell 25:15-30. 2007
  6. ncbi request reprint Regulation of MLL1 H3K4 methyltransferase activity by its core components
    Yali Dou
    Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021, USA
    Nat Struct Mol Biol 13:713-9. 2006
  7. ncbi request reprint A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias
    Alexander J Ruthenburg
    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA
    J Biol Chem 280:26177-84. 2005
  8. ncbi request reprint Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase
    Hua Wei
    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA
    J Biol Chem 280:37041-7. 2005
  9. ncbi request reprint Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
    Alexander J Ruthenburg
    Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA
    Nat Struct Mol Biol 13:704-12. 2006

Collaborators

Detail Information

Publications9

  1. ncbi request reprint Multivalent engagement of chromatin modifications by linked binding modules
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10065, USA
    Nat Rev Mol Cell Biol 8:983-94. 2007
    ..We propose that multivalent interactions on a single histone tail and beyond may have a significant, if not dominant, role in chromatin transactions...
  2. ncbi request reprint How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    Sean D Taverna
    Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10021, USA
    Nat Struct Mol Biol 14:1025-40. 2007
    ..Changes in these interactions may have far-reaching implications for human biology and disease, notably cancer...
  3. pmc Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, 1230 York Avenue, New York, NY, 10065, USA
    Cell 145:692-706. 2011
    ..Together, our data call attention to nucleosomal patterning of covalent marks in dictating critical chromatin associations...
  4. pmc Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis
    Thomas A Milne
    Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY 10065, USA
    Mol Cell 38:853-63. 2010
    ..Since wild-type MLL1 and oncogenic MLL1 fusion proteins have overlapping yet distinct recruitment mechanisms, this creates a window of opportunity that could be exploited for the development of targeted therapies...
  5. ncbi request reprint Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
    Alexander J Ruthenburg
    Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10021, USA
    Mol Cell 25:15-30. 2007
    ..Finally, we hypothesize how the unique properties of the polyvalent chromatin fiber and associated effectors may amplify small differences in methyl-lysine recognition, simultaneously allowing for a dynamic chromatin architecture...
  6. ncbi request reprint Regulation of MLL1 H3K4 methyltransferase activity by its core components
    Yali Dou
    Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021, USA
    Nat Struct Mol Biol 13:713-9. 2006
    ..Mechanistic insights gained from this study can be generalized to the whole family of SET1-like histone methyltransferases in mammals...
  7. ncbi request reprint A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias
    Alexander J Ruthenburg
    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA
    J Biol Chem 280:26177-84. 2005
    ..We propose a model wherein the right-handed ((+) solenoidal) wrapping of DNA around the E. coli GyrA-CTD enforces unidirectional (-) DNA supercoiling...
  8. ncbi request reprint Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase
    Hua Wei
    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA
    J Biol Chem 280:37041-7. 2005
    ..Comparison of these structures revealed rigid-body movement of the structural modules within the ATPase domain, suggestive of the motions of a molecular gate...
  9. ncbi request reprint Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
    Alexander J Ruthenburg
    Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA
    Nat Struct Mol Biol 13:704-12. 2006
    ..Contrary to predictions, the structures reveal that WDR5 does not read out the methylation state of K4 directly, but instead serves to present the K4 side chain for further methylation by SET1-family complexes...