Research Topics
| Alexander J RuthenburgSummaryAffiliation: The Rockefeller University Country: USA Publications
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Detail Information
Publications
Multivalent engagement of chromatin modifications by linked binding modulesAlexander 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...- How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickersSean 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... 
Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactionsAlexander 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...- Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesisThomas 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... - Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic markAlexander 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... - Regulation of MLL1 H3K4 methyltransferase activity by its core componentsYali 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... - A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling biasAlexander 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... - Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomeraseHua 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... - Histone H3 recognition and presentation by the WDR5 module of the MLL1 complexAlexander 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...