about
Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactionsMultivalent engagement of chromatin modifications by linked binding modulesMultiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesisHistone H3 recognition and presentation by the WDR5 module of the MLL1 complexRecombinant antibodies to histone post-translational modificationsTraceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks.Calibrating ChIP-Seq with Nucleosomal Internal Standards to Measure Histone Modification Density Genome Wide.Chromatin-enriched lncRNAs can act as cell-type specific activators of proximal gene transcription.Does activation of the anti proton, rather than concertedness, determine the stereochemistry of base-catalyzed 1,2-elimination reactions? Anti stereospecificity in E1cB eliminations of β-3-trifluoromethylphenoxy esters, thioesters, and ketones.Quantitative and Structural Assessment of Histone Methyllysine Analogue Engagement by Cognate Binding Proteins Reveals Affinity Decrements Relative to Those of Native Counterparts.Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.Transcription-factor-dependent enhancer transcription defines a gene regulatory network for cardiac rhythm.A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias.Facile target validation in an animal model with intracellularly expressed monobodiesWDR76 promotes MLL-rearranged leukemia via selective recognition of 5-hydroxymethylcytosine in DNAThe United States of histone ubiquitylation and methylationValidation of histone-binding partners by peptide pull-downs and isothermal titration calorimetryChromatin-enriched RNAs mark active and repressive cis-regulation: An analysis of nuclear RNA-seqNative internally calibrated chromatin immunoprecipitation for quantitative studies of histone post-translational modifications
P50
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P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-2709-4564
@en
name
Alexander J Ruthenburg
@ast
Alexander J Ruthenburg
@en
Alexander J Ruthenburg
@nl
type
label
Alexander J Ruthenburg
@ast
Alexander J Ruthenburg
@en
Alexander J Ruthenburg
@nl
prefLabel
Alexander J Ruthenburg
@ast
Alexander J Ruthenburg
@en
Alexander J Ruthenburg
@nl
P106
P21
P31
P496
0000-0003-2709-4564