WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket

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WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M806900200
P3181OpenCitations bibliographic resource ID4841524
P932PMC publication ID2596411
P698PubMed publication ID18840606

P2093author name stringJi-Joon Song
Robert E Kingston
P2860cites workCrystal structure of the nucleosome core particle at 2.8 A resolutionQ22122355
Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expressionQ24297027
Structural basis for molecular recognition and presentation of histone H3 by WDR5Q24301311
Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5Q24314963
Structural basis of histone H4 recognition by p55Q27650473
WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate developmentQ29614526
Mechanisms of transcriptional memoryQ34271573
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complexQ34546055
Molecular recognition of histone H3 by the WD40 protein WDR5.Q34546063
Chromatin remodeling and cancer, Part I: Covalent histone modificationsQ34682092
P433issue50
P407language of work or nameEnglishQ1860
P921main subjectcell biologyQ7141
leukemiaQ29496
methylated histone bindingQ14911714
WD repeat domain 5Q21171851
binding pocketQ61659196
P304page(s)35258-64
P577publication date2008-12-12
P1433published inJournal of Biological ChemistryQ867727
P1476titleWDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket
P478volume283

Reverse relations

cites work (P2860)
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