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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

WD repeat domain 5

WDR5, WD-repeat protein-5
This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Papers using WDR5 antibodies
Identification of a PRMT5-dependent repressor complex linked to silencing of human fetal globin gene expression.
Lau Andy T. Y., In PLoS ONE, 2009
... Anti-WDR5, anti-H3K4me2, and anti-H3K27me3 antibodies were purchased from Abcam.
Papers on WDR5
Structural basis for WDR5 interaction (Win) motif recognition in human SET1 family histone methyltransferases.
Cosgrove et al., Syracuse, United States. In J Biol Chem, 2012
WDR5-Win motif interaction is important for the assembly of the MLL1 core complex in vivo.
Synergistic effect of SRY and its direct target, WDR5, on Sox9 expression.
Zhao et al., Nanjing, China. In Plos One, 2011
findings show that WDR5 is a direct target of SRY; the interaction of WDR5 and SRY activates Sox9 expression; results suggest that, in conjunction with SRY, WDR5 plays an important role in sex determination
X-linked mental retardation gene CUL4B targets ubiquitylation of H3K4 methyltransferase component WDR5 and regulates neuronal gene expression.
Xiong et al., Chapel Hill, United States. In Mol Cell, 2011
WDR5 as a critical substrate of CUL4B in regulating neuronal gene expression.
Structural and biochemical insights into MLL1 core complex assembly.
Couture et al., Ottawa, Canada. In Structure, 2011
crystal structure of WDR5 in ternary complex with RbBP5 and MLL1
The effect of Asp-His-Ser/Thr-Trp tetrad on the thermostability of WD40-repeat proteins.
Wu et al., Shenzhen, China. In Biochemistry, 2010
the change of folding free energy by mutations mainly corresponds to the deletion of hydrogen bonds.
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