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Aiping Dong
Structural Genomics Consortium
329Publications
31H-index
3,222Citations
Publications 329
Newest
#1Yanli Liu (SGC: Structural Genomics Consortium)H-Index: 3
#2Su Qin (SGC: Structural Genomics Consortium)H-Index: 11
Last.Jinrong Min (U of T: University of Toronto)H-Index: 37
view all 11 authors...
MLL3 and MLL4 are two closely related members of the SET1/MLL family of histone H3K4 methyltransferases and are responsible for monomethylating histone H3K4 on enhancers, which are essential in regulating cell-type-specific gene expression. Mutations of MLL3 or MLL4 have been reported in different types of cancer. Recently, the PHD domains of MLL3/4 have been reported to recruit the MLL3/4 complexes to their target genes by binding to histone H4 during the NT2/D1 stem cell differentiation. Here ...
2 CitationsSource
#1Xiao-Chuan Cai (MSK: Memorial Sloan Kettering Cancer Center)
#2Tuo Zhang (Cornell University)H-Index: 25
Last.Minkui Luo (MSK: Memorial Sloan Kettering Cancer Center)H-Index: 24
view all 35 authors...
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#1L. HalabelianH-Index: 2
Last.Cheryl H. ArrowsmithH-Index: 78
view all 7 authors...
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#2Aiping DongH-Index: 31
Last.Cheryl H. ArrowsmithH-Index: 78
view all 7 authors...
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#1Alexandria P. Taylor (Pfizer)H-Index: 5
Last.Dafydd R. Owen (Pfizer)H-Index: 14
view all 21 authors...
The first chemical probe to primarily occupy the co-factor binding site of a Su(var)3−9, enhancer of a zeste, trithorax (SET) domain containing protein lysine methyltransferase (PKMT) is reported. Protein methyltransferases require S-adenosylmethionine (SAM) as a co-factor (methyl donor) for enzymatic activity. However, SAM itself represents a poor medicinal chemistry starting point for a selective, cell-active inhibitor given its extreme physicochemical properties and its role in multiple cellu...
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#1P. Mader (SGC: Structural Genomics Consortium)H-Index: 1
#2Rodrigo Mendoza-Sanchez (U of T: University of Toronto)H-Index: 3
Last.Cheryl H. Arrowsmith (Princess Margaret Cancer Centre)H-Index: 78
view all 23 authors...
Abstract SET domain bifurcated protein 1 (SETDB1) is a human histone-lysine methyltransferase which is amplified in human cancers and was shown to be crucial in the growth of non-small and small cell lung carcinoma. In addition to its catalytic domain, SETDB1 harbors a unique tandem tudor domain which recognizes histone sequences containing both methylated and acetylated lysines, and likely contributes to its localization on chromatin. Using X-ray crystallography and NMR spectroscopy fragment sc...
1 CitationsSource
#1L. HalabelianH-Index: 2
Last.Cheryl H. ArrowsmithH-Index: 78
view all 7 authors...
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#1L. HalabelianH-Index: 2
Last.Cheryl H. ArrowsmithH-Index: 78
view all 9 authors...
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#1L. HalabelianH-Index: 2
#2Aiping DongH-Index: 31
Last.Peter BrownH-Index: 42
view all 10 authors...
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