Browsing by Author "Paulk, Joshiawa"
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Modulators of Cellular and Biochemical PRC2 Activity
Paulk, Joshiawa Lanair James (2014-10-21)EZH2 is a SET domain-containing methyltransferase and the catalytic component of the multimeric Polycomb- group (PcG) protein complex, PRC2. When in complex with other PRC2 members (EED, SUZ12, AEBP2, and RBBP4), EZH2 ... -
An oncogenic Ezh2 mutation cooperates with particular genetic alterations to induce tumors in mice and redistributes H3K27 trimethylation throughout the genome
Souroullas, George P.; Jeck, William R.; Parker, Joel S.; Simon, Jeremy M.; Liu, Jie-Yu; Paulk, Joshiawa; Xiong, Jessie; Clark, Kelly S.; Fedoriw, Yuri; Qi, Jun; Burd, Christin E.; Bradner, James E.; Sharpless, Norman E. (2016)B-cell lymphoma and melanoma harbor recurrent mutations in the gene encoding the EZH2 histone methyltransferase, but the carcinogenic role of these mutations is unclear. Here we describe a mouse model in which the most ... -
A Small-Molecule Probe of the Histone Methyltransferase G9a Induces Cellular Senescence in Pancreatic Adenocarcinoma
Yuan, Yuan; Wang, Qiu; Paulk, Joshiawa Lanair James; Kubicek, Stefan; Kemp, Melissa M.; Adams, Drew J.; Shamji, Alykhan Farid; Wagner, Bridget K.; Schreiber, Stuart L. (American Chemical Society, 2012)Post-translational modifications of histones alter chromatin structure and play key roles in gene expression and specification of cell states. Small molecules that target chromatin-modifying enzymes selectively are useful ... -
An Unbiased Approach To Identify Endogenous Substrates of “Histone” Deacetylase 8
Olson, David E.; Udeshi, Namrata D.; Wolfson, Noah A.; Pitcairn, Carol Ann; Sullivan, Eric D.; Jaffe, Jacob D.; Svinkina, Tanya; Natoli, Ted; Lu, Xiaodong; Paulk, Joshiawa; McCarren, Patrick; Wagner, Florence F.; Barker, Doug; Howe, Eleanor; Lazzaro, Fanny; Gale, Jennifer P.; Zhang, Yan-Ling; Subramanian, Aravind; Fierke, Carol A.; Carr, Steven A.; Holson, Edward B. (American Chemical Society, 2014)Despite being extensively characterized structurally and biochemically, the functional role of histone deacetylase 8 (HDAC8) has remained largely obscure due in part to a lack of known cellular substrates. Herein, we ...