BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Slaughter MJ, Shanle EK, Khan A, et al. (2021) HDAC inhibition results in widespread alteration of the histone acetylation landscape and BRD4 targeting to gene bodies. Cell Reports. 34: 108638 |
| Slaughter MJ, Shanle EK, McFadden AW, et al. (2018) Polybromo-1 (PBRM1) bromodomains variably influence nucleosome interactions and cellular function. The Journal of Biological Chemistry |
| Shanle EK, Shinsky SA, Bridgers JB, et al. (2017) Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions. Epigenetics & Chromatin. 10: 12 |
| Savitsky P, Krojer T, Fujisawa T, et al. (2016) Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin. Cell Reports. 17: 2724-2737 |
| Andrews FH, Shinsky SA, Shanle EK, et al. (2016) The Taf14 YEATS domain is a reader of histone crotonylation. Nature Chemical Biology |
| Andrews FH, Shanle EK, Strahl BD, et al. (2016) The essential role of acetyllysine binding by the YEATS domain in transcriptional regulation. Transcription. 7: 14-20 |
| Shanle EK, Tsun IK, Strahl BD. (2016) A course-based undergraduate research experience investigating p300 bromodomain mutations. Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology. 44: 68-74 |
| Shanle EK, Andrews FH, Meriesh H, et al. (2015) Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response. Genes & Development. 29: 1795-800 |
| Rothbart SB, Dickson BM, Raab JR, et al. (2015) An Interactive Database for the Assessment of Histone Antibody Specificity. Molecular Cell. 59: 502-11 |
| Dumesic PA, Homer CM, Moresco JJ, et al. (2015) Product binding enforces the genomic specificity of a yeast polycomb repressive complex. Cell. 160: 204-18 |