Daniel Purcell, Ph.D. - Publications

Affiliations: 
2011 Genetic, Molecular, and Cell Biology University of Southern California, Los Angeles, CA, United States 
Area:
Biochemistry, Molecular Biology

6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2015 Purcell DJ, Chauhan S, Jimenez-Stinson D, Elliott KR, Tsewang TD, Lee YH, Marples B, Lee DY. Novel CARM1 Interacting Protein, DZIP3, is a Transcriptional Coactivator of Estrogen Receptor alpha. Molecular Endocrinology (Baltimore, Md.). me20151083. PMID 26505218 DOI: 10.1210/me.2015-1083  0.48
2012 Won Jeong K, Chodankar R, Purcell DJ, Bittencourt D, Stallcup MR. Gene-specific patterns of coregulator requirements by estrogen receptor-α in breast cancer cells. Molecular Endocrinology (Baltimore, Md.). 26: 955-66. PMID 22543272 DOI: 10.1210/me.2012-1066  0.56
2012 Purcell DJ, Khalid O, Ou CY, Little GH, Frenkel B, Baniwal SK, Stallcup MR. Recruitment of coregulator G9a by Runx2 for selective enhancement or suppression of transcription. Journal of Cellular Biochemistry. 113: 2406-14. PMID 22389001 DOI: 10.1002/jcb.24114  0.56
2011 Purcell DJ, Jeong KW, Bittencourt D, Gerke DS, Stallcup MR. A distinct mechanism for coactivator versus corepressor function by histone methyltransferase G9a in transcriptional regulation. The Journal of Biological Chemistry. 286: 41963-71. PMID 21984853 DOI: 10.1074/jbc.M111.298463  0.56
2008 Khalid O, Baniwal SK, Purcell DJ, Leclerc N, Gabet Y, Stallcup MR, Coetzee GA, Frenkel B. Modulation of Runx2 activity by estrogen receptor-alpha: implications for osteoporosis and breast cancer. Endocrinology. 149: 5984-95. PMID 18755791 DOI: 10.1210/en.2008-0680  0.56
2007 Lee DY, Ianculescu I, Purcell D, Zhang X, Cheng X, Stallcup MR. Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function. Molecular Endocrinology (Baltimore, Md.). 21: 1381-93. PMID 17426288 DOI: 10.1210/me.2006-0389  0.56
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