Year |
Citation |
Score |
2012 |
Bittencourt D, Wu DY, Jeong KW, Gerke DS, Herviou L, Ianculescu I, Chodankar R, Siegmund KD, Stallcup MR. G9a functions as a molecular scaffold for assembly of transcriptional coactivators on a subset of glucocorticoid receptor target genes. Proceedings of the National Academy of Sciences of the United States of America. 109: 19673-8. PMID 23151507 DOI: 10.1073/Pnas.1211803109 |
0.563 |
|
2012 |
Ianculescu I, Wu DY, Siegmund KD, Stallcup MR. Selective roles for cAMP response element-binding protein binding protein and p300 protein as coregulators for androgen-regulated gene expression in advanced prostate cancer cells. The Journal of Biological Chemistry. 287: 4000-13. PMID 22174411 DOI: 10.1074/Jbc.M111.300194 |
0.623 |
|
2012 |
Ianculescu I, Wu DY, Siegmund KD, Stallcup MR. Selective roles for cAMP response element-binding protein binding protein and p300 protein as coregulators for androgen-regulated gene expression in advanced prostate cancer cells (Journal of Biological Chemistry (2012), 287 (4000-4013)) Journal of Biological Chemistry. 287: 35985. DOI: 10.1074/jbc.A111.300194 |
0.58 |
|
2011 |
Ou CY, LaBonte MJ, Manegold PC, So AYL, Ianculescu I, Gerke DS, Yamamoto KR, Ladner RD, Kahn M, Kim JH, Stallcup MR. A coactivator role of CARM1 in the dysregulation of β-catenin activity in colorectal cancer cell growth and gene expression Molecular Cancer Research. 9: 660-670. PMID 21478268 DOI: 10.1158/1541-7786.Mcr-10-0223 |
0.566 |
|
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 |
0.559 |
|
2004 |
Shan L, Vincent J, Brunzelle JS, Dussault I, Lin M, Ianculescu I, Sherman MA, Forman BM, Fernandez EJ. Structure of the murine constitutive androstane receptor complexed to androstenol: a molecular basis for inverse agonism. Molecular Cell. 16: 907-17. PMID 15610734 DOI: 10.1016/J.Molcel.2004.11.037 |
0.351 |
|
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