Year |
Citation |
Score |
2016 |
Liu WH, Roemer SC, Zhou Y, Shen ZJ, Dennehey BK, Balsbaugh JL, Liddle JC, Nemkov T, Ahn NG, Hansen KC, Tyler JK, Churchill ME. The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones. Elife. 5. PMID 27690308 DOI: 10.7554/Elife.18023 |
0.402 |
|
2013 |
Wysoczynski CL, Roemer SC, Dostal V, Barkley RM, Churchill ME, Malarkey CS. Reversed-phase ion-pair liquid chromatography method for purification of duplex DNA with single base pair resolution. Nucleic Acids Research. 41: e194. PMID 24013567 DOI: 10.1093/Nar/Gkt815 |
0.449 |
|
2013 |
Liu WH, Roemer SC, Port AM, Churchill ME. Thermodynamic insights into histone transfer among chaperones Epigenetics & Chromatin. 6. DOI: 10.1186/1756-8935-6-S1-P111 |
0.406 |
|
2012 |
Liu WH, Roemer SC, Port AM, Churchill ME. CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA. Nucleic Acids Research. 40: 11229-39. PMID 23034810 DOI: 10.1093/Nar/Gks906 |
0.366 |
|
2012 |
Hill KK, Roemer SC, Churchill ME, Edwards DP. Structural and functional analysis of domains of the progesterone receptor. Molecular and Cellular Endocrinology. 348: 418-29. PMID 21803119 DOI: 10.1016/J.Mce.2011.07.017 |
0.651 |
|
2009 |
Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP. A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. The Journal of Biological Chemistry. 284: 24415-24. PMID 19553667 DOI: 10.1074/Jbc.M109.003244 |
0.637 |
|
2008 |
Roemer SC, Adelman J, Churchill ME, Edwards DP. Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding. Nucleic Acids Research. 36: 3655-66. PMID 18474528 DOI: 10.1093/Nar/Gkn249 |
0.695 |
|
2006 |
Roemer SC, Donham DC, Sherman L, Pon VH, Edwards DP, Churchill ME. Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements. Molecular Endocrinology (Baltimore, Md.). 20: 3042-52. PMID 16931575 DOI: 10.1210/Me.2005-0511 |
0.721 |
|
2002 |
Melvin VS, Roemer SC, Churchill ME, Edwards DP. The C-terminal extension (CTE) of the nuclear hormone receptor DNA binding domain determines interactions and functional response to the HMGB-1/-2 co-regulatory proteins. The Journal of Biological Chemistry. 277: 25115-24. PMID 12006575 DOI: 10.1074/Jbc.M110400200 |
0.713 |
|
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