Sarah C. Roemer, Ph.D.
Affiliations: | 2005 | University of Colorado Anschutz Medical Campus, Denver, Aurora, CO |
Area:
Molecular BiologyGoogle:
"Sarah Roemer"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Dean P. Edwards | grad student | 2005 | University of Colorado, Denver | |
| (Structural and functional analysis of progesterone receptor-DNA interaction.) | ||||
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| Liu WH, Roemer SC, Zhou Y, et al. (2016) The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones. Elife. 5 |
| Wysoczynski CL, Roemer SC, Dostal V, et al. (2013) Reversed-phase ion-pair liquid chromatography method for purification of duplex DNA with single base pair resolution. Nucleic Acids Research. 41: e194 |
| Liu WH, Roemer SC, Port AM, et al. (2013) Thermodynamic insights into histone transfer among chaperones Epigenetics & Chromatin. 6 |
| Liu WH, Roemer SC, Port AM, et al. (2012) 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 |
| Hill KK, Roemer SC, Churchill ME, et al. (2012) Structural and functional analysis of domains of the progesterone receptor. Molecular and Cellular Endocrinology. 348: 418-29 |
| Hill KK, Roemer SC, Jones DN, et al. (2009) 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 |
| Roemer SC, Adelman J, Churchill ME, et al. (2008) Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding. Nucleic Acids Research. 36: 3655-66 |
| Roemer SC, Donham DC, Sherman L, et al. (2006) 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 |
| Melvin VS, Roemer SC, Churchill ME, et al. (2002) 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 |