Paul Prendergast

Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo.

D. Edwards, T. Yip, T. Hutchens, 1997, Molecular endocrinology.

Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody.

D. Edwards, P. Prendergast, N. Weigel, 1992, Molecular endocrinology.

High-Mobility Group Chromatin Proteins 1 and 2 Functionally Interact with Steroid Hormone Receptors To Enhance Their DNA Binding In Vitro and Transcriptional Activity in Mammalian Cells

D. Edwards, M. Bianchi, P. Prendergast, 1998, Molecular and Cellular Biology.

The high mobility group protein 1 enhances binding of the estrogen receptor DNA binding domain to the estrogen response element.

D. Edwards, L. Romine, L. E. Romine, 1998, Molecular endocrinology.

The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences

D. Edwards, M. Nissen, R. Reeves, 1994, Molecular and cellular biology.

Nuclear accessory factors enhance the binding of progesterone receptor to specific target DNA

D. Edwards, S. Oñate, P. Prendergast, 1994, The Journal of Steroid Biochemistry and Molecular Biology.

Facilitated Binding of Steroid Hormone Receptors to Target DNA by the Chromatin High-Mobility Group Protein-1: Protein Manipulation of DNA Structure

D. Edwards, P. Prendergast, Paul Prendergast, 1997 .

Direct binding of progesterone receptor to nonconsensus DNA sequences represses rat GnRH

D. Edwards, B. Jacobsen, J. Kepa, 1996, Molecular and Cellular Endocrinology.