P. Prendergast

发表

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, S. Oñate, P. Prendergast, 1994 .

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.

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

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

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.

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.

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.

Progesterone receptor-induced bending of its target DNA: distinct effects of the A and B receptor forms.

D. Edwards, P. Prendergast, Z. Pan, 1996, Molecular endocrinology.

A 361 base pair region of the rat FSH-β promoter contains multiple progesterone receptor-binding sequences and confers progesterone responsiveness

D. Edwards, P. Prendergast, V. Mahesh, 1997, Molecular and Cellular Endocrinology.

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 .

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.

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.