Neil McKenna, Ph.D.
Department of Molecular and Cellular Biology
Ph.D.: National University of Ireland, Galway, Ireland
Postdoctoral training: Baylor College of Medicine, Houston
Steroid Receptor, Coactivator, Corepressor, Bioinformatics, nuclear receptor, coregulator, database
Advances in the field of nuclear receptor signaling rely both on the generation of novel data and, to an increasing extent in the post-genomic era, on the effective management and analysis of existing information. Our group has developed one of the most comprehensive web-based research resources in the nuclear receptor field, www.nursa.org. We have a close working relationship with BCM’s Bioinformatics Research Resource, led by Dr. David Steffen. Current projects include:
1. Nuclear Receptor Signaling A PubMed-indexed, Open Access journal which publishes reviews and methods in the nuclear receptor and coregulator field. The software for NRS has been developed entirely by our group.
2. Microarray analysis. The nuclear receptor field has produced large amounts of microarray data that has not been organized into a single central database to enable researchers to fully leverage the data available in these studies. We are gathering public microarray data in the field and exploring ways in which data from different microarray experiments can be meaningfully compared.
3. The coregulator proteome. Nuclear receptor coregulators form large complexes in cells, the composition of which may hold clues to their function. Along with Dr Rainer Lanz and Dr Jun Qin, we are developing software solutions to enable the composition of these protein complexes to be more effectively mined.
4. Nuclear receptors and target gene interactions. In another collaboration with Dr Rainer Lanz, we are developing web-based tools for analysis of gene regulation data in the field of nuclear receptor signaling.
5. Alliances with journals. Traditional models of distribution of scientific data are being re-evaluated with the advent of technologies capable of generating large/high-throughout datasets. We are collaborating with The Endocrine Society to develop web-based approaches to enhancing the experience of readers using electronic versions of journal articles.
Baylor College of Medicine
One Baylor Plaza, M620
Houston, TX 77030
- Lanz RB, Jericevic Z, Zuercher WJ, Watkins C, Steffen DL, Margolis R and McKenna NJ. (2006). Nuclear Receptor Signaling Atlas (www.nursa.org): hyperlinking the nuclear receptor signaling community. Nucleic Acids Res 34:D221-226.
- McKenna NJ and O'Malley BW. (2005). Teaching resources. An interactive course in nuclear receptor signaling: concepts and models. Sci STKE 2005, tr22.
- Cheskis BJ, McKenna NJ, Wong CW, Wong J, Komm B, Lyttle CR and O'Malley BW. (2003). Hierarchical affinities and a bipartite interaction model for estrogen receptor isoforms and full-length steroid receptor coactivator (SRC/p160) family members. J Biol Chem 278:13271-13277.
- McKenna NJ and O'Malley BW. (2002). Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465-474.
- McKenna NJ and O'Malley BW. (2001). Nuclear receptors, coregulators, ligands, and selective receptor modulators: making sense of the patchwork quilt. Ann N Y Acad Sci 949:3-5.
- McKenna NJ and O'Malley BW. (2000). An issue of tissues: divining the split personalities of selective estrogen receptor modulators. Nat Med 6:960-962.
- McKenna NJ, Lanz RB and O'Malley BW. (1999). Nuclear receptor coregulators: cellular and molecular biology. Endocr Rev 20:321-344.
- Lanz RB, McKenna NJ, Onate SA, Albrecht U, Wong J, Tsai SY, Tsai MJ and O'Malley BW. (1999). A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex. Cell 97:17-27.
- McKenna NJ, Nawaz Z, Tsai SY, Tsai MJ and O'Malley BW. (1998). Distinct steady-state nuclear receptor coregulator complexes exist in vivo. Proc Natl Acad Sci USA 95:11697-11702.
- Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ and O'Malley BW. (1997). Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194-198.