Margaret K. Nelson 

 
Associate Professor of Biology
Chair, Biochemistry Program
Allegheny College
Meadville, PA  16335

 
Ph: (814) 332-2788
Fax: (814) 332-2789
E-mail: mnelson@allegheny.edu

Educational and Professional Background

    B. A., Biology, Williams College, Williamstown, MA
    M.A., Ph.D., Princeton University, Princeton, NJ
    Post-Doctoral Research Fellow, Cancer Research UK and University College London
    Sabbatical Research Fellow, Wellcome Trust Biocentre, University of Dundee, Scotland

Courses

    FS  101:  Cancer: Facts, Fallacies, Fads, and Fantasies
    Bio 060:  Cancer: Causes & Consequences
    Bio 221:  Genetics, Development, and Evolution
    FSBio 201:  Investigative Approaches in Biology (previously cross-listed as Bio290)
    Bio 320:  Cell Biology
    Bio 580:  Signal Transduction


Research Interests

My research interests lie in exploring several of the fundamental questions of developmental biology. For example, how do cells adopt and maintain a specific identity? What is the molecular basis of pattern formation? How is a series of morphological movements coordinated to produce a properly formed terminal structure? 

I use as my experimental organism the cellular slime mold Dictyostelium discoideum, a simple eukaryote that spans the unicellular/multicellular divide. In spite of the relative simplicity of its developmental program, Dictyostelium has proved to be a powerful model system for developmental biology. Not only do its cells carry out many of the same processes as our own; they also do so via similar mechanisms. 

Recently, my research has focused on the molecular genetic characterization of the developmental mutant fbxA (F-Box A). The FbxA protein plays a role in establishing and maintaining the correct prespore: prestalk ratio during development.  Sequence analysis suggests that FbxA is a member of a family of proteins that target proteins for degradation via the ubiquitin-proteasome pathway.  My students and I are currently studying another protein involved in pattern formation, FbiA (FbxA-interacting protein), that we believe is a target of FbxA-mediated degradation.


 
More information
about FbxA
Recent Student ProjectsCellular Slime Mold 
WWW Site
Society for Developmental Biology WWW Site

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Last modified :21 August 2008