Biology

Dr. Scott C. Mateer
 

Associate Professor
CST Coordinator of Undergraduate Research
Office: SC1016
912.344.3101
Scott.Mateer@armstrong.edu

Armstrong's Biocatalysis Group

Research Website


Courses Taught

  • BIOL 1107 – Principles of Biology I
  • BIOL 1107H – Principles of Biology I (Honors)
  • BIOL 3000 – Cell Biology
  • BIOL 4000 – Cancer Biology
  • BIOL 4090 – Molecular Biology
  • BIOL 4510 – Molecular Development
  • BIOL 4910 – Research
  • BIOL 4950 - Internship

Academic Profile

  • Postdoctoral Fellow - Neural and Behavioral Development, University of Virginia, 2001-04
  • Ph.D. - Division of Biomedical Sciences, University of Texas Southwestern Medical Center, 1998
  • B.S. - Biology, Minor Philosophy - University of Nebraska-Omaha, 1989
  • Adjunct Faculty - Eastfield Community College - Mesquite, Texas, 1999
  • Lecturer - University of Virginia - Charlottesville, Virginia, 2003-04
  • Visiting Assistant Professor - Allegheny College - Meadville, Pennsylvania, 2004-05
  • Assistant Professor - Armstrong Atlantic State University, 2005-2012
  • Associate Professor - Armstrong Atlantic State University, 2012-present

Research Interests

  • The field of biocatalysis uses enzymes to synthesize organic compounds. I am currently collaborating with Drs. Feske and Padgett in the chemistry department attempting to understand the molecular mechanisms that regulate the synthesis of these organic molecules.
  • Actin polymerization is the driving force that causes a cell to move and is therefore a key cellular process central to various physiological phenomena such as wound healing, embryogenesis, and even metastasis. In the past I have been involved in an effort to elucidate how the cellular protein, IQGAP 1 regulates actin polymerization and ultimately cell motility.
  • Protein phosphatase removes phosphates from various molecules, and therefore, act to reverse the activities of protein kinases. While a graduate student, I investigated how the viral protein, SV40 Small T Antigen, regulated the activity of Protein Phosphatase 2A.