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College of Engineering and Information Technology
UMBC Chemical and Biochemical Engineering
Theresa Good
Contact Information

tgood@umbc.edu

410-455-3405

ECS 317

 

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Theresa Good

Title

Professor

Education

Ph.D. – University of Wisconsin-Madison, 1996
M.S. – Cornell University, 1985 
B.S. – Bucknell University, 1983 

Professional Interests

The research we do in our lab is in the area of cellular engineering. We use a variety of engineering tools to analyze reactions that occur on the surface of cells and/or within cells to try to understand the mechanism of various diseases. We then use that information to try to alter the selectivity of those reactions such that we prevent or slow the progression of disease. For example, some proteins, such as beta amyloid of Alzheimer's disease, interact with neurons. If the protein is in a normal or "healthy" conformation, the interaction is benign, while if the protein is in its amyloid or "pathogenic" conformation, the protein-cell interaction leads to cell death. We would like to understand the mechanism of the protein-cell interaction and be able to prevent it.

Publications

Cells Under Stress

D. Triyoso and T. Good. Pulsatile Shear Stress leads to DNA Fragmentation in Human SH-SY5Y Neuroblastoma Cell Line. J. Physiology ,  515: 355-365, 1999.

M. Edwards, S-S Wang, and T. Good. Role of Viscoelastic Properties of Differentiated SH-SY5Y Human Neuroblastoma Cells in Cyclic Shear Stress Injury.  Biotechnology Progress 17:  760-767, 2001.

M. Edwards and T. Good. Use of a Mathematical Model to Estimate Stress and Strain During Elevated Pressure Induced Lamina Cribrosa Deformation.  Current Eye Research. 23: 215-225, 2001.

S.-S. Wang and T. Good. Effect of Culture in a Rotating Wall Bioreactor on the Physiology of Differentiated Neuron-like PC12 and SH-SY5Y Cells, J. Cellular Biochemistry. 83: 574-584. 2001.

Amyloids

D. Rymer and T. Good.  The Role of Prion Peptide Structure and Aggregation in Toxicity and Membrane Binding. J. Neurochem, 75: 2536-2545, 2000.

D. Rymer and T. Good.  Amyloidogenic β (1-40), β (25-35) and Bovine Calcitonin Are Toxic Via A Common Pathway Involving G Protein Activation.  J. Biol. Chem., 276: 2523-2530, 2001.

S.-S. Wang, D. Rymer and T. Good. Cholesterol and Sialic Acid Removal Protects Cells from the Toxic Effects of β-Amyloid Peptides.  J. Biol. Chem. 276:  42027-42034, 2001.

S.-S. Wang, A. Becerra-Arteaga, and T.Good.  Development of a novel diffusion-based method to estimate the size of the aggregated Aβ species responsible for neurotoxicity.   Biotechnology and Bioengineering, 80, 50-59, 2002.

S.-S. Wang, V. Kazantzi and T. Good.  Kinetic analysis of the mechanism of β-amyloid induced G protein activation.  J Theoretical Biology. 221: 269-278, 2003.

S.-S. Wang, S. Tobler, T. Good, and E. Fernandez.  Hydrogen exchange-mass spectrometry analysis of β-amyloid peptide structure.  Biochemistry. 42: 9507-14, 2003.

S. Lee, K. Carson, A. Ficht., and T. Good. Hsp20, a novel a-crystallin, prevents Aβ fibril formation and toxicity.  Protein Science. 14: 593-601,2005.

S. Lee, K. Carson, A. Ficht and T. Good.  Small heat shock proteins differentially affect Aβ aggregation and toxicity.  BBRC 347: 527-533, 2006.

D. Patel, J. Henry and T. Good.  Attenuation of beta-amyloid induced toxicity by sialic acid-conjugated dendritic polymers. BBA General Subjects 1760: 1802-1809, 2006

D. Patel and T. Good.  A rapid method to measure β-amyloid induced toxicity in vitro.  J. Neuroscience Methods  161: 1-10, 2007.

S. Lee, E. Fernandez and T. Good.  Role of aggregation conditions in structure, stability and toxicity of intermediates in the Aβ fibril formation pathway.  Protein Science.  16: 723-732, 2007.

D. Patel, J. Henry and T. Good.  Attenuation of beta-amyloid induced toxicity by sialic acid-conjugated dendrimers:  role of sialic acid attachment. Brain Research 1161: 95-105, 2007.

T cells

R. Linares, J. Ruiz Pacheco, and T. Good. Efficacy of Different Targeting Agents in the Photolysis of Interleukin-2 Receptor Bearing Cells.   J Photochemistry and Photobiology, B.  77:  17-26, 2004.

Sensors

B. Jung, S. Lee, I.H. Yang, T. Good, and G. Cote’.  Automated On Line Noninvasive Optical Glucose Monitoring in Cell Culture System, Applied Spectroscopy. 56: 511-57, 2002.

J. Henry, A. Anand, M. Chowdhury, G. Cote’, R. Moreira, and T. Good. Development of a nanoparticle based - surface modified fluorescence assay for the detection of prion proteins.  Analytical Biochemistry.  334:1-8, 2004.

A. Simonian, T. Good, S.-S. Wang, and J. R. Wild. Nanoparticles-based Optical Biosensor for Direct Detection of Organophosphate CW Agents and Pesticides.  Analytica Chimica Acta.  534: 69-77, 2005.

A. Anand, R. Moreira, J. Henry, M. Chowdhury, G. Cote' and T. Good. A bio-sensing strategy for the detection of prions. LWT - Food Science and Technology.  38:  849-858, 2005.

H. Beier, C. Cowan, I.H. Chow, J. Pallikal, J. Henry, M. Benford, J. Jackson, T. Good, and G. Cote’.  Application of Surface Enhanced Raman Spectroscopy for Detection of Beta Amyloid Using Nanoshells.  Plasmonics. 2:  55-64, 2007.

Biocomplexity

N. Kazantzis and T. Good.  Invariant Manifolds and the Calculation of the Long Term Asymptotic Response of Nonlinear Processes Using Singular PDEs.  Comput. Chem. Eng. 26: 999-1012, 2002.

M. Rodriguez, T. Good, M. Wales, J. Hua, and J. Wild. Modeling Allosteric Regulation of de novo Pyrimidine Biosynthesis in Escherichia coli.  J. Theoretical Biology .  234: 299-310, 2005. 

N. Kazantzis, N. Huynh, and T. Good.  A model based characterization of the long term asymptotic behavior of non-linear discrete time processes using invariance functional equations.  Computers in Chemical Engineering. 29:2346-2354, 2005.