Theresa A. Good

Affiliations: 
Engineering, Chemical and Biochemical University of Maryland, Baltimore County, Baltimore, MD, United States 
Area:
Chemical Engineering, Biomedical Engineering
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"Theresa Good"

Children

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Dhara A. Patel grad student 2007 UMBC
Irina Ramos grad student 2009 UMBC
Ben Keshet grad student 2010 UMBC
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Publications

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Simpson LW, Szeto GL, Boukari H, et al. (2020) Impact of Four Common Hydrogels on Amyloid-β (Aβ) Aggregation and Cytotoxicity: Implications for 3D Models of Alzheimer's Disease. Acs Omega. 5: 20250-20260
Simpson LW, Szeto GL, Boukari H, et al. (2020) Collagen hydrogel confinement of Amyloid-β (Aβ) accelerates aggregation and reduces cytotoxic effects. Acta Biomaterialia
Venkatasubramaniam A, Drude A, Good T. (2014) Role of N-terminal residues in Aβ interactions with integrin receptor and cell surface. Biochimica Et Biophysica Acta. 1838: 2568-77
Keshet B, Gray JJ, Good TA. (2010) Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril. Protein Science : a Publication of the Protein Society. 19: 2291-304
Keshet B, Yang IH, Good TA. (2010) Can size alone explain some of the differences in toxicity between beta-amyloid oligomers and fibrils? Biotechnology and Bioengineering. 106: 333-7
Keshet B, Good T. (2010) P1-254: Aβ toxicity inhibitors as probes of Aβ “active-site” Alzheimer's & Dementia. 6: S247-S247
Qi W, Zhang A, Good TA, et al. (2009) Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability. Biochemistry. 48: 8908-19
Ramos I, Fabris D, Qi W, et al. (2009) Kinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry. Biotechnology and Bioengineering. 104: 181-92
Cowan CB, Patel DA, Good TA. (2009) Exploring the mechanism of beta-amyloid toxicity attenuation by multivalent sialic acid polymers through the use of mathematical models. Journal of Theoretical Biology. 258: 189-97
Zhang A, Qi W, Good TA, et al. (2009) Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange. Biophysical Journal. 96: 1091-104
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