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Theresa A. Good - Publications

Affiliations: 
Engineering, Chemical and Biochemical University of Maryland, Baltimore County, Baltimore, MD, United States 
Area:
Chemical Engineering, Biomedical Engineering
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37 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Simpson LW, Szeto GL, Boukari H, Good TA, Leach JB. 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. PMID 32832778 DOI: 10.1021/acsomega.0c02046  0.431
2020 Simpson LW, Szeto GL, Boukari H, Good TA, Leach JB. Collagen hydrogel confinement of Amyloid-β (Aβ) accelerates aggregation and reduces cytotoxic effects. Acta Biomaterialia. PMID 32464268 DOI: 10.1016/J.Actbio.2020.05.030  0.392
2014 Venkatasubramaniam A, Drude A, Good T. Role of N-terminal residues in Aβ interactions with integrin receptor and cell surface. Biochimica Et Biophysica Acta. 1838: 2568-77. PMID 24955499 DOI: 10.1016/J.Bbamem.2014.06.011  0.501
2010 Keshet B, Gray JJ, Good TA. Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril. Protein Science : a Publication of the Protein Society. 19: 2291-304. PMID 20882638 DOI: 10.1002/Pro.509  0.725
2010 Keshet B, Yang IH, Good TA. Can size alone explain some of the differences in toxicity between beta-amyloid oligomers and fibrils? Biotechnology and Bioengineering. 106: 333-7. PMID 20148403 DOI: 10.1002/Bit.22691  0.749
2010 Keshet B, Good T. P1-254: Aβ toxicity inhibitors as probes of Aβ “active-site” Alzheimer's & Dementia. 6: S247-S247. DOI: 10.1016/J.Jalz.2010.05.806  0.732
2009 Qi W, Zhang A, Good TA, Fernandez EJ. Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability. Biochemistry. 48: 8908-19. PMID 19637920 DOI: 10.1021/Bi9006397  0.506
2009 Ramos I, Fabris D, Qi W, Fernandez EJ, Good TA. Kinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry. Biotechnology and Bioengineering. 104: 181-92. PMID 19418563 DOI: 10.1002/Bit.22367  0.703
2009 Cowan CB, Patel DA, Good TA. 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. PMID 19217912 DOI: 10.1016/J.Jtbi.2009.02.003  0.618
2009 Zhang A, Qi W, Good TA, Fernandez EJ. Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange. Biophysical Journal. 96: 1091-104. PMID 19186145 DOI: 10.1016/J.Bpj.2008.10.022  0.526
2008 Cowan CB, Coté GL, Good TA. Development of photocrosslinked sialic acid containing polymers for use in Abeta toxicity attenuation. Biomaterials. 29: 3408-14. PMID 18508118 DOI: 10.1016/J.Biomaterials.2008.05.001  0.556
2008 Chou IH, Benford M, Beier HT, Coté GL, Wang M, Jing N, Kameoka J, Good TA. Nanofluidic biosensing for beta-amyloid detection using surface enhanced Raman spectroscopy. Nano Letters. 8: 1729-35. PMID 18489171 DOI: 10.1021/Nl0808132  0.498
2008 Qi W, Zhang A, Patel D, Lee S, Harrington JL, Zhao L, Schaefer D, Good TA, Fernandez EJ. Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis. Biotechnology and Bioengineering. 100: 1214-27. PMID 18351682 DOI: 10.1002/Bit.21846  0.661
2008 Benford ME, Chou IH, Beier HT, Wang M, Kameoka J, Good TA, Coté GL. In vitro detection of beta amyloid exploiting surface enhanced Raman scattering (SERS) using a nanofluidic biosensor Progress in Biomedical Optics and Imaging - Proceedings of Spie. 6869. DOI: 10.1117/12.763913  0.453
2008 Beier HT, Cowan CB, Good TA, Coté GL. A surface enhanced Raman spectroscopy platform based on nanoshells for detection of β-amyloid Progress in Biomedical Optics and Imaging - Proceedings of Spie. 6869. DOI: 10.1117/12.763888  0.449
2008 Keshet B, Good T. P1-408: The role of aggregate size and concentration in Aβ neurotoxicity and elucidation of key amino acids in Aβ-cell interaction Alzheimer's & Dementia. 4: T339-T339. DOI: 10.1016/J.Jalz.2008.05.990  0.733
2008 Ramos I, Good T. P1-423: Kinetic study of β-amyloid residue accessibility by chemical modification and mass spectrometry Alzheimer's & Dementia. 4: T343-T343. DOI: 10.1016/J.Jalz.2008.05.1005  0.621
2007 Patel DA, Henry JE, Good TA. Attenuation of beta-amyloid-induced toxicity by sialic-acid-conjugated dendrimers: role of sialic acid attachment. Brain Research. 1161: 95-105. PMID 17604005 DOI: 10.1016/J.Brainres.2007.05.055  0.645
2007 Lee S, Fernandez EJ, Good TA. Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathway. Protein Science : a Publication of the Protein Society. 16: 723-32. PMID 17327396 DOI: 10.1110/Ps.062514807  0.561
2007 Patel D, Good T. A rapid method to measure beta-amyloid induced neurotoxicity in vitro. Journal of Neuroscience Methods. 161: 1-10. PMID 17083984 DOI: 10.1016/J.Jneumeth.2006.10.004  0.689
2007 Beier HT, Cowan CB, Chou IH, Pallikal J, Henry JE, Benford ME, Jackson JB, Good TA, Coté GL. Application of surface-enhanced raman spectroscopy for detection of beta amyloid using nanoshells Plasmonics. 2: 55-64. DOI: 10.1007/S11468-007-9027-X  0.5
2006 Patel D, Henry J, Good T. Attenuation of beta-amyloid induced toxicity by sialic acid-conjugated dendrimeric polymers. Biochimica Et Biophysica Acta. 1760: 1802-9. PMID 16982154 DOI: 10.1016/J.Bbagen.2006.08.008  0.666
2006 Lee S, Carson K, Rice-Ficht A, Good T. Small heat shock proteins differentially affect Abeta aggregation and toxicity. Biochemical and Biophysical Research Communications. 347: 527-33. PMID 16828710 DOI: 10.1016/J.Bbrc.2006.06.128  0.54
2005 Wang SS, Good TA, Rymer DL. The influence of phospholipid membranes on bovine calcitonin peptide's secondary structure and induced neurotoxic effects. The International Journal of Biochemistry & Cell Biology. 37: 1656-69. PMID 15896672 DOI: 10.1016/J.Biocel.2005.02.006  0.486
2005 Wang SS, Good TA, Rymer DL. The influence of phospholipid membranes on bovine calcitonin secondary structure and amyloid formation. Protein Science : a Publication of the Protein Society. 14: 1419-28. PMID 15883181 DOI: 10.1110/ps.041240105  0.357
2005 Lee S, Carson K, Rice-Ficht A, Good T. Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity. Protein Science : a Publication of the Protein Society. 14: 593-601. PMID 15722443 DOI: 10.1110/Ps.041020705  0.551
2005 Lee S, Good TA. Role of aggregation conditions in structure, stability and toxicity of intermediates in the beta amyloid fibril formation pathway Aiche Annual Meeting, Conference Proceedings. 586.  0.409
2005 Lee S, Good TA. The effect of various small heat shock proteins on prevention of beta amyloid aggregation and toxicity Aiche Annual Meeting, Conference Proceedings. 8162.  0.343
2004 Good T, Ramos I, Henry J, Joon Yoo JS. P4-391 Use of sialic acid containing compounds to prevent beta amyloid toxicity Neurobiology of Aging. 25: S586. DOI: 10.1016/S0197-4580(04)81949-3  0.654
2004 Patel D, Good T. P1-237 Role of beta amyloid structure in G protein activation Neurobiology of Aging. 25: S163-S164. DOI: 10.1016/S0197-4580(04)80550-5  0.604
2003 Wang SS, Tobler SA, Good TA, Fernandez EJ. Hydrogen exchange-mass spectrometry analysis of beta-amyloid peptide structure. Biochemistry. 42: 9507-14. PMID 12899638 DOI: 10.1021/Bi0342766  0.457
2003 Wang SS, Kazantzi V, Good TA. A Kinetic Analysis of the Mechanism of beta-Amyloid Induced G Protein Activation. Journal of Theoretical Biology. 221: 269-78. PMID 12628233 DOI: 10.1006/Jtbi.2003.3189  0.401
2002 Wang SS, Becerra-Arteaga A, Good TA. Development of a novel diffusion-based method to estimate the size of the aggregated Abeta species responsible for neurotoxicity. Biotechnology and Bioengineering. 80: 50-9. PMID 12209786 DOI: 10.1002/Bit.10347  0.539
2001 Wang SS, Rymer DL, Good TA. Reduction in cholesterol and sialic acid content protects cells from the toxic effects of beta-amyloid peptides. The Journal of Biological Chemistry. 276: 42027-34. PMID 11557751 DOI: 10.1074/Jbc.M102834200  0.521
2001 Rymer DL, Good TA. The role of G protein activation in the toxicity of amyloidogenic Abeta-(1-40), Abeta-(25-35), and bovine calcitonin. The Journal of Biological Chemistry. 276: 2523-30. PMID 11060290 DOI: 10.1074/Jbc.M005800200  0.504
2000 Rymer DL, Good TA. The role of prion peptide structure and aggregation in toxicity and membrane binding. Journal of Neurochemistry. 75: 2536-45. PMID 11080207 DOI: 10.1046/J.1471-4159.2000.0752536.X  0.451
1995 Good TA, Murphy RM. Aggregation state-dependent binding of beta-amyloid peptide to protein and lipid components of rat cortical homogenates. Biochemical and Biophysical Research Communications. 207: 209-15. PMID 7857267 DOI: 10.1006/bbrc.1995.1174  0.355
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