Odbert A. Triplett
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Also affiliated: United States Food and Drug Administration (2012–2022)
Research Areas
Biomedical Subjects
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Biography and Research Information
OverviewAI-generated summary
Odbert A. Triplett's research focuses on the study of toxins and their effects, particularly in the context of food safety and potential biological agents. His work has involved microcalorimetric investigations into the unfolding of staphylococcal enterotoxins, a method used to understand protein behavior under different conditions. Triplett has also explored the effects of temperature, such as refrigeration and high heat, on these toxins. His research utilizes cell lines and animal models, including mice, to assess toxicity and biological responses.
Triplett has a publication record that includes work on both ricin and abrin, potent toxins derived from plants. His scholarship metrics indicate an h-index of 4 with a total of 5 publications and 49 citations. He has collaborated with researchers such as William H. Tolleson and Mark E. Hart on shared publications, contributing to a network of scientific inquiry within toxicological research.
Metrics
- h-index: 4
- Publications: 5
- Citations: 49
Selected Publications
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Microcalorimetric Investigations of Reversible Staphylococcal Enterotoxin Unfolding (2022)
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Immunomagnetic Capture of Big Six Shiga Toxin–Producing Escherichia coli Strains in Apple Juice with Detection by Multiplex Real-Time PCR Eliminates Interference from the Food Matrix (2019)
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Influence of yogurt fermentation and refrigerated storage on the stability of protein toxin contaminants (2015)
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Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates (2013)
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Chemical Inactivation of Protein Toxins on Food Contact Surfaces (2012)
Collaboration Network
Top Collaborators
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Influence of yogurt fermentation and refrigerated storage on the stability of protein toxin contaminants
- Immunomagnetic Capture of Big Six Shiga Toxin–Producing Escherichia coli Strains in Apple Juice with Detection by Multiplex Real-Time PCR Eliminates Interference from the Food Matrix
- Microcalorimetric Investigations of Reversible Staphylococcal Enterotoxin Unfolding
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Influence of yogurt fermentation and refrigerated storage on the stability of protein toxin contaminants
- Microcalorimetric Investigations of Reversible Staphylococcal Enterotoxin Unfolding
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Thermal inactivation reaction rates for ricin are influenced by pH and carbohydrates
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Chemical Inactivation of Protein Toxins on Food Contact Surfaces
- Immunomagnetic Capture of Big Six Shiga Toxin–Producing Escherichia coli Strains in Apple Juice with Detection by Multiplex Real-Time PCR Eliminates Interference from the Food Matrix
- Immunomagnetic Capture of Big Six Shiga Toxin–Producing Escherichia coli Strains in Apple Juice with Detection by Multiplex Real-Time PCR Eliminates Interference from the Food Matrix
- Immunomagnetic Capture of Big Six Shiga Toxin–Producing Escherichia coli Strains in Apple Juice with Detection by Multiplex Real-Time PCR Eliminates Interference from the Food Matrix
- Microcalorimetric Investigations of Reversible Staphylococcal Enterotoxin Unfolding
- Microcalorimetric Investigations of Reversible Staphylococcal Enterotoxin Unfolding
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