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Eric D. Dodds

Researcher at University of Nebraska–Lincoln

Publications -  60
Citations -  1895

Eric D. Dodds is an academic researcher from University of Nebraska–Lincoln. The author has contributed to research in topics: Mass spectrometry & Tandem mass spectrometry. The author has an hindex of 23, co-authored 60 publications receiving 1685 citations. Previous affiliations of Eric D. Dodds include University of Alaska Anchorage & University of California, Davis.

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Gas chromatographic quantification of fatty acid methyl esters: flame ionization detection vs. electron impact mass spectrometry.

TL;DR: The capacity to combine spectrometric examination and quantitative determination advances GC-MS as a powerful alternative to GC-FID for FAME analysis—an approach that would be particularly advantageous for Fame determination in complex biological samples, where spectromaetric confirmation of analytes is advisable.
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Ion Mobility Studies of Carbohydrates as Group I Adducts: Isomer Specific Collisional Cross Section Dependence on Metal Ion Radius

TL;DR: The determination of collisional cross sections for four groups of isomeric carbohydrates suggest a role for the charge carrier as a probe of carbohydrate structure and thus have significant implications for the continued development and application of ion mobility spectrometry for the distinction and resolution of isomers.
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Glycoprotein expression in human milk during lactation.

TL;DR: Variations in expression or glycosylation levels are demonstrated for several other abundant whey proteins, including tenascin, bile salt-stimulated lipase, xanthine dehydrogenase, and mannose receptor.
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Alterations in Energy/Redox Metabolism Induced by Mitochondrial and Environmental Toxins: A Specific Role for Glucose-6-Phosphate-Dehydrogenase and the Pentose Phosphate Pathway in Paraquat Toxicity

TL;DR: It is suggested that paraquat “hijacks” the PPP to increase NADPH reducing equivalents and stimulate paraqu at redox cycling, oxidative stress, and cell death, which demonstrates that alterations in energy metabolism are not bystanders to energy failure but also contribute significant to cell death progression.
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Revealing the quaternary structure of a heterogeneous noncovalent protein complex through surface-induced dissociation.

TL;DR: The surface-induced dissociation of a heterohexamer, toyocamycin nitrile hydratase, directly into its constituent trimers is illustrated and it is proposed that the single-step nature of this activation in combination with high energy deposition allows for dissociation prior to significant unfolding or other large-scale rearrangement.