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Eric A. Gaucher

Researcher at Georgia State University

Publications -  87
Citations -  4633

Eric A. Gaucher is an academic researcher from Georgia State University. The author has contributed to research in topics: Gene & Molecular evolution. The author has an hindex of 38, co-authored 83 publications receiving 4061 citations. Previous affiliations of Eric A. Gaucher include Parker H. Petit Institute for Bioengineering & Bioscience & University of Maryland, Baltimore.

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Palaeotemperature trend for Precambrian life inferred from resurrected proteins

TL;DR: The convergence of results from natural and physical sciences suggest that ancient life has continually adapted to changes in environmental temperatures throughout its evolutionary history.
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Resurrecting ancestral alcohol dehydrogenases from yeast.

TL;DR: The resurrection of the last common ancestor of Adh1 and Adh2, called AdhA is reported, which suggests that the ancestor was optimized to make (not consume) ethanol, consistent with the hypothesis that before the Adh 1-Adh2 duplication, yeast did not accumulate ethanol for later consumption but rather used AdHA to recycle NADH generated in the glycolytic pathway.
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Inferring the palaeoenvironment of ancient bacteria on the basis of resurrected proteins

TL;DR: This study resurrects candidate sequences for elongation factors of the Tu family found at ancient nodes in the bacterial evolutionary tree, and measures their activities as a function of temperature to suggest that the ancient bacteria that hosted these particular genes were thermophiles, and neither hyperthermophiles nor mesophiles.
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Evolutionary history and metabolic insights of ancient mammalian uricases

TL;DR: This paper used evolutionary models to understand the history of primate uricases by resurrecting ancestral mammalian intermediates before the pseudogenization events of this gene family, revealing that ancestral uricase have steadily decreased in activity since the last common ancestor of mammals gave rise to descendent primate lineages.
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Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases.

TL;DR: Results support the notions that Precambrian life was thermophilic and that proteins can evolve from substrate-promiscuous generalists into specialists during the course of natural evolution and highlight the biotechnological potential of laboratory resurrection of Precambrians proteins.