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Daniel Amador-Noguez

Researcher at University of Wisconsin-Madison

Publications -  94
Citations -  4884

Daniel Amador-Noguez is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Chemistry & Clostridium thermocellum. The author has an hindex of 26, co-authored 80 publications receiving 3800 citations. Previous affiliations of Daniel Amador-Noguez include Baylor College of Medicine & Great Lakes Bioenergy Research Center.

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Evidence for an Alternative Glycolytic Pathway in Rapidly Proliferating Cells

TL;DR: It is demonstrated that phosphoenolpyruvate (PEP), the substrate for pyruVate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells.
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Metabolomic Analysis via Reversed-Phase Ion-Pairing Liquid Chromatography Coupled to a Stand Alone Orbitrap Mass Spectrometer

TL;DR: A liquid chromatography-mass spectrometry method that capitalizes on the mass-resolving power of the orbitrap to enable sensitive and specific measurement of known and unanticipated metabolites in parallel, with a focus on water-soluble species involved in core metabolism.

Evidence for an Alternative Glycolytic Pathway in Rapidly Proliferating Cells

TL;DR: In this paper, the authors demonstrate that phosphoenolpyruvate (PEP) can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells.
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Intestinal Microbiota Composition Modulates Choline Bioavailability from Diet and Accumulation of the Proatherogenic Metabolite Trimethylamine-N-Oxide

TL;DR: Members of the human gut microbiota responsible for both the accumulation of trimethylamine (TMA), the precursor of the proatherogenic compound TMAO, and subsequent decreased choline bioavailability to the host are identified.
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Metabolite concentrations, fluxes, and free energies imply efficient enzyme usage

TL;DR: Across metabolism, the observed conservation of metabolite concentrations and ΔG are substantially conserved, and that most substrate (but not inhibitor) concentrations exceed the associated enzyme binding site affinity.