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Fariba M. Assadi-Porter

Researcher at University of Wisconsin-Madison

Publications -  45
Citations -  1803

Fariba M. Assadi-Porter is an academic researcher from University of Wisconsin-Madison. The author has contributed to research in topics: Brazzein & Receptor. The author has an hindex of 19, co-authored 43 publications receiving 1561 citations. Previous affiliations of Fariba M. Assadi-Porter include Texas Tech University.

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Calorie Restriction and SIRT3 Trigger Global Reprogramming of the Mitochondrial Protein Acetylome

TL;DR: This work developed and applied a quantitative mass spectrometry method to probe the liver mitochondrial acetyl-proteome during CR versus control diet in mice that were wild-type or lacked the protein deacetylase SIRT3, and revealed widespread reprogramming of mitochondrial protein acetylation in response to CR.
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Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor.

TL;DR: Results from this study support a multi-point interaction between brazzein and the sweet receptor by some mechanism other than the proposed wedge models and suggest that the Venus flytrap module of T1R2 is important for brazzesin agonism.
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Artificial Sweeteners Stimulate Adipogenesis and Suppress Lipolysis Independently of Sweet Taste Receptors

TL;DR: In mature adipocytes, artificial sweetener treatment suppressed lipolysis even in the presence of forskolin, and lipolytic responses were correlated with phosphorylation of hormone-sensitive lipase, suggesting that effects of artificial sweeteners on adipose tissue biology may be largely independent of the classical sweet taste receptors, T 1R2 and T1R3.
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Sweetness Determinant Sites of Brazzein, a Small, Heat-Stable, Sweet-Tasting Protein

TL;DR: Overall, the results suggest that two regions of theprotein are critical for the sweetness of brazzein: a region that includes the N- and C-termini of the protein, which are located close to one another, and a region That includes the flexible loop around Arg43.
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Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin

TL;DR: This work has designed a gene for des-pGlu1- brazzein that incorporates codons that are optimal for protein production in Escherichia coli that resulted in recombinant protein with sweetness similar to that of brazZEin isolated from the original source.