Avital Percher
Rockefeller University
5 Papers
Avital Percher is an academic researcher from Rockefeller University. The author has contributed to research in topics: Transmembrane protein & Fatty acylation. The author has an hindex of 3, co-authored 5 publications.
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Papers
Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation.
Avital Percher,Srinivasan Ramakrishnan,Emmanuelle Thinon,Xiaoqiu Yuan,Jacob S. Yount,Jacob S. Yount,Howard C. Hang +6 more
TL;DR: It is demonstrated that the biochemical exchange of acyl groups on cysteines with defined mass-tags enables the direct visualization of endogenous S-fatty acylated protein levels and enables sensitive detection of protein S-acylation levels and is broadly applicable to different classes of S-palmitoylated membrane proteins.
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Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins.
TL;DR: Quantitative proteomics analysis revealed that unsaturated fatty acids modify similar protein targets to saturated fatty acids, including several immunity‐associated proteins, demonstrating that unsaturation fatty acids can directly modify many proteins to exert their unique and often beneficial physiological effects in vivo.
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Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity.
Emma H. Garst,Hwayoung Lee,Tandrila Das,Shibani Bhattacharya,Avital Percher,Rafal P. Wiewiora,Isaac P. Witte,Yumeng Li,Tao Peng,Wonpil Im,Howard C. Hang,Howard C. Hang +11 more
TL;DR: In this article, site-specific lipidation of cysteine 72 enhances the antiviral activity of interferon-induced transmembrane proteins (IFITMs) by modulating its conformation and interaction with lipid membranes.
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Site-specific lipidation enhances IFITM3 membrane interactions and antiviral activity
Emma H. Garst,Hwayoung Lee,Tandrila Das,Shibani Bhattacharya,Avital Percher,Rafal P. Wiewiora,Isaac P. Witte,Yumeng Li,Michael Goger,Tao Peng,Wonpil Im,Howard C. Hang,Howard C. Hang +12 more
TL;DR: Computational, chemical, and biophysical approaches are employed to demonstrate that site-specific lipidation of IFITM3 at highly conserved cysteine 72 modulates its conformation and interaction with lipid membranes leading to enhanced antiviral activity of IFitM3 in mammalian cells.
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Mass-Tag Labeling Using Acyl-PEG Exchange for the Determination of Endogenous Protein S-Fatty Acylation.
TL;DR: The acyl-PEG exchange (APE) is developed that utilizes cysteine-specific chemistry to exchange S-fatty acylation sites with mass-tags of defined size, which can be readily observed by western blotting and complements the current toolbox of methods for thioester-based post-translational modifications.