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James E. Melnyk

Researcher at University of California, San Francisco

Publications -  17
Citations -  4755

James E. Melnyk is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Innate immune system & Immune system. The author has an hindex of 7, co-authored 15 publications receiving 3063 citations. Previous affiliations of James E. Melnyk include University of Delaware & Howard Hughes Medical Institute.

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A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.

David E. Gordon, +128 more
- 30 Apr 2020 - 
TL;DR: A human–SARS-CoV-2 protein interaction map highlights cellular processes that are hijacked by the virus and that can be targeted by existing drugs, including inhibitors of mRNA translation and predicted regulators of the sigma receptors.
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The Global Phosphorylation Landscape of SARS-CoV-2 Infection.

Mehdi Bouhaddou, +77 more
- 06 Aug 2020 - 
TL;DR: A quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells reveals dramatic rewiring of phosphorylation on host and viral proteins, revealing potential COVID-19 therapies.
Posted ContentDOI

A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing

David E. Gordon, +123 more
- 22 Mar 2020 - 
TL;DR: The identification of host dependency factors mediating virus infection may provide key insights into effective molecular targets for developing broadly acting antiviral therapeutics against SARS-CoV-2 and other deadly coronavirus strains.
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The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment.

TL;DR: Using novel MDP self-assembled monolayers (SAMs), this work provides the first biochemical evidence for a direct, high-affinity interaction between Nod2 and MDP.
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Peptidoglycan Modifications Tune the Stability and Function of the Innate Immune Receptor Nod2.

TL;DR: The ligand structure can be adjusted to tune the Nod2 response, suggesting that other innate immune receptors and their ligands could use a similar strategy.