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Joseph Marcotrigiano

Researcher at Center for Advanced Biotechnology and Medicine

Publications -  40
Citations -  3095

Joseph Marcotrigiano is an academic researcher from Center for Advanced Biotechnology and Medicine. The author has contributed to research in topics: RNA & Hepatitis C virus. The author has an hindex of 22, co-authored 40 publications receiving 2667 citations. Previous affiliations of Joseph Marcotrigiano include Rutgers University & Rockefeller University.

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Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA

TL;DR: This work identifies the polyuridine motif of the HCV genome 3′ non-translated region and its replication intermediate as the PAMP substrate of RIG-I, and shows that this and similar homopolyuridine or homopolyriboadenine motifs present in the genomes of RNA viruses are the chief feature of Rig-I recognition and immune triggering in human and murine cells.
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Structural basis of RNA recognition and activation by innate immune receptor RIG-I

TL;DR: A detailed view of the role of helicase in dsRNA recognition, the synergy between the RD and the helicase for RNA binding and the organization of full-length RIG-I bound to ds RNA is provided, and evidence of a conformational change upon RNA binding is provided.
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Exosome RNA Unshielding Couples Stromal Activation to Pattern Recognition Receptor Signaling in Cancer

TL;DR: Results demonstrate that regulation of RNA unshielding couples stromal activation with deployment of RNA DAMPs that promote aggressive features of cancer.
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Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2

TL;DR: Solution-based studies demonstrate that the full-length E2 ectodomain has a similar globular architecture and does not undergo significant conformational or oligomeric rearrangements on exposure to low pH, and provides unprecedented insights into HCV entry.
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Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I.

TL;DR: It is shown that RIG-I accommodates the m7G base while maintaining the 5′ppp contacts and can recognize Cap-0 RNAs but not Cap-1, and a single H830A mutation restores both high-affinity binding and signaling activity with 2′-O-methylated dsRNAs.