Stephen Cusack
Immunology · 2009–2015
A researcher in the Science corpus: 4 papers; trusts 2 researchers and is trusted by 3 researchers here, as inferred from the citation graph.
Subfields
- Immunology — 63 citations into it; #968 of 2,160 by trust here, #1,169 by citations
- Molecular Biology — 48 citations into it; #15,292 of 17,773 by trust here, #12,008 by citations
Whom Stephen Cusack trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts Stephen Cusack overall
Papers from Stephen Cusack's perspective
Ordered by how strongly the researchers Stephen Cusack trusts endorse each paper. Same corpus, a different order for every researcher.
- Cytosolic viral sensor RIG-I is a 5′-triphosphate dependent translocase on double stranded RNA
- Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA.
- VISA is an adapter protein required for virus-triggered IFN-beta signaling. (Molecules and Cells)
- MAVS Forms Functional Prion-Like Aggregates To Activate and Propagate Antiviral Innate Immune Response (Cell)
- TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity (Nature)
- IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction (Nature Immunology)
- Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing
- Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. (Cell)
- 5'-Triphosphate RNA Is the Ligand for RIG-I
- Structural Basis of RNA Recognition and Activation by Innate Immune Receptor RIG-I
Their papers
- Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 (2015) — 56 citations
- A structure-based model of RIG-I activation. (2012) — 152 citations
- Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. (2011) — 667 citations
- The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit (2009) — 789 citations