Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain

1 Jan 2008

Abstract excerpt

BACKGROUND: IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral response two RNA helicases, retinoic acid inducible gene-I (RIG-I) and melanoma differentiation-association gene 5 (MDA5), are independently able to bind viral RNA in the cytoplasm. The 62 kDa protein...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytokine Signaling Pathways and Interactions
Share to Inflammasome and immune disorders
Share to interferon and immune responses

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18307765
DOI: 10.1186/1472-6807-8-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domainPMID 18307765Read ↗

Toward a crystal-clear view of the viral RNA sensing and response by RIG-I-like receptorsSemantic proximity Read ↗

Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction.Semantic proximity Read ↗

Origin and evolution of the RIG-I like RNA helicase gene familySemantic proximity Read ↗

TRAF5 is a downstream target of MAVS in antiviral innate immune signaling.Semantic proximity Read ↗

Annexin A2 mediates RIG-I-like receptor responses to viral infectionSemantic proximity Read ↗

Structure-based alignment of human caspase recruitment domains provides a framework for understanding their functionSemantic proximity Read ↗

Shared and Unique Functions of the DExD/H-Box Helicases RIG-I, MDA5, and LGP2 in Antiviral Innate ImmunitySemantic proximity Read ↗

The autoinhibitory CARD2-Hel2i Interface of RIG-I governs RNA selectionSemantic proximity Read ↗

PCSK9 potentiates innate immune response to RNA viruses by preventing AIP4-mediated polyubiquitination and degradation of VISA/MAVSSemantic proximity Read ↗

Human DICER helicase domain recruits PKR and modulates its antiviral activitySemantic proximity Read ↗

Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5' triphosphate.Semantic proximity Read ↗

Opposite actions of two dsRNA-binding proteins PACT and TRBP on RIG-I mediated signaling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.