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

Unique conformational dynamics and protein recognition of A-to-I hyper-edited dsRNA

20 Jun 2025

Abstract excerpt

Adenosine-to-inosine (A-to-I) editing is a highly abundant modification of double-stranded RNA (dsRNA) and plays an important role in posttranscriptional gene regulation. Editing of multiple inosines by the ADAR1 enzyme leads to A-to-I hyper-editing of non-coding dsRNA, such as 3'UTRs, transposable elements, or foreign pathogenic RNAs, and is implicated in immune response and human diseases including cancer. The...

Read the complete abstract on PubMed

Topics

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

Share to RNA and protein synthesis mechanisms
Share to RNA regulation and disease
Share to Viral Infections and Immunology Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 40568935
DOI: 10.1093/nar/gkaf550

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 17 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unique conformational dynamics and protein recognition of A-to-I hyper-edited dsRNAPMID 40568935Read ↗

Structural perspectives on adenosine to inosine RNA editing by ADARsSemantic proximity Read ↗

Biochemical Profiling and Structural Basis of ADAR1-Mediated RNA EditingSemantic proximity Read ↗

Structural Impacts of Two Disease-linked ADAR1 Mutants: A Molecular Dynamics StudySemantic proximity Read ↗

The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove.Semantic proximity Read ↗

Unraveling the structural complexity in a single-stranded RNA tail: implications for efficient ligand binding in the prequeuosine riboswitch.Semantic proximity Read ↗

Structural impacts of two disease-linked ADAR1 mutants: a molecular dynamics study.Semantic proximity Read ↗

Inosine-Induced Base Pairing Diversity during Reverse TranscriptionSemantic proximity Read ↗

Biochemical profiling and structural basis of ADAR1-mediated RNA editing.Semantic proximity Read ↗

Conformation and structural dynamics of the Xist lncRNA A-repeatsSemantic proximity Read ↗

Adenosine-to-Inosine (A-to-I) RNA Editing by ADAR1 to Control RNA Sensing in Cardiovascular Disease.Semantic proximity Read ↗

Adenosine Deaminases Acting on RNA (ADARs) and Viral InfectionsSemantic proximity Read ↗

Adenosine Deaminases Acting on RNA, RNA Editing, and Interferon ActionSemantic proximity Read ↗

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