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 a tick-borne flavivirus RNA-dependent RNA polymerase suggests a host adaptation hotspot in RNA viruses

15 Dec 2020

Abstract excerpt

The RNA-dependent RNA polymerases (RdRPs) encoded by RNA viruses represent a unique class of nucleic acid polymerases. RdRPs are essential in virus life cycle due to their central role in viral genome replication/transcription processes. However, their contribution in host adaption has not been well documented. By solving the RdRP crystal structure of the tick-borne encephalitis virus (TBEV), a tick-borne...

Read the complete abstract on PubMed

Topics

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

Share to HIV Research and Treatment
Share to Mosquito-borne diseases and control
Share to Viral Infections and Vectors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33406260
DOI: 10.1093/nar/gkaa1250

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of a tick-borne flavivirus RNA-dependent RNA polymerase suggests a host adaptation hotspot in RNA virusesPMID 33406260Read ↗

A Structure-Function Diversity Survey of the RNA-Dependent RNA Polymerases From the Positive-Strand RNA VirusesSemantic proximity Read ↗

A Structural Overview of RNA-Dependent RNA Polymerases from the Flaviviridae FamilySemantic proximity Read ↗

An updated evolutionary study of Flaviviridae NS3 helicase and NS5 RNA-dependent RNA polymerase reveals novel invariable motifs as potential pharmacological targetsSemantic proximity Read ↗

Identification of a Conserved RNA-dependent RNA Polymerase (RdRp)-RNA Interface Required for Flaviviral ReplicationSemantic proximity Read ↗

Virus-host protein-protein interactions as molecular drug targets for arboviral infectionsSemantic proximity Read ↗

Bunyaviridae RdRps: structure, motifs, and RNA synthesis machinerySemantic proximity Read ↗

Structural and Functional Basis of the Fidelity of Nucleotide Selection by Flavivirus RNA-Dependent RNA PolymerasesSemantic proximity Read ↗

Structural and Functional Diversity of Nairovirus-Encoded Nucleoproteins.Semantic proximity Read ↗

Structure of Rift Valley Fever Virus RNA-Dependent RNA PolymeraseSemantic proximity Read ↗

Virus-Host Coevolution: Common Patterns of Nucleotide Motif Usage in Flaviviridae and Their HostsSemantic proximity Read ↗

A jingmenvirus RNA-dependent RNA polymerase structurally resembles the flavivirus counterpart but with different features at the initiation phaseSemantic proximity Read ↗

Targeting the RdRp of Emerging RNA Viruses: The Structure-Based Drug Design ChallengeSemantic proximity Read ↗

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