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

The Interface between Methyltransferase and Polymerase of NS5 Is Essential for Flavivirus Replication

22 May 2014

Abstract excerpt

The flavivirus NS5 harbors both a methyltransferase (MTase) and an RNA-dependent RNA polymerase (RdRP). Both enzyme activities of NS5 are critical for viral replication. Recently, the full-length NS5 crystal structure of Japanese encephalitis virus reveals a conserved MTase-RdRP interface that features two conserved components: a six-residue hydrophobic network and a GTR sequence. Here we showed for the first...

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 Insect symbiosis and bacterial influences
Share to Mosquito-borne diseases and control

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 24852307
DOI: 10.1371/journal.pntd.0002891

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Interface between Methyltransferase and Polymerase of NS5 Is Essential for Flavivirus ReplicationPMID 24852307Read ↗

Crystal Structure of the Full-Length Japanese Encephalitis Virus NS5 Reveals a Conserved Methyltransferase-Polymerase InterfaceSemantic proximity Read ↗

Perturbation in the Conserved Methyltransferase-Polymerase Interface of Flavivirus NS5 Differentially Affects Polymerase Initiation and ElongationSemantic proximity Read ↗

Structural and functional insights in flavivirus NS5 proteins gained by the structure of Ntaya virus polymerase and methyltransferaseSemantic proximity Read ↗

Identification of a Small Interface between the Methyltransferase and RNA Polymerase of NS5 that is Essential for Zika Virus ReplicationSemantic proximity Read ↗

Flavivirus RNA-Dependent RNA Polymerase Interacts with Genome UTRs and Viral Proteins to Facilitate Flavivirus RNA ReplicationSemantic proximity Read ↗

A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymeraseSemantic proximity Read ↗

A Crystal Structure of the Dengue Virus NS5 Protein Reveals a Novel Inter-domain Interface Essential for Protein Flexibility and Virus ReplicationSemantic proximity Read ↗

Perspectives on the current antiviral developments towards RNA-dependent RNA polymerase (RdRp) and methyltransferase (MTase) domains of dengue virus non-structural protein 5 (DENV-NS5)Semantic proximity Read ↗

Structure and function of the Zika virus full-length NS5 proteinSemantic proximity Read ↗

Crystal Structure of the RNA Polymerase Domain of the West Nile Virus Non-structural Protein 5Semantic proximity Read ↗

Acetylation of the NS3 helicase by KAT5γ is essential for flavivirus replicationSemantic proximity Read ↗

Genetic Interactions among the West Nile Virus Methyltransferase, the RNA-Dependent RNA Polymerase, and the 5′ Stem-Loop of Genomic RNASemantic proximity Read ↗

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