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

Insights into Two-Metal-Ion Catalytic Mechanism of Cap-Snatching Endonuclease of Ebinur Lake Virus in Bunyavirales.

Journal of virology - 23 Mar 2022

Kuang Wenhua, Zhang Huanyu, Cai Yan, Zhang Guilin, Deng Fei, Li Hailong, Hu Zhihong, Guo Yu, Wang Manli, Zhou Yiwu, Gong Peng

Abstract excerpt

The cap-snatching endonuclease (EN) of segmented negative-strand RNA viruses (sNSVs) produces short capped primers for viral transcription by cleaving the host mRNAs. EN requires divalent metals as cofactors for nucleic acid substrates cleavage; however, the detailed mechanism of metal ion-dependent catalysis of ENs remains obscure. In this work, we reported the EN crystal structure of the Ebinur Lake virus...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Endonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Mutation

Share to RNA Caps

Share to RNA, Messenger

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 35044209
DOI: 10.1128/jvi.02085-21
PMCID: PMC8941914

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into Two-Metal-Ion Catalytic Mechanism of Cap-Snatching Endonuclease of Ebinur Lake Virus in Bunyavirales.PMID 35044209Read ↗

Biochemical and structural studies reveal differences and commonalities among cap-snatching endonucleases from segmented negative-strand RNA virusesSemantic proximity Read ↗

Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching EndonucleasesSemantic proximity Read ↗

Crimean–Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyavirusesSemantic proximity Read ↗

Sin Nombre hantavirus nucleocapsid protein exhibits a metal-dependent DNA-specific endonucleolytic activity.Semantic proximity Read ↗

Identification of tanshinone I as cap-dependent endonuclease inhibitor with broad-spectrum antiviral effectSemantic proximity Read ↗

Structural insights into the substrate specificity of the endonuclease activity of the influenza virus cap-snatching mechanismSemantic proximity Read ↗

Bunyaviridae RNA Polymerases (L-Protein) Have an N-Terminal, Influenza-Like Endonuclease Domain, Essential for Viral Cap-Dependent TranscriptionSemantic proximity Read ↗

Second-Shell Basic Residues Expand the Two-Metal-Ion Architecture of DNA and RNA Processing Enzymes.Semantic proximity Read ↗

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

Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.Semantic proximity Read ↗

Archaeoglobus fulgidus RNase HII in DNA replication: enzymological functions and activity regulation via metal cofactors.Semantic proximity Read ↗

Structure and function of the Toscana virus cap-snatching endonucleaseSemantic proximity Read ↗

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