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

Nonstructural Proteins 7 and 8 of Feline Coronavirus Form a 2:1 Heterotrimer That Exhibits Primer-Independent RNA Polymerase Activity

9 Feb 2012

Abstract excerpt

Nonstructural proteins 7 and 8 of severe acute respiratory syndrome coronavirus (SARS-CoV) have previously been shown by X-ray crystallography to form an 8:8 hexadecamer. In addition, it has been demonstrated that N-terminally His(6)-tagged SARS-CoV Nsp8 is a primase able to synthesize RNA oligonucleotides with a length of up to 6 nucleotides. We present here the 2.6-Å crystal structure of the feline coronavirus...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

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

Source

Identifiers

PMID: 22318142
DOI: 10.1128/jvi.06635-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 9 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nonstructural Proteins 7 and 8 of Feline Coronavirus Form a 2:1 Heterotrimer That Exhibits Primer-Independent RNA Polymerase ActivityPMID 22318142Read ↗

The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extensionSemantic proximity Read ↗

One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.Semantic proximity Read ↗

The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependentSemantic proximity Read ↗

Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role in <i>Betacoronavirus</i> replicationSemantic proximity Read ↗

Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2Semantic proximity Read ↗

Structure–function analysis of the nsp14 N7–guanine methyltransferase reveals an essential role in Betacoronavirus replicationSemantic proximity Read ↗

An alphacoronavirus polymerase structure reveals conserved co-factor functionsSemantic proximity Read ↗

Two conserved oligomer interfaces of NSP7 and NSP8 underpin the dynamic assembly of SARS-CoV-2 RdRP.Semantic proximity Read ↗

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factorsSemantic proximity Read ↗

Hallmarks of <i>Alpha</i> - and <i>Betacoronavirus</i> non-structural protein 7+8 complexesSemantic proximity Read ↗

An alphacoronavirus polymerase structure reveals conserved replication factor functionsSemantic proximity Read ↗

Towards a structural understanding of RNA synthesis by negative strand RNA viral polymerasesSemantic proximity Read ↗

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