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

Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activity.

The Journal of biological chemistry - 14 Aug 2009

Adams Peter, Kandiah Eaazhisai, Effantin Grégory, Steven Alasdair C, Ehrenfeld Ellie

Abstract excerpt

The poliovirus protein 2C plays an essential role in viral RNA replication, although its precise biochemical activities or structural requirements have not been elucidated. The protein has several distinctive properties, including ATPase activity and membrane and RNA binding, that are conserved among orthologs of many positive-strand RNA viruses. Sequence alignments have placed these proteins in the SF3 helicase...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Chromatography, Gel

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

Share to Cross-Linking Reagents

Share to Gene Expression Regulation, Viral

Share to Hydrolysis

Share to Microscopy, Electron, Scanning

Share to Microscopy, Electron, Transmission

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19520852
DOI: 10.1074/jbc.M109.031807
PMCID: PMC2755925

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activity.PMID 19520852Read ↗

Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a coordinated ATP hydrolysis mechanism.Semantic proximity Read ↗

The Structure of the Picornaviral 2C:RNA holoenzyme: Molecular Basis of RNA binding and specificity by a AAA+ proteinSemantic proximity Read ↗

Poliovirus protein 2C contains two regions involved in RNA binding activity.Semantic proximity Read ↗

A cardioviral 2C-ATP complex structure reveals the essential role of a conserved arginine in regulation of cardioviral 2C activity.Semantic proximity Read ↗

A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro.Semantic proximity Read ↗

Human Enterovirus Nonstructural Protein 2CATPase Functions as Both an RNA Helicase and ATP-Independent RNA ChaperoneSemantic proximity Read ↗

RNA helicasesSemantic proximity Read ↗

Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/2CATPase interactions are essential for morphogenesis.Semantic proximity Read ↗

Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus HelicaseSemantic proximity Read ↗

A Single Amino Acid Substitution in Poliovirus Nonstructural Protein 2CATPase Causes Conditional Defects in Encapsidation and Uncoating.Semantic proximity Read ↗

D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP.Semantic proximity Read ↗

AAA+ superfamily ATPases: common structure--diverse function.Semantic proximity Read ↗

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