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 C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.

The Journal of general virology - 1 Feb 2001

Li Xiaoyu, Lu Hui-Hua, Mueller Steffen, Wimmer Eckard

Abstract excerpt

Poliovirus proteinase 2A(pro) is an essential enzyme involved in cleavages of viral and cellular proteins during the infectious cycle. Evidence has been obtained that 2A(pro) is also involved in genome replication. All enteroviruses have a negatively charged cluster of amino acids at their C terminus (E(E)/(D)(E)/(D)AMEQ-NH(2)), a common motif suggesting function. When aligned with enterovirus sequences, the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Cysteine Endopeptidases

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

Share to Genes, Lethal

Share to HeLa Cells

Share to Poliovirus

Share to Protein Biosynthesis

Share to Viral Proteins

Share to Virus Assembly

Source

Identifiers

PMID: 11161279
DOI: 10.1099/0022-1317-82-2-397

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

The C-terminal residues of poliovirus proteinase 2A(pro) are critical for viral RNA replication but not for cis- or trans-proteolytic cleavage.PMID 11161279Read ↗

Interaction of 2A proteinase of human rhinovirus genetic group A with eIF4E is required for eIF4G cleavage during infection.Semantic proximity Read ↗

Substrate requirements of a human rhinoviral 2A proteinase.Semantic proximity Read ↗

Defining residues involved in human rhinovirus 2A proteinase substrate recognition.Semantic proximity Read ↗

Mutational analyses support a model for the HRV2 2A proteinase.Semantic proximity Read ↗

Human rhinovirus 2 2Apro recognition of eukaryotic initiation factor 4GI. Involvement of an exosite.Semantic proximity Read ↗

The 2A proteins of three diverse picornaviruses are related to each other and to the H-rev107 family of proteins involved in the control of cell proliferationSemantic proximity Read ↗

Identification of a short, highly conserved, motif required for picornavirus capsid precursor processing at distal sitesSemantic proximity Read ↗

Defining substrate selection by rhinoviral 2A proteinase through its crystal structure with the inhibitor zVAM.fmk.Semantic proximity Read ↗

Proteinase 2Apro is essential for enterovirus replication in type I interferon-treated cells.Semantic proximity Read ↗

N-Terminomics TAILS Identifies Host Cell Substrates of Poliovirus and Coxsackievirus B3 3C Proteinases That Modulate Virus InfectionSemantic proximity Read ↗

Rhinovirus 2A is the predominant protease responsible for instigating the early block to gene expression encountered in infected cellsSemantic proximity Read ↗

The cis-acting replication elements define human enterovirus and rhinovirus speciesSemantic proximity Read ↗

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