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

Defining residues involved in human rhinovirus 2A proteinase substrate recognition.

FEBS letters - 16 Oct 2006

Sousa Carla, Schmid Eva M, Skern Tim

Abstract excerpt

The 2A proteinase (2A(pro)) of human rhinoviruses (HRVs) initiates proteolytic processing by cleaving between the C-terminus of VP1 and its own N-terminus. It subsequently cleaves the host protein eIF4GI. HRV2 and HRV14 2A(pro) cleave at IITTA *GPSD and DIKSY *GLGP on their respective polyproteins. The HRV2 2A(pro) cleavage site on eIF4GI is TLSTR *GPPR. We show that HRV2 2A(pro) can self-process at the eIF4GI...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cysteine Endopeptidases
Share to Eukaryotic Initiation Factor-4G

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

Share to Models, Molecular

Share to Protein Structure, Tertiary

Share to Rhinovirus

Share to Substrate Specificity

Share to Viral Proteins

Source

Identifiers

PMID: 17007846
DOI: 10.1016/j.febslet.2006.09.023

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

Defining residues involved in human rhinovirus 2A proteinase substrate recognition.PMID 17007846Read ↗

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

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

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

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

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

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

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

Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro.Semantic proximity Read ↗

Mutations at KFRDI and VGK domains of enterovirus 71 3C protease affect its RNA binding and proteolytic activitiesSemantic proximity Read ↗

Site-directed mutagenesis suggests close functional relationship between a human rhinovirus 3C cysteine protease and cellular trypsin-like serine proteases.Semantic proximity Read ↗

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