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

Processing of SeMV polyproteins revisited.

Virology - 5 Jan 2010

Nair Smita, Savithri H S

Abstract excerpt

Processing of Sesbania mosaic virus (SeMV) polyprotein 2a and 2ab was reanalyzed in the view of the new genome organization of sobemoviruses. Polyprotein 2a when expressed in E. coli, from the new cDNA clone, got cleaved at the earlier identified sites E325-T326, E402-T403 and E498-S499 to release protease, VPg, P10 and P8, respectively. Additionally, a novel cleavage was identified within the protease domain at...

Read the complete abstract on PubMed

Topics

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

Share to RNA-Dependent RNA Polymerase
Share to Viral Proteins
Share to Protein Structure, Tertiary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Mosaic Viruses

Share to Mutation

Share to Peptide Hydrolases

Source

Identifiers

PMID: 19861224
DOI: 10.1016/j.virol.2009.09.025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Processing of SeMV polyproteins revisited.PMID 19861224Read ↗

Polyprotein processing: cis and trans proteolytic activities of Sesbania mosaic virus serine protease.Semantic proximity Read ↗

"Natively unfolded" VPg is essential for Sesbania mosaic virus serine protease activity.Semantic proximity Read ↗

A new type of signal peptidase cleavage site identified in an RNA virus polyprotein.Semantic proximity Read ↗

Structure of Senecavirus A 3C Protease Revealed the Cleavage Pattern of 3C Protease in PicornavirusesSemantic proximity Read ↗

Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62Semantic proximity Read ↗

Differential role of N-terminal polyprotein processing in coronavirus genome replication and minigenome amplification.Semantic proximity Read ↗

Downstream Sequences Control the Processing of the Pestivirus Erns-E1 Precursor.Semantic proximity Read ↗

Regulation of the sequential processing of Semliki Forest virus replicase polyprotein.Semantic proximity Read ↗

Timeliness of Proteolytic Events Is Prerequisite for Efficient Functioning of the Alphaviral Replicase.Semantic proximity Read ↗

Proteolytic processing of tomato ringspot nepovirus 3C-like protease precursors: definition of the domains for the VPg, protease and putative RNA-dependent RNA polymerase.Semantic proximity Read ↗

Protein-RNA linkage and post-translational modifications of two sobemovirus VPgs.Semantic proximity Read ↗

Envelope Glycoprotein of ArenavirusesSemantic proximity Read ↗

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