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

Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus.

Virology - 1 Jul 1990

Hardy W R, Hahn Y S, de Groot R J, Strauss E G, Strauss J H

Abstract excerpt

We have examined the synthesis and processing of nonstructural polyproteins by several temperature-sensitive mutants of Sindbis virus, representing the four known RNA-minus complementation groups. Four mutants that possess mutations in the C-terminal domain of nonstructural protein nsP2 all demonstrated aberrant processing patterns when cells infected with these mutants were shifted from a permissive (30 degrees)...

Read the complete abstract on PubMed

Topics

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

Share to Capsid
Share to Cells, Cultured
Share to Electrophoresis, Polyacrylamide Gel

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

Share to Kinetics

Share to Molecular Weight

Share to Mutation

Share to Protein Processing, Post-Translational

Share to Temperature

Source

Identifiers

PMID: 2141204
DOI: 10.1016/0042-6822(90)90473-5

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

Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus.PMID 2141204Read ↗

Requirement for an aromatic amino acid or histidine at the N terminus of Sindbis virus RNA polymerase.Semantic proximity Read ↗

Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesisSemantic proximity Read ↗

Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo.Semantic proximity Read ↗

Role for Conserved Residues of Sindbis Virus Nonstructural Protein 2 Methyltransferase-Like Domain in Regulation of Minus-Strand Synthesis and Development of Cytopathic InfectionSemantic proximity Read ↗

Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123.Semantic proximity Read ↗

Temperature sensitive shut-off of alphavirus minus strand RNA synthesis maps to a nonstructural protein, nsP4.Semantic proximity Read ↗

Sindbis virus nsP1 functions in negative-strand RNA synthesis.Semantic proximity Read ↗

Altered proteolytic processing of the polymerase polyprotein in RNA(-) temperature sensitive mutants of murine coronavirus.Semantic proximity Read ↗

Modification of Asn374 of nsP1 Suppresses a Sindbis Virus nsP4 Minus-Strand Polymerase MutantSemantic proximity Read ↗

Mutations which alter the level or structure of nsP4 can affect the efficiency of Sindbis virus replication in a host-dependent manner.Semantic proximity Read ↗

Enzymatic defects of the nsP2 proteins of Semliki Forest virus temperature-sensitive mutants.Semantic proximity Read ↗

Identification of mutations causing temperature-sensitive defects in Semliki Forest virus RNA synthesis.Semantic proximity Read ↗

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