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

Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants.

The EMBO journal - 15 Mar 1994

Dolja V V, Haldeman R, Robertson N L, Dougherty W G, Carrington J C

Abstract excerpt

Tobacco etch potyvirus engineered to express the reporter protein beta-glucuronidase (TEV-GUS) was used for direct observation and quantitation of virus translocation in plants. Four TEV-GUS mutants were generated containing capsid proteins (CPs) with single amino acid substitutions (R154D and D198R), a double substitution (DR), or a deletion of part of the N-terminal domain (delta N). Each modified virus...

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 Cell Movement
Share to Genetic Complementation Test

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

Share to Genome, Viral

Share to Microscopy, Electron

Share to Molecular Sequence Data

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 7511101
DOI: 10.1002/j.1460-2075.1994.tb06403.x
PMCID: PMC394968

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

Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants.PMID 7511101Read ↗

Capsid protein determinants involved in cell-to-cell and long distance movement of tobacco etch potyvirus.Semantic proximity Read ↗

Evidence that the potyvirus P1 proteinase functions in trans as an accessory factor for genome amplification.Semantic proximity Read ↗

The N-terminal region of the Plantago asiatica mosaic virus coat protein is required for cell-to-cell movement but is dispensable for virion assembly.Semantic proximity Read ↗

Capsid protein-mediated recruitment of host DnaJ-like proteins is required for Potato virus Y infection in tobacco plants.Semantic proximity Read ↗

Suppression of long-distance movement of tobacco etch virus in a nonsusceptible host.Semantic proximity Read ↗

Capsid protein and helper component-proteinase function as potyvirus cell-to-cell movement proteins.Semantic proximity Read ↗

The cis-expression of the coat protein of turnip mosaic virus is essential for viral intercellular movement in plants.Semantic proximity Read ↗

Analysis of the VPg-proteinase (NIa) encoded by tobacco etch potyvirus: effects of mutations on subcellular transport, proteolytic processing, and genome amplification.Semantic proximity Read ↗

Cell-to-cell movement of potato virus X involves distinct functions of the coat protein.Semantic proximity Read ↗

Mutations in the coat protein gene of plum pox virus suppress particle assembly, heterologous encapsidation and complementation in transgenic plants of Nicotiana benthamiana.Semantic proximity Read ↗

Movement of plant viruses is delayed in a beta-1,3-glucanase-deficient mutant showing a reduced plasmodesmatal size exclusion limit and enhanced callose deposition.Semantic proximity Read ↗

Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro.Semantic proximity Read ↗

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