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

Misfolded plant virus proteins: elicitors and targets of ubiquitylation.

FEBS letters - 19 Jun 2003

Jockusch Harald, Wiegand Christiane

Abstract excerpt

Mutant tobacco mosaic virus (TMV) coat proteins (CPs) with known amino acid replacements provide well defined examples of destabilized tertiary structures. Here we show that misfolded TMV CPs, but not functional wild-type CPs, induce massive ubiquitylation in tobacco cells and that denatured, insoluble CP subunits are the main substrates of ubiquitin conjugation. As TMV CPs can be easily manipulated they are...

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins
Share to Amino Acid Substitution
Share to Plants, Toxic

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

Share to Protein Conformation

Share to Protein Denaturation

Share to Temperature

Share to Tobacco Mosaic Virus

Share to Ubiquitin

Source

Identifiers

PMID: 12804781
DOI: 10.1016/s0014-5793(03)00549-0

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Misfolded plant virus proteins: elicitors and targets of ubiquitylation.PMID 12804781Read ↗

The Great Game between Plants and Viruses: A Focus on Protein HomeostasisSemantic proximity Read ↗

MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana.Semantic proximity Read ↗

K63-linked ubiquitin chains are a global signal for endocytosis and contribute to selective autophagy in plantsSemantic proximity Read ↗

Stability of Begomoviral pathogenicity determinant βC1 is modulated by mutually antagonistic SUMOylation and SIM interactionsSemantic proximity Read ↗

Geminiviruses subvert ubiquitination by altering CSN-mediated derubylation of SCF E3 ligase complexes and inhibit jasmonate signaling in Arabidopsis thaliana.Semantic proximity Read ↗

Ubiquitylation in plants: a post-genomic look at a post-translational modificationSemantic proximity Read ↗

Conformational behavior of coat protein in plants and association with coat protein-mediated resistance against TMV.Semantic proximity Read ↗

Synthetic MicroProteins: Versatile Tools for Posttranslational Regulation of Target Proteins.Semantic proximity Read ↗

Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote.Semantic proximity Read ↗

Ubiquitylome Analysis Reveals a Central Role for the Ubiquitin-Proteasome System in Plant Innate ImmunitySemantic proximity Read ↗

Temporal Proteomics of Inducible RNAi Lines of Clp Protease Subunits Identifies Putative Protease Substrates.Semantic proximity Read ↗

Ubiquitylome analysis reveals a central role for the ubiquitin-proteasome system in plant innate immunitySemantic proximity Read ↗

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