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

Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis.

Proceedings of the National Academy of Sciences of the United States of America - 11 Jan 2011

Su Wei, Liu Yidan, Xia Yang, Hong Zhi, Li Jianming

Abstract excerpt

Endoplasmic reticulum (ER)-associated degradation (ERAD) is an integral part of the ER quality-control system that removes toxic misfolded proteins via ubiquitin/proteasome-mediated degradation. Most of our knowledge on ERAD comes from biochemical and genetic studies in yeast and mammalian cells. Although ERAD is known to operate in plant cells, little is known about its molecular components and its biochemical...

Read the complete abstract on PubMed

Topics

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

Share to Cycloheximide
Share to Endoplasmic Reticulum

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

Share to Glycoproteins

Share to Immunoprecipitation

Share to Protein Denaturation

Share to Protein Folding

Share to Receptors, Steroid

Share to Transgenes

Source

Open in PubMed Open full text

Identifiers

PMID: 21187394
DOI: 10.1073/pnas.1013251108
PMCID: PMC3021050

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

Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis.PMID 21187394Read ↗

Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis.Semantic proximity Read ↗

Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins.Semantic proximity Read ↗

Arabidopsis homologs of gp78 modulate the HRD1 complex component AtOS9 by ERAD tuning.Semantic proximity Read ↗

Genetic evidence for an indispensable role of somatic embryogenesis receptor kinases in brassinosteroid signaling.Semantic proximity Read ↗

A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.Semantic proximity Read ↗

Intragenic suppression of a trafficking-defective brassinosteroid receptor mutant in Arabidopsis.Semantic proximity Read ↗

EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis.Semantic proximity Read ↗

SERK5 genetically compensates for the loss of BAK1 and BKK1 in regulating elf18-triggered immune signaling in Arabidopsis.Semantic proximity Read ↗

The Role of SBI2/ALG12/EBS4 in the Regulation of Endoplasmic Reticulum-Associated Degradation (ERAD) Studied by a Null Allele.Semantic proximity Read ↗

Disrupting ER-associated protein degradation suppresses the abscission defect of a weak hae hsl2 mutant in Arabidopsis.Semantic proximity Read ↗

Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.Semantic proximity Read ↗

Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control.Semantic proximity Read ↗

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