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

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

The New phytologist - 1 Oct 2018

Park Joung Hun, Kang Chang Ho, Nawkar Ganesh M, Lee Eun Seon, Paeng Seol Ki, Chae Ho Byoung, Chi Yong Hun, Kim Woe Yeon, Yun Dae-Jin, Lee Sang Yeol

Abstract excerpt

Investigation of the endoplasmic reticulum-associated degradation (ERAD) system in plants led to the identification of ERAD-mediating RING finger protein (EMR) as a plant-specific ERAD E3 ligase from Arabidopsis. EMR was significantly up-regulated under endoplasmic reticulum (ER) stress conditions. The EMR protein purified from bacteria displayed high E3 ligase activity, and tobacco leaf-produced EMR mediated...

Read the complete abstract on PubMed

Topics

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

Share to Acyltransferases
Share to Brassinosteroids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to Endoplasmic Reticulum-Associated Degradation

Share to Endoplasmic Reticulum Stress

Share to Proteolysis

Share to Ubiquitin-Conjugating Enzymes

Share to Ubiquitin-Protein Ligases

Source

Identifiers

PMID: 29932218
DOI: 10.1111/nph.15279

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

EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis.PMID 29932218Read ↗

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

The prolific ATL family of RING-H2 ubiquitin ligasesSemantic proximity Read ↗

Characterization of three Arabidopsis homologs of human RING membrane anchor E3 ubiquitin ligase.Semantic proximity Read ↗

Comprehensive analysis of the rice RING E3 ligase family reveals their functional diversity in response to abiotic stress.Semantic proximity Read ↗

The protein quality control system manages plant defence compound synthesis.Semantic proximity Read ↗

The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates.Semantic proximity Read ↗

Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR.Semantic proximity Read ↗

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

An E3 Ubiquitin Ligase-BAG Protein Module Controls Plant Innate Immunity and Broad-Spectrum Disease Resistance.Semantic proximity Read ↗

ERMO3/MVP1/GOLD36 is involved in a cell type-specific mechanism for maintaining ER morphology in Arabidopsis thaliana.Semantic proximity Read ↗

Quantitative Proteomic Analysis of ER Stress Response Reveals both Common and Specific Features in Two Contrasting Ecotypes of Arabidopsis thalianaSemantic proximity Read ↗

Advanced genomics identifies growth effectors for proteotoxic ER stress recovery in Arabidopsis thalianaSemantic proximity Read ↗

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