ReviewFrontiers in plant science2014
Endoplasmic reticulum-mediated protein quality control in Arabidopsis.
Review in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
60 citing papers in PubMed.
- Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts.Nature communications · 2026Review
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- Transcriptomic analysis of reduced thermotolerance inFrontiers in plant science · 2026Article
- A ubiquitin-GhUBX-GhCDC48 module regulates secondary cell wall thickening in cotton fiber.Plant physiology · 2025Article
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Proteolysis in plant immunity.The Plant cell · 2024Review
- Recruitment of Cdc48 to chloroplasts by a UBX-domain protein in chloroplast-associated protein degradation.Nature plants · 2024Article
- Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- The Great Game between Plants and Viruses: A Focus on Protein Homeostasis.International journal of molecular sciences · 2023Review
- An Integrated Analysis of Metabolome, Transcriptome, and Physiology Revealed the Molecular and Physiological Response ofPlants (Basel, Switzerland) · 2023Article
- Autophagy and multivesicular body pathways cooperate to protect sulfur assimilation and chloroplast functions.Plant physiology · 2023Article
- Article
- CRISPR-Cas-mediated unfolded protein response control for enhancing plant stress resistance.Frontiers in plant science · 2023Review
- Endoplasmic reticulum-quality control pathway and endoplasmic reticulum-associated degradation mechanism regulate the N-glycoproteins and N-glycan structures in the diatom Phaeodactylum tricornutum.Microbial cell factories · 2022Article
- POD1-SUN-CRT3 chaperone complex guards the ER sorting of LRR receptor kinases in Arabidopsis.Nature communications · 2022Article
- Improving Protein Quantity and Quality-The Next Level of Plant Molecular Farming.International journal of molecular sciences · 2022Review
- Thicker Ice Improves the Integrity and Angular Distribution of CDC48A Hexamers on Cryo-EM Grids.Frontiers in molecular biosciences · 2022Article
- A Predominant Role of AtEDEM1 in Catalyzing a Rate-Limiting Demannosylation Step of an Arabidopsis Endoplasmic Reticulum-Associated Degradation Process.Frontiers in plant science · 2022Article
- Endoplasmic reticulum-related E3 ubiquitin ligases: Key regulators of plant growth and stress responses.Plant communications · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A correct three-dimensional structure is crucial for the physiological functions of a protein, yet the folding of proteins to acquire native conformation is a fundamentally error-prone process. Eukaryotic organisms have evolved a highly conserved endoplasmic reticulum-mediated protein quality control (ERQC) mechanism to monitor folding processes of secretory and membrane proteins, allowing export of only correctly folded proteins to their physiological destinations, retaining incompletely/mis-folded ones in the ER for additional folding attempts, marking and removing terminally misfolded ones via a unique multiple-step degradation process known as ER-associated degradation (ERAD). Most of our current knowledge on ERQC and ERAD came from genetic and biochemical investigations in yeast and mammalian cells. Recent studies in the reference plant Arabidopsis thaliana uncovered homologous components and similar mechanisms in plants for monitoring protein folding and for retaining, repairing, and removing misfolded proteins. These studies also revealed critical roles of the plant ERQC/ERAD systems in regulating important biochemical/physiological processes, such as abiotic stress tolerance and plant defense. In this review, we discuss our current understanding about the molecular components and biochemical mechanisms of the plant ERQC/ERAD system in comparison to yeast and mammalian systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.