ArticlePlant physiology2005
Identification and characterization of endoplasmic reticulum-associated degradation proteins differentially affected by endoplasmic reticulum stress.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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Who cites it
29 citing papers in PubMed, 61 citations in OpenAlex.
- Signal peptide peptidase-like proteases OsSPPL1 and OsSPPL2 facilitate ER-associated protein degradation in rice.Nature communications · 2026Article
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- Unraveling the interactive effect of opaque2 and waxy1 genes on kernel nutritional qualities and physical properties in maize (Zea mays L.).Scientific reports · 2025Article
- Autophagy induced by Helicobacter Pylori infection can lead to gastric cancer dormancy, metastasis, and recurrence: new insights.Human cell · 2024Review
- PILS proteins provide a homeostatic feedback on auxin signaling output.Development (Cambridge, England) · 2022Article
- Article
- Salt stress induces endoplasmic reticulum stress-responsive genes in a grapevine rootstock.PloS one · 2020Article
- OsDER1 Is an ER-Associated Protein Degradation Factor That Responds to ER Stress.Plant physiology · 2018Article
- Protein Quality Control in the Endoplasmic Reticulum of Plants.Annual review of plant biology · 2018Review
- Maize network analysis revealed gene modules involved in development, nutrients utilization, metabolism, and stress response.BMC plant biology · 2017Article
- Introgression of opaque2 into Waxy Maize Causes Extensive Biochemical and Proteomic Changes in Endosperm.PloS one · 2016Article
- Identification and Characterization of Maize floury4 as a Novel Semidominant Opaque Mutant That Disrupts Protein Body Assembly.Plant physiology · 2014Article
- Endoplasmic reticulum-mediated protein quality control in Arabidopsis.Frontiers in plant science · 2014Review
- Recombinant antibody production in Arabidopsis seeds triggers an unfolded protein response.Plant physiology · 2013Article
- Transcriptome-wide mapping of pea seed ageing reveals a pivotal role for genes related to oxidative stress and programmed cell death.PloS one · 2013Article
- The unfolded protein response is triggered by a plant viral movement protein.Plant physiology · 2011Article
- 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 · 2011Article
- Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants.The Plant cell · 2010Review
- Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein.PloS one · 2010Article
- Bax Inhibitor-1, a conserved cell death suppressor, is a key molecular switch downstream from a variety of biotic and abiotic stress signals in plants.International journal of molecular sciences · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The disposal of misfolded proteins from the lumen of the endoplasmic reticulum (ER) is one of the quality control mechanisms present in the protein secretory pathway. Through ER-associated degradation, misfolded substrates are targeted to the cytosol where they are degraded by the proteasome. We have identified four maize (Zea mays) Der1-like genes (Zm Derlins) that encode homologs of Der1p, a yeast (Saccharomyces cerevisiae) protein implicated in ER-associated degradation. Zm Derlins are capable of functionally complementing a yeast Der1 deletion mutant. Such complementation indicates that the Der1p function is conserved among species. Zm Derlin genes are expressed at low levels throughout the plant, but appear prevalent in tissues with high activity of secretory protein accumulation, including developing endosperm cells. Expression of three of the four Zm Derlin genes increases during ER stress, with Zm Derlin1-1 showing the strongest induction. Subcellular fractionation experiments localized Zm Derlin proteins to the membrane fraction of microsomes. In maize endosperm, Zm Derlin proteins were found primarily associated with ER-derived protein bodies regardless of the presence of an ER stress response.
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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.