ReviewFrontiers in plant science2016
Where do Protein Bodies of Cereal Seeds Come From?
Review in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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
22 citing papers in PubMed.
- Genome-wide association study identifies consistent genomic loci for yield and nutritional quality in Ethiopian sorghum landraces.The plant genome · 2026Article
- Protein Biosynthesis and Maturation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- In order to lower the antinutritional activity of serine protease inhibitors, we need to understand their role in seed development.Frontiers in plant science · 2023Article
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- The molecular basis of cereal grain proteostasis.Essays in biochemistry · 2022Review
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Protein turnover in the developing Triticum aestivum grain.The New phytologist · 2022Article
- Cell Biology Methods to Study Recombinant Proteins in Seeds.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Unconventional Pathways of Protein Secretion: MammalsFrontiers in cell and developmental biology · 2022Review
- StresSeed: The Unfolded Protein Response During Seed Development.Frontiers in plant science · 2022Review
- Microautophagy Mediates Vacuolar Delivery of Storage Proteins in Maize Aleurone Cells.Frontiers in plant science · 2022Article
- Progressive Aggregation of 16 kDa Gamma-Zein during Seed Maturation in TransgenicInternational journal of molecular sciences · 2021Article
- Crosstalk during the Carbon-Nitrogen Cycle That Interlinks the Biosynthesis, Mobilization and Accumulation of Seed Storage Reserves.International journal of molecular sciences · 2021Review
- Two γ-zeins induce the unfolded protein response.Plant physiology · 2021Article
- Viscoelastic properties of wheat gluten in a molecular dynamics study.PLoS computational biology · 2021Article
- Towards coeliac-safe bread.Plant biotechnology journal · 2020Article
- Article
- The Arabidopsis Protein Disulfide Isomerase Subfamily M Isoform, PDI9, Localizes to the Endoplasmic Reticulum and Influences Pollen Viability and Proper Formation of the Pollen Exine During Heat Stress.Frontiers in plant science · 2020Article
- Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation.Scientific reports · 2019Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein bodies of cereal seeds consist of ordered, largely insoluble heteropolymers formed by prolamin storage proteins within the endoplasmic reticulum (ER) of developing endosperm cells. Often these structures are permanently unable to traffic along the secretory pathway, thus representing a unique example for the use of the ER as a protein storage compartment. In recent years, marked progress has been made in understanding what is needed to make a protein body and in formulating hypotheses on how protein body formation might have evolved as an efficient mechanism to store large amounts of protein during seed development, as opposed to the much more common system of seed storage protein accumulation in vacuoles. The major key evolutionary events that have generated prolamins appear to have been insertions or deletions that have disrupted the conformation of the eight-cysteine motif, a protein folding motif common to many proteins with different functions and locations along the secretory pathway, and, alternatively, the fusion between the eight-cysteine motif and domains containing additional cysteine residues.
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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.