ReviewFrontiers in plant science2014
Disorder and function: a review of the dehydrin protein family.
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 129 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
129 citing papers in PubMed, 326 citations in OpenAlex.
- The dehydrin protein COR15 enhances antiviral RNA silencing by preventing viral protein-mediated SGS3 degradation and promoting SGS3 condensate formation.Plant communications · 2026Article
- Article
- Fine scale gene expression dynamics at the foliar level reveal grapevine strategies to cope with recurrent drought stress.BMC plant biology · 2026Article
- Hyperactive ice-binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans.FEBS open bio · 2026Article
- The Enhancement of Abiotic Stress Tolerance inPlants (Basel, Switzerland) · 2026Article
- Article
- Molecular Mechanisms and Experimental Strategies for Understanding Plant Drought Response.Plants (Basel, Switzerland) · 2026Review
- Bulk RNA-seq datasets analysis integration identifies robust drought-responsive genes and functional networks inFrontiers in bioinformatics · 2026Article
- Heterologous Expression of Bacterial Dehydrin Promotes Arabidopsis Tolerance to Cadmium and Arsenic Stress.Genes · 2025Article
- Heterologous expression of heat-resistant obscure (Hero) proteins enhances thermotolerance in plants.iScience · 2025Article
- Comprehensive analysis of dehydrin genes reveals ZmDHN3 contributes to drought resistance in maize (Zea Mays L.).BMC plant biology · 2025Article
- Population Genetic Differentiation and Evolutionary History inEcology and evolution · 2025Article
- Article
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Understanding and optimizing plant growth in water-limited environments: 'growth versus defence' or 'growth versus risk mitigation'?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Identification and Functional Validation of thePlants (Basel, Switzerland) · 2025Article
- Mechanisms of Salt and Drought Stress Responses in Foxtail Millet.Plants (Basel, Switzerland) · 2025Review
- Morpho-Physiological Traits and Dehydration Tolerance of High-Altitude Andean Wetland Vegetation in the Chilean Atacama Region.Plant-environment interactions (Hoboken, N.J.) · 2025Article
- Overexpression ofInternational journal of molecular sciences · 2025Article
- Order in Chaos: Lesser-Conserved and Repeat Structures in Dehydrins.Biomolecules · 2025Article
69 more citing papers are in PubMed but not listed here.
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydration proteins (dehydrins) are group 2 members of the late embryogenesis abundant (LEA) protein family. The protein architecture of dehydrins can be described by the presence of three types of conserved sequence motifs that have been named the K-, Y-, and S-segments. By definition, a dehydrin must contain at least one copy of the lysine-rich K-segment. Abiotic stresses such as drought, cold, and salinity cause the upregulation of dehydrin mRNA and protein levels. Despite the large body of genetic and protein evidence of the importance of these proteins in stress response, the in vivo protective mechanism is not fully known. In vitro experimental evidence from biochemical assays and localization experiments suggests multiple roles for dehydrins, including membrane protection, cryoprotection of enzymes, and protection from reactive oxygen species. Membrane binding by dehydrins is likely to be as a peripheral membrane protein, since the protein sequences are highly hydrophilic and contain many charged amino acids. Because of this, dehydrins in solution are intrinsically disordered proteins, that is, they have no well-defined secondary or tertiary structure. Despite their disorder, dehydrins have been shown to gain structure when bound to ligands such as membranes, and to possibly change their oligomeric state when bound to ions. We review what is currently known about dehydrin sequences and their structures, and examine the various ligands that have been shown to bind to this family of proteins.
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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.