ArticleFrontiers in plant science2014
Dissecting the cryoprotection mechanisms for dehydrins.
Article 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 26 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
26 citing papers in PubMed, 60 citations in OpenAlex.
- MsLEA_3-6 overexpression enhances drought tolerance in Medicago sativa L.BMC plant biology · 2025Article
- Comprehensive analysis of dehydrin genes reveals ZmDHN3 contributes to drought resistance in maize (Zea Mays L.).BMC plant biology · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- DNAJA2 and Hero11 mediate similar conformational extension and aggregation suppression of TDP-43.RNA (New York, N.Y.) · 2024Article
- Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity.Scientific reports · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Dehydrin CaDHN2 Enhances Drought Tolerance by Affecting Ascorbic Acid Synthesis under Drought in Peppers.Plants (Basel, Switzerland) · 2023Article
- Article
- Tandem Mass Tag-Based Quantitative Proteomics Reveals Implication of a Late Embryogenesis Abundant Protein (BnLEA57) in Seed Oil Accumulation inFrontiers in plant science · 2022Article
- Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status.Frontiers in plant science · 2022Article
- Characterization of a NovelFrontiers in plant science · 2022Article
- Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses.Biomolecules · 2021Review
- The in vitro structure and functions of the disordered late embryogenesis abundant three proteins.Protein science : a publication of the Protein Society · 2021Article
- Multiple Genetic Trajectories to Extreme Abiotic Stress Adaptation in Arctic Brassicaceae.Molecular biology and evolution · 2020Article
- Identification of small RNAs during cold acclimation in Arabidopsis thaliana.BMC plant biology · 2020Article
- Article
- Genome-wide identification of and functional insights into the late embryogenesis abundant (LEA) gene family in bread wheat (Triticum aestivum).Scientific reports · 2019Article
- Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat.Scientific reports · 2019Article
- MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress inFrontiers in plant science · 2018Article
- Molecular Cloning and Functional Characterization of the Dehydrin (Frontiers in plant science · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the common responses of plants to water deficit is the accumulation of the so-called late embryogenesis abundant (LEA) proteins. In vitro studies suggest that these proteins can protect other macromolecules and cellular structural components from the impairments caused by water limitation. Their binding to phospholipids, nucleic acids and/or to divalent cations has suggested multi-functionality. Genetic analyses indicate that these proteins are required for an optimal adjustment of plants to this insult. This diverse information has conducted to propose different models for LEA proteins action mechanisms. Many of these properties are shared by group 2 LEA proteins or dehydrins (DHNs), one of the LEA protein families for which large amount of data is available. This manuscript focuses on the different mechanisms proposed for this LEA protein group by analyzing published data derived from in vitro cryoprotection assays. We compared the molar ratio of protectant:enzyme needed to preserve 50% of the initial activity per enzyme monomer to assess different mechanisms of action. Our results add evidence for protein-protein interaction as a protection mechanism but also indicate that some DHNs might protect by different means. The strength and weakness of the proposed protection mechanisms are discussed.
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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.