ArticleThe Journal of biological chemistry2015
Structural and Functional Insights into the Cryoprotection of Membranes by the Intrinsically Disordered Dehydrins.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Order in Chaos: Lesser-Conserved and Repeat Structures in Dehydrins.Biomolecules · 2025Article
- Article
- Dynamic conformational changes of a tardigrade group-3 late embryogenesis abundant protein modulate membrane biophysical properties.PNAS nexus · 2024Article
- Plant dehydrins and dehydrin-like proteins: characterization and participation in abiotic stress response.Frontiers in plant science · 2023Review
- The Effect of Positive Charge Distribution on the Cryoprotective Activity of Dehydrins.Biomolecules · 2022Article
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- The Halophyte Dehydrin Sequence Landscape.Biomolecules · 2022Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins.Frontiers in plant science · 2022Review
- Expression, Purification, and Preliminary Protection Study of Dehydrin PicW1 From the Biomass ofFrontiers in bioengineering and biotechnology · 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
- Regulation of ABA-Non-Activated SNF1-Related Protein Kinase 2 Signaling Pathways by Phosphatidic Acid.International journal of molecular sciences · 2020Article
- The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions.Journal of lipid research · 2020Article
- Sequence composition versus sequence order in the cryoprotective function of an intrinsically disordered stress-response protein.Protein science : a publication of the Protein Society · 2019Article
- The disordered plant dehydrin Lti30 protects the membrane during water-related stress by cross-linking lipids.The Journal of biological chemistry · 2019Article
- Structural and Functional Dynamics of Dehydrins: A Plant Protector Protein under Abiotic Stress.International journal of molecular sciences · 2018Review
- The Many Faces of Amphipathic Helices.Biomolecules · 2018Review
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydration can be due to desiccation caused by a lack of environmental water or to freezing caused by a lack of liquid water. Plants have evolved a large family of proteins called LEA (late embryogenesis abundant) proteins, which include the intrinsically disordered dehydrin (dehydration protein) family, to combat these abiotic stresses. Although transcription and translation studies have shown a correlation between dehydration stress and the presence of dehydrins, the biochemical mechanisms have remained somewhat elusive. We examine here the effect and structure of a small model dehydrin (Vitis riparia K2) on the protection of membranes from freeze-thaw stress. This protein is able to bind to liposomes containing phosphatidic acid and protect the liposomes from fusing after freeze-thaw treatment. The presence of K2 did not measurably affect liposome surface accessibility or lipid mobility but did lower its membrane transition temperature by 3 °C. Using sodium dodecyl sulfate as a membrane model, we examined the NMR structure of K2 in the presence and absence of the micelle. Biochemical and NMR experiments show that the conserved, lysine-rich segments are involved in the binding of the dehydrin to a membrane, whereas the poorly conserved φ segments play no role in binding or protection.
Indexed as
Identifiers
What OpenQuestion holds
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.