ArticleProtein science : a publication of the Protein Society2011
Cryoprotective mechanism of a small intrinsically disordered dehydrin protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed, 112 citations in OpenAlex.
- Deciphering the PgLEA2-50 interactome: implications for abiotic stress responses inPlant signaling & behavior · 2026Article
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Molecular propensity and stress tolerance of dehydrins from desert plants.Scientific reports · 2025Article
- Prokaryotic expression, purification, and the in vitro and in vivo protection study of dehydrin WDHN2 from Triticum aestivum.Protoplasma · 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
- Evaluation of a bacterial group 1 LEA protein as an enzyme protectant from stress-induced inactivation.Applied microbiology and biotechnology · 2022Article
- Investigating the Functional Role of the Cysteine Residue in Dehydrin from the Arctic Mouse-Ear ChickweedMolecules (Basel, Switzerland) · 2022Article
- The Halophyte Dehydrin Sequence Landscape.Biomolecules · 2022Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- Salt stress proteins in plants: An overview.Frontiers in plant science · 2022Review
- Expression, Purification, and Preliminary Protection Study of Dehydrin PicW1 From the Biomass ofFrontiers in bioengineering and biotechnology · 2022Article
- Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins.Frontiers in plant science · 2022Review
- Evolutionary analysis of angiosperm dehydrin gene family reveals three orthologues groups associated to specific protein domains.Scientific reports · 2021Article
- 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
- Article
- Lysine, Lysine-Rich, Serine, and Serine-Rich Proteins: Link Between Metabolism, Development, and Abiotic Stress Tolerance and the Role of ncRNAs in Their Regulation.Frontiers in plant science · 2020Review
- Protecting Enzymes from Stress-Induced Inactivation.Biochemistry · 2019Review
- 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
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 expressed during dehydration stress in plants and are thought to protect plant proteins and membranes from the loss of water during drought and at cold temperatures. Several different dehydrins have been shown to protect lactate dehydrogenase (LDH) from damage from being frozen and thawed. We show here that a 48 residue K₂ dehydrin from Vitis riparia protects LDH more effectively than bovine serum albumin, a protein with known cryoprotective function. Light scattering and 8-anilino-1-naphthalene sulfonate fluorescence experiments show that dehydrins prevent aggregation and unfolding of the enzyme. The cryoprotective effects of LDH are reduced by the addition of salt, suggesting that the positively charged K-segments are attracted to a negatively charged surface but this does not result in binding. Overall K₂ is an intrinsically disordered protein; nuclear magnetic resonance relaxation experiments indicate that the two-terminal, Lys-rich K-segments show a weak propensity for α-helicity and are flexible, and that the central, polar rich phi-segment has no secondary structure preference and is highly flexible. We propose that the phi-segments in dehydrins are important for maintaining the disordered structure so that the protein can act as a molecular shield to prevent partially denatured proteins from interacting with one another, whereas the K-segments may help to localize the dehydrin near the enzyme surface.
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.