ReviewPlants (Basel, Switzerland)2020
Late Embryogenesis Abundant Protein-Client Protein Interactions.
Review in Plants (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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
22 citing papers in PubMed, 35 citations in OpenAlex.
- Hyperactive ice-binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans.FEBS open bio · 2026Article
- Structural flexibility of a recombinant intrinsically disordered LEA protein from Ramonda serbica.Scientific reports · 2025Article
- Physiological and molecular responses of bread wheat and its wild relative species to drought stress.Molecular biology reports · 2025Article
- Ethylene Signaling Modulates Dehydrin Expression inInternational journal of molecular sciences · 2025Article
- Article
- LEA proteins and ABA signaling: reciprocal regulation in stress adaptation.Frontiers in plant science · 2025Review
- Article
- Self-association and multimer formation in AtLEA4-5, a desiccation-induced intrinsically disordered protein from plants.Protein science : a publication of the Protein Society · 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
- Liquid-liquid phase separation in plants: Advances and perspectives from model species to crops.Plant communications · 2024Review
- Application of ethanol alleviates heat damage to leaf growth and yield in tomato.Frontiers in plant science · 2024Article
- Article
- Identification and expression analysis of LEA gene family members in pepper (Capsicum annuum L.).FEBS open bio · 2023Article
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Desiccation Tolerance inPlants (Basel, Switzerland) · 2022Article
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- Grape ASR-Silencing Sways Nuclear Proteome, Histone Marks and Interplay of Intrinsically Disordered Proteins.International journal of molecular sciences · 2022Article
- Landscape of biomolecular condensates in heat stress responses.Frontiers in plant science · 2022Review
- The Orthodox Dry Seeds Are Alive: A Clear Example of Desiccation Tolerance.Plants (Basel, Switzerland) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
Abstract
The intrinsically disordered proteins belonging to the LATE EMBRYOGENESIS ABUNDANT protein (LEAP) family have been ascribed a protective function over an array of intracellular components. We focus on how LEAPs may protect a stress-susceptible proteome. These examples include instances of LEAPs providing a shield molecule function, possibly by instigating liquid-liquid phase separations. Some LEAPs bind directly to their client proteins, exerting a holdase-type chaperonin function. Finally, instances of LEAP-client protein interactions have been documented, where the LEAP modulates (interferes with) the function of the client protein, acting as a surreptitious rheostat of cellular homeostasis. From the examples identified to date, it is apparent that client protein modulation also serves to mitigate stress. While some LEAPs can physically bind and protect client proteins, some apparently bind to assist the degradation of the client proteins with which they associate. Documented instances of LEAP-client protein binding, even in the absence of stress, brings to the fore the necessity of identifying how the LEAPs are degraded post-stress to render them innocuous, a first step in understanding how the cell regulates their abundance.
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.