Evidence map›Paper›PMID 17479232›Full record

ReviewDie Naturwissenschaften2007

The continuing conundrum of the LEA proteins.

Alan Tunnacliffe, Michael J Wise

Abstract readReview
PubMed Publisher
In one paragraph

Review in Die Naturwissenschaften, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 papers.

0numbers the graph read from it
0cells of the map it votes in
283citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

283 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Understanding the genetics of quality traits in groundnut: GWAS highlights drought-responsive markers and candidate genes.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Article
  7. Review
  8. Overexpression of theInternational journal of molecular sciences · 2026
    Article
  9. Article
  10. Salt Tolerance in Soybean (Plants (Basel, Switzerland) · 2025
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  17. Article
  18. The promise of resurrection plants in enhancing crop tolerance to water scarcity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  19. Rice Responses to Abiotic Stress: Key Proteins and Molecular Mechanisms.International journal of molecular sciences · 2025
    Review
  20. Article

223 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Alan TunnacliffeInstitute of Biotechnology, University of Cambridge, Cambridge, UK. at10004@cam.ac.uk
Michael J Wise

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?

Indexed as

Amino Acid SequenceAnimalsAntigens, SurfaceBacterial ProteinsDesiccationDisastersInvertebratesMembrane GlycoproteinsPhylogenyPlant ProteinsSeedsWaterAntigens, SurfaceBacterial ProteinsMembrane GlycoproteinsPlant ProteinsWater

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.