Evidence map›Paper›PMID 33148259›Full record

ReviewCell communication and signaling : CCS2020

The biology of tardigrade disordered proteins in extreme stress tolerance.

Cherie Hesgrove, Thomas C Boothby

Open access · goldAbstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
18.5field-weighted citation impact, top 1% of its field
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

59 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
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  15. Article
  16. Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025
    Review
  17. Review
  18. Review
  19. Article
  20. Article
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 at 1 institution in 1 country.

Cherie HesgroveDepartment of Molecular Biology, University of Wyoming, Laramie, WY, 82071, USA.
Thomas C BoothbyDepartment of Molecular Biology, University of Wyoming, Laramie, WY, 82071, USA. tboothby@uwyo.edu.ORCID 0000-0002-8807-3268
University of Wyoming · US

Funding

Wyoming INBRE Phase 4- Equipment Supplement for x-ray diffractometer for Center for Advanced Scientific InstrumentationP20GM103432 · NIGMS · UNIVERSITY OF WYOMING · PI Nicolas A. Blouin · 2012 to 2026
$56.8M
NIGMS NIH HHS P20 GM103432
6 · The paper itself

Abstract

Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardigrades, microscopic animals capable of surviving a battery of environmental extremes. These three families include the Cytoplasmic-, Secreted-, and Mitochondrial- Abundant Heat Soluble (CAHS, SAHS, and MAHS) proteins, which are collectively termed Tardigrade Disordered Proteins (TDPs). At the level of sequence conservation TDPs are unique to tardigrades, and beyond their high degree of disorder the CAHS, SAHS, and MAHS families do not resemble one another. All three families are either highly expressed constitutively, or significantly enriched in response to desiccation. In vivo, ex vivo, and in vitro experiments indicate functional roles for members of each TDP family in mitigating cellular perturbations induced by various abiotic stresses. What is currently lacking is a comprehensive and holistic understanding of the fundamental mechanisms by which TDPs function, and the properties of TDPs that allow them to function via those mechanisms. A quantitative and systematic approach is needed to identify precisely what cellular damage TDPs work to prevent, what sequence features are important for these functions, and how those sequence features contribute to the underlying mechanisms of protection. Such an approach will inform us not only about these fascinating proteins, but will also provide insights into how the sequence of a disordered protein can dictate its functional, structural, and dynamic properties. Video Abstract.

Indexed as

Adaptation, PhysiologicalStress, PhysiologicalAmino Acid SequenceAnimalsHeat-Shock ProteinsIntrinsically Disordered ProteinsMitochondrial ProteinsTardigradaHeat-Shock ProteinsIntrinsically Disordered ProteinsMitochondrial ProteinsAnhydrobiosisCytoplasmic abundant heat soluble proteinIntrinsically disordered proteinsLate embryogenesis abundant proteinMitochondrial abundant heat soluble proteinSecreted abundant heat soluble proteinStress toleranceTardigradeTardigrade disordered proteinVitrification

Identifiers

PMID33148259
PMCPMC7640644
OpenAlexW3094776055

What OpenQuestion holds

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LicenceCC BY
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.