ArticleProtein science : a publication of the Protein Society2019
Protecting activity of desiccated enzymes.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed.
- Tardigrade-Derived Strategy for Low-Cost Storage of Cell-Free Expression Lysates.ACS synthetic biology · 2026Article
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Integrative bioinformatics analysis of potential convergent evolution in tardigrade stress-response proteins.Stress biology · 2026Article
- Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- OsmoFold: A high-throughput tool for predicting the impact of osmolytes on protein structure.Biophysical journal · 2025Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic-abundant heat-soluble proteins during drying.Protein science : a publication of the Protein Society · 2025Article
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Article
- Radioprotection redefined: drug discovery at the intersection of tardigrade biology and translational pharmacology.Frontiers in pharmacology · 2025Article
- Metabolite phosphatase from anhydrobiotic tardigrades.The FEBS journal · 2024Article
- Disordered proteins interact with the chemical environment to tune their protective function during drying.eLife · 2024Article
- An evaluation of thermal tolerance in six tardigrade species in an active and dry state.Biology open · 2024Article
- Trimethylamine N-oxide (TMAO) doubly locks the hydrophobic core and surfaces of protein against desiccation stress.Protein science : a publication of the Protein Society · 2024Article
- Tardigrade secretory proteins protect biological structures from desiccation.Communications biology · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Protective roles of highly conserved motif 1 in tardigrade cytosolic-abundant heat soluble protein in extreme environments.Protein science : a publication of the Protein Society · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Protein-based biological drugs and many industrial enzymes are unstable, making them prohibitively expensive. Some can be stabilized by formulation with excipients, but most still require low temperature storage. In search of new, more robust excipients, we turned to the tardigrade, a microscopic animal that synthesizes cytosolic abundant heat soluble (CAHS) proteins to protect its cellular components during desiccation. We find that CAHS proteins protect the test enzymes lactate dehydrogenase and lipoprotein lipase against desiccation-, freezing-, and lyophilization-induced deactivation. Our data also show that a variety of globular and disordered protein controls, with no known link to desiccation tolerance, protect our test enzymes. Protection of lactate dehydrogenase correlates, albeit imperfectly, with the charge density of the protein additive, suggesting an approach to tune protection by modifying charge. Our results support the potential use of CAHS proteins as stabilizing excipients in formulations and suggest that other proteins may have similar potential.
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.