ReviewInternational journal of molecular sciences2009
Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.
Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- A multidomain hydrolase from the thermophile Thermanaeromonas toyohensis degrades high molecular mass forms of polyhydroxybutyrate.Protein science : a publication of the Protein Society · 2025Article
- Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.Acta crystallographica. Section D, Structural biology · 2024Article
- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results.International journal of molecular sciences · 2018Review
- Article
- Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues.Scientific reports · 2015Article
- Interactions with the bifunctional interface of the transcriptional coactivator DCoH1 are kinetically regulated.The Journal of biological chemistry · 2015Article
- Article
- Article
- Psychrophilic enzymes: from folding to function and biotechnology.Scientifica · 2013Review
- Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins.BMC evolutionary biology · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on the differences in their optimal growth temperatures microorganisms can be classified into psychrophiles, mesophiles, thermophiles, and hyperthermophiles. Proteins from hyperthermophiles generally exhibit greater stability than those from other organisms. In this review, we collect data about the stability and folding of monomeric proteins from hyperthermophilies with reversible unfolding, from the equilibrium and kinetic aspects. The results indicate that slow unfolding is a general strategy by which proteins from hyperthermophiles adapt to higher temperatures. Hydrophobic interaction is one of the factors in the molecular mechanism of the slow unfolding of proteins from hyperthermophiles.
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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.