ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2002
Molecular basis of cold adaptation.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 278 citations in OpenAlex.
- Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation.The FEBS journal · 2026Article
- Crystallography of Extremophile Proteins-Structural Comparisons of Psychrophilic and Hyperthermophilic Rubredoxins.Biomolecules · 2026Article
- Some Like It Hot -Structural Changes in Extremophile Rubredoxin at 120 °C.Angewandte Chemie (International ed. in English) · 2026Article
- Structural and Functional Variations of Enzymes Indicate Latitudinal Adaptations of Subarctic and Arctic Sea Urchins.Ecology and evolution · 2025Article
- Evolutionary-scale enzymology enables exploration of a rugged catalytic landscape.Science (New York, N.Y.) · 2025Article
- Novel Antarctic Endo-Polygalacturonase for Pectin Extraction and Vegetal Tissue Maceration at Mild Temperatures.Applied biochemistry and biotechnology · 2025Article
- High-Spin States of Manganese(III) Enable Robust Cold-Adapted Activity of MnOAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Dynamic energy conversion in protein catalysis: From brownian motion to enzymatic function.Computational and structural biotechnology journal · 2025Review
- Macrogenomic Analysis Reveals Soil Microbial Diversity in Different Regions of the Antarctic Peninsula.Microorganisms · 2024Article
- Psychrotrophic Bacteria Threatening the Safety of Animal-Derived Foods: Characteristics, Contamination, and Control Strategies.Food science of animal resources · 2024Review
- Temperature-dependent iron motion in extremophile rubredoxins - no need for 'corresponding states'.Scientific reports · 2024Article
- Complete genome sequence data of an Antarctic bacteriumData in brief · 2024Article
- Adaptation strategies of giant viruses to low-temperature marine ecosystems.The ISME journal · 2024Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Ribosomal proteins can hold a more accurate record of bacterial thermal adaptation compared to rRNA.Nucleic acids research · 2023Article
- Isolation and Identification of Bacteria of GenusMicroorganisms · 2023Article
- Effects of Salinity and Temperature on the Flexibility and Function of a Polyextremophilic Enzyme.International journal of molecular sciences · 2022Article
- Rising floor and dropping ceiling: organ heterogeneity in response to cold acclimation of the largest extant amphibian.Proceedings. Biological sciences · 2022Article
- Evidence of selection in the uncoupling protein 1 gene region suggests local adaptation to solar irradiance in savannah monkeys (Proceedings. Biological sciences · 2022Article
- Cold-Active Enzymes and Their Potential Industrial Applications-A Review.Molecules (Basel, Switzerland) · 2022Review
30 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cold-adapted, or psychrophilic, organisms are able to thrive at low temperatures in permanently cold environments, which in fact characterize the greatest proportion of our planet. Psychrophiles include both prokaryotic and eukaryotic organisms and thus represent a significant proportion of the living world. These organisms produce cold-evolved enzymes that are partially able to cope with the reduction in chemical reaction rates induced by low temperatures. As a rule, cold-active enzymes display a high catalytic efficiency, associated however, with a low thermal stability. In most cases, the adaptation to cold is achieved through a reduction in the activation energy that possibly originates from an increased flexibility of either a selected area or of the overall protein structure. This enhanced plasticity seems in turn to be induced by the weak thermal stability of psychrophilic enzymes. The adaptation strategies are beginning to be understood thanks to recent advances in the elucidation of the molecular characteristics of cold-adapted enzymes derived from X-ray crystallography, protein engineering and biophysical methods. Psychrophilic organisms and their enzymes have, in recent years, increasingly attracted the attention of the scientific community due to their peculiar properties that render them particularly useful in investigating the possible relationship existing between stability, flexibility and specific activity and as valuable tools for biotechnological purposes.
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