ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural flexibility and protein adaptation to temperature: Molecular dynamics analysis of malate dehydrogenases of marine molluscs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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114 citing papers in PubMed, 310 citations in OpenAlex.
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- Structural mechanisms for cold-adapted activity of phosphoenolpyruvate carboxykinase.Protein science : a publication of the Protein Society · 2025Article
- Temperature adaptation in structure and function in lactate dehydrogenase-A reflects convergent evolution in a few key protein regions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Analysing protein complexes in plant science: insights and limitation with AlphaFold 3.Botanical studies · 2025Review
- RNA editing generates mRNA isoforms with distinct stabilities that may expand the thermal tolerance of mRNA and proteins inZoological research · 2025Article
- Network pharmacology, molecular docking, molecular dynamics simulation, and experiment verification analysis to reveal the action mechanism of RenShen Guipi Wan in the treatment of anemia.Biotechnology letters · 2025Article
- Bioactive structures for inhibitors ofFuture medicinal chemistry · 2025Article
- Thermal Adaptation of Cytosolic Malate Dehydrogenase Revealed by Deep Learning and Coevolutionary Analysis.Journal of chemical theory and computation · 2025Article
- Phylogenetic history and temperature adaptation contribute to structural and functional stability of proteins in marine mollusks.Communications biology · 2025Article
- An insight for the inhibition of anxiolytic and anti-convulsant effects in zebrafish using the curcumins via exploring molecular docking and molecular dynamics simulations.Molecular diversity · 2025Article
54 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
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Abstract
Orthologous proteins of species adapted to different temperatures exhibit differences in stability and function that are interpreted to reflect adaptive variation in structural "flexibility." However, quantifying flexibility and comparing flexibility across proteins has remained a challenge. To address this issue, we examined temperature effects on cytosolic malate dehydrogenase (cMDH) orthologs from differently thermally adapted congeners of five genera of marine molluscs whose field body temperatures span a range of ∼60 °C. We describe consistent patterns of convergent evolution in adaptation of function [temperature effects on
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