ArticleEvolution; international journal of organic evolution2008
Enzyme isoforms may increase phenotypic robustness.
Article in Evolution; international journal of organic evolution, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed.
- Modelling the prebiotic origins of regulation and agency in evolving protocell ecologies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Advances in Activity-Based Sensing Probes for Isoform-Selective Imaging of Enzymatic Activity.Angewandte Chemie (International ed. in English) · 2021Review
- Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.Open biology · 2020Review
- Flexible selection of diversified Na(+)/K(+)-ATPase α-subunit isoforms for osmoregulation in teleosts.Zoological letters · 2016Article
- Determining the contributions of divisive and subtractive feedback in the Hodgkin-Huxley model.Journal of computational neuroscience · 2014Article
- Genomic identification of a putative circadian system in the cladoceran crustacean Daphnia pulex.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2011Article
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Authors and funding
3 authors.
Funding
Abstract
Enzyme isoforms are found in many cellular reactions, and can differ in the kind of reaction they catalyze, in their substrate affinity, or in their reaction rates. The evolutionary significance of enzyme isoforms is only partially understood. We used mathematical modeling to investigate the hypothesis that isoforms may be favored by selection because they can increase the phenotypic robustness of the system. We modify a model for circadian clock gene expression in Drosophila to incorporate the presence of isoforms in the phosphorylation pathway of the period gene. We consider the case in which different isoforms catalyze the same reaction but have different affinities for the substrate. Stability is increased if there is dynamic control of the expression of isoforms relative to each other. Thus, we show that controlling isoform proportion can be a powerful mechanism for reducing the effects of variations in the values of system parameters, increasing system robustness.
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Registered trials
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