ArticleJournal of molecular biology2011
Thermodynamic analysis of mutant lac repressors.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- LacI strikes a balance between stability and inducibility.Nucleic acids research · 2026Article
- The Dynamics of Inducible Genetic Circuits.ArXiv · 2026Article
- Model-guided design of regulatable promoters for synthetic biology.Current opinion in microbiology · 2026Review
- Synthetic Biology of Plants and Microbes for Agriculture, Environment, and Future Applications.Chemical reviews · 2026Review
- A parameterized two-domain thermodynamic model explains diverse mutational effects on protein allostery.eLife · 2024Article
- A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery.bioRxiv : the preprint server for biology · 2024Article
- Genetic switching by the Lac repressor is based on two-state Monod-Wyman-Changeux allostery.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Quantifying the regulatory role of individual transcription factors in Escherichia coli.Cell reports · 2021Article
- The genotype-phenotype landscape of an allosteric protein.Molecular systems biology · 2021Article
- Engineered signal-coupled inducible promoters: measuring the apparent RNA-polymerase resource budget.Nucleic acids research · 2020Article
- Homolog comparisons further reconcile in vitro and in vivo correlations of protein activities by revealing over-looked physiological factors.Protein science : a publication of the Protein Society · 2019Article
- Predictive shifts in free energy couple mutations to their phenotypic consequences.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Figure 1 Theory Meets Figure 2 Experiments in the Study of Gene Expression.Annual review of biophysics · 2019Review
- Mapping DNA sequence to transcription factor binding energy in vivo.PLoS computational biology · 2019Article
- Escherichia coli "Marionette" strains with 12 highly optimized small-molecule sensors.Nature chemical biology · 2019Article
- Tuning Transcriptional Regulation through Signaling: A Predictive Theory of Allosteric Induction.Cell systems · 2018Article
- Tuning the dynamic range of bacterial promoters regulated by ligand-inducible transcription factors.Nature communications · 2018Article
- Theoretical analysis of inducer and operator binding for cyclic-AMP receptor protein mutants.PloS one · 2018Article
- Theory in Biology: Figure 1 or Figure 7?Trends in cell biology · 2015Review
- An Autogenously Regulated Expression System for Gene Therapeutic Ocular Applications.Scientific reports · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The lactose (lac) repressor is an allosteric protein that can respond to environmental changes. Mutations introduced into the DNA binding domain and the effector binding pocket affect the repressor's ability to respond to its environment. We have demonstrated how the observed phenotype is a consequence of altering the thermodynamic equilibrium constants. We discuss mutant repressors, which (1) show tighter repression; (2) induce with a previously noninducing species, orthonitrophenyl-β-D-galactoside; and (3) transform an inducible switch to one that is corepressed. The ability of point mutations to change multiple thermodynamic constants, and hence drastically alter the repressor's phenotype, shows how allosteric proteins can perform a wide array of similar yet distinct functions such as that exhibited in the Lac/Gal family of bacterial repressors.
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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.