ArticleBiochemistry2010
Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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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
19 citing papers in PubMed, 39 citations in OpenAlex.
- Mutations to transcription factor MAX allosterically increase DNA selectivity by altering folding and binding pathways.Nature communications · 2025Article
- Asymmetry of Motif Conservation Within Their Homotypic Pairs Distinguishes DNA-Binding Domains of Target Transcription Factors in ChIP-Seq Data.International journal of molecular sciences · 2025Article
- NMR-identification of the interaction between BRCA1 and the intrinsically disordered monomer of the Myc-associated factor X.Protein science : a publication of the Protein Society · 2024Article
- Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces.Science advances · 2022Article
- Hyperpolarized water as universal sensitivity booster in biomolecular NMR.Nature protocols · 2022Review
- Polymorphic tandem DNA repeats activate the human telomerase reverse transcriptase gene.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein.Cells · 2020Review
- Zinc-finger protein YY1 suppresses tumor growth of human nasopharyngeal carcinoma by inactivating c-Myc-mediatedThe Journal of biological chemistry · 2019Article
- Dual regulation ofThe Journal of cell biology · 2019Article
- Myc phosphorylation in its basic helix-loop-helix region destabilizes transient α-helical structures, disrupting Max and DNA binding.The Journal of biological chemistry · 2018Article
- Associating transcription factors and conserved RNA structures with gene regulation in the human brain.Scientific reports · 2017Article
- Quantification of Cooperativity in Heterodimer-DNA Binding Improves the Accuracy of Binding Specificity Models.The Journal of biological chemistry · 2016Article
- Analytical methods for kinetic studies of biological interactions: A review.Journal of pharmaceutical and biomedical analysis · 2015Review
- Article
- Single molecule fluorescence methodologies for investigating transcription factor binding kinetics to nucleosomes and DNA.Methods (San Diego, Calif.) · 2014Article
- The roles of HLH transcription factors in epithelial mesenchymal transition and multiple molecular mechanisms.Clinical & experimental metastasis · 2014Review
- Sequence specificity incompletely defines the genome-wide occupancy of Myc.Genome biology · 2014Article
- Article
- Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translation.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Myc, Mad, and Max proteins belong to the basic helix-loop-helix leucine zipper family of transcription factors. They bind to a specific hexanucleotide element of DNA, the E-box (CACGTG). To be biologically active, Myc and Mad require dimerization with Max. For the route of complex assembly of these dimers, there are two proposed pathways. In the monomer pathway, two monomers bind DNA sequentially and assemble their dimerization interface while bound to DNA. In the dimer pathway, two monomers form a dimer first prior to association with DNA. The monomer pathway is kinetically favored. In this report, stopped-flow polarization was utilized to determine the rates and temperature dependence of all of the individual steps for both assembly pathways. Myc.Max dimerization had a rate constant approximately 5- and approximately 2-fold higher than those of Max.Max and Mad.Max dimerization, respectively. The protein dimerization rates as well as the dimer-DNA rates were found to be independent of concentration, suggesting conformational changes were rate-limiting. The Arrhenius activation energies for the dimerization of Myc, Mad, and Max with Max were 20.4 +/- 0.8, 29 +/- 0.6, and 40 +/- 0.2 kJ/mol, respectively. Further, rate constants for Max.Max homodimer DNA binding are significantly higher than for Myc.Max and Mad.Max heterodimers binding to DNA. Monomer-DNA binding showed a faster rate than dimer-DNA binding. These studies show the rate-limiting step for the dimer pathway is the formation of protein dimers, and this reaction is slower than formation of protein dimers on the DNA interface, kinetically favoring the monomer pathway.
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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.