ArticleFrontiers in molecular biosciences2021
Unraveling the Thermodynamics of Ultra-tight Binding of Intrinsically Disordered Proteins.
Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025Review
- ChiraKit: an online tool for the analysis of circular dichroism spectroscopy data.Nucleic acids research · 2025Article
- A single vector system for tunable and homogeneous dual gene expression in Escherichia coli.Scientific reports · 2025Article
- Extending MeCP2 interactome: canonical nucleosomal histones interact with MeCP2.Nucleic acids research · 2024Article
- Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae.Nature communications · 2024Article
- The Thermodynamic Fingerprints of Ultra-Tight Nanobody-Antigen Binding Probed via Two-Color Single-Molecule Coincidence Detection.International journal of molecular sciences · 2023Article
- The free energy folding penalty accompanying binding of intrinsically disordered α-helical motifs.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein interactions mediated by the intrinsically disordered proteins (IDPs) are generally associated with lower affinities compared to those between globular proteins. Here, we characterize the association between the intrinsically disordered HigA2 antitoxin and its globular target HigB2 toxin from
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Registered trials
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