ReviewJournal of the Royal Society, Interface2013
On the binding affinity of macromolecular interactions: daring to ask why proteins interact.
Review in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
198 citing papers in PubMed, 1 synthesis or guideline pooled it.
- An Experimental Framework for Developing Point-of-Need Biosensors: Connecting Bio-Layer Interferometry and Electrochemical Impedance Spectroscopy.Biosensors · 2022Pooled it
- Article
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- Evolutionary Divergence, Predicted Interaction Interface, and Regulatory Specialization of MTB as a Non-Catalytic Scaffold in the Plant m6A Writer Complex.Current issues in molecular biology · 2026Article
- Mapping the dynamic plant interactome: from in vitro assays to in vivo quantitative approaches.Plant methods · 2026Review
- Comparative structural analysis of protein complexes with SPICE.Nucleic acids research · 2026Article
- USP-ddG: a unified structural paradigm with data efficacy and mixture-of-experts for predicting mutational effects on protein-protein interactions.Bioinformatics (Oxford, England) · 2026Article
- Pharmacological principles of intravitreal drug therapy and their implications for clinical practice: a primer for the ophthalmologist.Eye (London, England) · 2026Review
- Comparative analysis of anti-MICA scFv affinities: Insights from three label-free biophysical methods and biological validation.Biotechnology reports (Amsterdam, Netherlands) · 2026Article
- Global protein-ligand binding affinity profiling via photocatalytic labeling.Nature communications · 2026Article
- Time-Resolved Native Mass Spectrometry for Direct Measurement of Biomolecular Kinetics.Journal of the American Chemical Society · 2026Article
- Quantifying Protein Homodimer Affinities and the Effect of Molecular Glues and Interface Residues Using Native Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Molecular dynamics reveals how calcium drives hetero- versus homotrimerization of type I collagen.Biophysical journal · 2026Article
- Antiemetic Efficacy of Nodakenin Through Muscarinic, Dopaminergic, and Serotonergic Receptor Modulation: Combined Experimental and Computational Approach.Cell biochemistry and biophysics · 2026Article
- Integrating deep learning with physics based modeling enables high precision antibody antigen interface prediction.Scientific reports · 2026Article
- A rapid test for protein-DNA interactions.Nucleic acids research · 2026Article
- Discovering, Integrating, and Reinterpreting the Molecular Logic of Life: From Classical Theories of Heredity to an Extended Functional Perspective on the Central Dogma.Life (Basel, Switzerland) · 2026Review
- Deciphering Protein Interaction Dynamics Using the Yeast Three-Hybrid System.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Integrative in vitro and in silico evaluation of HSP60-derived peptides as immunomodulators of the TLR4/MD-2 complex.Scientific reports · 2025Article
- Skin-Integrated Soft Wearable XR Interfaces for Seamless and Realistic User Experience.Chemical reviews · 2025Review
138 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions between proteins are orchestrated in a precise and time-dependent manner, underlying cellular function. The binding affinity, defined as the strength of these interactions, is translated into physico-chemical terms in the dissociation constant (K(d)), the latter being an experimental measure that determines whether an interaction will be formed in solution or not. Predicting binding affinity from structural models has been a matter of active research for more than 40 years because of its fundamental role in drug development. However, all available approaches are incapable of predicting the binding affinity of protein-protein complexes from coordinates alone. Here, we examine both theoretical and experimental limitations that complicate the derivation of structure-affinity relationships. Most work so far has concentrated on binary interactions. Systems of increased complexity are far from being understood. The main physico-chemical measure that relates to binding affinity is the buried surface area, but it does not hold for flexible complexes. For the latter, there must be a significant entropic contribution that will have to be approximated in the future. We foresee that any theoretical modelling of these interactions will have to follow an integrative approach considering the biology, chemistry and physics that underlie protein-protein recognition.
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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.