ArticleInternational journal of molecular sciences2019
Structural and Computational Characterization of Disease-Related Mutations Involved in Protein-Protein Interfaces.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Decoding the functional impact of the cancer genome through protein-protein interactions.Nature reviews. Cancer · 2025Review
- A Multivalent DNA Nanoparticle/Peptide Hybrid Molecular Modality for the Modulation of Protein-Protein Interactions in the Tumor Microenvironment.Advanced nanobiomed research · 2024Article
- On the linkage of thermodynamics and pathogenicity.Current opinion in structural biology · 2023Review
- Porphyromonas gingivalis induction of TLR2 association with Vinculin enables PI3K activation and immune evasion.PLoS pathogens · 2023Article
- PROT-ON: A structure-based detection of designer PROTein interface MutatiONs.Frontiers in molecular biosciences · 2023Article
- A Comprehensive Study of De Novo Mutations on the Protein-Protein Interaction Interfaces Provides New Insights into Developmental Delay.Biomolecules · 2022Article
- The properties of human disease mutations at protein interfaces.PLoS computational biology · 2022Article
- Implications of disease-related mutations at protein-protein interfaces.Current opinion in structural biology · 2022Review
- Using collections of structural models to predict changes of binding affinity caused by mutations in protein-protein interactions.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
One of the known potential effects of disease-causing amino acid substitutions in proteins is to modulate protein-protein interactions (PPIs). To interpret such variants at the molecular level and to obtain useful information for prediction purposes, it is important to determine whether they are located at protein-protein interfaces, which are composed of two main regions, core and rim, with different evolutionary conservation and physicochemical properties. Here we have performed a structural, energetics and computational analysis of interactions between proteins hosting mutations related to diseases detected in newborn screening. Interface residues were classified as core or rim, showing that the core residues contribute the most to the binding free energy of the PPI. Disease-causing variants are more likely to occur at the interface core region rather than at the interface rim (
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Registered trials
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