ArticleFrontiers in molecular biosciences2022
Shape Complementarity Optimization of Antibody-Antigen Interfaces: The Application to SARS-CoV-2 Spike Protein.
Article in Frontiers in molecular biosciences, 2022. 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, 14 citations in OpenAlex.
- Preventing Pathogenic Dimerization in a Misfolded Antibody Light Chain through the Design of an Inhibitory Peptide.The journal of physical chemistry. B · 2026Article
- Antibody Screening and Binding Prediction Analysis Targeting Stx2.Antibodies (Basel, Switzerland) · 2026Article
- Zepyros: a webserver to evaluate the shape complementarity of protein-protein interfaces.Bioinformatics advances · 2025Article
- Insights into the role of dynamical features in protein complex formation: The case of SARS-CoV-2 spike binding with ACE2.Computational and structural biotechnology journal · 2025Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Radiothermal Emission of Nanoparticles with a Complex Shape as a Tool for the Quality Control of Pharmaceuticals Containing Biologically Active Nanoparticles.Pharmaceutics · 2023Article
- Structural Complementarity of Bruton's Tyrosine Kinase and Its Inhibitors for Implication in B-Cell Malignancies and Autoimmune Diseases.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Design of protein-binding peptides with controlled binding affinity: the case of SARS-CoV-2 receptor binding domain and angiotensin-converting enzyme 2 derived peptides.Frontiers in molecular biosciences · 2023Article
- Computational structural-based GPCR optimization for user-defined ligand: Implications for the development of biosensors.Computational and structural biotechnology journal · 2023Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many factors influence biomolecule binding, and its assessment constitutes an elusive challenge in computational structural biology. In this aspect, the evaluation of shape complementarity at molecular interfaces is one of the main factors to be considered. We focus on the particular case of antibody-antigen complexes to quantify the complementarities occurring at molecular interfaces. We relied on a method we recently developed, which employs the 2D Zernike descriptors, to characterize the investigated regions with an ordered set of numbers summarizing the local shape properties. Collecting a structural dataset of antibody-antigen complexes, we applied this method and we statistically distinguished, in terms of shape complementarity, pairs of the interacting regions from the non-interacting ones. Thus, we set up a novel computational strategy based on
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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.