Resistance to small-molecule drugs is the main cause of the failure of therapeutic drugs in
clinical practice. Missense mutations altering the binding of ligands to proteins are one of the …

Purpose Mutation-induced variation of protein-ligand binding affinity is the key to many
genetic diseases and the emergence of drug resistance, and therefore predicting such …

Quantitative evaluation of binding affinity changes upon mutations is crucial for protein
engineering and drug design. Machine learning‐based methods are gaining increasing …

Protein–protein Interactions are involved in most fundamental biological processes, with
disease causing mutations enriched at their interfaces. Here we present mCSM-PPI2, a …

Understanding the impact of mutations on protein–protein binding affinity is a key objective
for a wide range of biotechnological applications and for shedding light on disease-causing …

Protein–protein interactions play a crucial role in all cellular functions and biological
processes and mutations leading to their disruption are enriched in many diseases. While a …

The crucial prerequisite for proper biological function is the protein's ability to establish
highly selective interactions with macromolecular partners. A missense mutation that alters …

Missense mutations may affect proteostasis by destabilizing or over-stabilizing protein
complexes and changing the pathway flux. Predicting the effects of stabilizing mutations on …

Modeling the impact of amino acid mutations on protein-protein interaction plays a crucial
role in protein engineering and drug design. In this study, we develop GeoPPI, a novel …

Motivation Protein–protein interactions are essential for the cell and mediate various
functions. However, mutations can disrupt these interactions and may cause diseases …