Computational Approaches to Predict Protein–Protein Interactions in Crowded Cellular Environments

G Grassmann, M Miotto, F Desantis… - Chemical …, 2024 - ACS Publications
Investigating protein–protein interactions is crucial for understanding cellular biological
processes because proteins often function within molecular complexes rather than in …

[HTML][HTML] Model-driven insights into the effects of temperature on metabolism

P Wendering, Z Nikoloski - Biotechnology Advances, 2023 - Elsevier
Temperature affects cellular processes at different spatiotemporal scales, and identifying the
genetic and molecular mechanisms underlying temperature responses paves the way to …

Spatial organization of hydrophobic and charged residues affects protein thermal stability and binding affinity

F Desantis, M Miotto, L Di Rienzo, E Milanetti… - Scientific Reports, 2022 - nature.com
What are the molecular determinants of protein–protein binding affinity and whether they are
similar to those regulating fold stability are two major questions of molecular biology, whose …

Electrostatic complementarity at the interface drives transient protein-protein interactions

G Grassmann, L Di Rienzo, G Gosti, M Leonetti… - Scientific Reports, 2023 - nature.com
Understanding the mechanisms driving bio-molecules binding and determining the resulting
complexes' stability is fundamental for the prediction of binding regions, which is the starting …

Differences in the organization of interface residues tunes the stability of the SARS-CoV-2 spike-ACE2 complex

M Miotto, L Di Rienzo, G Grassmann… - Frontiers in Molecular …, 2023 - frontiersin.org
The continuous emergence of novel variants represents one of the major problems in
dealing with the SARS-CoV-2 virus. Indeed, also due to its prolonged circulation, more than …

Potential of dissimilarity measure-based computation of protein thermal stability data for determining protein interactions

J Teitz, J Sander, H Sarker… - Briefings in …, 2023 - academic.oup.com
Determining the interacting proteins in multiprotein complexes can be technically
challenging. An emerging biochemical approach to this end is based on the 'thermal …

Zepyros: A webserver to evaluate the shape complementarity of protein-protein interfaces

M Miotto, L Di Rienzo, L Bo, G Ruocco… - arXiv preprint arXiv …, 2024 - arxiv.org
Shape complementarity of molecular surfaces at the interfaces is a well-known characteristic
of protein-protein binding regions, and it is critical in influencing the stability of the complex …

[HTML][HTML] DeepTM: A deep learning algorithm for prediction of melting temperature of thermophilic proteins directly from sequences

M Li, H Wang, Z Yang, L Zhang, Y Zhu - Computational and Structural …, 2023 - Elsevier
Thermally stable proteins find extensive applications in industrial production,
pharmaceutical development, and serve as a highly evolved starting point in protein …

Computational evidences of a misfolding event in an aggregation‐prone light chain preceding the formation of the non‐native pathogenic dimer

F Desantis, M Miotto, E Milanetti… - Proteins: Structure …, 2024 - Wiley Online Library
Antibody light chain amyloidosis is a disorder in which protein aggregates, mainly
composed of immunoglobulin light chains, deposit in diverse tissues impairing the correct …

Compact assessment of molecular surface complementarities enhances neural network-aided prediction of key binding residues

G Grassmann, L Di Rienzo, G Ruocco, M Miotto… - arXiv preprint arXiv …, 2024 - arxiv.org
Predicting interactions between biomolecules, such as protein-protein complexes, remains a
challenging problem. Despite the many advancements done so far, the performances of …