activity
20202024
most citedInvestigating the side-chain structural organization behind the stability of protein folding and binding

101 citations · 319 across the 9 of their papers we have counts for

collaborators

9 papers

q-bio.BM2024★ 2 cited

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

Greta Grassmann, Lorenzo Di Rienzo, Giancarlo Ruocco +2

Predicting interactions between biomolecules, such as protein-protein complexes, remains a challenging problem. Despite the many advancements done so far, the performances of docki…

q-bio.QM2024★ 2 cited

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

Mattia Miotto, Lorenzo Di Rienzo, Leonardo Bo' +2

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…

q-bio.BM2022★ 58 cited

Electrostatic complementarity at the interface drives transient protein-protein interactions

Greta Grassmann, Lorenzo Di Rienzo, Giorgio Gosti +4

Understanding the molecular mechanisms driving the binding between bio-molecules is a crucial challenge in molecular biology. In this respect, characteristics like the preferential…

physics.bio-ph2021★ 101 cited

Investigating the side-chain structural organization behind the stability of protein folding and binding

Fausta Desantis, Mattia Miotto, Lorenzo Di Rienzo +2

What are the molecular mechanisms that dictate protein-protein binding stability and whether those are related to the ones behind protein fold stability are still largely open ques…

physics.bio-ph2021

New algorithm to determine a minimal representation of the molecular surface

Greta Grassmann, Mattia Miotto, Lorenzo Di Rienzo +3

Most proteins perform their biological function by interacting with one or more molecular partners. In this respect, characterizing the features of the molecular surface, especiall…

q-bio.BM2021★ 14 cited

Shape Complementarity Optimization of Antibody-Antigen Interfaces: the Application to SARS-CoV-2 Spike Protein

Alfredo De Lauro, Lorenzo Di Rienzo, Mattia Miotto +3

Many factors influence biomolecules binding, and its assessment constitutes an elusive challenge in computational structural biology. In this respect, the evaluation of shape compl…

q-bio.BM2020★ 47 cited

Molecular mechanisms behind anti SARS-CoV-2 action of lactoferrin

Mattia Miotto, Lorenzo Di Rienzo, Leonardo Bò +3

Despite the huge effort to contain the infection, the novel SARS-CoV-2 coronavirus has rapidly become pandemics, mainly due to its extremely high human-to-human transmission capabi…

q-bio.PE2020★ 43 cited

Does blood type affect the COVID-19 infection pattern?

Mattia Miotto, Lorenzo Di Rienzo, Giorgio Gosti +2

Among the many aspects that characterize the COVID-19 pandemic, two seem particularly challenging to understand: (i) the great geographical differences in the degree of virus conta…

physics.bio-ph2020★ 52 cited

In-Silico evidence for two receptors based strategy of SARS-CoV-2

Edoardo Milanetti, Mattia Miotto, Lorenzo Di Rienzo +3

We propose a novel numerical method able to determine efficiently and effectively the relationship of complementarity between portions of proteins surfaces. This innovative and gen…