Francesco Luigi Gervasio

The paper uses simulations to show that V2Rpp binding broadens the conformational landscape of arrestin-2 beyond C-tail detachment, with interdomain rotation angles being less favored without V2Rpp.

This study designs metamorphic proteins that switch between multiple conformations and shows how mutations can shift their conformational equilibrium.

This study shows that disrupting pathological EGFR catalytic trimers reverses gefitinib resistance by rewiring signaling and slowing tumor growth.

The paper investigates how structural differences in Bcl2 proteins affect BH3 domain interactions and apoptotic function using simulations and experimental validation.

This study uses simulations to show that buprenorphine restricts the conformational states of the μ-opioid receptor compared to endomorphin-1, affecting signaling bias and efficacy.

This study provides the structural model of the Bcl-xL/tBid complex at the mitochondrial membrane, revealing its dynamic architecture and mechanism of indirect apoptosis inhibition.

The paper determines cryo-EM structures of MEK1 activating ERK2, elucidating specificity and activation mechanisms in the MAPK pathway.

CryptoBank identifies cryptic binding sites in proteins using structural alignments and a machine learning model, enabling prediction from sequence data with high precision.

This paper introduces a computational framework to calculate activation free energies for class A GPCRs, showing agreement with previous methods and providing new insights for the μ-opioid receptor.

This study uses molecular dynamics to analyze TREK-2 channel conformational changes, linking them to disease mechanisms and drug discovery.

This paper introduces a data-driven method to construct solvation-based collective variables for molecular dynamics simulations, achieving accurate binding free energy landscapes with improved efficiency.

This paper introduces bio-inspired collective variables to improve protein folding simulations, accurately resolving free energy landscapes and identifying intermediates like the dry molten globule.

This study uses OneOPES to analyze the activation mechanism of ADRB1, revealing water-mediated interactions and structural changes important for receptor activation.

This paper introduces an automated OneOPES protocol to improve binding free energy estimation in host-guest systems by enhancing sampling and enabling systematic force field comparison.

This study uses machine learning to simulate conformational changes in pre-miR21, showing how L50 affects its structure and suggesting a computational platform for inhibitor screening.

The paper reports the cryo-EM structure of connexin-36 bound to mefloquine, revealing how small molecules inhibit gap junction channels by partially occluding the pore and altering electrostatics.