F. Pesce

WWP2 MEDIATES THE METABOLIC REPROGRAMMING OF RENAL MYOFIBROBLASTS TO PROMOTE KIDNEY FIBROSIS

This paper identifies WWP2 as a regulator of myofibroblast metabolic reprogramming in renal fibrosis, showing it suppresses PGC-1 to alter metabolic pathways and reduce fibrosis severity.

Design of intrinsically disordered protein variants with diverse structural properties

This paper introduces a physics-based algorithm to design intrinsically disordered proteins with specified structural properties, demonstrating high accuracy in predicting compaction and phase separation behavior.

Revisiting the use of dioxane as a reference compound for determination of the hydrodynamic radius of proteins by pulsed field gradient NMR spectroscopy

The paper revisits the use of dioxane as a reference compound in PFG NMR to determine protein hydrodynamic radius, finding the current reference value underestimated and proposing a new value.

Conformational ensembles of the human intrinsically disordered proteome: Bridging chain compaction with function and sequence conservation

The paper develops a model to predict conformational ensembles of human intrinsically disordered regions (IDRs) from sequence, showing correlations between chain compaction, function, localization, and sequence conservation across orthologs.

Combining experiments and simulations to examine the temperature-dependent behaviour of a disordered protein

The paper combines molecular dynamics simulations and experimental data to study temperature effects on Histatin 5's conformational behavior, finding agreement with some data but not all.

Deciphering the alphabet of disorder -- Glu and Asp act differently on local but not global properties

This study compares the functional and structural differences between glutamate and aspartate in intrinsically disordered proteins using experimental and computational methods.

Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins

The paper evaluates models for calculating the hydrodynamic radius of intrinsically disordered proteins using conformational ensembles validated by small-angle X-ray scattering and finds the Kirkwood-Riseman equation to be the most accurate.

Improving Martini 3 for disordered and multidomain proteins

This study improves the Martini 3 force field for simulating disordered and multidomain proteins by adjusting protein-water interactions to better match experimental data.

Refining conformational ensembles of flexible proteins against small-angle X-ray scattering data

This paper presents a protocol to refine conformational ensembles of flexible proteins using SAXS data and a Bayesian/Maximum Entropy framework, identifying robust parameter sets for accurate modeling.