Bruno E. Correia

May 28, 2024 | nature.com | Aaron S. Petruzzella |Marine Bruand |Albert Santamaria-Martínez |Natalya Katanayeva |Luc Reymond |Sandrine Georgeon | +6 more

AbstractCysteine cathepsins are a family of proteases that are relevant therapeutic targets for the treatment of different cancers and other diseases. However, no clinically approved drugs for these proteins exist, as their systemic inhibition can induce deleterious side effects. To address this problem, we developed a modular antibody-based platform for targeted drug delivery by conjugating non-natural peptide inhibitors (NNPIs) to antibodies.

Feb 2, 2024 | biorxiv.org | Bruno E. Correia

AbstractA major challenge in the field of computational de novo protein design is the exploration of uncharted areas within protein structural space, i.e., generating "designable" protein structures that nature has not explored. However, the large degrees of freedom of protein structural backbones complicate the sampling process during protein design.

Sep 22, 2023 | cell.com | Sanford Research |Pablo Gainza |Bruno E. Correia

Highlights•Systematic analysis of GPCR enzymatic activity unveils G protein selectivity across 124 GPCRs•Functional rank-order-based classification for GPCRs is introduced•Machine learning accurately predicts GPRC-Gα selectivity•Natural genetic variation in GPCRs influences their G protein preferencesSummaryG protein-coupled receptors (GPCRs) convert extracellular stimuli into intracellular signaling by coupling to heterotrimeric G proteins of four classes: Gi/o, Gq, Gs, and G12/13.