Biomedical subjects

Silvio C E Tosatto

Publications and source records attributed to Silvio C E Tosatto.

3 recordsLinked to original sources

PubMed2026

Open and sustainable AI: challenges, opportunities and the road ahead in the life sciences.

Artificial intelligence (AI) has seen transformative breakthroughs in the life sciences, expanding possibilities to interpret biological information at an unprecedented capacity. To maximize return on growing investments and accelerate progress, it is urgent to address long-standing research challenges arising from the rapid adoption of AI methods. We review the erosion of trust in AI outputs driven by poor reusability and reproducibility, and highlight their impact on environmental sustainability. Furthermore, we discuss the fragmented components of the AI ecosystem and lack of guiding pathways to support open and sustainable AI model development. In response, this Perspective introduces practical open and sustainable AI recommendations mapped to over 300 ecosystem components and provides guiding implementation pathways. Our work connects researchers with relevant AI resources, facilitating the implementation of sustainable, reusable and reproducible AI. Built upon community consensus and aligned to existing efforts, these outputs will aid future policy development and structured pathways for guiding AI implementation.

Artificial Intelligence↗

PubMed2025

GeomeTRe: accurate calculation of geometrical descriptors of tandem repeat proteins.

MOTIVATION: Structured tandem repeat proteins (STRPs) are characterized by preserved structural motifs arranged in a modular way. The structural and functional diversity of STRPs makes them particularly important for studying evolution and novel structure-function relationships, and ultimately for designing new synthetic proteins with specific functions. One crucial aspect of their classification is the estimation of geometrical parameters, which can provide better insight into their properties and the relationship between the spatial arrangement of repeated units and protein function. Calculating geometric descriptors for STRPs is challenging because naturally occurring repeats are not "perfect" and often contain insertions and deletions. Existing tools for predicting structural symmetry work well on simple cases but often fail for most natural proteins. RESULTS: Here, we present GeomeTRe, an algorithm that calculates geometrical descriptors such as curvature (yaw), twist (roll), and pitch for a protein structure with known repeat unit positions. The algorithm simulates the movement of consecutive units, identifies rotational axes, and calculates the corresponding Tait-Bryan angles. GeomeTRe's parameters can enhance STRP annotation and classification by identifying variations in geometric arrangements among different functional groups. The package is fast and suitable for processing large protein structure datasets when repeat region information (e.g. from RepeatsDB) is available. AVAILABILITY AND IMPLEMENTATION: GeomeTRe is available as a Python package; source code and documentation can be found at https://github.com/BioComputingUP/GeomeTRe.

Algorithms↗

PubMed2025

MobiDB-lite 4.0: faster prediction of intrinsic protein disorder and structural compactness.

MOTIVATION: In recent years, many disorder predictors have been developed to identify intrinsically disordered regions (IDRs) in proteins, achieving high accuracy. However, it may be difficult to interpret differences in predictions across methods. Consensus methods offer a simple solution, highlighting reliable predictions while filtering out uncertain positions. Here, we present a new version of MobiDB-lite, a consensus method designed to predict long IDRs and classify them based on compositional biases and conformational properties. RESULTS: MobiDB-lite 4.0 pipeline was optimized to be ten times faster than the previous version. It now provides compactness annotations based on predicted apparent scaling exponent. The newly added features and disorder subclassifications allow the users to get a comprehensive insight into the protein's function and characteristics. MobiDB-lite 4.0 is integrated into the MobiDB and DisProt databases. A version without the compactness predictor is integrated into InterProScan, propagating MobiDB-lite annotations to UniProtKB. AVAILABILITY AND IMPLEMENTATION: The MobiDB-lite 4.0 source code and a Docker container are available from the GitHub repository: https://github.com/BioComputingUP/MobiDB-lite.

Intrinsically Disordered Proteins↗