Evidence map›Paper›PMID 39799516›Full record

ArticleBioinformatics (Oxford, England)2024

DDGemb: predicting protein stability change upon single- and multi-point variations with embeddings and deep learning.

Castrense Savojardo, Matteo Manfredi, Pier Luigi Martelli, Rita Casadio

Abstract read
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Article in Bioinformatics (Oxford, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

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  6. Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026
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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Castrense SavojardoBiocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, Via San Giacomo 9/2, Bologna, 40126, Italy.ORCID 0000-0002-7359-0633
Matteo ManfrediBiocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, Via San Giacomo 9/2, Bologna, 40126, Italy.ORCID 0000-0001-5479-1723
Pier Luigi MartelliBiocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, Via San Giacomo 9/2, Bologna, 40126, Italy.ORCID 0000-0002-0274-5669
Rita CasadioBiocomputing Group, Department of Pharmacy and Biotechnology, University of Bologna, Via San Giacomo 9/2, Bologna, 40126, Italy.ORCID 0000-0002-7462-7039

Funding

Italian Ministry of University and Research
6 · The paper itself

Abstract

motivationThe knowledge of protein stability upon residue variation is an important step for functional protein design and for understanding how protein variants can promote disease onset. Computational methods are important to complement experimental approaches and allow a fast screening of large datasets of variations.

resultsIn this work, we present DDGemb, a novel method combining protein language model embeddings and transformer architectures to predict protein ΔΔG upon both single- and multi-point variations. DDGemb has been trained on a high-quality dataset derived from literature and tested on available benchmark datasets of single- and multi-point variations. DDGemb performs at the state of the art in both single- and multi-point variations. AVAILABILITY AND IMPLEMENTATION: DDGemb is available as web server at https://ddgemb.biocomp.unibo.it. Datasets used in this study are available at https://ddgemb.biocomp.unibo.it/datasets.

Indexed as

Computational BiologyDeep LearningProteinsSoftwareDatabases, ProteinProtein StabilityProteins

Identifiers

PMID39799516
PMCPMC11783275

What Socratic holds

Textmetadata
LicenceCC BY
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.