Litcius/Paper detail

ENTAIL: yEt aNoTher amyloid fIbrils cLassifier

Alessia Auriemma Citarella, Luigi Di Biasi, Fabiola De Marco, Genoveffa Tortora

2022BMC Bioinformatics21 citationsDOIOpen Access PDF

Abstract

BACKGROUND: This research aims to increase our knowledge of amyloidoses. These disorders cause incorrect protein folding, affecting protein functionality (on structure). Fibrillar deposits are the basis of some wellknown diseases, such as Alzheimer, Creutzfeldt-Jakob diseases and type II diabetes. For many of these amyloid proteins, the relative precursors are known. Discovering new protein precursors involved in forming amyloid fibril deposits would improve understanding the pathological processes of amyloidoses. RESULTS: A new classifier, called ENTAIL, was developed using over than 4000 molecular descriptors. ENTAIL was based on the Naive Bayes Classifier with Unbounded Support and Gaussian Kernel Type, with an accuracy on the test set of 81.80%, SN of 100%, SP of 63.63% and an MCC of 0.683 on a balanced dataset. CONCLUSIONS: The analysis carried out has demonstrated how, despite the various configurations of the tests, performances are superior in terms of performance on a balanced dataset.

Topics & Concepts

Classifier (UML)Naive Bayes classifierComputer scienceAmyloid fibrilProtein foldingComputational biologyArtificial intelligencePattern recognition (psychology)FibrillogenesisAmyloid (mycology)FibrilBayes' theoremMachine learningSupport vector machineBioinformaticsChemistryBiologyAmyloid βMedicinePathologyDiseaseBayesian probabilityBiochemistryMachine Learning in BioinformaticsBioinformatics and Genomic Networksvaccines and immunoinformatics approaches