{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T15:49:23Z","timestamp":1783698563255,"version":"3.55.0"},"reference-count":96,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2024,1,20]],"date-time":"2024-01-20T00:00:00Z","timestamp":1705708800000},"content-version":"vor","delay-in-days":19,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,1,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The post-translational modifications occur as crucial molecular regulatory mechanisms utilized to regulate diverse cellular processes. Malonylation of proteins, a reversible post-translational modification of lysine\/k residues, is linked to a variety of biological functions, such as cellular regulation and pathogenesis. This modification plays a crucial role in metabolic pathways, mitochondrial functions, fatty acid oxidation and other life processes. However, accurately identifying malonylation sites is crucial to understand the molecular mechanism of malonylation, and the experimental identification can be a challenging and costly task. Recently, approaches based on machine learning (ML) have been suggested to address this issue. It has been demonstrated that these procedures improve accuracy while lowering costs and time constraints. However, these approaches also have specific shortcomings, including inappropriate feature extraction out of protein sequences, high-dimensional features and inefficient underlying classifiers. As a result, there is an urgent need for effective predictors and calculation methods. In this study, we provide a comprehensive analysis and review of existing prediction models, tools and benchmark datasets for predicting malonylation sites in protein sequences followed by a comparison study. The review consists of the specifications of benchmark datasets, explanation of features and encoding methods, descriptions of the predictions approaches and their embedding ML or deep learning models and the description and comparison of the existing tools in this domain. To evaluate and compare the prediction capability of the tools, a new bunch of data has been extracted based on the most updated database and the tools have been assessed based on the extracted data. Finally, a hybrid architecture consisting of several classifiers including classical ML models and a deep learning model has been proposed to ensemble the prediction results. This approach demonstrates the better performance in comparison with all prediction tools included in this study (the source codes of the models presented in this manuscript are available in https:\/\/github.com\/Malonylation).<\/jats:p>\n               <jats:p>Database URL: https:\/\/github.com\/A-Golshan\/Malonylation<\/jats:p>","DOI":"10.1093\/database\/baad094","type":"journal-article","created":{"date-parts":[[2024,1,21]],"date-time":"2024-01-21T01:32:20Z","timestamp":1705800740000},"source":"Crossref","is-referenced-by-count":9,"title":["Analysis and review of techniques and tools based on machine learning and deep learning for prediction of lysine malonylation sites in protein sequences"],"prefix":"10.1093","volume":"2024","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4131-2919","authenticated-orcid":false,"given":"Shahin","family":"Ramazi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seyed Amir Hossein","family":"Tabatabaei","sequence":"additional","affiliation":[{"name":"Department of Computer Science, Faculty of Mathematical Sciences, University of Guilan , Namjoo St. Postal, Rasht 41938-33697, Iran"},{"name":"Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University , Jalal AleAhmad, Tehran 14117-13116, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elham","family":"Khalili","sequence":"additional","affiliation":[{"name":"Department of Plant Sciences, Faculty of Science, Tarbiat Modares University , Jalal AleAhmad, Tehran 14117-13116, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amirhossein Golshan","family":"Nia","sequence":"additional","affiliation":[{"name":"Department of Mathematics and Computer Science, Amirkabir University of Technology , No. 350, Hafez Ave, Tehran 15916-34311, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiomars","family":"Motarjem","sequence":"additional","affiliation":[{"name":"Department of Statistics, Faculty of Mathematical Sciences, Tarbiat Modares University , Jalal AleAhmad, Tehran 14117-13116, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,1,19]]},"reference":[{"key":"2024062912161593900_R1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12038-020-00099-2","article-title":"Evaluation of post-translational modifications in histone proteins: a review on histone modification defects in developmental and neurological disorders","volume":"45","author":"Ramazi","year":"2020","journal-title":"J. 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