{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T22:08:31Z","timestamp":1772575711301,"version":"3.50.1"},"reference-count":19,"publisher":"Springer Science and Business Media LLC","issue":"S11","license":[{"start":{"date-parts":[[2020,9,1]],"date-time":"2020-09-01T00:00:00Z","timestamp":1598918400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T00:00:00Z","timestamp":1600041600000},"content-version":"vor","delay-in-days":13,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Bioinformatics"],"published-print":{"date-parts":[[2020,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Background<\/jats:title>\n                <jats:p>S-glutathionylation is the formation of disulfide bonds between the tripeptide glutathione and cysteine residues of the protein, protecting them from irreversible oxidation and in some cases causing change in their functions. Regulatory glutathionylation of proteins is a controllable and reversible process associated with cell response to the changing redox status. Prediction of cysteine residues that undergo glutathionylation allows us to find new target proteins, which function can be altered in pathologies associated with impaired redox status. We set out to analyze this issue and create new tool for predicting S-glutathionylated cysteine residues.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>One hundred forty proteins with experimentally proven S-glutathionylated cysteine residues were found in the literature and the RedoxDB database. These proteins contain 1018 non-S-glutathionylated cysteines and 235\u2009S-glutathionylated ones. Based on 235\u2009S-glutathionylated cysteines, non-redundant positive dataset of 221 heptapeptide sequences of S-glutathionylated cysteines was made. Based on 221 heptapeptide sequences, a position-specific matrix was created by analyzing the protein sequence near the cysteine residue (three amino acid residues before and three after the cysteine). We propose the method for calculating the glutathionylation propensity score, which utilizes the position-specific matrix and a criterion for predicting glutathionylated peptides.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusion<\/jats:title>\n                <jats:p>Non-S-glutathionylated sites were enriched by cysteines in \u2212\u20093 and\u2009+\u20093 positions. The proposed prediction method demonstrates 76.6% of correct predictions of S-glutathionylated cysteines. This method can be used for detecting new glutathionylation sites, especially in proteins with an unknown structure.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s12859-020-03571-w","type":"journal-article","created":{"date-parts":[[2020,9,14]],"date-time":"2020-09-14T01:02:41Z","timestamp":1600045361000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["A novel approach for predicting protein S-glutathionylation"],"prefix":"10.1186","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1763-300X","authenticated-orcid":false,"given":"Anastasia A.","family":"Anashkina","sequence":"first","affiliation":[]},{"given":"Yuri M.","family":"Poluektov","sequence":"additional","affiliation":[]},{"given":"Vladimir A.","family":"Dmitriev","sequence":"additional","affiliation":[]},{"given":"Eugene N.","family":"Kuznetsov","sequence":"additional","affiliation":[]},{"given":"Vladimir A.","family":"Mitkevich","sequence":"additional","affiliation":[]},{"given":"Alexander A.","family":"Makarov","sequence":"additional","affiliation":[]},{"given":"Irina Yu.","family":"Petrushanko","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2020,9,14]]},"reference":[{"key":"3571_CR1","doi-asserted-by":"publisher","first-page":"9092328","DOI":"10.1155\/2016\/9092328","volume":"2016","author":"VA Mitkevich","year":"2016","unstructured":"Mitkevich VA, Petrushanko IY, Poluektov YM, Burnysheva KM, Lakunina VA, Anashkina AA, et al. Basal glutathionylation of Na,K-ATPase \u03b1-subunit depends on redox status of cells during the enzyme biosynthesis. Oxidative Med Cell Longev. 2016;2016:9092328. https:\/\/doi.org\/10.1155\/2016\/9092328.","journal-title":"Oxidative Med Cell Longev"},{"key":"3571_CR2","doi-asserted-by":"publisher","first-page":"1941","DOI":"10.1089\/ars.2008.2089","volume":"10","author":"JJ Mieyal","year":"2008","unstructured":"Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA, Shelton MD. Molecular mechanisms and clinical implications of reversible protein S-Glutathionylation. Antioxid Redox Signal. 2008;10:1941\u201388.","journal-title":"Antioxid Redox Signal"},{"key":"3571_CR3","doi-asserted-by":"publisher","first-page":"32195","DOI":"10.1074\/jbc.M112.391094","volume":"287","author":"IY Petrushanko","year":"2012","unstructured":"Petrushanko IY, Yakushev S, Mitkevich VA, Kamanina YV, Ziganshin RH, Meng X, et al. 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