{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,25]],"date-time":"2026-05-25T14:14:37Z","timestamp":1779718477190,"version":"3.53.1"},"reference-count":16,"publisher":"Institute of Biochemistry","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BIOMED KHIM"],"published-print":{"date-parts":[[2026,5]]},"abstract":"<jats:p>In this study we have reanalyzed the original proteomic data from studies of hippocampal [DOI: 10.1172\/jci.insight.188612] and temporal cortex [DOI: 10.1016\/j.expneurol.2025.115361] tissues of patients with temporal lobe epilepsy. The goal was to identify proteins whose levels of post-translational modifications (PTMs) could be altered in this disease. Three datasets (PXD064519, ZMP8KU, and PXD010154) deposited at PRIDE and Texas Data Repository were used. Phosphorylation and N-terminal acetylation were considered as target PTMs. During re-identification of peptides we considered only peptides, for which both variants (with and without PTMs) were identified. A data comparison algorithm independent of experimental data alignment between individual samples was used. As a result, 35 proteins were selected that showed significant changes in phosphorylation levels. For 12 of these proteins, significant changes were recorded in both data sets. Twenty-nine proteins from this list have been linked to epilepsy pathogenesis in the literature.<\/jats:p>","DOI":"10.18097\/pbmcr1641","type":"journal-article","created":{"date-parts":[[2026,5,25]],"date-time":"2026-05-25T13:31:56Z","timestamp":1779715916000},"page":"118-127","source":"Crossref","is-referenced-by-count":0,"title":["Identification of proteins with altered PTM levels in patients with temporal lobe epilepsy in different regions of the human brain"],"prefix":"10.18097","volume":"72","author":[{"given":"Yu.V.","family":"Miroshnichenko","sequence":"first","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.V.","family":"Rybina","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.S.","family":"Skvortsov","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"7443","published-online":{"date-parts":[[2026]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","unstructured":"Miroshnichenko Yu.V., Rybina A.V., Skvortsov V.S. (2025) Identification of proteins with variable levels of post-translational modifications in human temporal lobe epilepsy. Biomeditsinskaya Khimiya, 71(5), 351\u2013363.","DOI":"10.18097\/PBMCR1612"},{"key":"ref2","doi-asserted-by":"publisher","unstructured":"Skvortsov V.S., Ivanova Ya.O., Voronina A.I. (2021) The bioinformatic identification of proteins with varying levels of post-translational modifications in experimental ischemic stroke in mice. Biomeditsinskaya Khimiya, 67(6), 475\u2013484.","DOI":"10.18097\/PBMC20216706475"},{"key":"ref3","doi-asserted-by":"publisher","unstructured":"Voronina A.I., Miroshnichenko Yu.V., Skvortsov V.S. (2024) Bioinformatic identification of proteins with altered PTM levels in a mouse line established to study the mechanisms of the development of fibromuscular dysplasia. Biomeditsinskaya Khimiya, 70(4), 248\u2013255.","DOI":"10.18097\/PBMC20247004248"},{"key":"ref4","doi-asserted-by":"publisher","unstructured":"Martens L., Hermjakob H., Jones P., Adamski M., Taylor C., States D., Gevaert K., Vandekerckhove J., Apweiler R. (2005) PRIDE: the proteomics identifications database. Proteomics, 5(13), 3537\u20133545.","DOI":"10.1002\/pmic.200401303"},{"key":"ref5","doi-asserted-by":"publisher","unstructured":"Salovska B., Liu Y. (2023) Post-translational modification and phenotype. Proteomics, 23(3\u20134), e2200535.","DOI":"10.1002\/pmic.202200535"},{"key":"ref6","doi-asserted-by":"publisher","unstructured":"Yamaguchi K., Hu Y.-Y., Kawajiri K., Itakura M., Nakashima F., Shibata T., Uchida K. (2025) Adductome-based identification of lysine monomethylation as a key post-translational protein modification in autoimmune diseases. J. Biol. Chem., 301(10), 110684.","DOI":"10.1016\/j.jbc.2025.110684"},{"key":"ref7","doi-asserted-by":"publisher","unstructured":"Mathoux J., Wilson M.-M., Srinivas S., Litovskich G., Villalba Benito L., Tran C., Kesavan J., Harnett A., Auer T., Sanz-Rodriguez A., Alkhayyat M.Kh.A.E., Sullivan M., Liu Z., Huang Y., Lacey A., Delanty N., Cryan J., Brett F.M., Farrell M.A., O'Brien D.F., Casillas-Espinosa P.M., Jimenez-Mateos E.M., Glennon J.C., Canavan M., Henshall D.C., Brennan G.P. (2025) N6-methyladenosine (m6A) dysregulation contributes to network excitability in temporal lobe epilepsy. JCI Insight, 10(14), e188612.","DOI":"10.1172\/jci.insight.188612"},{"key":"ref8","doi-asserted-by":"publisher","unstructured":"Li Y., Sadri Z., Blandin K.J., Narvaiz D.A., Aryal U.K., Lugo J.N., Poolos N.P., Brewster A.L. (2025) Sex-specific proteomic analysis of epileptic brain tissues from Pten knockout mice and human refractory epilepsy. Exp. Neurol., 392, 115361.","DOI":"10.1016\/j.expneurol.2025.115361"},{"key":"ref9","doi-asserted-by":"publisher","unstructured":"Wang D., Eraslan B., Wieland T., Hallstr\u00f6m B., Hopf T., Zolg D.P., Zecha J., Asplund A., Li L.-H., Meng C., Frejno M., Schmidt T., Schnatbaum K., Wilhelm M., Ponten F., Uhlen M., Gagneur J., Hahne H., Kuster B. (2019) A deep proteome and transcriptome abundance atlas of 29 healthy human tissues. Mol. Syst. Biol., 15(2), e8503.","DOI":"10.15252\/msb.20188503"},{"key":"ref10","doi-asserted-by":"publisher","unstructured":"Ma B., Zhang K., Hendrie C., Liang C., Li M., Doherty-Kirby A., Lajoie G. (2003) PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry. Rapid Commun. Mass Spectrom., 17(20), 2337\u20132342.","DOI":"10.1002\/rcm.1196"},{"key":"ref11","doi-asserted-by":"publisher","unstructured":"The UniProt Consortium (2020) UniProt: the universal protein knowledgebase in 2021. Nucleic Acids Res., 49(D1), D480\u2013D489.","DOI":"10.1093\/nar\/gkaa1100"},{"key":"ref12","unstructured":"Progenesis LC-MS version 4.0, Nonlinear Dynamics, Newcastle upon Tyne, UK."},{"key":"ref13","doi-asserted-by":"publisher","unstructured":"Berthold M.R., Cebron N., Dill F., Gabriel T.R., K\u00f6tter T., Meinl T., Ohl P., Thiel K., Wiswedel B. (2009) KNIME \u2014 the Konstanz Information Miner: version 2.0 and beyond. ACM SIGKDD Explorations Newsletter, 11(1), 26\u201331.","DOI":"10.1145\/1656274.1656280"},{"key":"ref14","doi-asserted-by":"publisher","unstructured":"Yeom J., Ju S., Choi Y., Paek E., Lee C. (2017) Comprehensive analysis of human protein N-termini enables assessment of various protein forms. Sci. Rep., 7, 6599.","DOI":"10.1038\/s41598-017-06314-9"},{"key":"ref15","doi-asserted-by":"publisher","unstructured":"Ashiuchi M., Yagami T., Willey R.J., Padovan J.C., Chait B.T., Popowicz A., Manning L.R., Manning J.M. (2005) N-terminal acetylation and protonation of individual hemoglobin subunits: position-dependent effects on tetramer strength and cooperativity. Protein Sci., 14(6), 1458\u20131471.","DOI":"10.1110\/ps.041267405"},{"key":"ref16","doi-asserted-by":"publisher","unstructured":"Xu A.S., Macdonald J.M., Labotka R.J., London R.E. (1999) NMR study of the sites of human hemoglobin acetylated by aspirin. Biochim. Biophys. 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