{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T05:20:35Z","timestamp":1787980835671,"version":"build-2784847793"},"reference-count":128,"publisher":"Pleiades Publishing Ltd","issue":"8","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biochemistry Moscow"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1134\/s0006297926601115","type":"journal-article","created":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T05:07:23Z","timestamp":1787980043000},"page":"1376-1395","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["EF-Hand Calcium-Binding Motif: Novel Structural and Functional Insights"],"prefix":"10.1134","volume":"91","author":[{"given":"Konstantin A.","family":"Denessiouk","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evgeny A.","family":"Permyakov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander I.","family":"Denesyuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey E.","family":"Permyakov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"137","published-online":{"date-parts":[[2026,8,29]]},"reference":[{"key":"3075_CR1","unstructured":"Krebs, J., and Michalak, M. (2007) Calcium: A Matter of Life or Death, Elsevier Science."},{"key":"3075_CR2","doi-asserted-by":"publisher","unstructured":"Permyakov, E. (2009) Metalloproteomics, John Wiley & Sons, Inc., Hoboken, New Jersey, \nhttps:\/\/doi.org\/10.1002\/9780470447758.","DOI":"10.1002\/9780470447758"},{"key":"3075_CR3","doi-asserted-by":"publisher","unstructured":"Permyakov, E. A., and Kretsinger, R. H. (2011) Calcium binding proteins, John Wiley & Sons, Inc., Hoboken, New Jersey, \nhttps:\/\/doi.org\/10.1002\/9780470872390.","DOI":"10.1002\/9780470872390"},{"key":"3075_CR4","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0025069","volume":"6","author":"B. Chouhan","year":"2011","unstructured":"Chouhan, B., Denesyuk, A., Heino, J., Johnson, M. S., and Denessiouk, K. (2011) Conservation of the human integrin-type beta-propeller domain in bacteria, PLoS One, 6, e25069, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0025069.","journal-title":"PLoS One"},{"key":"3075_CR5","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1111\/j.1365-2958.2004.04276.x","volume":"54","author":"D. C. Dominguez","year":"2004","unstructured":"Dominguez, D. C. (2004) Calcium signalling in bacteria, Mol.Microbiol., 54, 291-297, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2004.04276.x.","journal-title":"Mol.Microbiol."},{"key":"3075_CR6","doi-asserted-by":"publisher","first-page":"1047","DOI":"10.1016\/j.cell.2007.11.028","volume":"131","author":"D. E. Clapham","year":"2007","unstructured":"Clapham, D. E. (2007) Calcium signaling, Cell, 131, 1047-1058, \nhttps:\/\/doi.org\/10.1016\/j.cell.2007.11.028.","journal-title":"Cell"},{"key":"3075_CR7","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ceca.2009.05.005","volume":"46","author":"Y. Zhou","year":"2009","unstructured":"Zhou, Y., Frey, T. K., and Yang, J. J. (2009) Viral calciomics: interplays between Ca2+ and virus, Cell Calcium, 46, 1-17, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2009.05.005.","journal-title":"Cell Calcium"},{"key":"3075_CR8","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/j.jinorgbio.2008.09.006","volume":"103","author":"E. A. Permyakov","year":"2009","unstructured":"Permyakov, E. A., and Kretsinger, R. H. (2009) Cell signaling, beyond cytosolic calcium in eukaryotes, J. Inorg. Biochem., 103, 77-86, \nhttps:\/\/doi.org\/10.1016\/j.jinorgbio.2008.09.006.","journal-title":"J. Inorg. Biochem."},{"key":"3075_CR9","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1007\/978-94-007-2888-2_35","volume":"740","author":"A. Marchand","year":"2012","unstructured":"Marchand, A., Abi-Gerges, A., Saliba, Y., Merlet, E., and Lompre, A. M. (2012) Calcium signaling in vascular smooth muscle cells: from physiology to pathology, Adv. Exp. Med. Biol., 740, 795-810, \nhttps:\/\/doi.org\/10.1007\/978-94-007-2888-2_35.","journal-title":"Adv. Exp. Med. Biol."},{"key":"3075_CR10","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1085\/jgp.201210773","volume":"139","author":"S. M. Baylor","year":"2012","unstructured":"Baylor, S. M., and Hollingworth, S. (2012) Intracellular calcium movements during excitation-contraction coupling in mammalian slow-twitch and fast-twitch muscle fibers, J.\u00a0Gen. Physiol., 139, 261-272, \nhttps:\/\/doi.org\/10.1085\/jgp.201210773.","journal-title":"J.\u00a0Gen. Physiol."},{"key":"3075_CR11","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1111\/j.1471-4159.2011.07372.x","volume":"118","author":"M. Mikhaylova","year":"2011","unstructured":"Mikhaylova, M., Hradsky, J., and Kreutz, M. R. (2011) Between promiscuity and specificity: novel roles of EF-hand calcium sensors in neuronal Ca2+ signalling, J.\u00a0Neurochem., 118, 695-713, \nhttps:\/\/doi.org\/10.1111\/j.1471-4159.2011.07372.x.","journal-title":"J.\u00a0Neurochem."},{"key":"3075_CR12","doi-asserted-by":"publisher","DOI":"10.3390\/ijms232214143","volume":"23","author":"A. Bej","year":"2022","unstructured":"Bej, A., and Ames, J. B. (2022) Retinal cyclic nucleotide-gated channel regulation by calmodulin, Int. J. Mol. Sci., 23, 14143, \nhttps:\/\/doi.org\/10.3390\/ijms232214143.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR13","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1038\/38310","volume":"389","author":"J. B. Ames","year":"1997","unstructured":"Ames, J. B., Ishima, R., Tanaka, T., Gordon, J. I., Stryer, L., and Ikura, M. (1997) Molecular mechanics of calcium-myristoyl switches, Nature, 389, 198-202, \nhttps:\/\/doi.org\/10.1038\/38310.","journal-title":"Nature"},{"key":"3075_CR14","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1007\/978-1-4615-0121-3_21","volume":"514","author":"K. W. Koch","year":"2002","unstructured":"Koch, K. W. (2002) Target recognition of guanylate cyclase by guanylate cyclase-activating proteins, Adv. Exp. Med. Biol., 514, 349-360, \nhttps:\/\/doi.org\/10.1007\/978-1-4615-0121-3_21.","journal-title":"Adv. Exp. Med. Biol."},{"key":"3075_CR15","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1016\/j.ceca.2011.05.004","volume":"49","author":"K. Machaca","year":"2011","unstructured":"Machaca, K. (2011) Ca2+ signaling, genes and the cell cycle, Cell Calcium, 49, 323-330, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2011.05.004.","journal-title":"Cell Calcium"},{"key":"3075_CR16","doi-asserted-by":"publisher","first-page":"31674","DOI":"10.1074\/jbc.R112.384982","volume":"287","author":"J. R. Naranjo","year":"2012","unstructured":"Naranjo, J. R., and Mellstrom, B. (2012) Ca2+-dependent transcriptional control of Ca2+ homeostasis, J. Biol. Chem., 287, 31674-31680, \nhttps:\/\/doi.org\/10.1074\/jbc.R112.384982.","journal-title":"J. Biol. Chem."},{"key":"3075_CR17","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0040698","volume":"7","author":"S. Santamaria-Hernando","year":"2012","unstructured":"Santamaria-Hernando, S., Krell, T., and Ramos-Gonzalez, M. I. (2012) Identification of a novel calcium binding motif based on the detection of sequence insertions in the animal peroxidase domain of bacterial proteins, PLoS One, 7, e40698, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0040698.","journal-title":"PLoS One"},{"key":"3075_CR18","doi-asserted-by":"publisher","first-page":"10958","DOI":"10.1074\/jbc.O113.539569","volume":"289","author":"S. S. Srivastava","year":"2014","unstructured":"Srivastava, S. S., Mishra, A., Krishnan, B., and Sharma, Y. (2014) Ca2+-binding motif of betagamma-crystallins, J. Biol. Chem., 289, 10958-10966, \nhttps:\/\/doi.org\/10.1074\/jbc.O113.539569.","journal-title":"J. Biol. Chem."},{"key":"3075_CR19","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1016\/j.jmb.2004.08.077","volume":"343","author":"D. J. Rigden","year":"2004","unstructured":"Rigden, D. J., and Galperin, M. Y. (2004) The DxDxDG motif for calcium binding: multiple structural contexts and implications for evolution, J. Mol. Biol., 343, 971-984, \nhttps:\/\/doi.org\/10.1016\/j.jmb.2004.08.077.","journal-title":"J. Mol. Biol."},{"key":"3075_CR20","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0021507","volume":"6","author":"D. J. Rigden","year":"2011","unstructured":"Rigden, D. J., Woodhead, D. D., Wong, P. W., and Galperin, M. Y. (2011) New structural and functional contexts of the Dx[DN]xDG linear motif: insights into evolution of calcium-binding proteins, PLoS One, 6, e21507, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0021507.","journal-title":"PLoS One"},{"key":"3075_CR21","doi-asserted-by":"publisher","first-page":"3313","DOI":"10.1016\/S0021-9258(19)44043-X","volume":"248","author":"R. H. Kretsinger","year":"1973","unstructured":"Kretsinger, R. H., and Nockolds, C. E. (1973) Carp muscle calcium-binding protein. II. Structure determination and general description, J. Biol. Chem., 248, 3313-3326, \nhttps:\/\/doi.org\/10.1016\/S0021-9258(19)44043-X.","journal-title":"J. Biol. Chem."},{"key":"3075_CR22","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1042\/BJ20070255","volume":"405","author":"J. L. Gifford","year":"2007","unstructured":"Gifford, J. L., Walsh, M. P., and Vogel, H. J. (2007) Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs, Biochem.\u00a0J., 405, 199-221, \nhttps:\/\/doi.org\/10.1042\/BJ20070255.","journal-title":"Biochem.\u00a0J."},{"key":"3075_CR23","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1016\/j.jmb.2006.03.066","volume":"359","author":"Z. Grabarek","year":"2006","unstructured":"Grabarek, Z. (2006) Structural basis for diversity of the EF-hand calcium-binding proteins, J. Mol. Biol., 359, 509-525, \nhttps:\/\/doi.org\/10.1016\/j.jmb.2006.03.066.","journal-title":"J. Mol. Biol."},{"key":"3075_CR24","doi-asserted-by":"publisher","first-page":"1898","DOI":"10.1002\/pro.3233","volume":"26","author":"H. Kawasaki","year":"2017","unstructured":"Kawasaki, H., and Kretsinger, R. H. (2017) Structural and functional diversity of EF-hand proteins: evolutionary perspectives, Protein Sci., 26, 1898-1920, \nhttps:\/\/doi.org\/10.1002\/pro.3233.","journal-title":"Protein Sci."},{"key":"3075_CR25","doi-asserted-by":"publisher","first-page":"D553","DOI":"10.1093\/nar\/gkab1054","volume":"50","author":"J. M. Chandonia","year":"2022","unstructured":"Chandonia, J. M., Guan, L., Lin, S., Yu, C., Fox, N. K., and Brenner, S. E. (2022) SCOPe: improvements to the structural classification of proteins \u2013 extended database to facilitate variant interpretation and machine learning, Nucleic Acids Res., 50, D553-D559, \nhttps:\/\/doi.org\/10.1093\/nar\/gkab1054.","journal-title":"Nucleic Acids Res."},{"key":"3075_CR26","doi-asserted-by":"publisher","first-page":"D376","DOI":"10.1093\/nar\/gkz1064","volume":"48","author":"A. Andreeva","year":"2020","unstructured":"Andreeva, A., Kulesha, E., Gough, J., and Murzin, A. G. (2020) The SCOP database in 2020: expanded classification of representative family and superfamily domains of known protein structures, Nucleic Acids Res., 48, D376-D382, \nhttps:\/\/doi.org\/10.1093\/nar\/gkz1064.","journal-title":"Nucleic Acids Res."},{"key":"3075_CR27","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1007\/978-3-030-12457-1_8","volume":"1131","author":"J. Elies","year":"2020","unstructured":"Elies, J., Yanez, M., Pereira, T. M. C., Gil-Longo, J., MacDougall, D. A., and Campos-Toimil, M. (2020) An update to calcium binding proteins, Adv. Exp. Med. Biol., 1131, 183-213, \nhttps:\/\/doi.org\/10.1007\/978-3-030-12457-1_8.","journal-title":"Adv. Exp. Med. Biol."},{"key":"3075_CR28","doi-asserted-by":"publisher","DOI":"10.3390\/cells14141066","volume":"14","author":"K. B. Kirkness","year":"2025","unstructured":"Kirkness, K. B., Sharkey, J., and Scarlata, S. (2025) Calcium unified: understanding how calcium's atomic properties impact human health, Cells, 14, 1066, \nhttps:\/\/doi.org\/10.3390\/cells14141066.","journal-title":"Cells"},{"key":"3075_CR29","doi-asserted-by":"publisher","DOI":"10.3390\/ijms20020400","volume":"20","author":"J. Urrutia","year":"2019","unstructured":"Urrutia, J., Aguado, A., Muguruza-Montero, A., Nunez, E., Malo, C., Casis, O., and Villarroel, A. (2019) The crossroad of ion channels and calmodulin in disease, Int. J. Mol. Sci., 20, 400, \nhttps:\/\/doi.org\/10.3390\/ijms20020400.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR30","doi-asserted-by":"publisher","first-page":"965","DOI":"10.2174\/0113895575403663250812115441","volume":"25","author":"N. Kurochkina","year":"2025","unstructured":"Kurochkina, N., and Rudrabhatla, P. (2025) Role of calmodulin in neurodegeneration and neuroprotection, Mini Rev. Med. Chem., 25, 965-974, \nhttps:\/\/doi.org\/10.2174\/0113895575403663250812115441.","journal-title":"Mini Rev. Med. Chem."},{"key":"3075_CR31","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21103680","volume":"21","author":"F. Tebar","year":"2020","unstructured":"Tebar, F., Chavero, A., Agell, N., Lu, A., Rentero, C., Enrich, C., and Grewal, T. (2020) Pleiotropic roles of calmodulin in the regulation of KRas and Rac1 GTPases: functional diversity in health and disease, Int. J. Mol. Sci., 21, 3680, \nhttps:\/\/doi.org\/10.3390\/ijms21103680.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR32","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26010403","volume":"26","author":"W. Li","year":"2025","unstructured":"Li, W., Chen, Q., Peng, C., Yang, D., Liu, S., Lv, Y., Jiang, L., Xu, S., and Huang, L. (2025) Roles of the receptor for advanced glycation end products and its ligands in the pathogenesis of Alzheimer's disease, Int. J. Mol. Sci., 26, 403, \nhttps:\/\/doi.org\/10.3390\/ijms26010403.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR33","doi-asserted-by":"publisher","DOI":"10.1155\/2021\/5488591","volume":"2021","author":"Z. Sattar","year":"2021","unstructured":"Sattar, Z., Lora, A., Jundi, B., Railwah, C., and Geraghty, P. (2021) The S100 Protein family as players and therapeutic targets in pulmonary diseases, Pulm. Med., 2021, 5488591, \nhttps:\/\/doi.org\/10.1155\/2021\/5488591.","journal-title":"Pulm. Med."},{"key":"3075_CR34","doi-asserted-by":"publisher","DOI":"10.1016\/j.intimp.2025.114348","volume":"151","author":"B. Cheng","year":"2025","unstructured":"Cheng, B., Bian, Y., Song, X., Li, W., Li, M., and Feng, R. (2025) Role of S100A1, S100A4, S100A8\/A9 and S100B in myocardial infarction and heart failure, Int. Immunopharmacol., 151, 114348, \nhttps:\/\/doi.org\/10.1016\/j.intimp.2025.114348.","journal-title":"Int. Immunopharmacol."},{"key":"3075_CR35","doi-asserted-by":"publisher","DOI":"10.1186\/s10020-023-00662-1","volume":"29","author":"Y. Zhou","year":"2023","unstructured":"Zhou, Y., Zha, Y., Yang, Y., Ma, T., Li, H., and Liang, J. (2023) S100 proteins in cardiovascular diseases, Mol. Med., 29, 68, \nhttps:\/\/doi.org\/10.1186\/s10020-023-00662-1.","journal-title":"Mol. Med."},{"key":"3075_CR36","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1016\/bs.acc.2020.02.006","volume":"98","author":"G. Sreejit","year":"2020","unstructured":"Sreejit, G., Flynn, M. C., Patil, M., Krishnamurthy, P., Murphy, A. J., and Nagareddy, P. R. (2020) S100 family proteins in inflammation and beyond, Adv. Clin. Chem., 98, 173-231, \nhttps:\/\/doi.org\/10.1016\/bs.acc.2020.02.006.","journal-title":"Adv. Clin. Chem."},{"key":"3075_CR37","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1111\/imm.13722","volume":"171","author":"P. Xia","year":"2024","unstructured":"Xia, P., Ji, X., Yan, L., Lian, S., Chen, Z., and Luo, Y. (2024) Roles of S100A8, S100A9 and S100A12 in infection, inflammation and immunity, Immunology, 171, 365-376, \nhttps:\/\/doi.org\/10.1111\/imm.13722.","journal-title":"Immunology"},{"key":"3075_CR38","doi-asserted-by":"publisher","DOI":"10.1111\/exd.15158","volume":"33","author":"W. Abdi","year":"2024","unstructured":"Abdi, W., Romasco, A., Alkurdi, D., Santacruz, E., Okinedo, I., Zhang, Y., Kannan, S., Shakiba, S., and Richmond, J. M. (2024) An overview of S100 proteins and their functions in skin homeostasis, interface dermatitis conditions and other skin pathologies, Exp. Dermatol., 33, e15158, \nhttps:\/\/doi.org\/10.1111\/exd.15158.","journal-title":"Exp. Dermatol."},{"key":"3075_CR39","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1038\/nrc3893","volume":"15","author":"A. R. Bresnick","year":"2015","unstructured":"Bresnick, A. R., Weber, D. J., and Zimmer, D. B. (2015) S100 proteins in cancer, Nat. Rev. Cancer, 15, 96-109, \nhttps:\/\/doi.org\/10.1038\/nrc3893.","journal-title":"Nat. Rev. Cancer"},{"key":"3075_CR40","doi-asserted-by":"publisher","DOI":"10.3390\/cancers12082037","volume":"12","author":"C. Allgower","year":"2020","unstructured":"Allgower, C., Kretz, A. L., von Karstedt, S., Wittau, M., Henne-Bruns, D., and Lemke, J. (2020) Friend or foe: S100 proteins in cancer, Cancers (Basel), 12, 2037, \nhttps:\/\/doi.org\/10.3390\/cancers12082037.","journal-title":"Cancers (Basel)"},{"key":"3075_CR41","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1007\/978-1-4939-9030-6_11","volume":"1929","author":"C. W. Heizmann","year":"2019","unstructured":"Heizmann, C. W. (2019) Ca2+-binding proteins of the EF-hand superfamily: diagnostic and prognostic biomarkers and novel therapeutic targets, Methods Mol. Biol., 1929, 157-186, \nhttps:\/\/doi.org\/10.1007\/978-1-4939-9030-6_11.","journal-title":"Methods Mol. Biol."},{"key":"3075_CR42","doi-asserted-by":"publisher","first-page":"958","DOI":"10.1016\/j.bbrc.2017.01.040","volume":"483","author":"A. I. Denesyuk","year":"2017","unstructured":"Denesyuk, A. I., Permyakov, S. E., Johnson, M. S., Permyakov, E. A., and Denessiouk, K. (2017) Novel calcium recognition constructions in proteins: calcium blade and EF-hand zone, Biochem. Biophys. Res. Commun., 483, 958-963, \nhttps:\/\/doi.org\/10.1016\/j.bbrc.2017.01.040.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"3075_CR43","doi-asserted-by":"publisher","first-page":"1633","DOI":"10.1006\/jmbi.1999.2552","volume":"286","author":"W. Y. Wan","year":"1999","unstructured":"Wan, W. Y., and Milner-White, E. J. (1999) A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead in sequence: their occurrence at alpha-helical N termini and in other situations, J.\u00a0Mol. Biol., 286, 1633-1649, \nhttps:\/\/doi.org\/10.1006\/jmbi.1999.2552.","journal-title":"J.\u00a0Mol. Biol."},{"key":"3075_CR44","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1021\/bi00455a009","volume":"29","author":"P. Chakrabarti","year":"1990","unstructured":"Chakrabarti, P. (1990) Systematics in the interaction of metal ions with the main-chain carbonyl group in protein structures, Biochemistry, 29, 651-658, \nhttps:\/\/doi.org\/10.1021\/bi00455a009.","journal-title":"Biochemistry"},{"key":"3075_CR45","doi-asserted-by":"publisher","first-page":"1076","DOI":"10.1016\/j.jmb.2008.11.007","volume":"385","author":"G. M. Torrance","year":"2009","unstructured":"Torrance, G. M., Leader, D. P., Gilbert, D. R., and Milner-White, E. J. (2009) A novel main chain motif in proteins bridged by cationic groups: the niche, J.\u00a0Mol. Biol., 385, 1076-1086, \nhttps:\/\/doi.org\/10.1016\/j.jmb.2008.11.007.","journal-title":"J.\u00a0Mol. Biol."},{"key":"3075_CR46","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/j.bbrc.2017.10.034","volume":"494","author":"A. I. Denesyuk","year":"2017","unstructured":"Denesyuk, A. I., Permyakov, S. E., Johnson, M. S., Permyakov, E. A., and Denessiouk, K. (2017) Building kit for metal cation binding sites in proteins, Biochem. Biophys. Res. Commun., 494, 311-317, \nhttps:\/\/doi.org\/10.1016\/j.bbrc.2017.10.034.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"3075_CR47","doi-asserted-by":"publisher","DOI":"10.3390\/biom10040588","volume":"10","author":"A. I. Denesyuk","year":"2020","unstructured":"Denesyuk, A. I., Permyakov, S. E., Johnson, M. S., Denessiouk, K., and Permyakov, E. A. (2020) System approach for building of calcium-binding sites in proteins, Biomolecules, 10, 588, \nhttps:\/\/doi.org\/10.3390\/biom10040588.","journal-title":"Biomolecules"},{"key":"3075_CR48","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0109287","volume":"9","author":"K. Denessiouk","year":"2014","unstructured":"Denessiouk, K., Permyakov, S., Denesyuk, A., Permyakov, E., and Johnson, M. S. (2014) Two structural motifs within canonical EF-hand calcium-binding domains identify five different classes of calcium buffers and sensors, PLoS One, 9, e109287, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0109287.","journal-title":"PLoS One"},{"key":"3075_CR49","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a035543","volume":"12","author":"B. Schwaller","year":"2020","unstructured":"Schwaller, B. (2020) Cytosolic Ca2+ buffers are inherently Ca2+ signal modulators, Cold Spring Harb. Perspect. Biol., 12, a035543, \nhttps:\/\/doi.org\/10.1101\/cshperspect.a035543.","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"3075_CR50","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1080\/07391102.2015.1132392","volume":"35","author":"A. S. Kazakov","year":"2017","unstructured":"Kazakov, A. S., Sokolov, A. S., Vologzhannikova, A. A., Permyakova, M. E., Khorn, P. A., Ismailov, R. G., Denessiouk, K. A., Denesyuk, A. I., Rastrygina, V. A., Baksheeva, V. E., Zernii, E. Y., Zinchenko, D. V., Glazatov, V. V., Uversky, V. N., Mirzabekov, T. A., Permyakov, E. A., and Permyakov, S. E. (2017) Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs, J. Biomol. Struct. Dyn., 35, 78-91, \nhttps:\/\/doi.org\/10.1080\/07391102.2015.1132392.","journal-title":"J. Biomol. Struct. Dyn."},{"key":"3075_CR51","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/j.ceca.2018.08.005","volume":"75","author":"S. E. Permyakov","year":"2018","unstructured":"Permyakov, S. E., Vologzhannikova, A. A., Khorn, P. A., Shevelyova, M. P., Kazakov, A. S., Emelyanenko, V. I., Denesyuk, A. I., Denessiouk, K., Uversky, V. N., and Permyakov, E. A. (2018) Comprehensive analysis of the roles of 'black' and 'gray' clusters in structure and function of rat beta-parvalbumin, Cell Calcium, 75, 64-78, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2018.08.005.","journal-title":"Cell Calcium"},{"key":"3075_CR52","doi-asserted-by":"publisher","DOI":"10.3390\/molecules24132494","volume":"24","author":"S. E. Permyakov","year":"2019","unstructured":"Permyakov, S. E., Vologzhannikova, A. S., Nemashkalova, E. L., Kazakov, A. S., Denesyuk, A. I., Denessiouk, K., Baksheeva, V. E., Zamyatnin, A. A., Jr., Zernii, E. Y., Uversky, V. N., and Permyakov, E. A. (2019) Experimental insight into the structural and functional roles of the 'black' and 'gray' clusters in recoverin, a calcium binding protein with four EF-hand motifs, Molecules (Basel), 24, 2494, \nhttps:\/\/doi.org\/10.3390\/molecules24132494.","journal-title":"Molecules (Basel)"},{"key":"3075_CR53","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.ceca.2019.03.008","volume":"80","author":"M. E. Permyakova","year":"2019","unstructured":"Permyakova, M. E., Permyakov, S. E., Kazakov, A. S., Denesyuk, A. I., Denessiouk, K., Uversky, V. N., and Permyakov, E. A. (2019) Analyzing the structural and functional roles of residues from the 'black' and 'gray' clusters of human S100P protein, Cell Calcium, 80, 46-55, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2019.03.008.","journal-title":"Cell Calcium"},{"key":"3075_CR54","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1023\/a:1011320027914","volume":"1","author":"K. L. Yap","year":"2000","unstructured":"Yap, K. L., Kim, J., Truong, K., Sherman, M., Yuan, T., and Ikura, M. (2000) Calmodulin target database, J. Struct. Funct. Genomics, 1, 8-14, \nhttps:\/\/doi.org\/10.1023\/a:1011320027914.","journal-title":"J. Struct. Funct. Genomics"},{"key":"3075_CR55","doi-asserted-by":"publisher","first-page":"368","DOI":"10.2183\/pjab.100.025","volume":"100","author":"K. Sobue","year":"2024","unstructured":"Sobue, K. (2024) Calmodulin: a highly conserved and ubiquitous Ca2+ sensor, Proc. Jpn. Acad. Ser. B Phys. Biol. Sci., 100, 368-386, \nhttps:\/\/doi.org\/10.2183\/pjab.100.025.","journal-title":"Proc. Jpn. Acad. Ser. B Phys. Biol. Sci."},{"key":"3075_CR56","doi-asserted-by":"publisher","DOI":"10.1080\/19336950.2023.2165278","volume":"17","author":"J. W. Hussey","year":"2023","unstructured":"Hussey, J. W., Limpitikul, W. B., and Dick, I. E. (2023) Calmodulin mutations in human disease, Channels (Austin), 17, 2165278, \nhttps:\/\/doi.org\/10.1080\/19336950.2023.2165278.","journal-title":"Channels (Austin)"},{"key":"3075_CR57","doi-asserted-by":"publisher","first-page":"2295","DOI":"10.1007\/s00726-014-1795-y","volume":"46","author":"P. Kursula","year":"2014","unstructured":"Kursula, P. (2014) The many structural faces of calmodulin: a multitasking molecular jackknife, Amino Acids, 46, 2295-2304, \nhttps:\/\/doi.org\/10.1007\/s00726-014-1795-y.","journal-title":"Amino Acids"},{"key":"3075_CR58","doi-asserted-by":"publisher","DOI":"10.3390\/ijms22010308","volume":"22","author":"C. Andrews","year":"2020","unstructured":"Andrews, C., Xu, Y., Kirberger, M., and Yang, J. J. (2020) Structural aspects and prediction of calmodulin-binding proteins, Int. J. Mol. Sci., 22, 308, \nhttps:\/\/doi.org\/10.3390\/ijms22010308.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR59","doi-asserted-by":"publisher","first-page":"1159","DOI":"10.1073\/pnas.0508640103","volume":"103","author":"M. Ikura","year":"2006","unstructured":"Ikura, M., and Ames, J. B. (2006) Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: two ways to promote multifunctionality, Proc. Natl. Acad. Sci. USA, 103, 1159-1164, \nhttps:\/\/doi.org\/10.1073\/pnas.0508640103.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"3075_CR60","doi-asserted-by":"publisher","first-page":"455","DOI":"10.2174\/092986606776819600","volume":"13","author":"H. Ishida","year":"2006","unstructured":"Ishida, H., and Vogel, H. J. (2006) Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding, Protein Pept. Lett., 13, 455-465, \nhttps:\/\/doi.org\/10.2174\/092986606776819600.","journal-title":"Protein Pept. Lett."},{"key":"3075_CR61","doi-asserted-by":"publisher","first-page":"1507","DOI":"10.1007\/s00424-013-1278-0","volume":"465","author":"N. V. Kovalevskaya","year":"2013","unstructured":"Kovalevskaya, N. V., van de Waterbeemd, M., Bokhovchuk, F. M., Bate, N., Bindels, R. J., Hoenderop, J. G., and Vuister, G. W. (2013) Structural analysis of calmodulin binding to ion channels demonstrates the role of its plasticity in regulation, Pflugers Arch., 465, 1507-1519, \nhttps:\/\/doi.org\/10.1007\/s00424-013-1278-0.","journal-title":"Pflugers Arch."},{"key":"3075_CR62","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1385\/MB:27:1:33","volume":"27","author":"A. P. Yamniuk","year":"2004","unstructured":"Yamniuk, A. P., and Vogel, H. J. (2004) Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides, Mol. Biotechnol., 27, 33-57, \nhttps:\/\/doi.org\/10.1385\/MB:27:1:33.","journal-title":"Mol. Biotechnol."},{"key":"3075_CR63","doi-asserted-by":"publisher","first-page":"D648","DOI":"10.1093\/nar\/gkab1006","volume":"50","author":"N. Del Toro","year":"2022","unstructured":"Del Toro, N., Shrivastava, A., Ragueneau, E., Meldal, B., Combe, C., Barrera, E., Perfetto, L., How, K., Ratan, P., Shirodkar, G., Lu, O., Meszaros, B., Watkins, X., Pundir, S., Licata, L., Iannuccelli, M., Pellegrini, M., Martin, M. J., Panni, S., Duesbury, M., et al. (2022) The IntAct database: efficient access to fine-grained molecular interaction data, Nucleic Acids Res., 50, D648-D653, \nhttps:\/\/doi.org\/10.1093\/nar\/gkab1006.","journal-title":"Nucleic Acids Res."},{"key":"3075_CR64","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-022-09574-2","volume":"12","author":"M. A. Simon","year":"2022","unstructured":"Simon, M. A., Bartus, \u00c9., Mag, B., Boros, E., Roszj\u00e1r, L., G\u00f3gl, G., Trav\u00e9, G., Martinek, T. A., and Nyitray, L. (2022) Promiscuity mapping of the S100 protein family using a high-throughput holdup assay, Sci. Rep., 12, 5904, \nhttps:\/\/doi.org\/10.1038\/s41598-022-09574-2.","journal-title":"Sci. Rep."},{"key":"3075_CR65","doi-asserted-by":"publisher","first-page":"6633","DOI":"10.1021\/bi00241a001","volume":"30","author":"S. H. Gellman","year":"1991","unstructured":"Gellman, S. H. (1991) On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces, Biochemistry, 30, 6633-6636, \nhttps:\/\/doi.org\/10.1021\/bi00241a001.","journal-title":"Biochemistry"},{"key":"3075_CR66","doi-asserted-by":"publisher","first-page":"7582","DOI":"10.1080\/07391102.2022.2123391","volume":"41","author":"A. I. Denesyuk","year":"2023","unstructured":"Denesyuk, A. I., Permyakov, S. E., Permyakov, E. A., Johnson, M. S., Denessiouk, K., and Uversky, V. N. (2023) Canonical structural-binding modes in the calmodulin-target protein complexes, J.\u00a0Biomol. Struct. Dyn., 41, 7582-7594, \nhttps:\/\/doi.org\/10.1080\/07391102.2022.2123391.","journal-title":"J.\u00a0Biomol. Struct. Dyn."},{"key":"3075_CR67","doi-asserted-by":"publisher","first-page":"5551","DOI":"10.1111\/febs.12296","volume":"280","author":"H. Tidow","year":"2013","unstructured":"Tidow, H., and Nissen, P. (2013) Structural diversity of calmodulin binding to its target sites, FEBS\u00a0J., 280, 5551-5565, \nhttps:\/\/doi.org\/10.1111\/febs.12296.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR68","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21082751","volume":"21","author":"B. M. M. Grant","year":"2020","unstructured":"Grant, B. M. M., Enomoto, M., Ikura, M., and Marshall, C. B. (2020) A non-canonical calmodulin target motif comprising a polybasic region and lipidated terminal residue regulates localization, Int. J. Mol. Sci., 21, 2751, \nhttps:\/\/doi.org\/10.3390\/ijms21082751.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR69","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/s0014-5793(01)03239-2","volume":"513","author":"M. Bahler","year":"2002","unstructured":"Bahler, M., and Rhoads, A. (2002) Calmodulin signaling via the IQ motif, FEBS Lett., 513, 107-113, \nhttps:\/\/doi.org\/10.1016\/s0014-5793(01)03239-2.","journal-title":"FEBS Lett."},{"key":"3075_CR70","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1152\/physrev.1999.79.3.661","volume":"79","author":"L. A. Jurado","year":"1999","unstructured":"Jurado, L. A., Chockalingam, P. S., and Jarrett, H. W. (1999) Apocalmodulin, Physiol. Rev., 79, 661-682, \nhttps:\/\/doi.org\/10.1152\/physrev.1999.79.3.661.","journal-title":"Physiol. Rev."},{"key":"3075_CR71","doi-asserted-by":"publisher","first-page":"8050","DOI":"10.1016\/S0021-9258(18)92938-8","volume":"266","author":"S. Linse","year":"1991","unstructured":"Linse, S., Helmersson, A., and Forsen, S. (1991) Calcium binding to calmodulin and its globular domains, J.\u00a0Biol. Chem., 266, 8050-8054, \nhttps:\/\/doi.org\/10.1016\/S0021-9258(18)92938-8.","journal-title":"J.\u00a0Biol. Chem."},{"key":"3075_CR72","doi-asserted-by":"publisher","first-page":"D609","DOI":"10.1093\/nar\/gkae1010","volume":"53","author":"C. UniProt","year":"2025","unstructured":"UniProt, C. (2025) UniProt: the Universal Protein Knowledgebase in 2025, Nucleic Acids Res., 53, D609-D617, \nhttps:\/\/doi.org\/10.1093\/nar\/gkae1010.","journal-title":"Nucleic Acids Res."},{"key":"3075_CR73","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1016\/s1357-2725(01)00046-2","volume":"33","author":"R. Donato","year":"2001","unstructured":"Donato, R. (2001) S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles, Int. J. Biochem. Cell Biol., 33, 637-668, \nhttps:\/\/doi.org\/10.1016\/s1357-2725(01)00046-2.","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"3075_CR74","doi-asserted-by":"publisher","first-page":"24","DOI":"10.2174\/156652413804486214","volume":"13","author":"R. Donato","year":"2013","unstructured":"Donato, R., Cannon, B. R., Sorci, G., Riuzzi, F., Hsu, K., Weber, D. J., and Geczy, C. L. (2013) Functions of S100 proteins, Curr. Mol. Med., 13, 24-57, \nhttps:\/\/doi.org\/10.2174\/156652413804486214.","journal-title":"Curr. Mol. Med."},{"key":"3075_CR75","doi-asserted-by":"publisher","DOI":"10.3390\/cells11152274","volume":"11","author":"P. Singh","year":"2022","unstructured":"Singh, P., and Ali, S. A. (2022) Multifunctional role of S100 protein family in the immune system: an update, Cells, 11, 2274, \nhttps:\/\/doi.org\/10.3390\/cells11152274.","journal-title":"Cells"},{"key":"3075_CR76","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2020.118677","volume":"1867","author":"L. L. Gonzalez","year":"2020","unstructured":"Gonzalez, L. L., Garrie, K., and Turner, M. D. (2020) Role of S100 proteins in health and disease, Biochim. Biophys. Acta Mol. Cell Res., 1867, 118677, \nhttps:\/\/doi.org\/10.1016\/j.bbamcr.2020.118677.","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"3075_CR77","doi-asserted-by":"publisher","unstructured":"Fritz, G., and Heizmann, C. W. (2004) 3D Structures of the Calcium and Zinc Binding S100 Proteins. in Handbook of Metalloproteins (John Wiley & Sons, L. ed.) John Wiley & Sons, Hoboken, NJ, USA, \nhttps:\/\/doi.org\/10.1002\/0470028637.met046.","DOI":"10.1002\/0470028637.met046"},{"key":"3075_CR78","doi-asserted-by":"publisher","first-page":"4578","DOI":"10.1111\/j.1742-4658.2010.07887.x","volume":"277","author":"G. Fritz","year":"2010","unstructured":"Fritz, G., Botelho, H. M., Morozova-Roche, L. A., and Gomes, C. M. (2010) Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity, FEBS\u00a0J., 277, 4578-4590, \nhttps:\/\/doi.org\/10.1111\/j.1742-4658.2010.07887.x.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR79","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/j.bpc.2010.06.003","volume":"151","author":"W. W. Streicher","year":"2010","unstructured":"Streicher, W. W., Lopez, M. M., and Makhatadze, G. I. (2010) Modulation of quaternary structure of S100 proteins by calcium ions, Biophys. Chem., 151, 181-186, \nhttps:\/\/doi.org\/10.1016\/j.bpc.2010.06.003.","journal-title":"Biophys. Chem."},{"key":"3075_CR80","doi-asserted-by":"publisher","first-page":"1859","DOI":"10.1111\/febs.14775","volume":"286","author":"D. E. Spratt","year":"2019","unstructured":"Spratt, D. E., Barber, K. R., Marlatt, N. M., Ngo, V., Macklin, J. A., Xiao, Y., Konermann, L., Duennwald, M. L., and Shaw, G. S. (2019) A subset of calcium-binding S100 proteins show preferential heterodimerization, FEBS\u00a0J., 286, 1859-1876, \nhttps:\/\/doi.org\/10.1111\/febs.14775.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR81","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/j.bbamcr.2004.09.002","volume":"1742","author":"S. Bhattacharya","year":"2004","unstructured":"Bhattacharya, S., Bunick, C. G., and Chazin, W. J. (2004) Target selectivity in EF-hand calcium binding proteins, Biochim. Biophys. Acta, 1742, 69-79, \nhttps:\/\/doi.org\/10.1016\/j.bbamcr.2004.09.002.","journal-title":"Biochim. Biophys. Acta"},{"key":"3075_CR82","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1042\/BJ20060195","volume":"396","author":"L. Santamaria-Kisiel","year":"2006","unstructured":"Santamaria-Kisiel, L., Rintala-Dempsey, A. C., and Shaw, G. S. (2006) Calcium-dependent and -independent interactions of the S100 protein family, Biochem.\u00a0J., 396, 201-214, \nhttps:\/\/doi.org\/10.1042\/BJ20060195.","journal-title":"Biochem.\u00a0J."},{"key":"3075_CR83","doi-asserted-by":"publisher","DOI":"10.3389\/Fphar.2012.00067","volume":"3","author":"A. Hermann","year":"2012","unstructured":"Hermann, A., Donato, R., Weiger, T. M., and Chazin, W. J. (2012) S100 calcium binding proteins and ion channels, Front. Pharmacol., 3, 67, \nhttps:\/\/doi.org\/10.3389\/Fphar.2012.00067.","journal-title":"Front. Pharmacol."},{"key":"3075_CR84","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2025.143667","volume":"311","author":"V. A. Rastrygina","year":"2025","unstructured":"Rastrygina, V. A., Kazakov, A. S., Fadeev, R. S., Meshcheriakova, E. I., Deryusheva, E. I., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2025) Soluble form of tumor necrosis factor-related apoptosis-inducing ligand interacts with S100P protein, Int. J. Biol. Macromol., 311, 143667, \nhttps:\/\/doi.org\/10.1016\/j.ijbiomac.2025.143667.","journal-title":"Int. J. Biol. Macromol."},{"key":"3075_CR85","doi-asserted-by":"publisher","first-page":"5936","DOI":"10.1111\/j.1742-4658.2009.07274.x","volume":"276","author":"J. Klingelhofer","year":"2009","unstructured":"Klingelhofer, J., Moller, H. D., Sumer, E. U., Berg, C. H., Poulsen, M., Kiryushko, D., Soroka, V., Ambartsumian, N., Grigorian, M., and Lukanidin, E. M. (2009) Epidermal growth factor receptor ligands as new extracellular targets for the metastasis-promoting S100A4 protein, FEBS\u00a0J., 276, 5936-5948, \nhttps:\/\/doi.org\/10.1111\/j.1742-4658.2009.07274.x.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR86","doi-asserted-by":"publisher","first-page":"3977","DOI":"10.7150\/thno.22274","volume":"8","author":"S. Pankratova","year":"2018","unstructured":"Pankratova, S., Klingelhofer, J., Dmytriyeva, O., Owczarek, S., Renziehausen, A., Syed, N., Porter, A. E., Dexter, D. T., and Kiryushko, D. (2018) The S100A4 protein signals through the ErbB4 receptor to promote neuronal survival, Theranostics, 8, 3977-3990, \nhttps:\/\/doi.org\/10.7150\/thno.22274.","journal-title":"Theranostics"},{"key":"3075_CR87","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2023.1110185","volume":"14","author":"A. Moller","year":"2023","unstructured":"Moller, A., Jauch-Speer, S. L., Gandhi, S., Vogl, T., Roth, J., and Fehler, O. (2023) The roles of toll-like receptor 4, CD33, CD68, CD69, or CD147\/EMMPRIN for monocyte activation by the DAMP S100A8\/S100A9, Front. Immunol., 14, 1110185, \nhttps:\/\/doi.org\/10.3389\/fimmu.2023.1110185.","journal-title":"Front. Immunol."},{"key":"3075_CR88","doi-asserted-by":"publisher","first-page":"14608","DOI":"10.1074\/jbc.M110.201954","volume":"286","author":"S. K. Mohan","year":"2011","unstructured":"Mohan, S. K., and Yu, C. (2011) The IL1alpha-S100A13 heterotetrameric complex structure: a component in the non-classical pathway for interleukin 1alpha secretion, J.\u00a0Biol. Chem., 286, 14608-14617, \nhttps:\/\/doi.org\/10.1074\/jbc.M110.201954.","journal-title":"J.\u00a0Biol. Chem."},{"key":"3075_CR89","doi-asserted-by":"publisher","first-page":"22224","DOI":"10.1074\/jbc.273.35.22224","volume":"273","author":"C. M. Carreira","year":"1998","unstructured":"Carreira, C. M., LaVallee, T. M., Tarantini, F., Jackson, A., Lathrop, J. T., Hampton, B., Burgess, W. H., and Maciag, T. (1998) S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro, J.\u00a0Biol. Chem., 273, 22224-22231, \nhttps:\/\/doi.org\/10.1074\/jbc.273.35.22224.","journal-title":"J.\u00a0Biol. Chem."},{"key":"3075_CR90","doi-asserted-by":"publisher","first-page":"2606","DOI":"10.1016\/j.bbapap.2013.09.012","volume":"1834","author":"A. A. Gupta","year":"2013","unstructured":"Gupta, A. A., Chou, R. H., Li, H. C., Yang, L. W., and Yu, C. (2013) Structural insights into the interaction of human S100B and basic fibroblast growth factor (FGF2): Effects on FGFR1 receptor signaling, Biochim. Biophys. Acta, 1834, 2606-2619, \nhttps:\/\/doi.org\/10.1016\/j.bbapap.2013.09.012.","journal-title":"Biochim. Biophys. Acta"},{"key":"3075_CR91","doi-asserted-by":"publisher","first-page":"2389","DOI":"10.1242\/jcs.084491","volume":"124","author":"F. Riuzzi","year":"2011","unstructured":"Riuzzi, F., Sorci, G., and Donato, R. (2011) S100B protein regulates myoblast proliferation and differentiation by activating FGFR1 in a bFGF-dependent manner, J. Cell Sci., 124, 2389-2400, \nhttps:\/\/doi.org\/10.1242\/jcs.084491.","journal-title":"J. Cell Sci."},{"key":"3075_CR92","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1016\/j.bbrc.2015.11.024","volume":"468","author":"A. S. Kazakov","year":"2015","unstructured":"Kazakov, A. S., Sokolov, A. S., Rastrygina, V. A., Solovyev, V. V., Ismailov, R. G., Mikhailov, R. V., Ulitin, A. B., Yakovenko, A. R., Mirzabekov, T. A., Permyakov, E. A., and Permyakov, S. E. (2015) High-affinity interaction between interleukin-11 and S100P protein, Biochem. Biophys. Res. Commun., 468, 733-738, \nhttps:\/\/doi.org\/10.1016\/j.bbrc.2015.11.024.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"3075_CR93","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/j.ijbiomac.2019.12.039","volume":"143","author":"A. S. Kazakov","year":"2020","unstructured":"Kazakov, A. S., Mayorov, S. A., Deryusheva, E. I., Avkhacheva, N. V., Denessiouk, K. A., Denesyuk, A. I., Rastrygina, V. A., Permyakov, E. A., and Permyakov, S. E. (2020) Highly specific interaction of monomeric S100P protein with interferon beta, Int. J. Biol. Macromol., 143, 633-639, \nhttps:\/\/doi.org\/10.1016\/j.ijbiomac.2019.12.039.","journal-title":"Int. J. Biol. Macromol."},{"key":"3075_CR94","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21249473","volume":"21","author":"A. S. Kazakov","year":"2020","unstructured":"Kazakov, A. S., Sofin, A. D., Avkhacheva, N. V., Denesyuk, A. I., Deryusheva, E. I., Rastrygina, V. A., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2020) Interferon beta activity is modulated via binding of specific S100 proteins, Int. J. Mol. Sci., 21, 9473, \nhttps:\/\/doi.org\/10.3390\/ijms21249473.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR95","doi-asserted-by":"publisher","DOI":"10.3390\/biom12010120","volume":"12","author":"A. S. Kazakov","year":"2022","unstructured":"Kazakov, A. S., Deryusheva, E. I., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Rastrygina, V. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2022) Erythropoietin interacts with specific S100 proteins, Biomolecules, 12, 120, \nhttps:\/\/doi.org\/10.3390\/biom12010120.","journal-title":"Biomolecules"},{"key":"3075_CR96","doi-asserted-by":"publisher","DOI":"10.3390\/ijms23041997","volume":"23","author":"A. S. Kazakov","year":"2022","unstructured":"Kazakov, A. S., Sofin, A. D., Avkhacheva, N. V., Deryusheva, E. I., Rastrygina, V. A., Permyakova, M. E., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2022) Interferon-\u03b2 activity is affected by S100B protein, Int. J. Mol. Sci., 23, 1997, \nhttps:\/\/doi.org\/10.3390\/ijms23041997.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR97","doi-asserted-by":"publisher","DOI":"10.1016\/j.ceca.2021.102520","volume":"101","author":"A. S. Kazakov","year":"2022","unstructured":"Kazakov, A. S., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2022) Specific cytokines of interleukin-6 family interact with S100 proteins, Cell Calcium, 101, 102520, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2021.102520.","journal-title":"Cell Calcium"},{"key":"3075_CR98","doi-asserted-by":"publisher","DOI":"10.3390\/ijms231912000","volume":"23","author":"A. S. Kazakov","year":"2022","unstructured":"Kazakov, A. S., Deryusheva, E. I., Permyakova, M. E., Sokolov, A. S., Rastrygina, V. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2022) Calcium-bound S100P protein is a promiscuous binding partner of the four-helical cytokines, Int. J. Mol. Sci., 23, 12000, \nhttps:\/\/doi.org\/10.3390\/ijms231912000.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR99","doi-asserted-by":"publisher","DOI":"10.3390\/ijms232415956","volume":"23","author":"A. S. Kazakov","year":"2022","unstructured":"Kazakov, A. S., Zemskova, M. Y., Rystsov, G. K., Vologzhannikova, A. A., Deryusheva, E. I., Rastrygina, V. A., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2022) Specific S100 proteins bind tumor necrosis factor and inhibit its activity, Int. J. Mol. Sci., 23, 15956, \nhttps:\/\/doi.org\/10.3390\/ijms232415956.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR100","doi-asserted-by":"publisher","DOI":"10.3390\/biom13091345","volume":"13","author":"A. S. Kazakov","year":"2023","unstructured":"Kazakov, A. S., Deryusheva, E. I., Rastrygina, V. A., Sokolov, A. S., Permyakova, M. E., Litus, E. A., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2023) Interaction of S100A6 protein with the four-helical cytokines, Biomolecules, 13, 1345, \nhttps:\/\/doi.org\/10.3390\/biom13091345.","journal-title":"Biomolecules"},{"key":"3075_CR101","doi-asserted-by":"publisher","DOI":"10.1016\/j.ceca.2024.102869","volume":"119","author":"A. S. Kazakov","year":"2024","unstructured":"Kazakov, A. S., Rastrygina, V. A., Vologzhannikova, A. A., Zemskova, M. Y., Bobrova, L. A., Deryusheva, E. I., Permyakova, M. E., Sokolov, A. S., Litus, E. A., Shevelyova, M. P., Uversky, V. N., Permyakov, E. A., and Permyakov, S. E. (2024) Recognition of granulocyte-macrophage colony-stimulating factor by specific S100 proteins, Cell Calcium, 119, 102869, \nhttps:\/\/doi.org\/10.1016\/j.ceca.2024.102869.","journal-title":"Cell Calcium"},{"key":"3075_CR102","doi-asserted-by":"publisher","DOI":"10.1016\/j.autrev.2023.103295","volume":"22","author":"M. Manfredi","year":"2023","unstructured":"Manfredi, M., Van Hoovels, L., Benucci, M., De Luca, R., Coccia, C., Bernardini, P., Russo, E., Amedei, A., Guiducci, S., Grossi, V., Bossuyt, X., Perricone, C., and Infantino, M. (2023) Circulating calprotectin (cCLP) in autoimmune diseases, Autoimmun Rev., 22, 103295, \nhttps:\/\/doi.org\/10.1016\/j.autrev.2023.103295.","journal-title":"Autoimmun Rev."},{"key":"3075_CR103","doi-asserted-by":"publisher","DOI":"10.1007\/s12672-024-00945-x","volume":"15","author":"X. Liang","year":"2024","unstructured":"Liang, X., Huang, X., Cai, Z., Deng, Y., Liu, D., Hu, J., Jin, Z., Zhou, X., Zhou, H., and Wang, L. (2024) The S100 family is a prognostic biomarker and correlated with immune cell infiltration in pan-cancer, Discov. Oncol., 15, 137, \nhttps:\/\/doi.org\/10.1007\/s12672-024-00945-x.","journal-title":"Discov. Oncol."},{"key":"3075_CR104","doi-asserted-by":"publisher","DOI":"10.1016\/J.Biopha.2020.110156","volume":"127","author":"X. Hua","year":"2020","unstructured":"Hua, X., Zhang, H. M., Jia, J. F., Chen, S. S., Sun, Y., and Zhu, X. L. (2020) Roles of S100 family members in drug resistance in tumors: status and prospects, Biomed. Pharmacother., 127, 110156, \nhttps:\/\/doi.org\/10.1016\/J.Biopha.2020.110156.","journal-title":"Biomed. Pharmacother."},{"key":"3075_CR105","doi-asserted-by":"publisher","first-page":"1617","DOI":"10.1007\/s12551-018-0471-y","volume":"10","author":"A. R. Bresnick","year":"2018","unstructured":"Bresnick, A. R. (2018) S100 proteins as therapeutic targets, Biophys. Rev., 10, 1617-1629, \nhttps:\/\/doi.org\/10.1007\/s12551-018-0471-y.","journal-title":"Biophys. Rev."},{"key":"3075_CR106","doi-asserted-by":"publisher","DOI":"10.3390\/molecules27196640","volume":"27","author":"K. Kurpet","year":"2022","unstructured":"Kurpet, K., and Chwatko, G. (2022) S100 Proteins as novel therapeutic targets in psoriasis and other autoimmune diseases, Molecules, 27, 6640, \nhttps:\/\/doi.org\/10.3390\/molecules27196640.","journal-title":"Molecules"},{"key":"3075_CR107","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1007\/978-1-4939-9030-6_43","volume":"1929","author":"A. L. Frauchiger","year":"2019","unstructured":"Frauchiger, A. L., Dummer, R., and Mangana, J. (2019) Serum S100B levels in melanoma, Methods Mol. Biol., 1929, 691-700, \nhttps:\/\/doi.org\/10.1007\/978-1-4939-9030-6_43.","journal-title":"Methods Mol. Biol."},{"key":"3075_CR108","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26136476","volume":"26","author":"K. Sejersen","year":"2025","unstructured":"Sejersen, K., Eriksson, M. B., and Larsson, A. O. (2025) Calprotectin as a biomarker for infectious diseases: a comparative review with conventional inflammatory markers, Int. J. Mol. Sci., 26, 6476, \nhttps:\/\/doi.org\/10.3390\/ijms26136476.","journal-title":"Int. J. Mol. Sci."},{"key":"3075_CR109","doi-asserted-by":"publisher","first-page":"2834","DOI":"10.1111\/febs.15175","volume":"287","author":"M. A. Simon","year":"2020","unstructured":"Simon, M. A., Ecsedi, P., Kovacs, G. M., Poti, A. L., Remenyi, A., Kardos, J., Gogl, G., and Nyitray, L. (2020) High-throughput competitive fluorescence polarization assay reveals functional redundancy in the S100 protein family, FEBS\u00a0J., 287, 2834-2846, \nhttps:\/\/doi.org\/10.1111\/febs.15175.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR110","doi-asserted-by":"crossref","first-page":"F39","DOI":"10.4149\/gpb_2009_01_39","volume":"28","author":"A. Rezvanpour","year":"2009","unstructured":"Rezvanpour, A., and Shaw, G. S. (2009) Unique S100 target protein interactions, Gen. Physiol. Biophys., 28, F39-F46.","journal-title":"Gen. Physiol. Biophys."},{"key":"3075_CR111","doi-asserted-by":"publisher","first-page":"943","DOI":"10.1016\/j.str.2020.05.001","volume":"28","author":"P. Ecs\u00e9di","year":"2020","unstructured":"Ecs\u00e9di, P., G\u00f3gl, G., H\u00f3f, H., Kiss, B., Harmat, V., and Nyitray, L. (2020) Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone, Structure, 28, 943-953.e944, \nhttps:\/\/doi.org\/10.1016\/j.str.2020.05.001.","journal-title":"Structure"},{"key":"3075_CR112","doi-asserted-by":"publisher","first-page":"2043","DOI":"10.1016\/j.str.2016.09.011","volume":"24","author":"L. Yatime","year":"2016","unstructured":"Yatime, L., Betzer, C., Jensen, R. K., Mortensen, S., Jensen, P. H., and Andersen, G. R. (2016) The structure of the RAGE:S100A6 complex reveals a unique mode of homodimerization for S100 proteins, Structure, 24, 2043-2052, \nhttps:\/\/doi.org\/10.1016\/j.str.2016.09.011.","journal-title":"Structure"},{"key":"3075_CR113","doi-asserted-by":"publisher","first-page":"16512","DOI":"10.1039\/d5cc04777c","volume":"61","author":"B. Devi","year":"2025","unstructured":"Devi, B., Nag, N., Uversky, V. N., and Tripathi, T. (2025) Conditional disorder in proteins: functional transitions between order and disorder, Chem. Commun. (Camb), 61, 16512-16528, \nhttps:\/\/doi.org\/10.1039\/d5cc04777c.","journal-title":"Chem. Commun. (Camb)"},{"key":"3075_CR114","doi-asserted-by":"publisher","first-page":"2164","DOI":"10.1039\/c0mb00305k","volume":"7","author":"S. E. Permyakov","year":"2011","unstructured":"Permyakov, S. E., Ismailov, R. G., Xue, B., Denesyuk, A. I., Uversky, V. N., and Permyakov, E. A. (2011) Intrinsic disorder in S100 proteins, Mol. Biosyst., 7, 2164-2180, \nhttps:\/\/doi.org\/10.1039\/c0mb00305k.","journal-title":"Mol. Biosyst."},{"key":"3075_CR115","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1023\/a:1012976615056","volume":"14","author":"D. S. Auld","year":"2001","unstructured":"Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites, Biometals, 14, 271-313, \nhttps:\/\/doi.org\/10.1023\/a:1012976615056.","journal-title":"Biometals"},{"key":"3075_CR116","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1007\/s11427-016-5088-4","volume":"59","author":"B. A. Gilston","year":"2016","unstructured":"Gilston, B. A., Skaar, E. P., and Chazin, W. J. (2016) Binding of transition metals to S100 proteins, Sci. China Life Sci., 59, 792-801, \nhttps:\/\/doi.org\/10.1007\/s11427-016-5088-4.","journal-title":"Sci. China Life Sci."},{"key":"3075_CR117","doi-asserted-by":"publisher","first-page":"761","DOI":"10.1007\/s00726-010-0540-4","volume":"41","author":"O. V. Moroz","year":"2011","unstructured":"Moroz, O. V., Wilson, K. S., and Bronstein, I. B. (2011) The role of zinc in the S100 proteins: insights from the X-ray structures, Amino Acids, 41, 761-772, \nhttps:\/\/doi.org\/10.1007\/s00726-010-0540-4.","journal-title":"Amino Acids"},{"key":"3075_CR118","doi-asserted-by":"publisher","first-page":"1712","DOI":"10.1016\/j.bbamcr.2012.07.009","volume":"1833","author":"K. Kizawa","year":"2013","unstructured":"Kizawa, K., Jinbo, Y., Inoue, T., Takahara, H., Unno, M., Heizmann, C. W., and Izumi, Y. (2013) Human S100A3 tetramerization propagates Ca2+\/Zn2+ binding states, Biochim. Biophys. Acta, 1833, 1712-1719, \nhttps:\/\/doi.org\/10.1016\/j.bbamcr.2012.07.009.","journal-title":"Biochim. Biophys. Acta"},{"key":"3075_CR119","doi-asserted-by":"publisher","first-page":"33092","DOI":"10.1074\/jbc.M200574200","volume":"277","author":"G. Fritz","year":"2002","unstructured":"Fritz, G., Mittl, P. R., Vasak, M., Grutter, M. G., and Heizmann, C. W. (2002) The crystal structure of metal-free human EF-hand protein S100A3 at 1.7-A resolution, J. Biol. Chem., 277, 33092-33098, \nhttps:\/\/doi.org\/10.1074\/jbc.M200574200.","journal-title":"J. Biol. Chem."},{"key":"3075_CR120","doi-asserted-by":"publisher","first-page":"5690","DOI":"10.1021\/bi0475830","volume":"44","author":"P. T. Wilder","year":"2005","unstructured":"Wilder, P. T., Varney, K. M., Weiss, M. B., Gitti, R. K., and Weber, D. J. (2005) Solution structure of zinc- and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy, Biochemistry, 44, 5690-5702, \nhttps:\/\/doi.org\/10.1021\/bi0475830.","journal-title":"Biochemistry"},{"key":"3075_CR121","doi-asserted-by":"publisher","first-page":"1776","DOI":"10.1111\/j.1742-4658.2009.06912.x","volume":"276","author":"H. M. Botelho","year":"2009","unstructured":"Botelho, H. M., Koch, M., Fritz, G., and Gomes, C. M. (2009) Metal ions modulate the folding and stability of the tumor suppressor protein S100A2, FEBS\u00a0J., 276, 1776-1786, \nhttps:\/\/doi.org\/10.1111\/j.1742-4658.2009.06912.x.","journal-title":"FEBS\u00a0J."},{"key":"3075_CR122","doi-asserted-by":"publisher","DOI":"10.3390\/biom11121823","volume":"11","author":"V. E. Baksheeva","year":"2021","unstructured":"Baksheeva, V. E., Roman, A. Y., Villard, C., Devred, F., Byrne, D., Yatoui, D., Zalevsky, A. O., Vologzhannikova, A. A., Sokolov, A. S., Permyakov, S. E., Golovin, A. V., Shaw, G. S., Tsvetkov, P. O., and Zernii, E. Y. (2021) Mechanism of Zn2+ and Ca2+ binding to human S100A1, Biomolecules, 11, 1823, \nhttps:\/\/doi.org\/10.3390\/biom11121823.","journal-title":"Biomolecules"},{"key":"3075_CR123","doi-asserted-by":"publisher","DOI":"10.3389\/fnmol.2018.00459","volume":"11","author":"P. O. Tsvetkov","year":"2018","unstructured":"Tsvetkov, P. O., Roman, A. Y., Baksheeva, V. E., Nazipova, A. A., Shevelyova, M. P., Vladimirov, V. I., Buyanova, M. F., Zinchenko, D. V., Zamyatnin, A. A., Devred, F., Golovin, A. V., Permyakov, S. E., and Zernii, E. Y. (2018) Functional status of neuronal calcium sensor-1 is modulated by zinc binding, Front. Mol. Neurosci., 11, 459, \nhttps:\/\/doi.org\/10.3389\/fnmol.2018.00459.","journal-title":"Front. Mol. Neurosci."},{"key":"3075_CR124","doi-asserted-by":"publisher","first-page":"1562","DOI":"10.1016\/j.str.2008.07.012","volume":"16","author":"H. Suzuki","year":"2008","unstructured":"Suzuki, H., Kawasaki, M., Inuzuka, T., Okumura, M., Kakiuchi, T., Shibata, H., Wakatsuki, S., and Maki, M. (2008) Structural basis for Ca2+-dependent formation of ALG-2\/Alix peptide complex: Ca2+\/EF3-driven arginine switch mechanism, Structure, 16, 1562-1573, \nhttps:\/\/doi.org\/10.1016\/j.str.2008.07.012.","journal-title":"Structure"},{"key":"3075_CR125","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1107\/s2052252523001501","volume":"10","author":"S. A. Mun","year":"2023","unstructured":"Mun, S. A., Park, J., Kang, J. Y., Park, T., Jin, M., Yang, J., and Eom, S. H. (2023) Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2, IUCrJ, 10, 233-245, \nhttps:\/\/doi.org\/10.1107\/s2052252523001501.","journal-title":"IUCrJ"},{"key":"3075_CR126","doi-asserted-by":"publisher","first-page":"517","DOI":"10.1016\/j.jmb.2007.09.048","volume":"374","author":"J. T. Warren","year":"2007","unstructured":"Warren, J. T., Guo, Q., and Tang, W. J. (2007) A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step, J.\u00a0Mol. Biol., 374, 517-527, \nhttps:\/\/doi.org\/10.1016\/j.jmb.2007.09.048.","journal-title":"J.\u00a0Mol. Biol."},{"key":"3075_CR127","doi-asserted-by":"publisher","first-page":"1086","DOI":"10.1016\/j.tibs.2025.09.002","volume":"50","author":"A. Rakshit","year":"2025","unstructured":"Rakshit, A., and Palmer, A. E. (2025) Zn2+ transients and signaling in mammalian systems, Trends Biochem. Sci., 50, 1086-1101, \nhttps:\/\/doi.org\/10.1016\/j.tibs.2025.09.002.","journal-title":"Trends Biochem. Sci."},{"key":"3075_CR128","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1007\/978-94-007-2888-2_2","volume":"740","author":"J. D. Bruton","year":"2012","unstructured":"Bruton, J. D., Cheng, A. J., and Westerblad, H. (2012) Methods to detect Ca2+ in living cells, Adv. Exp. Med. Biol., 740, 27-43, \nhttps:\/\/doi.org\/10.1007\/978-94-007-2888-2_2.","journal-title":"Adv. Exp. Med. Biol."}],"container-title":["Biochemistry (Moscow)"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297926601115.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1134\/S0006297926601115","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297926601115.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T05:07:25Z","timestamp":1787980045000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1134\/S0006297926601115"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":128,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,8]]}},"alternative-id":["3075"],"URL":"https:\/\/doi.org\/10.1134\/s0006297926601115","relation":{},"ISSN":["0006-2979","1608-3040"],"issn-type":[{"value":"0006-2979","type":"print"},{"value":"1608-3040","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"9 April 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"7 July 2026","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 August 2026","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 August 2026","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Ethics approval and consent to participate.\n                      This work does not contain any studies involving human and animal subjects.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics declarations"}},{"value":"Conflict of interest.\n                      The authors of this work declare that they have no conflicts of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics declarations"}}]}}