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Proteomic profiles of proteins bound to the full-length RNLS and its peptide RP211-223 were significantly different, whereas RP224-232 bound a small number of proteins (6), similar to those bound to the full-length RNLS. However, most proteins bound to RNLS and its peptides were multifunctional and associated with neurodegenerative pathology (Alzheimer\u2019s and Parkinson\u2019s diseases, etc.).<\/jats:p>","DOI":"10.18097\/pbmcr1704","type":"journal-article","created":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T13:10:51Z","timestamp":1784034651000},"page":"220-229","source":"Crossref","is-referenced-by-count":0,"title":["Interaction of renalase and its peptides RP211-223 and RP224-232 with the mitochondrial fraction of rat brain: a link to neurodegeneration?"],"prefix":"10.18097","volume":"72","author":[{"given":"O.A.","family":"Buneeva","sequence":"first","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.I.","family":"Fedchenko","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.A.","family":"Kaloshina","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.A.","family":"Kaloshin","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.G.","family":"Zgoda","sequence":"additional","affiliation":[{"name":"Institute of Biomedical Chemistry, Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.E.","family":"Medvedev","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":"Xu J., Li G., Wang P., Velazquez H., Yao X., Li Y., Wu Y., Peixoto A., Crowley S., Desir G.V. (2005) Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure. J. Clin. Invest., 115(5), 1275\u20131280.","DOI":"10.1172\/JCI24066"},{"key":"ref2","doi-asserted-by":"publisher","unstructured":"Medvedev A.E., Veselovsky A.V., Fedchenko V.I. (2010) Renalase, a new secretory enzyme responsible for selective degradation of catecholamines: achievements and unsolved problems. Biochemistry (Moscow), 75(8), 951\u2013958.","DOI":"10.1134\/S0006297910080018"},{"key":"ref3","doi-asserted-by":"publisher","unstructured":"Baroni S., Milani M., Pandini V., Pavesi G., Horner D., Aliverti A. (2013) Is renalase a novel player in catecholaminergic signaling? The mystery of the catalytic activity of an intriguing new flavoenzyme. Curr. Pharm. Des., 19(14), 2540\u20132551.","DOI":"10.2174\/1381612811319140005"},{"key":"ref4","doi-asserted-by":"publisher","unstructured":"Desir G.V., Peixoto A.J. (2014) Renalase in hypertension and kidney disease. Nephrol. Dial. Transplant., 29(1), 22\u201328.","DOI":"10.1093\/ndt\/gft083"},{"key":"ref5","doi-asserted-by":"publisher","unstructured":"Moran G.R., Hoag M.R. (2017) The enzyme: renalase. Arch. Biochem. Biophys., 632, 66\u201376.","DOI":"10.1016\/j.abb.2017.05.015"},{"key":"ref6","doi-asserted-by":"publisher","unstructured":"Beaupre B.A., Hoag M.R., Roman J., F\u00f6rsterling F.H., Moran G.R. (2015) Metabolic function for human renalase: oxidation of isomeric forms of \u03b2-NAD(P)H that are inhibitory to primary metabolism. Biochemistry, 54(3), 795\u2013806.","DOI":"10.1021\/bi5013436"},{"key":"ref7","doi-asserted-by":"publisher","unstructured":"Wang Y., Safirstein R., Velazquez H., Guo X.-J., Hollander L., Chang J., Chen T.-M., Mu J.-J., Desir G.V. (2017) Extracellular renalase protects cells and organs by outside-in signalling. J. Cell. Mol. 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Hypotheses, 165, 110895.","DOI":"10.1016\/j.mehy.2022.110895"},{"key":"ref11","doi-asserted-by":"publisher","unstructured":"Buneeva O.A., Fedchenko V.I., Kaloshina S.A., Zavyalova M.G., Zgoda V.G., Medvedev A.E. (2024) Proteomic profiling of renal tissue of normo- and hypertensive rats with the renalase peptide RP220 as an affinity ligand. Biomeditsinskaya Khimiya, 70(3), 145\u2013155.","DOI":"10.18097\/PBMC20247003145"},{"key":"ref12","doi-asserted-by":"publisher","unstructured":"Xiong X., Xu Y.-Z., Zhang Y., Zhang H.-F., Dou T.-M., Li X.-Y., Xu Z.-Y., Cui C.-P., Li X.-L., Li B.-Y. (2025) Renalase overexpression-mediated excessive metabolism of peripheral dopamine, DOPAL accumulation, \u03b1-synuclein aggregation in baroreflex afferents contribute to neuronal degeneration and autonomic dysfunction. 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Science, 357(6357), 1255\u20131261.","DOI":"10.1126\/science.aam9080"},{"key":"ref15","doi-asserted-by":"publisher","unstructured":"Guo X., Chen R., Shugrue C., Shang F.-F., Milian R.G., Moller H., Licznerski P., Chen T., Kibbey R., M\u2019Saad O., Tian Y., Bewersdorf J., Giordano F., Gorelick F.S., Safirstein R., Jonas E.A., Desir G.V. (2025) Renalase activates mitochondrial leak metabolism in response to cellular stress and to repair damage after injury. bioRxiv [Preprint], 2025.08.19.671117.","DOI":"10.1101\/2025.08.19.671117"},{"key":"ref16","doi-asserted-by":"publisher","unstructured":"Fedchenko V.I., Kaloshin A.A. (2019) A simplified method for obtaining cDNA of low-copy and silent eukaryotic genes using human renalase as an example. Biomedical Chemistry: Research and Methods, 2(2), e00101.","DOI":"10.18097\/BMCRM00101"},{"key":"ref17","doi-asserted-by":"publisher","unstructured":"Fedchenko V., Kaloshin A., Mezhevikina L., Buneeva O., Medvedev A. 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(Engl.), 134(15), 1771\u20131779.","DOI":"10.1097\/CM9.0000000000001581"},{"key":"ref23","doi-asserted-by":"publisher","unstructured":"Gawinecka J., Ciesielczyk B., Sanchez-Juan P., Schmitz M., Heinemann U., Zerr I. (2012) Desmoplakin as a potential candidate for cerebrospinal fluid marker to rule out 14-3-3 false positive rates in sporadic Creutzfeldt-Jakob disease differential diagnosis. Neurodegener. Dis., 9(3), 139\u2013144.","DOI":"10.1159\/000334499"},{"key":"ref24","doi-asserted-by":"publisher","unstructured":"Bass-Zubek A.E., Godsel L.M., Delmar M., Green K.J. (2009) Plakophilins: multifunctional scaffolds for adhesion and signaling. Curr. Opin. Cell Biol., 21(5), 708\u2013716.","DOI":"10.1016\/j.ceb.2009.07.002"},{"key":"ref25","doi-asserted-by":"publisher","unstructured":"Wang H., Sun C., Liang Y., Zhang H., Tan Y. (2013) Identification of regulatory relationships in Parkinson\u2019s disease. J. Mol. Neurosci., 51(1), 9\u201312.","DOI":"10.1007\/s12031-012-9937-8"},{"key":"ref26","doi-asserted-by":"publisher","unstructured":"Didonna A., Opal P. (2019) The role of neurofilament aggregation in neurodegeneration: lessons from rare inherited neurological disorders. Mol. Neurodegener., 14, 19.","DOI":"10.1186\/s13024-019-0318-4"},{"key":"ref27","doi-asserted-by":"publisher","unstructured":"Leite A.C., Martins T.S., Campos A., Costa V., Pereira C. (2022) Phosphoregulation of the ATP synthase beta subunit stimulates mitochondrial activity for G2\/M progression. Adv. Biol. Regul., 85, 100905.","DOI":"10.1016\/j.jbior.2022.100905"},{"key":"ref28","doi-asserted-by":"publisher","unstructured":"Li J.-L., Lin T.-Y., Chen P.-L., Guo T.-N., Huang S.-Y., Chen C.-H., Lin C.-H., Chan C.-C. (2021) Mitochondrial function and Parkinson\u2019s disease: from the perspective of the electron transport chain. Front. Mol. Neurosci., 14, 797833.","DOI":"10.3389\/fnmol.2021.797833"},{"key":"ref29","doi-asserted-by":"publisher","unstructured":"Wang T., Zhao D., Zhang Y., Yu D., Liu G., Zhang K. (2024) Annexin A2: a double-edged sword in pathogen infection. Pathogens, 13(7), 564.","DOI":"10.3390\/pathogens13070564"},{"key":"ref30","doi-asserted-by":"publisher","unstructured":"Astillero-Lopez V., Villar-Conde S., Gonzalez-Rodriguez M., Flores-Cuadrado A., Ubeda-Banon I., Saiz-Sanchez D., Martinez-Marcos A. (2024) Proteomic analysis identifies HSP90AA1, PTK2B, ANXA2 in the human entorhinal cortex in Alzheimer\u2019s disease: potential role in synaptic homeostasis and A\u03b2 pathology through microglial and astroglial cells. Brain Pathol., 34(4), e13235.","DOI":"10.1111\/bpa.13235"},{"key":"ref31","doi-asserted-by":"publisher","unstructured":"Young S.M. Jr., Neher E. (2009) Synaptotagmin has an essential function in synaptic vesicle positioning for synchronous release in addition to its role as a calcium sensor. Neuron, 63(4), 482\u2013496.","DOI":"10.1016\/j.neuron.2009.07.028"},{"key":"ref32","doi-asserted-by":"publisher","unstructured":"Glavan G., Schliebs R., Zivin M. (2009) Synaptotagmins in neurodegeneration. Anat. Rec., 292(12), 1849\u20131862.","DOI":"10.1002\/ar.21026"},{"key":"ref33","doi-asserted-by":"publisher","unstructured":"Herrmann D.N., Horvath R., Sowden J.E., Gonzalez M., Sanchez-Mejias A., Guan Z., Whittaker R.G., Almodovar J.L., Lane M., Bansagi B., Pyle A., Boczonadi V., Lochm\u00fcller H., Griffin H., Chinnery P.F., Lloyd T.E., Littleton J.T., Zuchner S. (2014) Synaptotagmin 2 mutations cause an autosomal-dominant form of Lambert-Eaton myasthenic syndrome and nonprogressive motor neuropathy. Am. J. Hum. Genet., 95(3), 332\u2013339.","DOI":"10.1016\/j.ajhg.2014.08.007"},{"key":"ref34","doi-asserted-by":"publisher","unstructured":"Sandiford S.L., Dong Y., Pike A., Blumberg B.J., Bahia A.C., Dimopoulos G. (2015) Cytoplasmic actin is an extracellular insect immune factor which is secreted upon immune challenge and mediates phagocytosis and direct killing of bacteria, is a Plasmodium antagonist. PLOS Pathog., 11(2), e1004631.","DOI":"10.1371\/journal.ppat.1004631"},{"key":"ref35","doi-asserted-by":"publisher","unstructured":"Sarkar S., Olsen A.L., Sygnecka K., Lohr K.M., Feany M.B. (2021) \u03b1-Synuclein impairs autophagosome maturation through abnormal actin stabilization. PLOS Genet., 17(2), e1009359.","DOI":"10.1371\/journal.pgen.1009359"},{"key":"ref36","doi-asserted-by":"publisher","unstructured":"Cartelli D., Goldwurm S., Casagrande F., Pezzoli G., Cappelletti G. (2012) Microtubule destabilization is shared by genetic and idiopathic Parkinson\u2019s disease patient fibroblasts. 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Neurodegener., 11, 70.","DOI":"10.1186\/s13024-016-0135-y"},{"key":"ref40","doi-asserted-by":"publisher","unstructured":"Pauly B.S., Drubin D.G. (2007) Clathrin: an amazing multifunctional dreamcoat? Cell Host Microbe, 2(5), 288\u2013290.","DOI":"10.1016\/j.chom.2007.10.007"},{"key":"ref41","doi-asserted-by":"publisher","unstructured":"Schreij A.M.A., Chaineau M., Ruan W., Lin S., Barker P.A., Fon E.A., McPherson P.S. (2015) LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation. EMBO Rep., 16(1), 79\u201386.","DOI":"10.15252\/embr.201438714"},{"key":"ref42","doi-asserted-by":"publisher","unstructured":"D\u00edaz-Ramos A., Roig-Borrellas A., Garc\u00eda-Melero A., L\u00f3pez-Alemany R. (2012) \u03b1-Enolase, a multifunctional protein: its role on pathophysiological situations. J. Biomed. Biotechnol., 2012, 156795.","DOI":"10.1155\/2012\/156795"},{"key":"ref43","doi-asserted-by":"publisher","unstructured":"Pancholi V. (2001) Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci., 58(7), 902\u2013920.","DOI":"10.1007\/pl00000910"},{"key":"ref44","doi-asserted-by":"publisher","unstructured":"Patel S., Sinha A., Singh M.P. (2007) Identification of differentially expressed proteins in striatum of maneb- and paraquat-induced Parkinson\u2019s disease phenotype in mouse. Neurotoxicol.Teratol., 29(5), 578\u2013585.","DOI":"10.1016\/j.ntt.2007.04.002"},{"key":"ref45","doi-asserted-by":"publisher","unstructured":"Poon H.F., Frasier M., Shreve N., Calabrese V., Wolozin B., Butterfield D.A. (2005) Mitochondrial associated metabolic proteins are selectively oxidized in A30P alpha-synuclein transgenic mice \u2014 a model of familial Parkinson\u2019s disease. Neurobiol. Dis., 18(3), 492\u2013498.","DOI":"10.1016\/j.nbd.2004.12.009"},{"key":"ref46","doi-asserted-by":"publisher","unstructured":"Blosa M., Sonntag M., J\u00e4ger C., Weigel S., Seeger J., Frischknecht R., Seidenbecher C.I., Matthews R.T., Arendt T., R\u00fcbsamen R., Morawski M. (2015) The extracellular matrix molecule brevican is an integral component of the machinery mediating fast synaptic transmission at the calyx of Held. J. Physiol., 593(19), 4341\u20134360.","DOI":"10.1113\/JP270849"},{"key":"ref47","doi-asserted-by":"publisher","unstructured":"Lin X., Shi M., Masilamoni J.G., Dator R., Movius J., Aro P., Smith Y., Zhang J. (2015) Proteomic profiling in MPTP monkey model for early Parkinson disease biomarker discovery. Biochim. Biophys. Acta, 1854(7), 779\u2013787.","DOI":"10.1016\/j.bbapap.2015.01.007"},{"key":"ref48","doi-asserted-by":"publisher","unstructured":"Jonesco D.S., Karsdal M.A., Henriksen K. 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(2021) Peroxiredoxin 1 \u2014 multifunctional antioxidant enzyme, protects from oxidative damages and increases the survival rate of mice exposed to total body irradiation. Arch. Biochem. Biophys., 697, 108671.","DOI":"10.1016\/j.abb.2020.108671"},{"key":"ref55","doi-asserted-by":"publisher","unstructured":"Roede J.R., Hansen J.M., Go Y.-M., Jones D.P. (2011) Maneb and paraquat-mediated neurotoxicity: involvement of peroxiredoxin\/thioredoxin system. Toxicol. Sci., 121(2), 368\u2013375.","DOI":"10.1093\/toxsci\/kfr058"},{"key":"ref56","doi-asserted-by":"publisher","unstructured":"Addison W.N., Pellicelli M., St-Arnaud R. (2019) Dephosphorylation of the transcriptional cofactor NACA by the PP1A phosphatase enhances cJUN transcriptional activity and osteoblast differentiation. J. Biol. Chem., 294(20), 8184\u20138196.","DOI":"10.1074\/jbc.RA118.006920"},{"key":"ref57","doi-asserted-by":"publisher","unstructured":"Labbadia J., Morimoto R.I. (2015) The biology of proteostasis in aging and disease.Annu. Rev. Biochem., 84, 435\u2013464.","DOI":"10.1146\/annurev-biochem-060614-033955"},{"key":"ref58","doi-asserted-by":"publisher","unstructured":"Kelly C.J., Couch R.K., Ha V.T., Bodart C.M., Wu J., Huff S., Herrel N.T., Kim H.D., Zimmermann A.O., Shattuck J., Pan Y.-C., Kaeberlein M., Grillo A.S. (2023) Iron status influences mitochondrial disease progression in Complex I-deficient mice. eLife, 12, e75825.","DOI":"10.7554\/eLife.75825"},{"key":"ref59","doi-asserted-by":"publisher","unstructured":"Shamilov R., Robinson V.L., Aneskievich B.J. (2021) Seeing keratinocyte proteins through the looking glass of intrinsic disorder. Int. J. Mol. Sci., 22(15), 7912.","DOI":"10.3390\/ijms22157912"},{"key":"ref60","doi-asserted-by":"publisher","unstructured":"Henrich M.T., Oertel W.H., Surmeier D.J., Geibl F.F. (2023) Mitochondrial dysfunction in Parkinson\u2019s disease \u2014 a key disease hallmark with therapeutic potential. Mol. 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(2024) Linking acetylated \u03b1-tubulin redistribution to \u03b1-synuclein pathology in brain of Parkinson\u2019s disease patients. NPJ Parkinsons Dis., 10, 2.","DOI":"10.1038\/s41531-023-00607-9"},{"key":"ref79","doi-asserted-by":"publisher","unstructured":"Hammond J.W., Cai D., Verhey K.J. (2008) Tubulin modifications and their cellular functions. Curr. Opin. Cell Biol., 20(1), 71\u201376.","DOI":"10.1016\/j.ceb.2007.11.010"},{"key":"ref80","doi-asserted-by":"publisher","unstructured":"Binarov\u00e1 P., Tuszynski J. (2019) Tubulin: structure, functions and roles in disease. Cells, 8(10), 1294.","DOI":"10.3390\/cells8101294"},{"key":"ref81","doi-asserted-by":"publisher","unstructured":"Michurina S., Beloglazova I., Agareva M., Alekseeva N., Parfyonova Y., Stafeev I. (2025) Creation of genetically modified adipocytes for tissue engineering: creatine kinase B overexpression leads to stimulated glucose uptake and mitochondrial potential growth, but lowered lipid synthesis. Life (Basel), 15(5), 753.","DOI":"10.3390\/life15050753"},{"key":"ref82","doi-asserted-by":"publisher","unstructured":"Vassilopoulos D., Jockers-Wretou E. (1987) Serum creatine kinase B levels in diseases of the central nervous system. Eur. Neurol., 27(2), 78\u201381.","DOI":"10.1159\/000116135"},{"key":"ref83","doi-asserted-by":"publisher","unstructured":"van Laar V.S., Dukes A.A., Cascio M., Hastings T.G. (2008) Proteomic analysis of rat brain mitochondria following exposure to dopamine quinone: implications for Parkinson disease. Neurobiol. Dis., 29(3), 477\u2013489.","DOI":"10.1016\/j.nbd.2007.11.007"},{"key":"ref84","doi-asserted-by":"publisher","unstructured":"Zhao Y., Xing C., Peng H. (2024) ALYREF (Aly\/REF export factor): a potential biomarker for predicting cancer occurrence and therapeutic efficacy. 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(2024) Dopamine modification of glycolytic enzymes impairs glycolysis: possible implications for Parkinson\u2019s disease. Cell Commun. Signal., 22, 75.","DOI":"10.1186\/s12964-024-01478-0"},{"key":"ref91","doi-asserted-by":"publisher","unstructured":"Dukes A.A., van Laar V.S., Cascio M., Hastings T.G. (2008) Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine. J. Neurochem., 106(1), 333\u2013346.","DOI":"10.1111\/j.1471-4159.2008.05392.x"},{"key":"ref92","doi-asserted-by":"crossref","unstructured":"Helfman D.M., Kuo J.F. (1982) A homogeneous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides. J. Biol. Chem., 257(2), 1044\u20131047.","DOI":"10.1016\/S0021-9258(19)68305-5"},{"key":"ref93","doi-asserted-by":"publisher","unstructured":"Takagi S., Hayakawa N., Kimoto H., Kato H., Araki T. (2007) Damage to oligodendrocytes in the striatum after MPTP neurotoxicity in mice. J. 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Innate Immun., 4(4), 349\u2013360.","DOI":"10.1159\/000336844"},{"key":"ref97","doi-asserted-by":"publisher","unstructured":"Yong S.J., Teoh S.L., Parhar I.S., Soga T., Lim W.L., Chew J. (2025) Antimicrobial peptides and proteins in Alzheimer\u2019s and Parkinson\u2019s diseases: implications for biomarker exploration. Rev. Neurosci., 36(8), 849\u2013879.","DOI":"10.1515\/revneuro-2025-0034"},{"key":"ref98","doi-asserted-by":"publisher","unstructured":"Hynes R.O., Yamada K.M. (1982) Fibronectins: multifunctional modular glycoproteins. J. Cell Biol., 95(2 Pt 1), 369\u2013377.","DOI":"10.1083\/jcb.95.2.369"},{"key":"ref99","doi-asserted-by":"publisher","unstructured":"Zhu S., Li H., Huang Z., Zeng Y., Huang J., Li G., Yang S., Zhou H., Chang Z., Xie Z., Que R., Wei X., Li M., Liang Y., Xian W., Li M., Pan Y., Huang F., Shi L., Yang C., Deng C., Batzu L., Poplawska-Domaszewicz K., Chen S., Chan L.-L., Ray Chaudhuri K., Tan E.-K., Wang Q. (2025) Plasma fibronectin is a prognostic biomarker of disability in Parkinson\u2019s disease: a prospective, multicenter cohort study. NPJ Parkinsons Dis., 11, 1.","DOI":"10.1038\/s41531-024-00865-1"},{"key":"ref100","doi-asserted-by":"publisher","unstructured":"Oikonomou K.G., Zachou K., Dalekos G.N. (2011) Alpha-actinin: a multidisciplinary protein with important role in B-cell driven autoimmunity. Autoimmun. Rev., 10(7), 389\u2013396.","DOI":"10.1016\/j.autrev.2010.12.009"},{"key":"ref101","doi-asserted-by":"publisher","unstructured":"Sahni A., Sahni S.K. (2026) Fibrinogen and fibrin as growth factor regulators: pathological implications, translational opportunities. 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Pharmacol., 230(Pt 3), 116633.","DOI":"10.1016\/j.bcp.2024.116633"},{"key":"ref108","doi-asserted-by":"publisher","unstructured":"Shi H., Fang W., Liu M., Fu D. (2017) Complement component 1, q subcomponent binding protein (C1QBP) in lipid rafts mediates hepatic metastasis of pancreatic cancer by regulating IGF-1\/IGF-1R signaling. Int. J. Cancer, 141(7), 1389\u20131401.","DOI":"10.1002\/ijc.30831"},{"key":"ref109","doi-asserted-by":"publisher","unstructured":"Barna J., Dim\u00e9n D., Puska G., Kov\u00e1cs D., Csik\u00f3s V., Ol\u00e1h S., Udvari E.B., P\u00e1l G., Dobolyi \u00c1. (2019) Complement component 1q subcomponent binding protein in the brain of the rat. Sci. Rep., 9, 4597.","DOI":"10.1038\/s41598-019-40788-z"},{"key":"ref110","doi-asserted-by":"publisher","unstructured":"Chant J. (1994) Multifunctional proteins. Calmodulin clarified. Curr. Biol., 4(5), 433\u2013435.","DOI":"10.1016\/s0960-9822(00)00095-6"},{"key":"ref111","doi-asserted-by":"publisher","unstructured":"Bohush A., Le\u015bniak W., Weis S., Filipek A. (2021) Calmodulin and its binding proteins in Parkinson\u2019s disease. Int. J. Mol. Sci., 22(6), 3016.","DOI":"10.3390\/ijms22063016"},{"key":"ref112","doi-asserted-by":"publisher","unstructured":"Hurley M.J., Brandon B., Gentleman S.M., DexterD.T. (2013) Parkinson\u2019s disease is associated with altered expression of CaV1 channels and calcium-binding proteins. Brain, 136(Pt 7), 2077\u20132097.","DOI":"10.1093\/brain\/awt134"},{"key":"ref113","doi-asserted-by":"publisher","unstructured":"O\u2019Day D.H. (2024) The complex interplay between toxic hallmark proteins, calmodulin-binding proteins, ion channels, receptors involved in calcium dyshomeostasis in neurodegeneration. Biomolecules, 14(2), 173.","DOI":"10.3390\/biom14020173"},{"key":"ref114","doi-asserted-by":"publisher","unstructured":"Buneeva O.A., Medvedev A.E. (2017) Atypical ubiquitination of proteins. Biomeditsinskaya Khimiya, 62(5), 496\u2013509.","DOI":"10.1134\/S1990750817010024"},{"key":"ref115","doi-asserted-by":"publisher","unstructured":"Buneeva O., Medvedev A. (2022) Atypical ubiquitination and Parkinson\u2019s disease. Int. J. Mol. Sci., 23(7), 3705.","DOI":"10.3390\/ijms23073705"},{"key":"ref116","doi-asserted-by":"publisher","unstructured":"McKeon J.E., Sha D., Li L., Chin L.-S. (2015) Parkin-mediated K63-polyubiquitination targets ubiquitin C-terminal hydrolase L1 for degradation by the autophagylysosome system. Cell. Mol. Life Sci., 72(9), 1811\u20131824.","DOI":"10.1007\/s00018-014-1781-2"},{"key":"ref117","doi-asserted-by":"publisher","unstructured":"Boggs J.M. (2006) Myelin basic protein: a multifunctional protein. Cell. Mol. 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