1. Научно-исследовательский институт биомедицинской химии имени В.Н. Ореховича, Москва, Россия 2. Федеральный исследовательский центр оригинальных и перспективных биомедицинских и фармацевтических технологий, Москва, Россия
Изатин (индол-2,3-дион) — эндогенный регулятор, присутствующий в организме человека и животных. Благодаря способности взаимодействовать с многочисленными белками-мишенями, изатин демонстрирует широкий спектр биологической активности, в том числе проявляет нейропротекторное действие в моделях болезни Паркинсона (БП) у грызунов с использованием нейротоксинов МФТП (1-метил-4-фенил-1,2,3,6- тетрагидропиридина) и ротенона. Антипсихотический препарат галоперидол, нарушая баланс нейромедиаторов в нигростриатном пути, моделирует дефицит дофамина и способствует развитию двигательных нарушений, свойственных БП. В данной работе исследовали действие двух доз изатина (10 мг/кг и 80 мг/кг) на индуцированную галоперидолом каталепсию и на протеомный профиль мозга мышей. Предварительное введение изатина (за 1 ч до введения галоперидола) снижало выраженность галоперидоловой каталепсии. Введение галоперидола и изатина совместно с галоперидолом оказывало влияние на относительное содержание ряда белков, ассоциированных с БП и другими нейродегенеративными заболеваниями.
Бунеева О.А., Капица И.Г., Завьялова М.Г., Калошина С.А., Згода В.Г., Медведев А.Е. (2026) Влияние нейропротектора изатина на индуцированную галоперидолом каталепсию и протеомный профиль мозга мышей. Биомедицинская химия, 72(4), 267-278.
Бунеева О.А. и др. Влияние нейропротектора изатина на индуцированную галоперидолом каталепсию и протеомный профиль мозга мышей // Биомедицинская химия. - 2026. - Т. 72. -N 4. - С. 267-278.
Бунеева О.А. и др., "Влияние нейропротектора изатина на индуцированную галоперидолом каталепсию и протеомный профиль мозга мышей." Биомедицинская химия 72.4 (2026): 267-278.
Бунеева, О. А., Капица, И. Г., Завьялова, М. Г., Калошина, С. А., Згода, В. Г., Медведев, А. Е. (2026). Влияние нейропротектора изатина на индуцированную галоперидолом каталепсию и протеомный профиль мозга мышей. Биомедицинская химия, 72(4), 267-278.
Список литературы
Medvedev A., Buneeva O., Glover V. (2007) Biological targets for isatin and its analogues: implications for therapy. Biologics, 1(2), 151–162. Scholar google search
Medvedev A., Buneeva O., Gnedenko O., Ershov P., Ivanov A. (2018) Isatin, an endogenous nonpeptide biofactor: a review of its molecular targets, mechanisms of actions, and their biomedical implications. Biofactors, 44(2), 95–108. CrossRef Scholar google search
Buneeva O., Medvedev A. (2025) Monoamine oxidase inhibitors in toxic models of parkinsonism. Int. J. Mol. Sci., 26(3), 1248. CrossRef Scholar google search
Бунеева О.А., Капица И.Г., Казиева Л.Ш., Вавилов Н.Э., Згода В.Г., Медведев А.Е. (2024) Отсроченное действие ротенона на относительное содержание изатин- связывающих белков мозга у крыс с экспериментальным паркинсонизмом. Биомедицинская химия, 70(1), 25–32. CrossRef Scholar google search
Buneeva O., Kopylov A., Kapitsa I., Ivanova E., Zgoda V., Medvedev A. (2018) The effect of neurotoxin MPTP and neuroprotector isatin on the profile of ubiquitinated brain mitochondrial proteins. Cells, 7(8), 91. CrossRef Scholar google search
Капица И.Г., Казиева Л.Ш., Вавилов Н.Э., Згода В.Г., Копылов А.Т., Медведев А.Е., Бунеева О.А. (2023) Особенности поведенческих реакций и профиля изатин-связывающих белков мозга у крыс с индуцированным ротеноном экспериментальным паркинсонизмом. Биомедицинская химия, 69(1), 46–54. CrossRef Scholar google search
Singer T.P., Ramsay R.R. (1990) Mechanism of the neurotoxicity of MPTP: an update. FEBS Lett., 274(1–2), 1–8. CrossRef Scholar google search
Бунеева О.А., Капица И.Г., Казиева Л.Ш., Вавилов Н.Э., Згода В.Г., Медведев А.Е. (2024) Нейропротекторное действие изатина в ротеноновой модели паркинсонизма у крыс: исследование отсроченных эффектов. Биомедицинская химия, 70(4), 231–239. CrossRef Scholar google search
Бунеева О.А., Капица И.Г., Казиева Л.Ш., Вавилов Н.Э., Згода В.Г. (2023) Количественные изменения изатин- связывающих белков мозга у крыс с индуцированным ротеноном экспериментальным паркинсонизмом. Биомедицинская химия, 69(3), 188–192. CrossRef Scholar google search
Waku I., Magalhães M.S., Alves C.O., de Oliveira A.R. (2021) Haloperidol-induced catalepsy as an animal model for parkinsonism: a systematic review of experimental studies. Eur. J. Neurosci., 53(11), 3743–3767. CrossRef Scholar google search
Sharma A.K., Gupta S., Patel R.K., Wardhan N. (2018) Haloperidol-induced parkinsonism is attenuated by varenicline in mice. J. Basic Clin. Physiol. Pharmacol., 29(4), 395–401. CrossRef Scholar google search
Kabra A., Baghel U.S., Hano C., Martins N., Khalid M., Sharma R. (2020) Neuroprotective potential of Myrica esculenta in haloperidol induced Parkinson’s disease. J. Ayurveda Integr. Med., 11(4), 448–454. CrossRef Scholar google search
Valdman E., Kapitsa I., Ivanova Е., Voronina T., Ardashov O., Volcho K., Khazanov V., Salakhutdinov N. (2017) Evolution of anti-parkinsonian activity of monoterpenoid (1R,2R,6S)-3-methyl-6-(prop-1-en-2-yl)cyclohex-3-ene- 1,2-diol in various in vivo models. Eur. J. Pharmacol., 815, 351–363. CrossRef Scholar google search
Hattori K., Uchino S., Isosaka T., Maekawa M., Iyo M., Sato T., Kohsaka S., Yagi T., Yuasa S. (2006) Fyn is required for haloperidol-induced catalepsy in mice. J. Biol. Chem., 281(11), 7129–7135. CrossRef Scholar google search
Иванова Е.А., Непоклонов А.В., Кокшенев И.И., Капица И.Г., Воронина Т.А., Вальдман Е.А. (2012) Изучение антикаталептической активности гимантана при различных путях введения и в комбинации с леводопой. Биомедицина, 1, 74–81. Scholar google search
Воронина Т.А., Вальдман Е.А., Неробкова Л.Н., Капица И.Г. (2012) Методические рекомендации по доклиническому изучению лекарственных средств с противопаркинсонической активностью. В кн.: Руководство по проведению доклинических исследований лекарственных средств. Часть первая (Миронов А.Н., ред.). М.: Гриф и К, с. 251–263. Scholar google search
Volpe J.J. (2008) Hyperammonemia and other disorders of amino acid metabolism. In: Neurology of the Newborn (Fifth Edition) (Volpe J.J., ed.). W.B. Saunders, Philadelphia, pp. 652–685. CrossRef Scholar google search
Zhang L., Zou Y., Lu Y., Li Z., Gao F. (2023) Unraveling the therapeutic potential of carbamoyl phosphate synthetase 1 (CPS1) in human diseases. Bioorg. Chem., 130, 106253. CrossRef Scholar google search
Häberle J., Shchelochkov O.A., Wang J., Katsonis P., Hall L., Reiss S., Eeds A., Willis A., Yadav M., Summar S.; Urea Cycle Disorders Consortium; Lichtarge O., Rubio V., Wong L.-J., Summar M. (2011) Molecular defects in human carbamoyl phosphate synthetase I: mutational spectrum, diagnostic and protein structure considerations. Hum. Mutat., 32(6), 579–589. CrossRef Scholar google search
Chen B., Zhang Q., Zhong X., Zhang X., Liu X., Wang H., Yang F., Zhang J., Huang J., Wong Y.-K., Luo P., Wang J., Sun J. (2024) Dopamine modification of glycolytic enzymes impairs glycolysis: possible implications for Parkinson’s disease. Cell Commun. Signal., 22, 75. CrossRef Scholar google search
Luo J.J., Zhang L., Dun N.J. (2022) Homocysteine and dementia in Parkinson disease. In: Dementia in Parkinson’s Disease — Everything You Need to Know. IntechOpen, 238 p. CrossRef Scholar google search
Martignoni E., Tassorelli C., Nappi G., Zangaglia R., Pacchetti C., Blandini F. (2007) Homocysteine and Parkinson’s disease: a dangerous liaison? J. Neurol. Sci., 257(1–2), 31–37. CrossRef Scholar google search
Naoi M., Maruyama W., Inaba-Hasegawa K. (2012) Type A and B monoamine oxidase in age-related neurodegenerative disorders: their distinct roles in neuronal death and survival. Curr. Top. Med. Chem., 12(20), 2177–2188. CrossRef Scholar google search
Alborghetti M., Bianchini E., de Carolis L., Galli S., Pontieri F.E., Rinaldi D. (2024) Type-B monoamine oxidase inhibitors in neurological diseases: clinical applications based on preclinical findings. Neural Regen. Res., 19(1), 16–21. CrossRef Scholar google search
Arnold S. (2012) Cytochrome c oxidase and its role in neurodegeneration and neuroprotection. Adv. Exp. Med. Biol., 748, 305–339. CrossRef Scholar google search
Erhardt B., Marcora M.S., Frenkel L., Bochicchio P.A., Bodin D.H., Silva B.A., Farías M.I., Allo M.Á., Höcht C., Ferrari C.C., Pitossi F.J., Leal M.C. (2021) Plasma membrane calcium ATPase downregulation in dopaminergic neurons alters cellular physiology and motor behaviour in Drosophila melanogaster. Eur. J. Neurosci., 54(6), 5915–5931. CrossRef Scholar google search
Ebanks B., Chakrabarti L. (2022) Mitochondrial ATP synthase is a target of oxidative stress in neurodegenerative diseases. Front. Mol. Biosci., 9, 854321. CrossRef Scholar google search
Anvret A., Ran C., Westerlund M., Sydow O., Willows T., Olson L., Galter D., Belin A.C. (2012) Genetic screening of the mitochondrial Rho GTPases MIRO1 and MIRO2 in Parkinson’s disease. Open Neurol. J., 6, 1–5. CrossRef Scholar google search
Alberio T., McMahon K., Cuccurullo M., Gethings L.A., Lawless C., Zibetti M., Lopiano L., Vissers J.P.C., Fasano M. (2014) Verification of a Parkinson’s disease protein signature in T-lymphocytes by multiple reaction monitoring. J. Proteome Res., 13(8), 3554–3561. CrossRef Scholar google search
Santulli C., Bon C., de Cecco E., Codrich M., Narkiewicz J., Parisse P., Perissinotto F., Santoro C., Persichetti F., Legname G., Espinoza S., Gustincich S. (2022) Neuronal haemoglobin induces loss of dopaminergic neurons in mouse substantia nigra, cognitive deficits and cleavage of endogenous α-synuclein. Cell Death Dis., 13(12), 1048. CrossRef Scholar google search
Graham J., Hobson D., Ponnampalam A. (2014) High affinity hemoglobin and Parkinson’s disease. Med. Hypotheses, 83(6), 819–821. CrossRef Scholar google search
Padhan P., Simran, Kumar N., Verma S. (2025) Glutathione S-transferase: a keystone in Parkinson’s disease pathogenesis and therapy. Mol. Cell. Neurosci., 132, 103981. CrossRef Scholar google search
Kim J.H., Lee H.-K., Takamiya K., Huganir R.L. (2003) The role of synaptic GTPase-activating protein in neuronal development and synaptic plasticity. J. Neurosci., 23(4), 1119–1124. CrossRef Scholar google search
Masoudi N., Ibanez-Cruceyra P., Offenburger S.-L., Holmes A., GartnerA. (2014) Tetraspanin (TSP-17) protects dopaminergic neurons against 6-OHDA-induced neurodegeneration in C. elegans. PLOS Genet., 10(12), e1004767. CrossRef Scholar google search
Warth Perez Arias C.C., Silbern I., Caldi Gomes L., Wartmann H., Dambeck V., Fanz J., Neuenroth L., Bähr M., Outeiro T.F., Bonn S., Stadelmann-Nessler C., Rizzoli S.O., Lenz C., Urlaub H., Lingor P. (2023) Proteomic analysis of the human hippocampus identifies neuronal pentraxin 1 (NPTX1) as synapto-axonal target in late-stage Parkinson’s disease. J. Neurochem., 166(5), 862–874. CrossRef Scholar google search
Gómez de San José N., Massa F., Halbgebauer S., Oeckl P., Steinacker P., Otto M. (2022) Neuronal pentraxins as biomarkers of synaptic activity: from physiological functions to pathological changes in neurodegeneration. J. Neural Transm., 129(2), 207–230. CrossRef Scholar google search
Wang C., Kang X., Zhou L., Chai Z., Wu Q., Huang R., Xu H., Hu M., Sun X., Sun S., Li J., Jiao R., Zuo P., Zheng L., Yue Z., Zhou Z. (2018) Synaptotagmin-11 is a critical mediator of parkin-linked neurotoxicity and Parkinson’s disease-like pathology. Nat. Commun., 9, 81. CrossRef Scholar google search
Ho G.P.H., Wilkie E.C., White A.J., Selkoe D.J. (2023) Palmitoylation of the Parkinson’s disease-associated protein synaptotagmin-11 links its turnover to α-synuclein homeostasis. Sci. Signal., 16(772), eadd7220. CrossRef Scholar google search
Mazzetti S., Giampietro F., Calogero A.M., Isilgan H.B., Gagliardi G., Rolando C., Cantele F., Ascagni M., Bramerio M., Giaccone G., Isaias I.U., Pezzoli G., Cappelletti G. (2024) Linking acetylated α-tubulin redistribution to α-synuclein pathology in brain of Parkinson’s disease patients. NPJ Parkinsons Dis., 10, 2. CrossRef Scholar google search
Ren Y., Zhao J., Feng J. (2003) Parkin binds to α/β tubulin and increases their ubiquitination and degradation. J. Neurosci., 23(8), 3316–3324. CrossRef Scholar google search
Shi X., Jiang X., Chen C., Zhang Y., Sun X. (2022) The interconnections between the microtubules and mitochondrial networks in cardiocerebrovascular diseases: implications for therapy. Pharmacol. Res., 184, 106452. CrossRef Scholar google search
Zhou X., Liao W.-J., Liao J.-M., Liao P., Lu H. (2015) Ribosomal proteins: functions beyond the ribosome. J. Mol. Cell Biol., 7(2), 92–104. CrossRef Scholar google search
Wang W., Nag S., Zhang X., Wang M.-H., Wang H., Zhou J., Zhang R. (2015) Ribosomal proteins and human diseases: pathogenesis, molecular mechanisms, and therapeutic implications. Med. Res. Rev., 35(2), 225–285. CrossRef Scholar google search
Egorova P.A., Bezprozvanny I.B. (2018) Inositol 1,4,5-trisphosphate receptors and neurodegenerative disorders. FEBS J., 285(19), 3547–3565. CrossRef Scholar google search
Duan W., Ladenheim B., Cutler R.G., Kruman I.I., Cadet J.L., Mattson M.P. (2002) Dietary folate deficiency and elevated homocysteine levels endanger dopaminergic neurons in models of Parkinson’s disease. J. Neurochem., 80(1), 101–110. CrossRef Scholar google search
Bhatt M., di Iacovo A., Romanazzi T., Roseti C., Bossi E. (2023) Betaine — the dark knight of the brain. Basic Clin. Pharmacol. Toxicol., 133(5), 485–495. CrossRef Scholar google search
Chen C.-H., Joshi A.U., Mochly-Rosen D. (2016) The role of mitochondrial aldehyde dehydrogenase 2 (ALDH2) in neuropathology and neurodegeneration. Acta Neurol. Taiwan., 25(4), 111–123. Scholar google search
Lee T.V., Chen C., Allison K.S., Li Y., Al-Ramahi I., Bagchi P., Levey A.I., Botas J., Seyfried N.T., Shulman J.M. (2023) The cytoskeletal protein plectin regulates Tau-induced neurotoxicity in Alzheimer’s disease. Alzheimers Dement., 19(S12), e078952. CrossRef Scholar google search
McMillan H.J., Worthylake T., Schwartzentruber J., Gottlieb C.C., Lawrence S.E., Mackenzie A., Beaulieu C.L., Mooyer P.A.W.; FORGE Canada Consortium; Wanders R.J.A., Majewski J., Bulman D.E., Geraghty M.T., Ferdinandusse S., Boycott K.M. (2012) Specific combination of compound heterozygous mutations in 17β-hydroxysteroid dehydrogenase type 4 (HSD17B4) defines a new subtype of D-bifunctional protein deficiency. Orphanet J. Rare Dis., 7, 90. CrossRef Scholar google search
Li X., Yu L., Liu X., Shi T., Zhang Y., Xiao Y., Wang C., Song L., Li N., Liu X., Chen Y., Petersen R.B., Cheng X., Xue W., Yu Y.V., Xu L., Zheng L., Chen H., Huang K. (2024) β-Synuclein regulates the phase transitions and amyloid conversion of α-synuclein. Nat. Commun., 15, 8748. CrossRef Scholar google search
Barba L., Paolini Paoletti F., Bellomo G., Gaetani L., Halbgebauer S., Oeckl P., Otto M., Parnetti L. (2022) Alpha and beta synucleins: from pathophysiology to clinical application as biomarkers. Mov. Disord., 37(4), 669–683. CrossRef Scholar google search
Chung I., Park H.-A, Kang J., Kim H., Hah S.M., Lee J., Kim H.S., Choi W.-S., Chung J.H., Shin M.-J. (2022) Neuroprotective effects of ATPase inhibitory factor 1 preventing mitochondrial dysfunction in Parkinson’s disease. Sci. Rep., 12, 3874. CrossRef Scholar google search
Severa M., Zhang J., Giacomini E., Rizzo F., Etna M.P., Cruciani M., Garaci E., Chopp M., Coccia E.M. (2019) Thymosins in multiple sclerosis and its experimental models: moving from basic to clinical application. Mult. Scler. Relat. Disord., 27, 52–60. CrossRef Scholar google search
Xing Y., Ye Y., Zuo H., Li Y. (2021) Progress on the function and application of thymosin β4. Front. Endocrinol., 12, 767785. CrossRef Scholar google search
Towns T.J. (2024) An investigation into the varied roles of phosphoprotein enriched in astrocytes-15kD (PEA15) in energy metabolism, metabolic flexibility, and gyrencephalic neurodevelopment. PhD Dissertation, Auburn University, Auburn, AL. Scholar google search
Ma X., Zhang H., Yin H., Geng S., Liu Y., Liu C., Zhao J., Liu Y., Wang X., Wang Y. (2021) Up-regulated microRNA-218-5p ameliorates the damage of dopaminergic neurons in rats with Parkinson’s disease via suppression of LASP1. Brain Res. Bull., 166, 92–101. CrossRef Scholar google search
Phillips G.R., Anderson T.R., Florens L., Gudas C., Magda G., Yates J.R. 3rd, Colman D.R. (2004) Actin-binding proteins in a postsynaptic preparation: lasp-1 is a component of central nervous system synapses and dendritic spines. J. Neurosci. Res., 78, 38–48. CrossRef Scholar google search
Walensky L.D., Shi Z.T., Blackshaw S., DeVries A.C., Demas G.E., Gascard P., Nelson R.J., Conboy J.G., Rubin E.M., Snyder S.H., Mohandas N. (1998) Neurobehavioral deficits in mice lacking the erythrocyte membrane cytoskeletal protein 4.1. Curr. Biol., 8(23), 1269–1272. CrossRef Scholar google search
Hagmeyer S., Romão M.A., Cristóvão J.S., Vilella A., Zoli M., Gomes C.M., Grabrucker A.M. (2019) Distribution and relative abundance of S100 proteins in the brain of the APP23 Alzheimer’s disease model mice. Front. Neurosci., 13, 640. CrossRef Scholar google search
Cristóvão J.S., Gomes C.M. (2019) S100 proteins in Alzheimer’s disease. Front. Neurosci., 13, 463. CrossRef Scholar google search
Bar-Am O., Yogev-Falach M., Amit T., Sagi Y., Youdim M.B.H. (2004) Regulation of protein kinase C by the anti-Parkinson drug, MAO-B inhibitor, rasagiline and its derivatives, in vivo. J. Neurochem., 89(5), 1119–1125. CrossRef Scholar google search
Chen Z., Zhang W., Selmi C., Ridgway W.M., Leung P.S.C., Zhang F., Gershwin M.E. (2021) The myristoylated alanine-rich C-kinase substrates (MARCKS): a membraneanchored mediator of the cell function. Autoimmun. Rev., 20(11), 102942. CrossRef Scholar google search
Gagliardi D., Pagliari E., Meneri M., Melzi V., Rizzo F., Comi G.P., Corti S., Taiana M., Nizzardo M. (2022) Stathmins and motor neuron diseases: pathophysiology and therapeutic targets. Biomedicines, 10(3), 711. CrossRef Scholar google search
Nelke A., García-López S., Martínez-Serrano A., Pereira M.P. (2022) Multifactoriality of Parkinson’s disease as explored through human neural stem cells and their transplantation in middle-aged Parkinsonian mice. Front. Pharmacol., 12, 773925. CrossRef Scholar google search
Dagda R.K., Banerjee T.D. (2015) Role of PKA in regulating mitochondrial function and neuronal development: implications to neurodegenerative diseases. Rev. Neurosci., 26(3), 359–370. CrossRef Scholar google search
Greggio E., Bubacco L., Russo I. (2017) Cross-talk between LRRK2 and PKA: implication for Parkinson’s disease? Biochem. Soc. Trans., 45(1), 261–267. CrossRef Scholar google search
Flerlage W.J., dell’Acqua M.L., Cox B.M., Nugent F.S. (2025) Emerging role of A-kinase anchoring protein 5 signaling in reward circuit function. Neural Regen. Res., 20(10), 2913–2914. CrossRef Scholar google search
Remnestål J., Just D., Mitsios N., Fredolini C., Mulder J., Schwenk J.M., UhlénM., Kultima K., IngelssonM., Kilander L., Lannfelt L., Svenningsson P., Nellgård B., Zetterberg H., Blennow K., Nilsson P., Häggmark-Månberg A. (2016) CSF profiling of the human brain enriched proteome reveals associations of neuromodulin and neurogranin to Alzheimer’s disease. Proteomics Clin. Appl., 10(12), 1242–1253. CrossRef Scholar google search
Calabresi P., Mechelli A., Natale G., Volpicelli-Daley L., di Lazzaro G., Ghiglieri V. (2023) Alpha-synuclein in Parkinson’s disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction. Cell Death Dis., 14(3), 176. CrossRef Scholar google search
Stefanis L. (2012) α-Synuclein in Parkinson’s disease. Cold Spring Harb. Perspect. Med., 2(2), a009399. CrossRef Scholar google search
Santaella A., Kuiperij H.B., van Rumund A., Esselink R.A.J., Bloem B.R., Verbeek M.M. (2020) Cerebrospinal fluid myelin basic protein is elevated in multiple system atrophy. Parkinsonism Relat. Disord., 76, 80–84. CrossRef Scholar google search
Alieva A.K., Zyrin V.S., Rudenok M.M., Kolacheva A.A., Shulskaya M.V., Ugryumov M.V., Slominsky P.A., Shadrina M.I. (2018) Whole-transcriptome analysis of mouse models with MPTP-induced early stages of Parkinson’s disease reveals stage-specific response of transcriptome and a possible role of myelin-linked genes in neurodegeneration. Mol. Neurobiol., 55(9), 7229–7241. CrossRef Scholar google search
Huang Z.-N., Chung H.M., Fang S.-C., Her L.-S. (2017) Adhesion regulating molecule 1 mediates HAP40 overexpression-induced mitochondrial defects. Int. J. Biol. Sci., 13(11), 1420–1437. CrossRef Scholar google search
Siddique I., Kamble K., Gupta S., Solanki K., Bhola S., Ahsan N., Gupta S. (2023) ARL6IP5 ameliorates α-synuclein burden by inducing autophagy via preventing ubiquitination and degradation of ATG12. Int. J. Mol. Sci., 24(13), 10499. CrossRef Scholar google search
Zhang X., Zhou J.-Y., Chin M.H., Schepmoes A.A., Petyuk V.A., Weitz K.K., Petritis B.O., Monroe M.E., Camp D.G.,Wood S.A., Melega W.P., Bigelow D.J., Smith D.J., Qian W.-J., Smith R.D. (2010) Region-specific protein abundance changes in the brain of MPTP-induced Parkinson’s disease mouse model. J. Proteome Res., 9(3), 1496–1509. CrossRef Scholar google search
Pellegrini L., Wetzel A., Grannó S., Heaton G., Harvey K. (2016) Back to the tubule: microtubule dynamics in Parkinson’s disease. Cell. Mol. Life Sci., 74(3), 409–434. CrossRef Scholar google search
Calogero A.M., Mazzetti S., Pezzoli G., Cappelletti G. (2019) Neuronal microtubules and proteins linked to Parkinson’s disease: a relevant interaction? Biol. Chem., 400(9), 1099–1112. CrossRef Scholar google search
Naren P., Samim K.S., Tryphena K.P., Vora L.K., Srivastava S., Singh S.B., Khatri D.K. (2023) Microtubule acetylation dyshomeostasis in Parkinson’s disease. Transl. Neurodegener., 12, 20. CrossRef Scholar google search
Ma L., Song J., Sun X., Ding W., Fan K., Qi M., Xu Y., Zhang W. (2019) Role of microtubule-associated protein 6 glycosylated with Gal-(β-1,3)-GalNAc in Parkinson’s disease. Aging (Albany NY), 11(13), 4597–4610. CrossRef Scholar google search
Brotchie J.M. (2003) CB1 cannabinoid receptor signalling in Parkinson’s disease. Curr. Opin. Pharmacol., 3(1), 54–61. CrossRef Scholar google search
Arrazola Sastre A., Luque Montoro M., Gálvez-Martín P., Lacerda H.M., Lucia A.M., Llavero F., Zugaza J.L. (2020) Small GTPases of the Ras and Rho families switch on/off signaling pathways in neurodegenerative diseases. Int. J. Mol. Sci., 21(17), 6312. CrossRef Scholar google search
Berger I., Hershkovitz E., Shaag A., Edvardson S., Saada A., Elpeleg O. (2008) Mitochondrial complex I deficiency caused by a deleterious NDUFA11 mutation. Ann. Neurol., 63(3), 405–408. CrossRef Scholar google search
Becic A., Leifeld J., Shaukat J., Hollmann M. (2022) Tetraspanins as potential modulators of glutamatergic synaptic function. Front. Mol. Neurosci., 14, 801882. CrossRef Scholar google search
Lau A., Tymianski M. (2010) Glutamate receptors, neurotoxicity and neurodegeneration. Pflugers Arch., 460(2), 525–542. CrossRef Scholar google search
Greig F.H., Nixon G.F. (2014) Phosphoprotein enriched in astrocytes (PEA)-15: a potential therapeutic target in multiple disease states. Pharmacol. Ther., 143(3), 265–274. CrossRef Scholar google search
Peng X., Wellard N., Ghosh A., Troakes C., Giese K.P. (2024) Different dysregulations of CYFIP1 and CYFIP2 in distinct types of dementia. Brain Res. Bull., 206, 110849. CrossRef Scholar google search
Liang Z., Liu F., Grundke-Iqbal I., Iqbal K., Gong C.-X. (2007) Down-regulation of cAMP-dependent protein kinase by over-activated calpain in Alzheimer disease brain. J. Neurochem., 103(6), 2462–2470. CrossRef Scholar google search
Wu X., Yang Z., Zou J., Gao H., Shao Z., Li C., Lei P. (2025) Protein kinases in neurodegenerative diseases: current understandings and implications for drug discovery. Signal Transduct. Target. Ther., 10, 146. CrossRef Scholar google search
Yang Y., Qin M., Bao P., Xu W., Xu J. (2017) Secretory carrier membrane protein 5 is an autophagy inhibitor that promotes the secretion of α-synuclein via exosome. PLOS One, 12(7), e0180892. CrossRef Scholar google search
Бунеева О.А., Капица И.Г., Згода В.Г., Медведев А.Е. (2023) Нейропротекторные эффекты изатина и афобазола сопровождаются увеличением уровня растворимого в Тритоне Х-100 альфа-синуклеина в мозге крыс с экспериментальным ротеноновым паркинсонизмом. Биомедицинская химия, 69(5), 290–299. CrossRef Scholar google search
Susa K.J., Kruse A.C., Blacklow S.C. (2024) Tetraspanins: structure, dynamics, and principles of partner-protein recognition. Trends Cell Biol., 34(6), 509–522. CrossRef Scholar google search
Guix F.X., Sannerud R., Berditchevski F., Arranz A.M., Horré K., Snellinx A., Thathiah A., Saido T., Saito T., Rajesh S., Overduin M., Kumar-Singh S., Radaelli E., Corthout N., Colombelli J., Tosi S., Munck S., Salas I.H., Annaert W., de Strooper B. (2017) Tetraspanin 6: a pivotal protein of the multiple vesicular body determining exosome release and lysosomal degradation of amyloid precursor protein fragments. Mol. Neurodegener., 12, 25. CrossRef Scholar google search