Abe K., Kimura H. The possible role of hydrogen sulfide as an endogenous neuromodulator. J. Neurosci. 1996; 16: 1066–1071. doi: 10.1523/JNEUROSCI.16-03-01066.1996.
Ajroud-Driss S., Siddique T. Sporadic and hereditary amyotrophic lateral sclerosis (ALS). Biochim. Biophys. Acta. 2015; 1852 (4): 679-684. doi.org/10.1016/j.bbadis.2014.08.010
Bae S.K., Heo C.H., Choi D.J., Sen D., Joe E.H., Cho B.R., Kim H.M. A Ratiometric two-photon fluorescent probe reveals reduction in mitochondrial H2S production in Parkinson’s disease gene knockout astrocytes. J. Am. Chem. Soc. 2013; 135 (26): 9915-9923. doi: 10.1021/ja404004v
Bates G.P., Mangiarini L., Mahal A., Davies S.W. Transgenic models of Huntingtons disease. Hum. Mol. Genet. 1997; 6 (10): 1633–1637. doi: 10.1093/hmg/6.10.1633
Borthwick G.M., Johnson M.A., Ince P.G., Shaw P.J., Turnbull D.M. Mitochondrial enzyme activity in amyotrophic lateral sclerosis: implication for the role of mitochondria in the neuronal cell death. Ann. Neurol. 1999; 46 (5): 787-790. doi: 10.1002/1531-8249(199911)46:5<787::AID-ANA17>3.0.CO;2-8
Bruijn L.I., Becher M.W., Lee M.K., Anderson K.L., Jenkins N.A., Copeland N.G., Sisodia S.S., Rothstein J.D., Borchelt D.R., Price D.L., Cleveland D.W. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron. 1997; 18 (2): 327–338. doi: 10.1016/S0896-6273(00)80272-X
Davies S.W., Turmaine M., Cozens B.A., DiFiglia M., Sharp A.H., Ross C.A., Scherzinger E., Wanker E.E., Mangiarini L., Bates G.P. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell. 1997; 90 (3): 537–548. doi: 10.1016/S0092-8674(00)80513-9
Davoli A., Greco V., Spalloni A., Guatteo E., Neri C., Rizzo G.R., Cordella A., Romigi A., Cortese C., Bernardini S., Sarchielli P., Cardaioli G., Calabresi P., Mercuri N.B., Urbani A., Longone P. Evidence of hydrogen sulfide involvement in amyotrophic lateral sclerosis. Ann. Neurol. 2015; 77 (4): 697-709. doi: 10.1002/ana.24372
Dusonchet J., Bensadoun J.C., Schneider B.L., Aebischer P. Targeted overexpression of the parkin substrate Pael-R in the nigrostriatal system of adult rats to model Parkinson's disease. Neurobiol. Dis. 2009; 35 (1): 32–41. doi: 10.1016/j.nbd.2009.03.013
Enokido Y., Suzuki E., Iwasawa K., Namekata K., Okazawa H., Kimura H. Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS. FASEB J. 2005; 19 (13): 1854–1856. doi: 10.1096/fj.05-3724fje
Eto K., Asada T., Arima K., Makifuchi T., Kimura H. Brain hydrogen sulfide is severely decreased in Alzheimer’s disease. Biochem. Biophys. Res. Commun. 2002; 293 (5): 1485–1488. doi: 10.1016/S0006-291X(02)00422-9
Gouras G.K., Tsai J., Naslund J., Vincent B., Edgar M., Checler F., Greenfield J.P., Haroutunian V., Buxbaum J.D., Xu H., Greengard P., Relkin N.R. Intraneuronal Aβ42 accumulation in human brain. Am. J. Pathol. 2000; 156: 15–20. doi: 10.1016/S0002-9440(10)64700-1
He X.L., Yan N., Zhang H., Qi Y.W., Zhu L.J., Liu M.J., Yan Y. Hydrogen sulfide improves spatial memory impairment and decreases production of Aβ in APP/PS1 transgenic mice. Neurochem Int. 2014; 67: 1-8. doi: 10.1016/j.neuint.2014.01.004
He J.T., Li H., Yang L., Mao C.Y. Role of hydrogen sulfide in cognitive deficits: Evidences and mechanisms. Eur. J. Pharmacol. 2019; 849: 146-153. doi: 10.1016/j.ejphar.2019.01.072
Hu L.F., Lu M., Tiong C.X., Dawe G.S., Hu G., Bian J.S. Neuroprotective effects of hydrogen sulfide on Parkinson’s disease rat models. Aging Cell. 2010; 9 (2): 135–146. doi: 10.1111/j.1474-9726.2009.00543.x
Illarioshkin S.N. Modern representation about the etiology of Parkinson's disease. Nevrologicheskiy zhurnal = Neurological Journal. 2015; 20 (4): 4-13. [In Russian].
Kamat P.K., Kyles P., Kalani A., Tyagi N. Hydrogen sulfide ameliorates homocysteine-induced Alzheimer’s diseaselike pathology, blood–brain barrier disruption, and synaptic disorder. Mol. Neurobiol. 2016; 53 (4): 2451–2467. doi: 10.1007/s12035-015-9212-4
Kamoun P. Endogenous production of hydrogen sulfide in mammals. Amino Acids. 2004; 26 (3): 243–254. doi: 10.1007/s00726-004-0072-x
Kimura H. Metabolic turnover of hydrogen sulfide. Front. Physiol. 2012; 3: 101. doi: 10.3389/fphys.2012.00101
Liu X.-Q., Jiang P., Huang H., Yan Y. Plasma levels of endogenous hydrogen sulfide and homocysteine in patients with Alzheimer’s disease and vascular dementia and the significance thereof. Zhonghua Yi Xue Za Zhi. 2008; 88 (32); 2246–2249. [In Chinese].
Longone P., Davoli A., Giada R.R., Ezia G., Alida S., Greco V., Urbani A., Mercuri N.B. The increased production of hydrogen sulfide in amyotrophic lateral sclerosis is a significant risk factor? CNS 2015; 1 (2): 35-37.
Longone P., Davoli V., Greco V., Spalloni A., Guatteo E., Neri C., Rizzo G.R., Cordella A., Romigi A., Cortese C., Bernardini S., Sarchielli P., Cardaioli G., Calabresi P., Urbani A., Mercuri N.B. Hydrogen sulphide “a double-faced Janus” in amyotrophic lateral sclerosis (ALS). Therapeutic Targets for Neurological Diseases. 2015; 2: e749. doi: 10.14800/ttnd.749
McCaddon A., Regland B. Homocysteine and cognition — no longer a hypothesis? Med. Hypotheses. 2006; 66 (3): 682–683. doi: 10.1016/j.mehy.2005.03.034
Mangiarini L., Sathasivam K., Seller M., Cozens B., Harper A., Hetherington C., Lawton M., Trottier Y., Lehrach H., Davies S.W., Bates G.P. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell. 1996; 87 (3): 493–506. doi: 10.1016/S0092-8674(00)81369-0
Mizuno Y., Hattori N., Kitada T., Matsumine H., Mori H., Shimura H., Kubo S., Kobayashi H., Asakawa S., Minoshima S., Shimizu N. Familial Parkinson's disease. Alpha-synuclein and parkin. Adv. Neurol. 2001; 86: 13-21.
de la Monte S.M., Vonsattel J.-P., Richardson E.P. Morphometric demonstration of atrophic changes in the cerebral cortex, white matter and neostriatum in Huntington’s disease. J. Neuropathol. Exp. Neurol. 1988; 47 (5): 516–525. doi: 10.1097/00005072-198809000-00003
Morrison L.D., Smith D.D., Kish S.J. Brain S-adenosylmethionine levels are severely decreased in Alzheimer’s disease. J. Neurochem. 1996; 67 (3): 1328–1331. doi: 10.1046/j.1471-4159.1996.67031328.x
Olson K.R., Donald J.A., Dombkowski R.A., Perry S.F. Evolutionary and comparative aspects of nitric oxide, carbon monoxide and hydrogen sulfide. Respir. Physiol. Neurobiol. 2012; 184 (2): 117–129. doi: 10.1016/j.resp.2012.04.004
Olson K.R., Straub K.D. The role of hydrogen sulfide in evolution and the evolution of hydrogen sulfide in metabolism and signaling. Physiology (Bethesda). 2015; 31 (1): 60-72. doi: 10.1152/physiol.00024.2015
Panthi S., Manandhar S., Gautam K. Hydrogen sulfide, nitric oxide, and neurodegenerative disorders. Transl. Neurodegener. 2018; 7: 3. doi: 10.1186/s40035-018-0108-x
Paul B D., Snyder S.H. Neurodegeneration in Huntington's disease involves loss of cystathionine γ-lyase. Cell Cycle. 2014; 13 (16): 2491–2493. doi: 10.4161/15384101.2014.950538
Paul B.D., Snyder S.H. Gasotransmitter hydrogen sulfide signaling in neuronal health and disease. Biochem. Pharmacol. 2018; 149: 101–109. doi: 10.1016/j.bcp.2017.11.019
Paul B.D., Sbodio J.I., Xu R., Vandiver M.S., Cha J.Y., Snowman A.M., Snyder S.H. Cystathionine gamma-lyase deficiency mediates neurodegeneration in Huntington's disease. Nature. 2014; 509 (7498): 96–100. doi: 10.1038/nature13136
Razdorskaya V.V., Voskresenskaya O.N., Yudina G.K. Parkinson's disease in Russia: prevalence and incidence. Saratovskiy nauchno-meditsinskiy zhurnal = Saratov Journal of Medical Scientific Research. 2016; 12 (3): 379-384. [In Russian].
Ripps M.E., Huntley G.W., Hof P.R., Morrison J.H., Gordon J.W. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 1995; 92 (3): 689–693. doi: 10.1073/pnas.92.3.689
Ross C.A., Tabrizi S.J. Huntington’s disease: from molecular pathogenesis to clinical treatment. Lancet Neurol. 2011; 10 (1): 83–98. doi: 10.1016/S1474-4422(10)70245-3
Sbodio J.I., Snyder S.H., Paul. B.D. Transcriptional control of amino acid homeostasis is disrupted in Huntington’s disease. Proc. Natl. Acad. Sci. U S A. 2016; 113 (31): 8843–8848. doi: 10.1073/pnas.1608264113
Sen N. Functional and molecular insights of hydrogen sulfide signaling and protein sulfhydration. J. Mol. Biol. 2017; 429 (4): 543–561. doi: 10.1016/j.jmb.2016.12.015
Shefa U., Kim M.S., Jeong N.Y., Jung J. Antioxidant and cell-signaling functions of hydrogen sulfide in the central nervous system. Oxid. Med. Cell. Longev. 2018; 2018: 1873962. doi: 10.1155/2018/1873962
Sunbramanian S., Snyder S.H. Huntington’s disease is a disorder of the corpus striatum: Focus on Rhes (Ras homologue enriched in the striatum). Neuropharmacol. 2011; 60 (7–8): 1187-1192. doi: 10.1016/j.neuropharm.2010.10.025
Tiong C.X., Lu M., Bian J.-S. Protective effect of hydrogen sulphide against 6-OHDA-induced cell injury in SH-SY5Y cells involves PKC/PI3K/Akt pathway. Br. J. Pharmacol. 2010; 161 (2): 467–480. doi: 10.1111/j.1476-5381.2010.00887.x
Valentino F., Bivona G., Butera D., Paladino P., Fazzari M., Piccoli T., Ciaccio M., La Bella V. Elevated cerebrospinal fluid and plasma homocysteine levels in ALS. Eur. J. Neurol. 2010; 17 (1): 84-89. doi: 10.1111/j.1468-1331.2009.02752.x
Vandiver M.S., Paul B.D., Xu R. et al. Sulfhydration mediates neuroprotective actions of parkin. Nat. Commun. 2013; 4: 1626. doi: 10.1038/ncomms2623
Vijayvergiya C., Beal M.F., Buck J., Manfredi G. Mutant superoxide dismutase 1 forms aggregate in the brain mitochondria matrix of amyotrophic lateral sclerosis mice. J. Neurosci. 2005; 25 (10): 2463-2470. doi: 10.1523/JNEUROSCI.4385-04.2005
Vural G., Gumusyayla S., Bektas H., Deniz O., Alisik M., Erel O. Impairment of dynamic thiol-disulphide homeostasis in patients with idiopathic Parkinson'sdisease and its relationship with clinical stage of disease. Clin. Neurol. Neurosurg. 2017; 153: 50-55. doi:10.1016/j.clineuro.2016.12.009
Wiedemann F.R., Manfredi G., Mawrin C., Beal M.F, Schon E.A. Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients. J. Neurochem. 2002; 80 (4): 616-625. doi: 10.1046/j.0022-3042.2001.00731.x