Longinetti E, Fang F. Epidemiology of amyotrophic lateral sclerosis: an update of recent literature. Curr Opin Neurol. 2019;32(5):771–6.

Article  Google Scholar 

Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;362(6415):59–62.

Article  Google Scholar 

Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG, et al. ALS-Linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron. 1997;18(2):327–38.

Article  Google Scholar 

Ryu H, Smith K, Camelo SI, Carreras I, Lee J, Iglesias AH, et al. Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice. J Neurochem. 2005;93(5):1087–98.

Article  Google Scholar 

Hatzipetros T, Kidd JD, Moreno AJ, Thompson K, Gill A, Vieira FG. A quick phenotypic neurological scoring system for evaluating disease progression in the SOD1-G93A mouse model of ALS. J Vis Exp. 2015;104:53257.

Google Scholar 

Martin LJ, Wong M. Skeletal muscle-restricted expression of human SOD1 in transgenic mice causes a fatal ALS-Like Syndrome. Front Neurol. 2020;11:592851.

Article  Google Scholar 

Schultz J. Disease-modifying treatment of amyotrophic lateral sclerosis. Am J Manag Care. 2018;24(15 Suppl):327-s35.

Google Scholar 

Ryu H, Ferrante RJ. Translational therapeutic strategies in amyotrophic lateral sclerosis. Mini Rev Med Chem. 2007;7(2):141–50.

Article  Google Scholar 

Yamashita T, Kushida Y, Wakao S, Tadokoro K, Nomura E, Omote Y, et al. Therapeutic benefit of Muse cells in a mouse model of amyotrophic lateral sclerosis. Sci Rep. 2020;10(1):17102.

Article  Google Scholar 

Xu X, Shen D, Gao Y, Zhou Q, Ni Y, Meng H, et al. A perspective on therapies for amyotrophic lateral sclerosis: can disease progression be curbed? Transl Neurodegener. 2021;10(1):29.

Article  Google Scholar 

Uttara B, Singh AV, Zamboni P, Mahajan RT. Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr Neuropharmacol. 2009;7(1):65–74.

Article  Google Scholar 

Zheng X, Sawalha AH. The role of oxidative stress in epigenetic changes underlying autoimmunity. Antioxid Redox Signal. 2022;36(7–9):423–40.

Article  Google Scholar 

Srivas S, Baghel MS, Singh P, Thakur MK. Neurodegeneration during aging: the role of oxidative stress through epigenetic modifications. In: Rath PC, editor. Models, molecules and mechanisms in biogerontology: physiological abnormalities, diseases and interventions. Singapore: Springer; 2019. p. 43–55.

Chapter  Google Scholar 

Carrì MT, Valle C, Bozzo F, Cozzolino M. Oxidative stress and mitochondrial damage: importance in non-SOD1 ALS. Front Cell Neurosci. 2015;9:41.

Google Scholar 

Tam OH, Rozhkov NV, Shaw R, Kim D, Hubbard I, Fennessey S, et al. Postmortem cortex samples identify distinct molecular subtypes of ALS: retrotransposon activation, oxidative stress, and activated glia. Cell Rep. 2019;29(5):1164-77.e5.

Article  Google Scholar 

Cunha-Oliveira T, Montezinho L, Mendes C, Firuzi O, Saso L, Oliveira PJ, et al. Oxidative stress in amyotrophic lateral sclerosis: pathophysiology and opportunities for pharmacological intervention. Oxid Med Cell Longev. 2020;2020:5021694.

Article  Google Scholar 

Petrov D, Daura X, Zagrovic B. Effect of oxidative damage on the stability and dimerization of superoxide dismutase 1. Biophys J. 2016;110(7):1499–509.

Article  Google Scholar 

Hemerková P, Vališ M. Role of oxidative stress in the pathogenesis of amyotrophic lateral sclerosis: antioxidant metalloenzymes and therapeutic strategies. Biomolecules. 2021;11(3):437.

Article  Google Scholar 

Blasco H, Mavel S, Corcia P, Gordon PH. The glutamate hypothesis in ALS: pathophysiology and drug development. Curr Med Chem. 2014;21(31):3551–75.

Article  Google Scholar 

Foran E, Trotti D. Glutamate transporters and the excitotoxic path to motor neuron degeneration in amyotrophic lateral sclerosis. Antioxid Redox Signal. 2009;11(7):1587–602.

Article  Google Scholar 

Kazama M, Kato Y, Kakita A, Noguchi N, Urano Y, Masui K, et al. Astrocytes release glutamate via cystine/glutamate antiporter upregulated in response to increased oxidative stress related to sporadic amyotrophic lateral sclerosis. Neuropathology. 2020;40(6):587–98.

Article  Google Scholar 

Lee J, Ryu H, Kowall NW. Motor neuronal protection by L-arginine prolongs survival of mutant SOD1 (G93A) ALS mice. Biochem Biophys Res Commun. 2009;384(4):524–9.

Article  Google Scholar 

Lee J, Ryu H, Ferrante RJ, Morris SM, Ratan RR. Translational control of inducible nitric oxide synthase expression by arginine can explain the arginine paradox. Proc Natl Acad Sci. 2003;100(8):4843.

Article  Google Scholar 

Zhu Q, Huang Y, Marton LJ, Woster PM, Davidson NE, Casero RA. Jr. Polyamine analogs modulate gene expression by inhibiting lysine-specific demethylase 1 (LSD1) and altering chromatin structure in human breast cancer cells. Amino Acids. 2012;42(2–3):887–98.

Article  Google Scholar 

Wang J, Hevi S, Kurash JK, Lei H, Gay F, Bajko J, et al. The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nat Genet. 2009;41(1):125–9.

Article  Google Scholar 

Yang G-J, Lei P-M, Wong S-Y, Ma D-L, Leung C-H. Pharmacological inhibition of LSD1 for cancer treatment. Molecules. 2018;23(12):3194.

Article  Google Scholar 

Anand R, Marmorstein R. Structure and mechanism of lysine-specific demethylase enzymes. J Biol Chem. 2007;282(49):35425–9.

Article  Google Scholar 

Huang J, Sengupta R, Espejo AB, Lee MG, Dorsey JA, Richter M, et al. p53 is regulated by the lysine demethylase LSD1. Nature. 2007;449(7158):105–8.

Article  Google Scholar 

Fang Y, Liao G, Yu B. LSD1/KDM1A inhibitors in clinical trials: advances and prospects. J Hematol Oncol. 2019;12(1):129.

Article  Google Scholar 

Fang Y, Yang C, Yu Z, Li X, Mu Q, Liao G, et al. Natural products as LSD1 inhibitors for cancer therapy. Acta Pharm Sin B. 2020;11:621–31.

Article  Google Scholar 

Mould DP, McGonagle AE, Wiseman DH, Williams EL, Jordan AM. Reversible inhibitors of LSD1 as therapeutic agents in acute myeloid leukemia: clinical significance and progress to date. Med Res Rev. 2015;35(3):586–618.

Article  Google Scholar 

Boulding T, McCuaig RD, Tan A, Hardy K, Wu F, Dunn J, et al. LSD1 activation promotes inducible EMT programs and modulates the tumour microenvironment in breast cancer. Sci Rep. 2018;8(1):73.

Article  Google Scholar 

Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, Mattevi A. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002;9(1):22–6.

Article  Google Scholar 

Yang M, Culhane JC, Szewczuk LM, Jalili P, Ball HL, Machius M, et al. Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine. Biochemistry. 2007;46(27):8058–65.

Article  Google Scholar 

Finberg JPM, Rabey JM. Inhibitors of MAO-A and MAO-B in psychiatry and neurology. Front Pharmacol. 2016;7:340.

Article  Google Scholar 

Fitzpatrick PF. Oxidation of amines by flavoproteins. Arch Biochem Biophys. 2010;493(1):13–25.

Article  Google Scholar 

Forneris F, Binda C, Battaglioli E, Mattevi A. LSD1: oxidative chemistry for multifaceted functions in chromatin regulation. Trends Biochem Sci. 2008;33(4):181–9.

Article  Google Scholar 

Naumenko N, Pollari E, Kurronen A, Giniatullina R, Shakirzyanova A, Magga J, et al. Gender-specific mechanism of synaptic impairment and its prevention by GCSF in a mouse model of ALS. Front Cell Neurosci. 2011;5:26.

Article  Google Scholar 

Lee J, Ryu H, Kowall NW. Differential regulation of neuronal and inducible nitric oxide synthase (NOS) in the spinal cord of mutant SOD1 (G93A) ALS mice. Biochem Biophys Res Commun. 2009;387(1):202–6.

Article  Google Scholar 

Luh LM, Das I, Bertolotti A. qMotor, a set of rules for sensitive, robust and quantitative measurement of motor performance in mice. Nat Protoc. 2017;12(7):1451–7.

Article  Google Scholar 

Heikkinen T, Bragge T, Bhattarai N, Parkkari T, Puoliväli J, Kontkanen O, et al. Rapid and robust patterns of spontaneous locomotor deficits in mouse models of Huntington’s disease. PLoS ONE. 2020;15(12):e0243052.

Article  Google Scholar 

Dobin A, Davis CA, Schlesinger F, Drenkow J, Zaleski C, Jha S, et al. STAR: ultrafast universal RNA-seq aligner. Bioinformatics. 2012;29(1):15–21.

Article  Google Scholar 

Anders S, Pyl PT, Huber W. HTSeq–a Python framework to work with high-throughput sequencing data. Bioinformatics. 2015;31(2):166–9.

Article  Google Scholar 

Langmead B, Salzberg SL. Fast gapped-read alignment with Bowtie 2. Nat Methods. 2012;9(4):357–9.

Article  Google Scholar 

Heinz S, Benner C, Spann N, Bertolino E, Lin YC, Laslo P, et al. Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. Mol Cell. 2010;38(4):576–89.

Article  Google Scholar 

Maiques-Diaz A, Lynch JT, Spencer GJ, Somervaille TCP. LSD1 inhibitors disrupt the GFI1 transcription repressor complex. Mol Cell Oncol. 2018;5(4):e1481813-e.

Article  Google Scholar 

Alrafiah AR. Evaluation of the role of an antioxidant gene in NSC-34 motor neuron-like cells as a model of a motor neuron disease. Folia Morphol (Warsz). 2019;78(1):1–9.

Google Scholar 

Yang Y, Chen S, Zhang Y, Lin X, Song Y, Xue Z, et al. Induction of autophagy by spermidine is neuroprotective via inhibition of caspase 3-mediated beclin 1 cleavage. Cell Death Dis. 2017;8(4):e2738-e.

Article  Google Scholar 

Wang I-F, Guo B-S, Liu Y-C, Wu C-C, Yang C-H, Tsai K-J, et al. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc Natl Acad Sci. 2012;109(37):15024–9.

Article  Google Scholar 

Diler AS, Ziylan YZ, Uzum G, Lefauconnier JM, Seylaz J, Pinard E. Passage of spermidine across the blood–brain barrier in short recirculation periods following global cerebral ischemia: effects of mild hyperthermia. Neurosci Res. 2002;43(4):335–42.

Article  Google Scholar 

Glantz L, Nates JL, Trembovler V, Bass R, Shohami E. Polyamines induce blood-brain barrier disruption and edema formation in the rat. J Basic Clin Physiol Pharmacol. 1996;7(1):1–10.

Article  Google Scholar