{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T07:00:31Z","timestamp":1775199631052,"version":"3.50.1"},"reference-count":101,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2021,9,15]],"date-time":"2021-09-15T00:00:00Z","timestamp":1631664000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1R21AG073684 \u2013 01"],"award-info":[{"award-number":["1R21AG073684 \u2013 01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"American Heart Association (AHA)\/Paul Allen Frontiers Group","award":["19PABH134580006"],"award-info":[{"award-number":["19PABH134580006"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Huntington\u2019s disease (HD) is caused by expansion of polyglutamine repeats in the protein huntingtin, which affects the corpus striatum of the brain. The polyglutamine repeats in mutant huntingtin cause its aggregation and elicit toxicity by affecting several cellular processes, which include dysregulated organellar stress responses. The Golgi apparatus not only plays key roles in the transport, processing, and targeting of proteins, but also functions as a sensor of stress, signaling through the Golgi stress response. Unlike the endoplasmic reticulum (ER) stress response, the Golgi stress response is relatively unexplored. This review focuses on the molecular mechanisms underlying the Golgi stress response and its intersection with cysteine metabolism in HD.<\/jats:p>","DOI":"10.3390\/antiox10091468","type":"journal-article","created":{"date-parts":[[2021,9,15]],"date-time":"2021-09-15T12:00:44Z","timestamp":1631707244000},"page":"1468","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Signaling Overlap between the Golgi Stress Response and Cysteine Metabolism in Huntington\u2019s Disease"],"prefix":"10.3390","volume":"10","author":[{"given":"Bindu D.","family":"Paul","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA"},{"name":"The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA"},{"name":"Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,9,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","article-title":"A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington\u2019s disease chromosomes","volume":"72","year":"1993","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"15005","DOI":"10.1038\/nrdp.2015.5","article-title":"Huntington disease","volume":"1","author":"Bates","year":"2015","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"9751","DOI":"10.1073\/pnas.1511810112","article-title":"Huntington\u2019s disease: Neural dysfunction linked to inositol polyphosphate multikinase","volume":"112","author":"Ahmed","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.neuron.2017.03.023","article-title":"Mutant Huntingtin Disrupts the Nuclear Pore Complex","volume":"94","author":"Grima","year":"2017","journal-title":"Neuron"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"8843","DOI":"10.1073\/pnas.1608264113","article-title":"Transcriptional control of amino acid homeostasis is disrupted in Huntington\u2019s disease","volume":"113","author":"Sbodio","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-21637-y","article-title":"Mutant Huntingtin stalls ribosomes and represses protein synthesis in a cellular model of Huntington disease","volume":"12","author":"Eshraghi","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3389\/fnmol.2019.00068","article-title":"Impaired Redox Signaling in Huntington\u2019s Disease: Therapeutic Implications","volume":"12","author":"Paul","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1089\/ars.2014.5851","article-title":"Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease","volume":"21","author":"Cao","year":"2014","journal-title":"Antioxid. Redox. Signal"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/nrm3958","article-title":"Diversity and selectivity in mRNA translation on the endoplasmic reticulum","volume":"16","author":"Reid","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s00018-015-2052-6","article-title":"The endoplasmic reticulum: Structure, function and response to cellular signaling","volume":"73","author":"Schwarz","year":"2016","journal-title":"Cell Mol. Life Sci."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Roscoe, J.M., and Sevier, C.S. (2020). Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum. Cells, 9.","DOI":"10.3390\/cells9102314"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"101169","DOI":"10.1016\/j.molmet.2021.101169","article-title":"A guide to understanding endoplasmic reticulum stress in metabolic disorders","volume":"47","author":"Lemmer","year":"2021","journal-title":"Mol. Metab."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/s41580-020-0250-z","article-title":"Mechanisms, regulation and functions of the unfolded protein response","volume":"21","author":"Hetz","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.1209038","article-title":"The unfolded protein response: From stress pathway to homeostatic regulation","volume":"334","author":"Walter","year":"2011","journal-title":"Science"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.molcel.2017.05.031","article-title":"The UPR(ER): Sensor and Coordinator of Organismal Homeostasis","volume":"66","author":"Frakes","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1016\/S1097-2765(00)00133-7","article-title":"ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs","volume":"6","author":"Ye","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3787","DOI":"10.1091\/mbc.10.11.3787","article-title":"Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress","volume":"10","author":"Haze","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1016\/j.molcel.2021.05.004","article-title":"Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms","volume":"81","author":"Lemberg","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jmb.2019.05.012","article-title":"Emerging Principles of Selective ER Autophagy","volume":"432","author":"Wilkinson","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.celrep.2013.08.001","article-title":"Golgi Protein ACBD3 Mediates Neurotoxicity Associated with Huntington\u2019s Disease","volume":"4","author":"Sbodio","year":"2013","journal-title":"Cell Rep."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1073\/pnas.1717877115","article-title":"Golgi stress response reprograms cysteine metabolism to confer cytoprotection in Huntington\u2019s disease","volume":"115","author":"Sbodio","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2818.1989.tb04294.x","article-title":"On the structure of nerve cells","volume":"155","author":"Golgi","year":"1989","journal-title":"J. Microsc."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1002\/aja.1001170109","article-title":"Osmium Impregnation of the Golgi Apparatus","volume":"117","author":"Friend","year":"1965","journal-title":"Am. J. Anat."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"385","DOI":"10.5115\/acb.20.196","article-title":"Camillo Golgi (1843\u20131926): Scientist extraordinaire and pioneer figure of modern neurology","volume":"53","author":"Ghosh","year":"2020","journal-title":"Anat. Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1159\/000064596","article-title":"The neuron theory","volume":"77","author":"Fodstad","year":"2001","journal-title":"Stereotact. Funct. Neurosurg."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.ceb.2010.10.004","article-title":"Structural organization of the Golgi apparatus","volume":"23","author":"Lowe","year":"2011","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1111\/j.1600-0854.2010.01114.x","article-title":"Unraveling the Golgi ribbon","volume":"11","author":"Wei","year":"2010","journal-title":"Traffic"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.ceb.2004.06.011","article-title":"Molecular basis for Golgi maintenance and biogenesis","volume":"16","author":"Sougrat","year":"2004","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1083\/jcb.21.3.429","article-title":"The Ultrastructure of a Mammalian Cell during the Mitotic Cycle","volume":"21","author":"Robbins","year":"1964","journal-title":"J. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1111\/boc.201700032","article-title":"Mitotic inheritance of the Golgi complex and its role in cell division","volume":"109","author":"Ayala","year":"2017","journal-title":"Biol. Cell"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"E6590","DOI":"10.1073\/pnas.1610844113","article-title":"Mitotic Golgi disassembly is required for bipolar spindle formation and mitotic progression","volume":"113","author":"Guizzunti","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"a005199","DOI":"10.1101\/cshperspect.a005199","article-title":"Golgi glycosylation","volume":"3","author":"Stanley","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1007\/s10545-015-9851-7","article-title":"Golgi post-translational modifications and associated diseases","volume":"38","author":"Potelle","year":"2015","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1093\/jb\/mvv010","article-title":"Organelle autoregulation-stress responses in the ER, Golgi, mitochondria and lysosome","volume":"157","author":"Sasaki","year":"2015","journal-title":"J. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1002\/1873-3468.13554","article-title":"Golgi stress response and organelle zones","volume":"593","author":"Sasaki","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1038\/ncb2865","article-title":"A CREB3\u2013ARF4 signalling pathway mediates the response to Golgi stress and susceptibility to pathogens","volume":"15","author":"Reiling","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1254\/jphs.09R03CR","article-title":"Emerging New Roles of GM130, a cis-Golgi Matrix Protein, in Higher Order Cell Functions","volume":"112","author":"Nakamura","year":"2010","journal-title":"J. Pharmacol. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"45298","DOI":"10.1074\/jbc.M108961200","article-title":"Identification and Characterization of a Novel Golgi Protein, GCP60, That Interacts with the Integral Membrane Protein Giantin","volume":"276","author":"Sohda","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1247\/csf.10014","article-title":"Novel Cis-acting Element GASE Regulates Transcriptional Induction by the Golgi Stress Response","volume":"36","author":"Oku","year":"2011","journal-title":"Cell Struct. Funct."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1247\/csf.14015","article-title":"TFE3 is a bHLH-ZIP-type transcription factor that regulates the mammalian Golgi stress response","volume":"40","author":"Taniguchi","year":"2015","journal-title":"Cell Struct. Funct."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1247\/csf.16005","article-title":"MLX Is a Transcriptional Repressor of the Mammalian Golgi Stress Response","volume":"41","author":"Taniguchi","year":"2016","journal-title":"Cell Struct. Funct."},{"key":"ref_42","first-page":"1","article-title":"Golgi organization is regulated by proteasomal degradation","volume":"11","author":"Benyair","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1083\/jcb.200110007","article-title":"Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis","volume":"156","author":"Lane","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Miyata, S., Mizuno, T., Koyama, Y., Katayama, T., and Tohyama, M. (2013). The Endoplasmic Reticulum-Resident Chaperone Heat Shock Protein 47 Protects the Golgi Apparatus from the Effects of O-Glycosylation Inhibition. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0069732"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1247\/csf.19009","article-title":"MGSE Regulates Crosstalk from the Mucin Pathway to the TFE3 Pathway of the Golgi Stress Response","volume":"44","author":"Jamaludin","year":"2019","journal-title":"Cell Struct. Funct."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.jns.2006.01.019","article-title":"Fragmentation of the Golgi apparatus in neurodegenerative diseases and cell death","volume":"246","author":"Gonatas","year":"2006","journal-title":"J. Neurol. Sci."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5472","DOI":"10.1073\/pnas.93.11.5472","article-title":"The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease","volume":"93","author":"Mourelatos","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"340","DOI":"10.3389\/fnins.2015.00340","article-title":"Golgi fragmentation in Alzheimer\u2019s disease","volume":"9","author":"Joshi","year":"2015","journal-title":"Front. Neurosci."},{"key":"ref_49","first-page":"671","article-title":"Golgi fragmentation is Rab and SNARE dependent in cellular models of Parkinson\u2019s disease","volume":"139","year":"2012","journal-title":"Histochem. Cell Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1093\/hmg\/ddl467","article-title":"Wild-type huntingtin participates in protein trafficking between the Golgi and the extracellular space","volume":"16","author":"Strehlow","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1007\/s004010000182","article-title":"Fragmentation of the Golgi apparatus of the ballooned neurons in patients with corticobasal degeneration and Creutzfeldt-Jakob disease","volume":"100","author":"Sakurai","year":"2000","journal-title":"Acta Neuropathol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2798","DOI":"10.1073\/pnas.90.7.2798","article-title":"Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus","volume":"90","author":"Campadelli","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1073\/pnas.1608576114","article-title":"Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice","volume":"114","author":"Liu","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","first-page":"47","article-title":"Fragmentation of the Golgi complex of dopaminergic neurons in human substantia nigra: New cytopathological findings in Parkinson\u2019s disease","volume":"36","author":"Tomas","year":"2021","journal-title":"Histol. Histopathol."},{"key":"ref_55","first-page":"415","article-title":"In Alzheimer\u2019s disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic","volume":"148","author":"Stieber","year":"1996","journal-title":"Am. J. Pathol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/S0002-9440(10)62366-8","article-title":"Fragmentation of the Golgi Apparatus Induced by the Overexpression of Wild-Type and Mutant Human Tau Forms in Neurons","volume":"166","author":"Liazoghli","year":"2005","journal-title":"Am. J. Pathol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/78078","article-title":"Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein","volume":"25","author":"Lewis","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.nbd.2007.08.015","article-title":"A Golgi fragmentation pathway in neurodegeneration","volume":"29","author":"Nakagomi","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"651","DOI":"10.3233\/JAD-170332","article-title":"Phospho-Tau Accumulation and Structural Alterations of the Golgi Apparatus of Cortical Pyramidal Neurons in the P301S Tauopathy Mouse Model","volume":"60","author":"Avila","year":"2017","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1016\/j.neurobiolaging.2013.11.022","article-title":"Golgin-84-associated Golgi fragmentation triggers tau hyperphosphorylation by activation of cyclin-dependent kinase-5 and extracellular signal-regulated kinase","volume":"35","author":"Jiang","year":"2014","journal-title":"Neurobiol. Aging"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1126\/science.1172871","article-title":"Rhes, a Striatal Specific Protein, Mediates Mutant-Huntingtin Cytotoxicity","volume":"324","author":"Subramaniam","year":"2009","journal-title":"Science"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"268ra178","DOI":"10.1126\/scitranslmed.3010523","article-title":"Targeting ATM ameliorates mutant Huntingtin toxicity in cell and animal models of Huntington\u2019s disease","volume":"6","author":"Lu","year":"2014","journal-title":"Sci. Transl. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"75","DOI":"10.3233\/JHD-200438","article-title":"DNA Mismatch Repair and its Role in Huntington\u2019s Disease","volume":"10","author":"Iyer","year":"2021","journal-title":"J. Huntingtons Dis."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1093\/hmg\/11.17.1911","article-title":"Dysregulation of gene expression in the R6\/2 model of polyglutamine disease: Parallel changes in muscle and brain","volume":"11","author":"Hanson","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.neuron.2015.10.038","article-title":"RAN Translation in Huntington Disease","volume":"88","author":"Ayhan","year":"2015","journal-title":"Neuron"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.arr.2018.11.006","article-title":"Targeting the proteostasis network in Huntington\u2019s disease","volume":"49","author":"Soares","year":"2019","journal-title":"Ageing Res. Rev."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1089\/ars.2006.8.1865","article-title":"Redefining Oxidative Stress","volume":"8","author":"Jones","year":"2006","journal-title":"Antioxid. Redox Signal."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1089\/ars.2017.7321","article-title":"Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Op-portunities","volume":"30","author":"Sbodio","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"e2024358118","DOI":"10.1073\/pnas.2024358118","article-title":"Redox imbalance links COVID-19 and myalgic encephalomyelitis\/chronic fatigue syndrome","volume":"118","author":"Paul","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/978-3-7091-0579-5_13","article-title":"Coenzyme Q10 serum levels in Huntington\u2019s disease","volume":"Volume 68","author":"Andrich","year":"2004","journal-title":"Focus on Extrapyramidal Dysfunction"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature13136","article-title":"Cystathionine gamma-lyase deficiency mediates neurodegeneration in Huntington\u2019s disease","volume":"509","author":"Paul","year":"2014","journal-title":"Nature"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1038\/ncomms3917","article-title":"A failure in energy metabolism and antioxidant uptake precede symptoms of Hun-tington\u2019s disease in mice","volume":"4","author":"Esparza","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"655","DOI":"10.3233\/JAD-2011-111244","article-title":"Age-dependent and tissue-related glutathione redox status in a mouse model of Alzheimer\u2019s disease","volume":"28","author":"Zhang","year":"2012","journal-title":"J. Alzheimers Dis."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.neuint.2014.06.017","article-title":"Dysregulation of system xc(-) expression induced by mutant huntingtin in a striatal neuronal cell line and in R6\/2 mice","volume":"76","author":"Frederick","year":"2014","journal-title":"Neurochem. Int."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"4552","DOI":"10.1523\/JNEUROSCI.5865-09.2010","article-title":"Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington\u2019s disease","volume":"30","author":"Li","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2238","DOI":"10.1126\/science.1072613","article-title":"Sp1 and TAFII130 transcriptional activity disrupted in early Huntington\u2019s disease","volume":"296","author":"Dunah","year":"2002","journal-title":"Science"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.4161\/15384101.2014.950538","article-title":"Neurodegeneration in Huntington\u2019s disease involves loss of cystathionine gamma-lyase","volume":"13","author":"Paul","year":"2014","journal-title":"Cell Cycle"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.tips.2018.02.007","article-title":"Cysteine Metabolism in Neuronal Redox Homeostasis","volume":"39","author":"Paul","year":"2018","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/j.tibs.2015.08.007","article-title":"H2S: A Novel Gasotransmitter that Signals by Sulfhydration","volume":"40","author":"Paul","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.molcel.2011.10.021","article-title":"Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its antiapoptotic actions","volume":"45","author":"Sen","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"H2S Signals Through Protein S-Sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bcp.2017.11.019","article-title":"Gasotransmitter hydrogen sulfide signaling in neuronal health and disease","volume":"149","author":"Paul","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"101772","DOI":"10.1016\/j.redox.2020.101772","article-title":"Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics","volume":"38","author":"Paul","year":"2021","journal-title":"Redox Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1016\/j.cmet.2019.10.007","article-title":"Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration","volume":"30","author":"Zivanovic","year":"2019","journal-title":"Cell Metab."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/S1097-2765(03)00105-9","article-title":"An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress","volume":"11","author":"Harding","year":"2003","journal-title":"Mol. Cell"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.tem.2009.05.008","article-title":"ATF4-dependent transcription mediates signaling of amino acid limitation","volume":"20","author":"Kilberg","year":"2009","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"4424","DOI":"10.1038\/onc.2010.191","article-title":"Regulation of autophagy by ATF4 in response to severe hypoxia","volume":"29","author":"Rzymski","year":"2010","journal-title":"Oncogene"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1126\/science.aad0489","article-title":"mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle","volume":"351","author":"Hoxhaj","year":"2016","journal-title":"Science"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1182\/blood.2020005301","article-title":"HRI-regulated transcription factor ATF4 activates BCL11A transcription to silence fetal hemoglobin expression","volume":"135","author":"Huang","year":"2020","journal-title":"Blood"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1128\/MCB.00911-15","article-title":"C\/EBPgamma Is a Critical Regulator of Cellular Stress Response Networks through Heterodimerization with ATF","volume":"36","author":"Huggins","year":"2015","journal-title":"Mol. Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"3720","DOI":"10.1073\/pnas.88.9.3720","article-title":"Cross-family dimerization of transcription factors Fos\/Jun and ATF\/CREB alters DNA binding specificity","volume":"88","author":"Hai","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"20858","DOI":"10.1074\/jbc.M101198200","article-title":"Identification of Activating Transcription Factor 4 (ATF4) as an Nrf2-interacting Protein","volume":"276","author":"He","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1084\/jem.20071460","article-title":"ATF4 is an oxidative stress-inducible, prodeath transcription factor in neurons in vitro and in vivo","volume":"205","author":"Lange","year":"2008","journal-title":"J. Exp. Med."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.tem.2017.07.003","article-title":"Surviving Stress: Modulation of ATF4-Mediated Stress Re-sponses in Normal and Malignant Cells","volume":"28","author":"Wortel","year":"2017","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"33165","DOI":"10.1074\/jbc.M110.167213","article-title":"Both Transcriptional Regulation and Translational Control of ATF4 Are Central to the Integrated Stress Response","volume":"285","author":"Dey","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.15252\/embr.201642195","article-title":"The integrated stress response","volume":"17","author":"Koryga","year":"2016","journal-title":"EMBO Rep."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"32340","DOI":"10.1074\/jbc.273.48.32340","article-title":"Characterization of the hemin-sensitive eukaryotic initiation factor 2alpha kinase from mouse nonerythroid cells","volume":"273","author":"Berlanga","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"7729","DOI":"10.1073\/pnas.88.17.7729","article-title":"Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: Homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase","volume":"88","author":"Chen","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"7499","DOI":"10.1128\/MCB.18.12.7499","article-title":"Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 \u03b1-Subunit Kinase, PEK, Involved in Translational Control","volume":"18","author":"Shi","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0092-8674(90)90374-N","article-title":"Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon","volume":"62","author":"Meurs","year":"1990","journal-title":"Cell"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3493","DOI":"10.1007\/s00018-012-1252-6","article-title":"The eIF2\u03b1 kinases: Their structures and functions","volume":"70","author":"Donnelly","year":"2013","journal-title":"Cell. Mol. Life Sci."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/9\/1468\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:00:01Z","timestamp":1760166001000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/9\/1468"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9,15]]},"references-count":101,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2021,9]]}},"alternative-id":["antiox10091468"],"URL":"https:\/\/doi.org\/10.3390\/antiox10091468","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,9,15]]}}}