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Neurosci."},{"issue":"1","key":"10.1016\/j.bbadis.2018.10.024_bb0335","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1093\/toxsci\/kfw030","article-title":"NAD+ supplementation attenuates methylmercury dopaminergic and mitochondrial toxicity in Caenorhabditis elegans","volume":"151","author":"Caito","year":"2016","journal-title":"Toxicol. Sci."},{"issue":"9","key":"10.1016\/j.bbadis.2018.10.024_bb0340","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.tips.2016.06.007","article-title":"Targeting oxidative stress in central nervous system disorders","volume":"37","author":"Patel","year":"2016","journal-title":"Trends Pharmacol. Sci."},{"issue":"2","key":"10.1016\/j.bbadis.2018.10.024_bb0345","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1002\/jcp.10111","article-title":"Mitochondria, the killer organelles and their weapons","volume":"192","author":"Ravagnan","year":"2002","journal-title":"J. Cell. Physiol."},{"issue":"4","key":"10.1016\/j.bbadis.2018.10.024_bb0350","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1023\/B:JOBB.0000041756.23918.11","article-title":"Neuronal apoptosis: BH3-only proteins the real killers?","volume":"36","author":"Ward","year":"2004","journal-title":"J. Bioenerg. Biomembr."},{"issue":"1","key":"10.1016\/j.bbadis.2018.10.024_bb0355","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1006\/taap.2001.9327","article-title":"Acute exposure to methylmercury opens the mitochondrial permeability transition pore in rat cerebellar granule cells","volume":"178","author":"Limke","year":"2002","journal-title":"Toxicol. Appl. 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Neurochem."},{"issue":"2","key":"10.1016\/j.bbadis.2018.10.024_bb0370","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1385\/NMM:2:2:215","article-title":"Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders","volume":"2","author":"Mattson","year":"2002","journal-title":"NeuroMolecular Med."},{"issue":"5","key":"10.1016\/j.bbadis.2018.10.024_bb0375","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.neuro.2011.07.006","article-title":"Role of oxidative stress and the mitochondrial permeability transition in methylmercury cytotoxicity","volume":"32","author":"Polunas","year":"2011","journal-title":"Neurotoxicology"},{"issue":"2","key":"10.1016\/j.bbadis.2018.10.024_bb0380","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/cr.2013.151","article-title":"Protein post-translational modifications and regulation of pluripotency in human stem cells","volume":"24","author":"Wang","year":"2014","journal-title":"Cell Res."},{"issue":"6","key":"10.1016\/j.bbadis.2018.10.024_bb0385","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/nrm1939","article-title":"Interpreting the protein language using proteomics","volume":"7","author":"Jensen","year":"2006","journal-title":"Nat. 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Med."},{"issue":"14","key":"10.1016\/j.bbadis.2018.10.024_bb0405","doi-asserted-by":"crossref","first-page":"8904","DOI":"10.1074\/jbc.M114.612796","article-title":"Ubiquitinated sirtuin 1 (SIRT1) function is modulated during DNA damage-induced cell death and survival","volume":"290","author":"Peng","year":"2015","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.bbadis.2018.10.024_bb0410","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1038\/cdd.2014.28","article-title":"Oxidative stress-induced p53 activity is enhanced by a redox-sensitive TP53INP1 SUMOylation","volume":"21","author":"Peuget","year":"2014","journal-title":"Cell Death Differ."},{"issue":"D1","key":"10.1016\/j.bbadis.2018.10.024_bb0415","doi-asserted-by":"crossref","first-page":"D306","DOI":"10.1093\/nar\/gks1230","article-title":"PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins","volume":"41","author":"Minguez","year":"2013","journal-title":"Nucleic Acids Res."},{"issue":"5","key":"10.1016\/j.bbadis.2018.10.024_bb0420","doi-asserted-by":"crossref","first-page":"E127","DOI":"10.1038\/ncb0502-e127","article-title":"The origins of protein phosphorylation","volume":"4","author":"Cohen","year":"2002","journal-title":"Nat. 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Sci."},{"issue":"3","key":"10.1016\/j.bbadis.2018.10.024_bb0480","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1007\/s12038-007-0050-z","article-title":"Protein stress and stress proteins: implications in aging and disease","volume":"32","author":"Soti","year":"2007","journal-title":"J. Biosci."},{"key":"10.1016\/j.bbadis.2018.10.024_bb0485","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/978-1-4939-6783-4_9","article-title":"Analysis of cysteine redox post-translational modifications in cell biology and drug pharmacology","volume":"1558","author":"Wani","year":"2017","journal-title":"Methods Mol. Biol."},{"issue":"2","key":"10.1016\/j.bbadis.2018.10.024_bb0490","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1161\/CIRCRESAHA.112.268680","article-title":"Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system","volume":"112","author":"Chung","year":"2013","journal-title":"Circ. Res."},{"issue":"1\u20133","key":"10.1016\/j.bbadis.2018.10.024_bb0495","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/0300-483X(94)90170-8","article-title":"Differential effects of methylmercury on the phosphorylation of protein species in the brain of acutely intoxicated rats","volume":"92","author":"Yagame","year":"1994","journal-title":"Toxicology"},{"issue":"3","key":"10.1016\/j.bbadis.2018.10.024_bb0500","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1111\/j.1471-4159.1990.tb04579.x","article-title":"Altered patterns of protein phosphorylation and synthesis caused by methyl mercury in cerebellar granule cell culture","volume":"55","author":"Sarafian","year":"1990","journal-title":"J. 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Lett."},{"issue":"3","key":"10.1016\/j.bbadis.2018.10.024_bb0520","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.taap.2014.12.008","article-title":"Methylmercury causes neuronal cell death through the suppression of the TrkA pathway: in vitro and in vivo effects of TrkA pathway activators","volume":"282","author":"Fujimura","year":"2015","journal-title":"Toxicol. Appl. Pharmacol."},{"issue":"1","key":"10.1016\/j.bbadis.2018.10.024_bb0525","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.devbrainres.2003.10.017","article-title":"Methylmercury inhibits TrkA signaling through the ERK1\/2 cascade after NGF stimulation of PC12 cells","volume":"149","author":"Parran","year":"2004","journal-title":"Brain Res. Dev. 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Rep."},{"issue":"2","key":"10.1016\/j.bbadis.2018.10.024_bb0585","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1006\/enrs.1993.1146","article-title":"Effects of methylmercury on protein kinase A and protein kinase C in the mouse brain","volume":"63","author":"Saijoh","year":"1993","journal-title":"Environ. Res."},{"issue":"1","key":"10.1016\/j.bbadis.2018.10.024_bb0590","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0165-3806(98)00039-X","article-title":"Effects of gestational methylmercury exposure on immunoreactivity of specific isoforms of PKC and enzyme activity during post-natal development of the rat brain","volume":"109","author":"Haykal-Coates","year":"1998","journal-title":"Brain Res. Dev. 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