{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T14:44:15Z","timestamp":1790347455291,"version":"4.1.0"},"reference-count":186,"publisher":"Impact Journals, LLC","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Aging"],"published-print":{"date-parts":[[2021,4,15]]},"DOI":"10.18632\/aging.202928","type":"journal-article","created":{"date-parts":[[2021,4,3]],"date-time":"2021-04-03T16:33:26Z","timestamp":1617467606000},"page":"10770-10795","source":"Crossref","is-referenced-by-count":58,"title":["Alzheimer\u2019s disease as a chronic maladaptive polyamine stress response"],"prefix":"10.18632","volume":"13","author":[{"given":"Baruh","family":"Polis","sequence":"first","affiliation":[{"name":"Drug Discovery Laboratory, The Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Karasik","sequence":"additional","affiliation":[{"name":"Hebrew SeniorLife, Hinda and Arthur Marcus Institute for Aging Research, Boston, MA 02131, USA"},{"name":"Musculoskeletal Genetics Laboratory, The Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abraham O.","family":"Samson","sequence":"additional","affiliation":[{"name":"Drug Discovery Laboratory, The Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"7892","published-online":{"date-parts":[[2021,4,3]]},"reference":[{"key":"1","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1111\/j.1582-4934.2007.00077.x","article-title":"Physiological polyamines: simple primordial stress molecules.","volume":"1","author":"Lee","year":"2007","journal-title":"J Cell Mol Med"},{"key":"2","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1002\/jcb.240460203","article-title":"A new perspective on ornithine decarboxylase regulation: prevention of polyamine toxicity is the overriding theme.","volume":"4","author":"Morris","year":"1991","journal-title":"J Cell Biochem"},{"key":"3","doi-asserted-by":"publisher","first-page":"18693","DOI":"10.1074\/jbc.TM118.005670","article-title":"Polyamine function in archaea and bacteria.","volume":"29","author":"Michael","year":"2018","journal-title":"J Biol Chem"},{"key":"4","doi-asserted-by":"publisher","first-page":"14896","DOI":"10.1074\/jbc.R116.734780","article-title":"Polyamines in Eukaryotes, Bacteria, and Archaea.","volume":"29","author":"Michael","year":"2016","journal-title":"J Biol Chem"},{"key":"5","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1007\/s40610-017-0052-z","article-title":"Polyamines: Emerging Hubs Promoting Drought and Salt Stress Tolerance in Plants.","volume":"3","author":"Fotopoulos","year":"2017","journal-title":"Curr Mol Biol Rep"},{"key":"6","doi-asserted-by":"publisher","first-page":"3389","DOI":"10.1016\/j.jmb.2015.06.020","article-title":"Remaining Mysteries of Molecular Biology: The Role of Polyamines in the Cell.","volume":"42","author":"Ralser","year":"2015","journal-title":"J Mol Biol"},{"key":"7","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1016\/0006-2952(92)90428-L","article-title":"Polyamines in neurotrauma. Ubiquitous molecules in search of a function.","volume":"4","author":"Gilad","year":"1992","journal-title":"Biochem Pharmacol"},{"key":"8","doi-asserted-by":"publisher","first-page":"5969","DOI":"10.1523\/JNEUROSCI.4668-14.2015","article-title":"Arginine deprivation and immune suppression in a mouse model of Alzheimer\u2019s disease.","volume":"3","author":"Colton","year":"2015","journal-title":"J Neurosci"},{"key":"9","doi-asserted-by":"publisher","first-page":"2364","DOI":"10.1038\/srep02364","article-title":"Metabolic profiling of Alzheimer\u2019s disease brains.","volume":"3","author":"Toyo\u2019oka","year":"2013","journal-title":"Sci Rep"},{"key":"10","doi-asserted-by":"publisher","first-page":"E11293","DOI":"10.1073\/pnas.1711243115","article-title":"Brain urea increase is an early Huntington\u2019s disease pathogenic event observed in a prodromal transgenic sheep model and HD cases.","volume":"11","author":"MacDonald","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"key":"11","doi-asserted-by":"publisher","first-page":"1036","DOI":"10.1007\/s13311-018-0669-5","article-title":"L-Norvaline Reverses Cognitive Decline and Synaptic Loss in a Murine Model of Alzheimer\u2019s Disease.","volume":"1","author":"Samson","year":"2018","journal-title":"Neurotherapeutics"},{"key":"12","doi-asserted-by":"publisher","first-page":"10","DOI":"10.3389\/fchem.2018.00010","article-title":"Polyamines: Bio-Molecules with Diverse Functions in Plant and Human Health and Disease.","volume":"6","author":"Mattoo","year":"2018","journal-title":"Front Chem"},{"key":"13","doi-asserted-by":"publisher","first-page":"4471","DOI":"10.1007\/s00018-017-2587-9","article-title":"Epithelial cell senescence: an adaptive response to pre-carcinogenic stresses?","volume":"7","author":"Pourtier","year":"2017","journal-title":"Cell Mol Life Sci"},{"key":"14","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1016\/j.tibs.2020.02.005","article-title":"Unfolded Protein Response (UPR) Controls Major Senescence Hallmarks.","volume":"4","author":"Pluquet","year":"2020","journal-title":"Trends Biochem Sci"},{"key":"15","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.tma.2019.01.002","article-title":"Senescence in aging and disorders of the central nervous system.","volume":"3","author":"Baker","year":"2019","journal-title":"Transl Med Aging"},{"key":"16","doi-asserted-by":"publisher","first-page":"16","DOI":"10.3389\/fncel.2020.00016","article-title":"Cellular Senescence in Neurodegenerative Diseases.","volume":"1","author":"Rueda","year":"2020","journal-title":"Front Cell Neurosci"},{"key":"17","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1023\/A:1025036532672","article-title":"Overview of the brain polyamine-stress-response: regulation, development, and modulation by lithium and role in cell survival.","volume":"2","author":"Gilad","year":"2003","journal-title":"Cell Mol Neurobiol"},{"key":"18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1042\/bj20031327","article-title":"A perspective of polyamine metabolism.","volume":"37","author":"Hughes","year":"2003","journal-title":"Biochem J"},{"key":"19","doi-asserted-by":"publisher","first-page":"39224","DOI":"10.1074\/jbc.M110.163154","article-title":"Evolution and multiplicity of arginine decarboxylases in polyamine biosynthesis and essential role in Bacillus subtilis biofilm formation.","volume":"28","author":"Michael","year":"2010","journal-title":"J Biol Chem"},{"key":"20","doi-asserted-by":"publisher","first-page":"1609","DOI":"10.1111\/j.1471-4159.1969.tb10360.x","article-title":"A radioisotopic method for measuring the formation of adenosine 3',5'-cyclic monophosphate in incubated slices of brain.","volume":"1","author":"Creveling","year":"1969","journal-title":"J Neurochem"},{"key":"21","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1007\/BF00963776","article-title":"The conversion of lysine into piperidine, cadaverine, and pipecolic acid in the brain and other organs of the mouse.","volume":"2","author":"Giacobini","year":"1977","journal-title":"Neurochem Res"},{"key":"22","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1038\/252158a0","article-title":"Cadaverine in the brain of axenic mice.","volume":"25","author":"Dolezalova","year":"1974","journal-title":"Nature"},{"key":"23","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1128\/JB.166.1.128-134.1986","article-title":"Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines.","volume":"16","author":"Matsuzaki","year":"1986","journal-title":"J Bacteriol"},{"key":"24","doi-asserted-by":"publisher","first-page":"966","DOI":"10.1126\/science.7906055","article-title":"Agmatine: an endogenous clonidine-displacing substance in the brain.","volume":"26","author":"Reis","year":"1994","journal-title":"Science"},{"key":"25","doi-asserted-by":"publisher","first-page":"1042","DOI":"10.1111\/j.1471-4159.2005.03544.x","article-title":"Expression of arginine decarboxylase in brain regions and neuronal cells.","volume":"9","author":"Regunathan","year":"2006","journal-title":"J Neurochem"},{"key":"26","doi-asserted-by":"publisher","first-page":"2319","DOI":"10.1016\/0024-3205(95)00226-V","article-title":"Agmatine, the bacterial amine, is widely distributed in mammalian tissues.","volume":"5","author":"Reis","year":"1995","journal-title":"Life Sci"},{"key":"27","doi-asserted-by":"publisher","first-page":"2201","DOI":"10.1046\/j.1471-4159.2000.0742201.x","article-title":"Characterization of arginine decarboxylase in rat brain and liver: distinction from ornithine decarboxylase.","volume":"7","author":"Reis","year":"2000","journal-title":"J Neurochem"},{"key":"28","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/0304-3940(96)12996-7","article-title":"Arginine and ornithine decarboxylation in rodent brain: coincidental changes during development and after ischemia.","volume":"21","author":"Rabey","year":"1996","journal-title":"Neurosci Lett"},{"key":"29","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0091-3057(01)00509-3","article-title":"Agmatine produces antinociception in tonic pain in mice.","volume":"6","author":"Soykan","year":"2001","journal-title":"Pharmacol Biochem Behav"},{"key":"30","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1196\/annals.1304.002","article-title":"Regulation of inducible nitric oxide synthase and agmatine synthesis in macrophages and astrocytes.","volume":"100","author":"Piletz","year":"2003","journal-title":"Ann N Y Acad Sci"},{"key":"31","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1023\/A:1025069407173","article-title":"Effect of agmatine against cell death induced by NMDA and glutamate in neurons and PC12 cells.","volume":"2","author":"Regunathan","year":"2003","journal-title":"Cell Mol Neurobiol"},{"key":"32","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/S0304-3940(00)01625-6","article-title":"Accelerated functional recovery and neuroprotection by agmatine after spinal cord ischemia in rats.","volume":"29","author":"Gilad","year":"2000","journal-title":"Neurosci Lett"},{"key":"33","doi-asserted-by":"publisher","first-page":"e66735","DOI":"10.1371\/journal.pone.0066735","article-title":"Arginase and Arginine Decarboxylase - Where Do the Putative Gate Keepers of Polyamine Synthesis Reside in Rat Brain?","volume":"8","author":"Laube","year":"2013","journal-title":"PLoS One"},{"key":"34","doi-asserted-by":"publisher","first-page":"2039","DOI":"10.1007\/s00018-008-7554-z","article-title":"Evolution of the arginase fold and functional diversity.","volume":"6","author":"Christianson","year":"2008","journal-title":"Cell Mol Life Sci"},{"key":"35","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/j.tips.2015.03.006","article-title":"Arginase: an old enzyme with new tricks.","volume":"3","author":"Caldwell","year":"2015","journal-title":"Trends Pharmacol Sci"},{"key":"36","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1006\/geno.1996.0606","article-title":"Cloning and characterization of the human type II arginase gene.","volume":"3","author":"Cederbaum","year":"1996","journal-title":"Genomics"},{"key":"37","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1006\/abbi.1994.1276","article-title":"Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors.","volume":"31","author":"Ash","year":"1994","journal-title":"Arch Biochem Biophys"},{"key":"38","doi-asserted-by":"publisher","first-page":"31107","DOI":"10.1074\/jbc.M001346200","article-title":"Drosophila arginase is produced from a nonvital gene that contains the elav locus within its third intron.","volume":"27","author":"Samson","year":"2000","journal-title":"J Biol Chem"},{"key":"39","doi-asserted-by":"publisher","first-page":"544","DOI":"10.3389\/fimmu.2014.00544","article-title":"Evolutionary roots of arginase expression and regulation.","volume":"5","author":"Dzik","year":"2014","journal-title":"Front Immunol"},{"key":"40","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/0305-0491(95)02138-8","article-title":"Comparative properties of arginases.","volume":"11","author":"Cederbaum","year":"1996","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"41","doi-asserted-by":"publisher","first-page":"2812S","DOI":"10.1093\/jn\/134.10.2812S","article-title":"Novel roles for arginase in cell survival, regeneration, and translation in the central nervous system.","volume":"13","author":"Ratan","year":"2004","journal-title":"J Nutr"},{"key":"42","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1111\/j.1471-4159.1977.tb07783.x","article-title":"Arginases of mouse brain and liver.","volume":"2","author":"Caron","year":"1977","journal-title":"J Neurochem"},{"key":"43","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.ymgme.2018.07.007","article-title":"Arginase overexpression in neurons and its effect on traumatic brain injury.","volume":"12","author":"Goodman","year":"2018","journal-title":"Mol Genet Metab"},{"key":"44","doi-asserted-by":"publisher","first-page":"4083","DOI":"10.1523\/JNEUROSCI.18-11-04083.1998","article-title":"Purification of a multipotent antideath activity from bovine liver and its identification as arginase: nitric oxide-independent inhibition of neuronal apoptosis.","volume":"1","author":"Ratan","year":"1998","journal-title":"J Neurosci"},{"key":"45","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/S0378-1119(97)00099-1","article-title":"Human type II arginase: sequence analysis and tissue-specific expression.","volume":"19","author":"Kepka-Lenhart","year":"1997","journal-title":"Gene"},{"key":"46","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1016\/0003-9861(61)90182-5","article-title":"Citrulline synthesis in rat tissues.","volume":"9","author":"Hodes","year":"1961","journal-title":"Arch Biochem Biophys"},{"key":"47","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1146\/annurev.nu.12.070192.000501","article-title":"Regulation of enzymes of urea and arginine synthesis.","volume":"1","author":"Morris","year":"1992","journal-title":"Annu Rev Nutr"},{"key":"48","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1111\/j.1476-5381.2011.01584.x","article-title":"Oxidative species increase arginase activity in endothelial cells through the RhoA\/Rho kinase pathway.","volume":"16","author":"Caldwell","year":"2012","journal-title":"Br J Pharmacol"},{"key":"49","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1016\/j.atherosclerosis.2010.10.044","article-title":"OxLDL-dependent activation of arginase II is dependent on the LOX-1 receptor and downstream RhoA signaling.","volume":"21","author":"Romer","year":"2011","journal-title":"Atherosclerosis"},{"key":"50","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1161\/CIRCRESAHA.115.304262","article-title":"OxLDL triggers retrograde translocation of arginase2 in aortic endothelial cells via ROCK and mitochondrial processing peptidase.","volume":"11","author":"Romer","year":"2014","journal-title":"Circ Res"},{"key":"51","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.3233\/JAD-190357","article-title":"Endothelial Mitochondrial Dysfunction in Cerebral Amyloid Angiopathy and Alzheimer\u2019s Disease.","volume":"7","author":"Fossati","year":"2019","journal-title":"J Alzheimers Dis"},{"key":"52","doi-asserted-by":"publisher","first-page":"e438","DOI":"10.1038\/emm.2017.254","article-title":"Arginase II inhibition prevents interleukin-8 production through regulation of p38 MAPK phosphorylation activated by loss of mitochondrial membrane potential in nLDL-stimulated hAoSMCs.","volume":"5","author":"Ryoo","year":"2018","journal-title":"Exp Mol Med"},{"key":"53","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1093\/cvr\/cvt036","article-title":"Arginase as a potential target in the treatment of cardiovascular disease: reversal of arginine steal?","volume":"9","author":"Jung","year":"2013","journal-title":"Cardiovasc Res"},{"key":"54","doi-asserted-by":"publisher","first-page":"119","DOI":"10.4236\/aad.2018.74009","article-title":"Arginase as a Potential Target in the Treatment of Alzheimer Disease.","volume":"0","author":"Samson","year":"2018","journal-title":"Adv Alzheimer\u2019s Dis"},{"key":"55","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1186\/1742-2094-3-27","article-title":"Expression profiles for macrophage alternative activation genes in AD and in mouse models of AD.","volume":"3","author":"Vitek","year":"2006","journal-title":"J Neuroinflammation"},{"key":"56","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1152\/physrev.00037.2016","article-title":"Arginase: A Multifaceted Enzyme Important in Health and Disease.","volume":"9","author":"Caldwell","year":"2018","journal-title":"Physiol Rev"},{"key":"57","doi-asserted-by":"publisher","first-page":"1575","DOI":"10.1007\/s10072-013-1289-9","article-title":"Alzheimer\u2019s disease: amino acid levels and brain metabolic status.","volume":"3","author":"Taibi","year":"2013","journal-title":"Neurol Sci"},{"key":"58","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1080\/15216540500307031","article-title":"The antizyme family: polyamines and beyond.","volume":"5","author":"Mangold","year":"2005","journal-title":"IUBMB Life"},{"key":"59","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/0092-8674(95)90450-6","article-title":"Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme.","volume":"8","author":"Hayashi","year":"1995","journal-title":"Cell"},{"key":"60","doi-asserted-by":"publisher","first-page":"e0151175","DOI":"10.1371\/journal.pone.0151175","article-title":"Expression of ODC Antizyme Inhibitor 2 (AZIN2) in Human Secretory Cells and Tissues.","volume":"1","author":"Andersson","year":"2016","journal-title":"PLoS One"},{"key":"61","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1111\/j.1750-3639.2009.00334.x","article-title":"Brain neurons express ornithine decarboxylase-activating antizyme inhibitor 2 with accumulation in Alzheimer\u2019s disease.","volume":"2","author":"Andersson","year":"2010","journal-title":"Brain Pathol"},{"key":"62","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1016\/j.bbrc.2006.03.191","article-title":"Altered subcellular localization of ornithine decarboxylase in Alzheimer\u2019s disease brain.","volume":"34","author":"Benedikz","year":"2006","journal-title":"Biochem Biophys Res Commun"},{"key":"63","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-1-61779-034-8_1","article-title":"Current status of the polyamine research field.","volume":"72","author":"Casero","year":"2011","journal-title":"Methods Mol Biol"},{"key":"64","doi-asserted-by":"publisher","first-page":"E995","DOI":"10.1152\/ajpendo.90217.2008","article-title":"Spermidine\/spermine-N(1)-acetyltransferase: a key metabolic regulator.","volume":"29","author":"Pegg","year":"2008","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"65","doi-asserted-by":"publisher","first-page":"1194","DOI":"10.1038\/bjc.1995.485","article-title":"Evaluation of the significance of polyamines and their oxidases in the aetiology of human cervical carcinoma.","volume":"7","author":"Monks","year":"1995","journal-title":"Br J Cancer"},{"key":"66","doi-asserted-by":"publisher","first-page":"15404","DOI":"10.1073\/pnas.0607031103","article-title":"Acrolein is a major cigarette-related lung cancer agent: preferential binding at p53 mutational hotspots and inhibition of DNA repair.","volume":"10","author":"Tang","year":"2006","journal-title":"Proc Natl Acad Sci USA"},{"key":"67","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/S0197-4580(00)00235-9","article-title":"Acrolein is increased in Alzheimer\u2019s disease brain and is toxic to primary hippocampal cultures.","volume":"2","author":"Markesbery","year":"2001","journal-title":"Neurobiol Aging"},{"key":"68","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1046\/j.1471-4159.1999.0720751.x","article-title":"Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer\u2019s disease.","volume":"7","author":"Gibson","year":"1999","journal-title":"J Neurochem"},{"key":"69","doi-asserted-by":"publisher","first-page":"66","DOI":"10.2174\/1874467211003020066","article-title":"Potential role of acrolein in neurodegeneration and in Alzheimer\u2019s disease.","volume":"3","author":"Ramassamy","year":"2010","journal-title":"Curr Mol Pharmacol"},{"key":"70","first-page":"296","article-title":"Neurodegeneration and aldehyde load: from concept to therapeutics.","volume":"3","author":"Wood","year":"2006","journal-title":"J Psychiatry Neurosci"},{"key":"71","doi-asserted-by":"publisher","first-page":"150","DOI":"10.1016\/j.brainres.2006.10.004","article-title":"The concept of \u201caldehyde load\u201d in neurodegenerative mechanisms: cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line.","volume":"114","author":"Moskal","year":"2007","journal-title":"Brain Res"},{"key":"72","doi-asserted-by":"publisher","first-page":"1514","DOI":"10.1246\/bcsj.37.1514","article-title":"On the melting temperature of nanoparticles.","volume":"3","author":"Masamichi","year":"1964","journal-title":"Bull Chem Soc Jpn"},{"key":"73","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1016\/0003-9861(82)90175-8","article-title":"Interaction between polyamines and nucleic acids or phospholipids.","volume":"21","author":"Hirose","year":"1982","journal-title":"Arch Biochem Biophys"},{"key":"74","doi-asserted-by":"publisher","first-page":"20803","DOI":"10.1016\/S0021-9258(18)54780-3","article-title":"Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver.","volume":"26","author":"Igarashi","year":"1991","journal-title":"J Biol Chem"},{"key":"75","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1007\/BF00944391","article-title":"Protective effect of spermine on DNA exposed to oxidative stress.","volume":"14","author":"Caldarera","year":"1995","journal-title":"Mol Cell Biochem"},{"key":"76","doi-asserted-by":"publisher","first-page":"11140","DOI":"10.1073\/pnas.95.19.11140","article-title":"The natural polyamine spermine functions directly as a free radical scavenger.","volume":"9","author":"Casero","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"77","doi-asserted-by":"publisher","first-page":"e0193595","DOI":"10.1371\/journal.pone.0193595","article-title":"Opposite effect of polyamines on In vitro gene expression: enhancement at low concentrations but inhibition at high concentrations.","volume":"1","author":"Yoshikawa","year":"2018","journal-title":"PLoS One"},{"key":"78","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1007\/BF01261388","article-title":"Concentration-dependent effects of natural polyamines on peptide chain initiation and elongation in a cell-free system of protein synthesis.","volume":"9","author":"Georgatsos","year":"1990","journal-title":"Mol Cell Biochem"},{"key":"79","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.nlm.2013.04.008","article-title":"Polyaminergic agents modulate the reconsolidation of conditioned fear.","volume":"10","author":"Rubin","year":"2013","journal-title":"Neurobiol Learn Mem"},{"key":"80","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1016\/j.ejphar.2014.02.035","article-title":"Spermidine improves fear memory persistence.","volume":"73","author":"Rubin","year":"2014","journal-title":"Eur J Pharmacol"},{"key":"81","doi-asserted-by":"publisher","first-page":"18779","DOI":"10.1074\/jbc.TM118.003344","article-title":"Polyamines and potassium channels: A 25-year romance.","volume":"29","author":"Lee","year":"2018","journal-title":"J Biol Chem"},{"key":"82","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1042\/bj3250289","article-title":"Interactions of polyamines with ion channels.","volume":"32","author":"Williams","year":"1997","journal-title":"Biochem J"},{"key":"83","doi-asserted-by":"publisher","first-page":"325","DOI":"10.3389\/fphys.2014.00325","article-title":"Inward rectifiers and their regulation by endogenous polyamines.","volume":"5","author":"Kurata","year":"2014","journal-title":"Front Physiol"},{"key":"84","first-page":"575","article-title":"Effects of polyamines on the binding of [3H]MK-801 to the N-methyl-D-aspartate receptor: pharmacological evidence for the existence of a polyamine recognition site.","volume":"3","author":"Molinoff","year":"1989","journal-title":"Mol Pharmacol"},{"key":"85","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1016\/0896-6273(95)90049-7","article-title":"Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block.","volume":"1","author":"Mayer","year":"1995","journal-title":"Neuron"},{"key":"86","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1016\/S0006-8993(00)01973-9","article-title":"Spermine is neuroprotective against anoxia and N-methyl-D-aspartate in hippocampal slices.","volume":"85","author":"Biello","year":"2000","journal-title":"Brain Res"},{"key":"87","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1038\/nn.2777","article-title":"A neuroprotective role for polyamines in a Xenopus tadpole model of epilepsy.","volume":"1","author":"Aizenman","year":"2011","journal-title":"Nat Neurosci"},{"key":"88","first-page":"102","article-title":"Implication of the polyamine system in mental disorders.","volume":"3","author":"Turecki","year":"2008","journal-title":"J Psychiatry Neurosci"},{"key":"89","doi-asserted-by":"publisher","first-page":"1477","DOI":"10.1038\/npp.2010.17","article-title":"Evidence of altered polyamine concentrations in cerebral cortex of suicide completers.","volume":"3","author":"Turecki","year":"2010","journal-title":"Neuropsychopharmacology"},{"key":"90","doi-asserted-by":"publisher","first-page":"843","DOI":"10.1038\/jcbfm.1988.141","article-title":"Ornithine decarboxylase activity and immunohistochemical location in postischemic brain.","volume":"8","author":"Olson","year":"1988","journal-title":"J Cereb Blood Flow Metab"},{"key":"91","doi-asserted-by":"publisher","first-page":"204","DOI":"10.1111\/j.1471-4159.1991.tb02117.x","article-title":"Cerebral polyamine metabolism in reversible hypoglycemia of rat: relationship to energy metabolites and calcium.","volume":"5","author":"Hossmann","year":"1991","journal-title":"J Neurochem"},{"key":"92","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/0304-3940(92)90878-B","article-title":"Differing effects of alpha-difluoromethylornithine and CGP 40116 on polyamine levels and infarct volume in a rat model of focal cerebral ischaemia.","volume":"14","author":"Fagg","year":"1992","journal-title":"Neurosci Lett"},{"key":"93","doi-asserted-by":"publisher","first-page":"1233","DOI":"10.1111\/j.1460-9568.1993.tb00978.x","article-title":"Elevated seizure threshold and impaired spatial learning in transgenic mice with putrescine overproduction in the brain.","volume":"5","author":"Riekkinen","year":"1993","journal-title":"Eur J Neurosci"},{"key":"94","doi-asserted-by":"publisher","first-page":"2046","DOI":"10.1046\/j.1460-9568.1998.00216.x","article-title":"Neuroprotective role of ornithine decarboxylase activation in transient focal cerebral ischaemia: a study using ornithine decarboxylase-overexpressing transgenic rats.","volume":"1","author":"J\u00e4nne","year":"1998","journal-title":"Eur J Neurosci"},{"key":"95","doi-asserted-by":"publisher","first-page":"945","DOI":"10.1097\/00004647-200108000-00007","article-title":"Ornithine decarboxylase knockdown exacerbates transient focal cerebral ischemia-induced neuronal damage in rat brain.","volume":"2","author":"Dempsey","year":"2001","journal-title":"J Cereb Blood Flow Metab"},{"key":"96","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/0014-4886(91)90102-I","article-title":"Polyamines can protect against ischemia-induced nerve cell death in gerbil forebrain.","volume":"11","author":"Gilad","year":"1991","journal-title":"Exp Neurol"},{"key":"97","doi-asserted-by":"publisher","first-page":"1255","DOI":"10.1038\/sj.bjp.0704986","article-title":"L-arginyl-3,4-spermidine is neuroprotective in severalmodels of neurodegeneration andischaemia without suppressing synaptic transmission.","volume":"13","author":"Sundstrom","year":"2002","journal-title":"Br J Pharmacol"},{"key":"98","doi-asserted-by":"publisher","first-page":"9545","DOI":"10.1523\/JNEUROSCI.1175-09.2009","article-title":"Increased synthesis of spermidine as a result of upregulation of arginase I promotes axonal regeneration in culture and","volume":"2","author":"Filbin","year":"2009","journal-title":"J Neurosci"},{"key":"99","doi-asserted-by":"publisher","first-page":"2799","DOI":"10.1038\/s41467-020-16629-3","article-title":"Polyamine regulation of ion channel assembly and implications for nicotinic acetylcholine receptor pharmacology.","volume":"1","author":"Bredt","year":"2020","journal-title":"Nat Commun"},{"key":"100","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1016\/j.pneurobio.2004.09.006","article-title":"Neuronal nicotinic receptors: from structure to pathology.","volume":"7","author":"Clementi","year":"2004","journal-title":"Prog Neurobiol"},{"key":"101","doi-asserted-by":"publisher","first-page":"19746","DOI":"10.1016\/S0021-9258(18)55055-9","article-title":"Transgenic mice aberrantly expressing human ornithine decarboxylase gene.","volume":"26","author":"Alhonen","year":"1991","journal-title":"J Biol Chem"},{"key":"102","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.phrs.2016.03.023","article-title":"Modulation of learning and memory by natural polyamines.","volume":"11","author":"Mello","year":"2016","journal-title":"Pharmacol Res"},{"key":"103","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1007\/BF00806001","article-title":"Toxic effects of putrescine in rat brain: polyamines can be involved in the action of excitotoxins.","volume":"3","author":"Mart\u00ednez","year":"1992","journal-title":"Amino Acids"},{"key":"104","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1016\/0028-3908(93)90128-P","article-title":"Antagonists of N-methyl-D-aspartate receptors block seizures induced by putrescine in the deep prepiriform cortex.","volume":"3","author":"Nistic\u00f2","year":"1993","journal-title":"Neuropharmacology"},{"key":"105","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1006\/exnr.1997.6627","article-title":"Neurotoxicity of polyamines and pharmacological neuroprotection in cultures of rat cerebellar granule cells.","volume":"14","author":"Contestabile","year":"1997","journal-title":"Exp Neurol"},{"key":"106","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1002\/jnr.21538","article-title":"Spermine induces cell death in cultured human embryonic cerebral cortical neurons through N-methyl-D-aspartate receptor activation.","volume":"8","author":"Sanfeliu","year":"2008","journal-title":"J Neurosci Res"},{"key":"107","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1111\/j.1748-1716.1985.tb07704.x","article-title":"Striatal ornithine decarboxylase activity following neurotoxic and mechanical lesions of the mesostriatal dopamine system of the male rat.","volume":"12","author":"Zoli","year":"1985","journal-title":"Acta Physiol Scand"},{"key":"108","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/0304-3940(85)90487-2","article-title":"Effects of neurotoxic and mechanical lesions of the mesostriatal dopamine pathway on striatal polyamine levels in the rat: modulation by chronic ganglioside GM1 treatment.","volume":"6","author":"Toffano","year":"1985","journal-title":"Neurosci Lett"},{"key":"109","doi-asserted-by":"publisher","first-page":"3430","DOI":"10.1523\/JNEUROSCI.06-12-03430.1986","article-title":"Induction of ornithine decarboxylase as a possible mediator of seizure-elicited changes in genomic expression in rat hippocampus.","volume":"6","author":"Gall","year":"1986","journal-title":"J Neurosci"},{"key":"110","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1111\/j.1471-4159.1989.tb10903.x","article-title":"Blood-brain barrier breakdown in cold-injured brain is linked to a biphasic stimulation of ornithine decarboxylase activity and polyamine synthesis: both are coordinately inhibited by verapamil, dexamethasone, and aspirin.","volume":"5","author":"Lu","year":"1989","journal-title":"J Neurochem"},{"key":"111","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/j.1471-4159.1991.tb02091.x","article-title":"Changes in polyamine levels in rat brain after systemic kainic acid administration: relationship to convulsant activity and brain damage.","volume":"5","author":"Mart\u00ednez","year":"1991","journal-title":"J Neurochem"},{"key":"112","doi-asserted-by":"publisher","first-page":"11818","DOI":"10.1073\/pnas.1716173114","article-title":"Twenty-five years of mTOR: uncovering the link from nutrients to growth.","volume":"11","author":"Sabatini","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"key":"113","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/j.neuron.2014.09.034","article-title":"The neurology of mTOR.","volume":"8","author":"Sahin","year":"2014","journal-title":"Neuron"},{"key":"114","doi-asserted-by":"publisher","first-page":"4211","DOI":"10.1111\/j.1742-4658.2005.04833.x","article-title":"Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer\u2019s disease brain.","volume":"27","author":"Pei","year":"2005","journal-title":"FEBS J"},{"key":"115","doi-asserted-by":"publisher","first-page":"1005","DOI":"10.1111\/acel.12001","article-title":"Positive crosstalk between arginase-II and S6K1 in vascular endothelial inflammation and aging.","volume":"1","author":"Yang","year":"2012","journal-title":"Aging Cell"},{"key":"116","doi-asserted-by":"publisher","first-page":"682","DOI":"10.3389\/fphys.2017.00682","article-title":"Arginase-II Deficiency Extends Lifespan in Mice.","volume":"8","author":"Yang","year":"2017","journal-title":"Front Physiol"},{"key":"117","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.31.1_supplement.256.4","article-title":"Targeting mTOR signaling to promote healthy longevity.","volume":"3","author":"Kaeberlein","year":"2017","journal-title":"FASEB J"},{"key":"118","doi-asserted-by":"publisher","first-page":"15008","DOI":"10.1038\/npjamd.2015.8","article-title":"The mammalian target of rapamycin at the crossroad between cognitive aging and Alzheimer\u2019s disease.","volume":"1","author":"Oddo","year":"2015","journal-title":"NPJ Aging Mech Dis"},{"key":"119","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1111\/jnc.13037","article-title":"Alteration of mTOR signaling occurs early in the progression of Alzheimer disease (AD): analysis of brain from subjects with pre-clinical AD, amnestic mild cognitive impairment and late-stage AD.","volume":"13","author":"Butterfield","year":"2015","journal-title":"J Neurochem"},{"key":"120","doi-asserted-by":"publisher","first-page":"e9979","DOI":"10.1371\/journal.pone.0009979","article-title":"Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer\u2019s disease.","volume":"5","author":"Galvan","year":"2010","journal-title":"PLoS One"},{"key":"121","doi-asserted-by":"publisher","first-page":"14042","DOI":"10.1523\/JNEUROSCI.2781-15.2015","article-title":"Reducing Ribosomal Protein S6 Kinase 1 Expression Improves Spatial Memory and Synaptic Plasticity in a Mouse Model of Alzheimer\u2019s Disease.","volume":"3","author":"Oddo","year":"2015","journal-title":"J Neurosci"},{"key":"122","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/j.molcel.2014.11.013","article-title":"mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation.","volume":"5","author":"Kim","year":"2015","journal-title":"Mol Cell"},{"key":"123","doi-asserted-by":"publisher","first-page":"728","DOI":"10.1016\/j.cell.2011.10.026","article-title":"Autophagy: renovation of cells and tissues.","volume":"14","author":"Komatsu","year":"2011","journal-title":"Cell"},{"key":"124","doi-asserted-by":"publisher","first-page":"590","DOI":"10.4161\/auto.6259","article-title":"Neurodegenerative lysosomal disorders: a continuum from development to late age.","volume":"4","author":"Lee","year":"2008","journal-title":"Autophagy"},{"key":"125","doi-asserted-by":"publisher","first-page":"4081","DOI":"10.1242\/jcs.019265","article-title":"Autophagy, amyloidogenesis and Alzheimer disease.","volume":"12","author":"Nixon","year":"2007","journal-title":"J Cell Sci"},{"key":"126","doi-asserted-by":"publisher","first-page":"2223","DOI":"10.4161\/15548627.2014.981789","article-title":"ARG2 impairs endothelial autophagy through regulation of MTOR and PRKAA\/AMPK signaling in advanced atherosclerosis.","volume":"1","author":"Ming","year":"2014","journal-title":"Autophagy"},{"key":"127","doi-asserted-by":"publisher","first-page":"149","DOI":"10.3389\/fimmu.2013.00149","article-title":"Arginase: the emerging therapeutic target for vascular oxidative stress and inflammation.","volume":"4","author":"Ming","year":"2013","journal-title":"Front Immunol"},{"key":"128","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1038\/s41419-018-0356-9","article-title":"Arginase-II activates mTORC1 through myosin-1b in vascular cell senescence and apoptosis.","volume":"9","author":"Ming","year":"2018","journal-title":"Cell Death Dis"},{"key":"129","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1146\/annurev.ento.50.071803.130409","article-title":"Evolutionary and mechanistic theories of aging.","volume":"5","author":"Reynolds","year":"2005","journal-title":"Annu Rev Entomol"},{"key":"130","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1016\/S0197-4580(00)00250-5","article-title":"Life span and synapses: will there be a primary senile dementia?","volume":"2","author":"Katzman","year":"2001","journal-title":"Neurobiol Aging"},{"key":"131","doi-asserted-by":"publisher","first-page":"398","DOI":"10.2307\/2406060","article-title":"Pleiotropy, Natural Selection, and the Evolution of Senescence.","volume":"1","author":"Williams","year":"1957","journal-title":"Evolution (N Y)"},{"key":"132","doi-asserted-by":"publisher","first-page":"135","DOI":"10.4436\/jass.91001","article-title":"Alzheimer\u2019s disease: an evolutionary approach.","volume":"9","author":"August\u00ed","year":"2013","journal-title":"J Anthropol Sci"},{"key":"133","doi-asserted-by":"publisher","first-page":"140","DOI":"10.1016\/j.arr.2018.07.008","article-title":"\u2018Evolutionary medicine\u2019 perspectives on Alzheimer\u2019s Disease: review and new directions.","volume":"4","author":"Fox","year":"2018","journal-title":"Ageing Res Rev"},{"key":"134","doi-asserted-by":"publisher","first-page":"1394","DOI":"10.1001\/jamaneurol.2014.1491","article-title":"Effects of multiple genetic loci on age at onset in late-onset Alzheimer disease: a genome-wide association study.","volume":"7","author":"Myers","year":"2014","journal-title":"JAMA Neurol"},{"key":"135","doi-asserted-by":"publisher","first-page":"726197","DOI":"10.4061\/2011\/726197","article-title":"The apolipoprotein e antagonistic pleiotropy hypothesis: review and recommendations.","volume":"201","author":"Han","year":"2011","journal-title":"Int J Alzheimers Dis"},{"key":"136","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1016\/j.jalz.2011.05.2408","article-title":"Some evolutionary perspectives on Alzheimer\u2019s disease pathogenesis and pathology.","volume":"8","author":"Arnold","year":"2012","journal-title":"Alzheimers Dement"},{"key":"137","doi-asserted-by":"publisher","first-page":"eaan2788","DOI":"10.1126\/science.aan2788","article-title":"Spermidine in health and disease.","volume":"35","author":"Kroemer","year":"2018","journal-title":"Science"},{"key":"138","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1016\/S0014-4827(77)80052-9","article-title":"Ornithine decarboxylase activity and polyamines in relation to aging of human fibroblasts.","volume":"10","author":"Kremzner","year":"1977","journal-title":"Exp Cell Res"},{"key":"139","first-page":"38","article-title":"Aging alters ornithine decarboxylase and decreases polyamines in regenerating rat liver but putrescine replacement has no effect.","volume":"11","author":"Zieve","year":"1992","journal-title":"J Lab Clin Med"},{"key":"140","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1186\/s12863-018-0660-5","article-title":"Skeletal muscle in aged mice reveals extensive transformation of muscle gene expression.","volume":"1","author":"Chen","year":"2018","journal-title":"BMC Genet"},{"key":"141","doi-asserted-by":"publisher","first-page":"1305","DOI":"10.1038\/ncb1975","article-title":"Induction of autophagy by spermidine promotes longevity.","volume":"1","author":"Hartl","year":"2009","journal-title":"Nat Cell Biol"},{"key":"142","doi-asserted-by":"publisher","first-page":"1704650","DOI":"10.1155\/2019\/1704650","article-title":"Age-Dependent Oxidative Stress Elevates Arginase 1 and Uncoupled Nitric Oxide Synthesis in Skeletal Muscle of Aged Mice.","volume":"201","author":"Fulzele","year":"2019","journal-title":"Oxid Med Cell Longev"},{"key":"143","doi-asserted-by":"publisher","first-page":"1632","DOI":"10.1152\/japplphysiol.90627.2008","article-title":"Arginase and vascular aging.","volume":"10","author":"Berkowitz","year":"2008","journal-title":"J Appl Physiol (1985)"},{"key":"144","doi-asserted-by":"publisher","first-page":"4935386","DOI":"10.1155\/2020\/4935386","article-title":"Norvaline Reduces Blood Pressure and Induces Diuresis in Rats with Inherited Stress-Induced Arterial Hypertension.","volume":"202","author":"Naumenko","year":"2020","journal-title":"Biomed Res Int"},{"key":"145","doi-asserted-by":"publisher","first-page":"134","DOI":"10.2337\/dc07-1198","article-title":"Insulin reduces plasma arginase activity in type 2 diabetic patients.","volume":"3","author":"DeFronzo","year":"2008","journal-title":"Diabetes Care"},{"key":"146","doi-asserted-by":"crossref","DOI":"10.15586\/alzheimersdisease.2019","volume-title":"Alzheimer\u2019s Disease","author":"Wisniewski","year":"2019"},{"key":"147","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1002\/alz.12012","article-title":"A unified model of dementias and age-related neurodegeneration.","volume":"1","author":"Fossel","year":"2020","journal-title":"Alzheimers Dement"},{"key":"148","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/0304-3940(95)11301-C","article-title":"Increased immunostaining for L-ornithine decarboxylase occurs in neocortical neurons of Alzheimer\u2019s disease patients.","volume":"18","author":"M\u00fcller","year":"1995","journal-title":"Neurosci Lett"},{"key":"149","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/0304-3940(95)11881-V","article-title":"Brain polyamine levels are altered in Alzheimer\u2019s disease.","volume":"19","author":"Kish","year":"1995","journal-title":"Neurosci Lett"},{"key":"150","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1046\/j.1471-4159.1998.71010288.x","article-title":"Ornithine decarboxylase in human brain: influence of aging, regional distribution, and Alzheimer\u2019s disease.","volume":"7","author":"Kish","year":"1998","journal-title":"J Neurochem"},{"key":"151","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/S0304-3940(99)00101-9","article-title":"Alzheimer\u2019s amyloid beta-peptide associated free radicals increase rat embryonic neuronal polyamine uptake and ornithine decarboxylase activity: protective effect of vitamin E.","volume":"26","author":"Butterfield","year":"1999","journal-title":"Neurosci Lett"},{"key":"152","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1002\/1097-4547(20010301)63:5<395::AID-JNR1034>3.0.CO;2-Q","article-title":"Role of spermine in amyloid beta-peptide-associated free radical-induced neurotoxicity.","volume":"6","author":"Butterfield","year":"2001","journal-title":"J Neurosci Res"},{"key":"153","doi-asserted-by":"publisher","first-page":"1040","DOI":"10.1038\/jcbfm.1994.136","article-title":"Blockade of ornithine decarboxylase enzyme protects against ischemic brain damage.","volume":"1","author":"Dempsey","year":"1994","journal-title":"J Cereb Blood Flow Metab"},{"key":"154","doi-asserted-by":"publisher","first-page":"60","DOI":"10.3389\/fnagi.2018.00060","article-title":"Use of Eflornithine (DFMO) in the Treatment of Early Alzheimer\u2019s Disease: A Compassionate Use, Single-Case Study.","volume":"1","author":"Snyder","year":"2018","journal-title":"Front Aging Neurosci"},{"key":"155","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1186\/s13195-019-0507-y","article-title":"Spermidine\/spermine-N-acetyltransferase ablation impacts tauopathy-induced polyamine stress response.","volume":"1","author":"Dickey","year":"2019","journal-title":"Alzheimers Res Ther"},{"key":"156","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.3233\/JAD-2010-100630","article-title":"Is the urea cycle involved in Alzheimer\u2019s disease?","volume":"2","author":"Mann","year":"2010","journal-title":"J Alzheimers Dis"},{"key":"157","doi-asserted-by":"publisher","first-page":"1084","DOI":"10.1016\/j.bbadis.2016.03.001","article-title":"Graded perturbations of metabolism in multiple regions of human brain in Alzheimer\u2019s disease: snapshot of a pervasive metabolic disorder.","volume":"186","author":"Cooper","year":"2016","journal-title":"Biochim Biophys Acta"},{"key":"158","doi-asserted-by":"publisher","first-page":"1992","DOI":"10.1016\/j.neurobiolaging.2014.03.013","article-title":"Altered arginine metabolism in Alzheimer\u2019s disease brains.","volume":"3","author":"Zhang","year":"2014","journal-title":"Neurobiol Aging"},{"key":"159","doi-asserted-by":"publisher","first-page":"e1003012","DOI":"10.1371\/journal.pmed.1003012","article-title":"Dysregulation of multiple metabolic networks related to brain transmethylation and polyamine pathways in Alzheimer disease: A targeted metabolomic and transcriptomic study.","volume":"1","author":"Thambisetty","year":"2020","journal-title":"PLoS Med"},{"key":"160","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1007\/s00726-006-0409-8","article-title":"Free amino acid and dipeptide changes in the body fluids from Alzheimer\u2019s disease subjects.","volume":"3","author":"Harrington","year":"2007","journal-title":"Amino Acids"},{"key":"161","doi-asserted-by":"publisher","first-page":"8532","DOI":"10.1021\/ac301243k","article-title":"Toward a predictive model of Alzheimer\u2019s disease progression using capillary electrophoresis-mass spectrometry metabolomics.","volume":"8","author":"Cifuentes","year":"2012","journal-title":"Anal Chem"},{"key":"162","doi-asserted-by":"publisher","first-page":"90","DOI":"10.3389\/fnagi.2019.00090","article-title":"Dysregulated Urinary Arginine Metabolism in Older Adults With Amnestic Mild Cognitive Impairment.","volume":"1","author":"Cheng","year":"2019","journal-title":"Front Aging Neurosci"},{"key":"163","doi-asserted-by":"publisher","first-page":"e0119452","DOI":"10.1371\/journal.pone.0119452","article-title":"Untargeted metabolomic analysis of human plasma indicates differentially affected polyamine and L-arginine metabolism in mild cognitive impairment subjects converting to Alzheimer\u2019s disease.","volume":"1","author":"Green","year":"2015","journal-title":"PLoS One"},{"key":"164","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/0304-3940(94)91073-1","article-title":"Polyamines inhibit nitric oxide synthase in rat cerebellum.","volume":"17","author":"el-Fakahany","year":"1994","journal-title":"Neurosci Lett"},{"key":"165","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1016\/j.ejphar.2010.02.029","article-title":"Agmatine prevents LPS-induced spatial memory impairment and hippocampal apoptosis.","volume":"63","author":"Moosavi","year":"2010","journal-title":"Eur J Pharmacol"},{"key":"166","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1186\/1471-2261-9-12","article-title":"Inhibition of S6K1 accounts partially for the anti-inflammatory effects of the arginase inhibitor L-norvaline.","volume":"9","author":"Yang","year":"2009","journal-title":"BMC Cardiovasc Disord"},{"key":"167","doi-asserted-by":"publisher","first-page":"1562","DOI":"10.4103\/1673-5374.255980","article-title":"L-Norvaline, a new therapeutic agent against Alzheimer\u2019s disease.","volume":"1","author":"Samson","year":"2019","journal-title":"Neural Regen Res"},{"key":"168","doi-asserted-by":"publisher","first-page":"4616","DOI":"10.3390\/ijms20184616","article-title":"Norvaline Restores the BBB Integrity in a Mouse Model of Alzheimer\u2019s Disease.","volume":"2","author":"Samson","year":"2019","journal-title":"Int J Mol Sci"},{"key":"169","doi-asserted-by":"publisher","first-page":"1133","DOI":"10.3390\/ijms21031133","article-title":"Arginase Inhibition Supports Survival and Differentiation of Neuronal Precursors in Adult Alzheimer\u2019s Disease Mice.","volume":"2","author":"Samson","year":"2020","journal-title":"Int J Mol Sci"},{"key":"170","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1128\/MCB.00805-14","article-title":"Cross talk between histone deacetylase 4 and STAT6 in the transcriptional regulation of arginase 1 during mouse dendritic cell differentiation.","volume":"3","author":"Zhou","year":"2015","journal-title":"Mol Cell Biol"},{"key":"171","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1186\/s40035-017-0089-1","article-title":"The development prospection of HDAC inhibitors as a potential therapeutic direction in Alzheimer\u2019s disease.","volume":"6","author":"Zhang","year":"2017","journal-title":"Transl Neurodegener"},{"key":"172","doi-asserted-by":"publisher","DOI":"10.1101\/2020.06.15.153346","article-title":"Citrulline supplementation improves spatial memory in a murine model for Alzheimer\u2019s disease.","author":"Garcia-delaTorre","year":"2020","journal-title":"BioRxiv"},{"key":"173","doi-asserted-by":"publisher","first-page":"14842","DOI":"10.1523\/JNEUROSCI.3959-14.2015","article-title":"Sustained Arginase 1 Expression Modulates Pathological Tau Deposits in a Mouse Model of Tauopathy.","volume":"3","author":"Dickey","year":"2015","journal-title":"J Neurosci"},{"key":"174","doi-asserted-by":"publisher","first-page":"582998","DOI":"10.3389\/fimmu.2020.582998","article-title":"Arginase 1 Insufficiency Precipitates Amyloid- \u03b2 Deposition and Hastens Behavioral Impairment in a Mouse Model of Amyloidosis.","volume":"1","author":"Orr","year":"2021","journal-title":"Front Immunol"},{"key":"175","doi-asserted-by":"publisher","first-page":"10637","DOI":"10.1523\/JNEUROSCI.3279-05.2005","article-title":"Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L).","volume":"2","author":"Ashe","year":"2005","journal-title":"J Neurosci"},{"key":"176","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1016\/j.ajhg.2020.02.014","article-title":"Bi-allelic LoF NRROS Variants Impairing Active TGF-\u03b21 Delivery Cause a Severe Infantile-Onset Neurodegenerative Condition with Intracranial Calcification.","volume":"10","author":"Tan","year":"2020","journal-title":"Am J Hum Genet"},{"key":"177","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1534\/genetics.111.136911","article-title":"Gene overexpression: uses, mechanisms, and interpretation.","volume":"19","author":"Prelich","year":"2012","journal-title":"Genetics"},{"key":"178","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1017\/mdh.2015.30","article-title":"A Knockout Experiment: Disciplinary Divides and Experimental Skill in Animal Behaviour Genetics.","volume":"5","author":"Nelson","year":"2015","journal-title":"Med Hist"},{"key":"179","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1038\/374314b0","article-title":"Knockout mouse fault lines.","volume":"37","author":"Routtenberg","year":"1995","journal-title":"Nature"},{"key":"180","doi-asserted-by":"publisher","first-page":"1628","DOI":"10.1016\/j.bbadis.2016.05.020","article-title":"Treatment with polyamine oxidase inhibitor reduces microglial activation and limits vascular injury in ischemic retinopathy.","volume":"186","author":"Narayanan","year":"2016","journal-title":"Biochim Biophys Acta"},{"key":"181","doi-asserted-by":"publisher","first-page":"956","DOI":"10.3389\/fnins.2018.00956","article-title":"Targeting Polyamine Oxidase to Prevent Excitotoxicity-Induced Retinal Neurodegeneration.","volume":"1","author":"Narayanan","year":"2019","journal-title":"Front Neurosci"},{"key":"182","doi-asserted-by":"publisher","first-page":"e64810","DOI":"10.1371\/journal.pone.0064810","article-title":"A New Transgenic Mouse Model for Studying the Neurotoxicity of Spermine Oxidase Dosage in the Response to Excitotoxic Injury.","volume":"8","author":"Mariottini","year":"2013","journal-title":"PLoS One"},{"key":"183","doi-asserted-by":"publisher","first-page":"9100","DOI":"10.1074\/jbc.M109.060061","article-title":"AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-beta peptide metabolism.","volume":"28","author":"Marambaud","year":"2010","journal-title":"J Biol Chem"},{"key":"184","doi-asserted-by":"publisher","first-page":"2323","DOI":"10.3892\/mmr.2015.3611","article-title":"Chloroquine exerts neuroprotection following traumatic brain injury via suppression of inflammation and neuronal autophagic death.","volume":"1","author":"Cui","year":"2015","journal-title":"Mol Med Rep"},{"key":"185","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/j.brainres.2013.05.011","article-title":"Oral L-citrulline administration improves memory deficits following transient brain ischemia through cerebrovascular protection.","volume":"152","author":"Fukunaga","year":"2013","journal-title":"Brain Res"},{"key":"186","doi-asserted-by":"publisher","first-page":"e1075","DOI":"10.1038\/cddis.2014.23","article-title":"Arginase 2 deficiency reduces hyperoxia-mediated retinal neurodegeneration through the regulation of polyamine metabolism.","volume":"5","author":"Caldwell","year":"2014","journal-title":"Cell Death Dis"}],"container-title":["Aging"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.aging-us.com\/lookup\/doi\/10.18632\/aging.202928","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,5,6]],"date-time":"2021-05-06T16:58:06Z","timestamp":1620320286000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.aging-us.com\/lookup\/doi\/10.18632\/aging.202928"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4,3]]},"references-count":186,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2021,4,15]]}},"alternative-id":["202928","33811757"],"URL":"https:\/\/doi.org\/10.18632\/aging.202928","relation":{},"ISSN":["1945-4589"],"issn-type":[{"value":"1945-4589","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,4,3]]}}}