Erratum: Glycation potentiates a-synuclein-associated neurodegeneration in synucleinopathies (Brain (2017) 140:5 (1399-1419) DOI: 10.1093/brain/awx056);Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

Brain

Volumn 140, Issue 5, 2017, Pages 1399-1419

  Vicente Miranda, Hugo ^a,b   Szego, Éva M ^c   Oliveira, Luís M A ^d,e   Breda, Carlo ^f   Darendelioglu, Ekrem ^f,g   De Oliveira, Rita M ^a,b   Ferreira, Diana G ^b,c   Gomes, Marcos A ^b   Rott, Ruth ^h   Oliveira, Márcia ^b   Munari, Francesca ^e,i   Enguita, Francisco J ^b   Simões, Tânia ^j   Rodrigues, Eva F ^c   Heinrich, Michael ^k   Martins, Ivo C ^b   Zamolo, Irina ^l   Riess, Olaf ^l   Cordeiro, Carlos ^m   Ponces Freire, Ana ^m   Lashuel, Hilal A ⁿ   Santos, Nuno C ^b   Lopes, Luisa V ^b   Xiang, Wei ^o   Jovin, Thomas M ^e   Penque, Deborah ^j   Engelender, Simone ^h   Zweckstetter, Markus ^c,e,i   Klucken, Jochen ^k   Giorgini, Flaviano ^f   Quintas, Alexandre ^d   Outeiro, Tiago F ^a,c,p   more..

^a NOVA MEDICAL SCHOOL   (Portugal)

^b INSTITUTO DE MEDICINA MOLECULAR   (Portugal)

^c UNIVERSITY MEDICAL CENTER GÖTTINGEN   (Germany)

^d INSTITUTO SUPERIOR DE CIÊNCIAS DA SAÚDE EGAS MONIZ   (Portugal)

^e MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^f UNIVERSITY OF LEICESTER   (United Kingdom)

^g BINGOL UNIVERSITY   (Turkey)

^h TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

ⁱ GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

^j NATIONAL INSTITUTE OF HEALTH DR RICARDO JORGE   (Portugal)

^k UNIVERSITY HOSPITAL ERLANGEN   (Germany)

^l UNIVERSITY OF TÜBINGEN   (Germany)

^m UNIVERSITY OF LISBON   (Portugal)

ⁿ EPFL   (Switzerland)

^o UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

^p MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

more..

Author keywords

alpha synuclein; glycation; neurodegeneration; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; AMINOGUANIDINE; METHYLGLYOXAL; OLIGOMER; RECOMBINANT PROTEIN; TENILSETAM; ENZYME INHIBITOR;

AGING; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CYTOTOXICITY; DEGENERATIVE DISEASE; DROSOPHILA; EVOKED RESPONSE; GLYCATION; HIPPOCAMPAL SLICE; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOBLOTTING; IMMUNOCYTOCHEMISTRY; IMMUNOPRECIPITATION; IN VITRO STUDY; IN VIVO STUDY; INDUCED PLURIPOTENT STEM CELL; LONG TERM POTENTIATION; MALE; MEMBRANE BINDING; MOLECULAR GENETICS; MOUSE; NERVE DEGENERATION; NEUROPATHOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; RAT; SIZE EXCLUSION CHROMATOGRAPHY; SYNAPTIC POTENTIAL; SYNAPTIC TRANSMISSION; SYNUCLEINOPATHY; UBIQUITINATION; ANIMAL; CELL CULTURE; CELL DIFFERENTIATION; CELL SURVIVAL; DISEASE MODEL; DRUG EFFECTS; FEMALE; GLYCOSYLATION; HIPPOCAMPUS; METABOLISM; PHYSIOLOGY; PROTEINOSIS; TRANSGENIC MOUSE; YEAST;

AGING; ALPHA-SYNUCLEIN; ANIMALS; CELL DIFFERENTIATION; CELL SURVIVAL; CELLS, CULTURED; DISEASE MODELS, ANIMAL; DROSOPHILA; ENZYME INHIBITORS; FEMALE; GLYCOSYLATION; HIPPOCAMPUS; HUMANS; INDUCED PLURIPOTENT STEM CELLS; MALE; MICE; MICE, TRANSGENIC; NEURODEGENERATIVE DISEASES; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN PROCESSING, POST-TRANSLATIONAL; PYRUVALDEHYDE; RATS; YEASTS;

EID: 85019609948     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awab175     Document Type: Erratum

References (94)

1. Ahmed MU, Brinkmann Frye E, Degenhardt TP, Thorpe SR, Baynes JW. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem J 1997; 324 (Pt 2): 565-70.
2. Ali YO, Escala W, Ruan K, Zhai RG. Assaying locomotor, learning, and memory deficits in Drosophila models of neurodegeneration. J Vis Exp 2011; 49: e2504.
3. Anderson JP, Walker DE, Goldstein JM, de Laat R, Banducci K, Caccavello RJ, et al. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J Biol Chem 2006; 281: 29739-52.
4. Anderson WW, Collingridge GL. The LTP program: a data acquisition program for on-line analysis of long-term potentiation and other synaptic events. J Neurosci Methods 2001; 108: 71-83.
5. Aviles-Olmos I, Dickson J, Kefalopoulou Z, Djamshidian A, Ell P, Soderlund T, et al. Exenatide and the treatment of patients with Parkinson's disease. J Clin Invest 2013; 123: 2730-6.
6. Basso E, Antas P, Marijanovic Z, Goncalves S, Tenreiro S, Outeiro TF. PLK2 modulates alpha-synuclein aggregation in yeast and mammalian cells. Mol Neurobiol 2013; 48: 854-62.
7. Baynes JW, Thorpe SR. Glycoxidation and lipoxidation in atherogenesis. Free Radic Biol Med 2000; 28: 1708-16.
8. Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001; 292: 1552-5.
9. Bertoncini CW, Jung YS, Fernandez CO, Hoyer W, Griesinger C, Jovin TM, et al. Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein. Proc Natl Acad Sci USA 2005; 102: 1430-5.
10. Beyer K, Ariza A. Alpha-synuclein posttranslational modification and alternative splicing as a trigger for neurodegeneration. Mol Neurobiol 2013; 47: 509-24.
11. Bierhaus A, Fleming T, Stoyanov S, Leffler A, Babes A, Neacsu C, et al. Methylglyoxal modification of Nav1.8 facilitates nociceptive neuron firing and causes hyperalgesia in diabetic neuropathy. Nat Med 2012; 18: 926-33.
12. Bierhaus A, Schiekofer S, Schwaninger M, Andrassy M, Humpert PM, Chen J, et al. Diabetes-associated sustained activation of the transcription factor nuclear factor-kappaB. Diabetes 2001; 50: 2792-808.
13. Byers B, Cord B, Nguyen HN, Schule B, Fenno L, Lee PC, et al. SNCA triplication Parkinson's patient's iPSC-derived DA neurons accumulate alpha-synuclein and are susceptible to oxidative stress. PloS One 2011; 6: e26159.
14. Castellani R, Smith MA, Richey PL, Perry G. Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease. Brain Res 1996; 737: 195-200.
15. Chang TJ, Tseng HC, Liu MW, Chang YC, Hsieh ML, Chuang LM. Glucagon-like peptide-1 prevents methylglyoxal-induced apoptosis of beta cells through improving mitochondrial function and suppressing prolonged AMPK activation. Sci Rep 2016; 6: 23403.
16. Chen TS, Richie JP Jr, Lang CA. The effect of aging on glutathione and cysteine levels in different regions of the mouse brain. Proc Soc Exp Biol Med 1989; 190: 399-402.
17. Crane PK, Walker R, Hubbard RA, Li G, Nathan DM, Zheng H, et al. Glucose levels and risk of dementia. N Engl J Med 2013; 369: 540-8.
18. Dalfo E, Portero-Otin M, Ayala V, Martinez A, Pamplona R, Ferrer I. Evidence of oxidative stress in the neocortex in incidental Lewy body disease. J Neuropathol Exp Neurol 2005; 64: 816-30.
19. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995; 6: 277-93.
20. Diogenes MJ, Costenla AR, Lopes LV, Jeronimo-Santos A, Sousa VC, Fontinha BM, et al. Enhancement of LTP in aged rats is dependent on endogenous BDNF. Neuropsychopharmacology 2011; 36: 1823-36.
21. Diogenes MJ, Dias RB, Rombo DM, Vicente Miranda H, Maiolino F, Guerreiro P, et al. Extracellular alpha-synuclein oligomers modulate synaptic transmission and impair LTP via NMDA-receptor activation. J Neurosci 2012; 32: 11750-62.
22. Ebrahimi-Fakhari D, Wahlster L, McLean PJ. Protein degradation pathways in Parkinson's disease: curse or blessing. Acta Neuropathol 2012; 124: 153-72.
23. Faustino AF, Carvalho FA, Martins IC, Castanho MA, Mohana-Borges R, Almeida FC, et al. Dengue virus capsid protein interacts specifically with very low-density lipoproteins. Nanomedicine 2014; 10: 247-55.
24. Feany MB, Bender WW. A Drosophila model of Parkinson's disease. Nature 2000; 404: 394-8.
25. Fredholm BB, Dunwiddie TV, Bergman B, Lindstrom K. Levels of adenosine and adenine nucleotides in slices of rat hippocampus. Brain Res 1984; 295: 127-36.
26. Frye EB, Degenhardt TP, Thorpe SR, Baynes JW. Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end productdependent increase in imidazolium cross-links in human lens proteins. J Biol Chem 1998; 273: 18714-19.
27. Gomes RA, Sousa Silva M, Vicente Miranda H, Ferreira AE, Cordeiro CA, Freire AP. Protein glycation in Saccharomyces cerevisiae. Argpyrimidine formation and methylglyoxal catabolism. FEBS J 2005; 272: 4521-31.
28. Gonçalves S, Vicente Miranda H, Outeiro TF. Novel molecular therapeutics in Parkinson's disease. In: Whitehouse D, Rapley R, editors. Molecular and cellular therapeutics. Chichester, UK: John Wiley & Sons, Ltd; 2012. p. 245-65.
29. Guerreiro PS, Huang Y, Gysbers A, Cheng D, Gai WP, Outeiro TF, et al. LRRK2 interactions with alpha-synuclein in Parkinson's disease brains and in cell models. J Mol Med 2013; 91: 513-22.
30. Guix FX, Ill-Raga G, Bravo R, Nakaya T, de Fabritiis G, Coma M, et al. Amyloid-dependent triosephosphate isomerase nitrotyrosination induces glycation and tau fibrillation. Brain 2009; 132 (Pt 5): 1335-45.
31. Hansen F, Battu CE, Dutra MF, Galland F, Lirio F, Broetto N, et al. Methylglyoxal and carboxyethyllysine reduce glutamate uptake and S100B secretion in the hippocampus independently of RAGE activation. Amino Acids 2016; 48: 375-85.
32. Hu G, Jousilahti P, Bidel S, Antikainen R, Tuomilehto J. Type 2 diabetes and the risk of Parkinson's disease. Diabetes care 2007; 30: 842-7.
33. Jo E, McLaurin J, Yip CM, St George-Hyslop P, Fraser PE. Alphasynuclein membrane interactions and lipid specificity. J Biol Chem 2000; 275: 34328-34.
34. Karpinar DP, Balija MB, Kugler S, Opazo F, Rezaei-Ghaleh N, Wender N, et al. Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models. EMBO J 2009; 28: 3256-68.
35. Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H, Acevedo Arozena A, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 2016; 12: 1-222.
36. Klucken J, Poehler AM, Ebrahimi-Fakhari D, Schneider J, Nuber S, Rockenstein E, et al. Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway. Autophagy 2012; 8: 754-66.
37. Klunk WE, Bacskai BJ, Mathis CA, Kajdasz ST, McLellan ME, Frosch MP, et al. Imaging Abeta plaques in living transgenic mice with multiphoton microscopy and methoxy-X04, a systemically administered Congo red derivative. J Neuropathol Exp Neurol 2002; 61: 797-805.
38. Kuhla B, Boeck K, Luth HJ, Schmidt A, Weigle B, Schmitz M, et al. Age-dependent changes of glyoxalase I expression in human brain. Neurobiol Aging 2006; 27: 815-22.
39. Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002a; 418: 291.
40. Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, et al. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 2002b; 322: 1089-102.
41. Lazaro DF, Rodrigues EF, Langohr R, Shahpasandzadeh H, Ribeiro T, Guerreiro P, et al. Systematic comparison of the effects of alphasynuclein mutations on its oligomerization and aggregation. PLoS Genet 2014; 10: e1004741.
42. Lee D, Park CW, Paik SR, Choi KY. The modification of alpha-synuclein by dicarbonyl compounds inhibits its fibril-forming process. Biochim Biophys Acta 2009; 1794: 421-30.
43. Lee JY, Song J, Kwon K, Jang S, Kim C, Baek K, et al. Human DJ-1 and its homologs are novel glyoxalases. Hum Mol Genet 2012; 21: 3215-25.
44. Lyles GA, Chalmers J. The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amine oxidase in human umbilical artery. Biochem Pharmacol 1992; 43: 1409-14.
45. Macedo D, Tavares L, McDougall GJ, Vicente Miranda H, Stewart D, Ferreira RB, et al. (Poly)phenols protect from alpha-synuclein toxicity by reducing oxidative stress and promoting autophagy. Hum Mol Genet 2015; 24: 1717-32.
46. Mak SK, Huang YA, Iranmanesh S, Vangipuram M, Sundararajan R, Nguyen L, et al. Small molecules greatly improve conversion of human-induced pluripotent stem cells to the neuronal lineage. Stem Cells Int 2012; 2012: 140427.
47. Marques O, Outeiro TF. Alpha-synuclein: from secretion to dysfunction and death. Cell Death Dis 2012; 3: e350.
48. Martins IC, Kuperstein I, Wilkinson H, Maes E, Vanbrabant M, Jonckheere W, et al. Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J 2008; 27: 224-33.
49. McLean PJ, Kawamata H, Hyman BT. Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 2001; 104: 901-12.
50. Mihoub M, Abdallah J, Gontero B, Dairou J, Richarme G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem Biophys Res Commun 2015; 463: 1305-10.
51. Munch G, Luth HJ, Wong A, Arendt T, Hirsch E, Ravid R, et al. Crosslinking of alpha-synuclein by advanced glycation endproducts - An early pathophysiological step in Lewy body formation?. J Chem Neuroanat 2000; 20: 253-7.
52. Naiki H, Higuchi K, Hosokawa M, Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 1989; 177: 244-9.
53. Naiki H, Higuchi K, Matsushima K, Shimada A, Chen WH, Hosokawa M, et al. Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, thioflavine T. Lab Invest 1990; 62: 768-73.
54. Nass N, Bromme HJ, Hartig R, Korkmaz S, Sel S, Hirche F, et al. Differential response to alpha-oxoaldehydes in tamoxifen resistant MCF-7 breast cancer cells. PloS One 2014; 9: e101473.
55. Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MK, et al. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron 2010; 65: 66-79.
56. Nonaka T, Iwatsubo T, Hasegawa M. Ubiquitination of alpha-synuclein. Biochemistry 2005; 44: 361-8.
57. Oliveira LM, Falomir-Lockhart LJ, Botelho MG, Lin KH, Wales P, Koch JC, et al. Elevated alpha-synuclein caused by SNCA gene triplication impairs neuronal differentiation and maturation in Parkinson's patient-derived induced pluripotent stem cells. Cell Death Dis 2015; 6: e1994.
58. Oliveira LM, Gomes RA, Yang D, Dennison SR, Familia C, Lages A, et al. Insights into the molecular mechanism of protein native-like aggregation upon glycation. Biochim Biophys Acta 2013; 1834: 1010-22.
59. Oliveira LM, Lages A, Gomes RA, Neves H, Familia C, Coelho AV, et al. Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formation. BMC Biochem 2011; 12: 41.
60. Orosz F, Olah J, Ovadi J. Triosephosphate isomerase deficiency: new insights into an enigmatic disease. Biochim Biophys Acta 2009; 1792: 1168-74.
61. Oueslati A, Fournier M, Lashuel HA. Role of post-translational modifications in modulating the structure, function and toxicity of alphasynuclein: implications for Parkinson's disease pathogenesis and therapies. Prog Brain Res 2010; 183: 115-45.
62. Outeiro TF, Lindquist S. Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 2003; 302: 1772-5.
63. Padmaraju V, Bhaskar JJ, Prasada Rao UJ, Salimath PV, Rao KS. Role of advanced glycation on aggregation and DNA binding properties of alpha-synuclein. J Alzheimers Dis 2011; 24 (Suppl 2): 211-21.
64. Pearce RK, Owen A, Daniel S, Jenner P, Marsden CD. Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease. J Neural Transm 1997; 104: 661-77.
65. Reichard GA Jr, Skutches CL, Hoeldtke RD, Owen OE. Acetone metabolism in humans during diabetic ketoacidosis. Diabetes 1986; 35: 668-74.
66. Richard JP. Mechanism for the formation of methylglyoxal from triosephosphates. Biochem Soc Trans 1993; 21: 549-53.
67. Richarme G, Mihoub M, Dairou J, Bui LC, Leger T, Lamouri A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal-and glyoxal-glycated cysteine, arginine, and lysine residues. J Biol Chem 2015; 290: 1885-97.
68. Rockenstein E, Mallory M, Hashimoto M, Song D, Shults CW, Lang I, et al. Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J Neurosci Res 2002; 68: 568-78.
69. Schiff SJ, Somjen GG. The effects of temperature on synaptic transmission in hippocampal tissue slices. Brain Res 1985; 345: 279-84.
70. Scholz D, Poltl D, Genewsky A, Weng M, Waldmann T, Schildknecht S, et al. Rapid, complete and large-scale generation of post-mitotic neurons from the human LUHMES cell line. J Neurochem 2011; 119: 957-71.
71. Scott DA, Tabarean I, Tang Y, Cartier A, Masliah E, Roy S. A pathologic cascade leading to synaptic dysfunction in alpha-synucleininduced neurodegeneration. J Neurosci 2010; 30: 8083-95.
72. Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M. Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc Natl Acad Sci USA 1998; 95: 6469-73.
73. Strohalm M, Kavan D, Novak P, Volny M, Havlicek V. mMass 3: a cross-platform software environment for precise analysis of mass spectrometric data. Anal Chem 2010; 82: 4648-51.
74. Sun Y, Chang YH, Chen HF, Su YH, Su HF, Li CY. Risk of Parkinson disease onset in patients with diabetes: a 9-year population-based cohort study with age and sex stratifications. Diabetes Care 2012; 35: 1047-9.
75. Szego EM, Gerhardt E, Kermer P, Schulz JB. A30P alpha-synuclein impairs dopaminergic fiber regeneration and interacts with L-DOPA replacement in MPTP-treated mice. Neurobiol Dis 2012; 45: 591-600.
76. Szego EM, Outeiro TF, Kermer P, Schulz JB. Impairment of the septal cholinergic neurons in MPTP-treated A30P alpha-synuclein mice. Neurobiol Aging 2013; 34: 589-601.
77. Teismann P, Sathe K, Bierhaus A, Leng L, Martin HL, Bucala R, et al. Receptor for advanced glycation endproducts (RAGE) deficiency protects against MPTP toxicity. Neurobiol Aging 2012; 33: 2478-90.
78. Tenreiro S, Eckermann K, Outeiro TF. Protein phosphorylation in neurodegeneration: friend or foe?. Front Mol Neurosci 2014a; 7: 42.
79. Tenreiro S, Outeiro TF. Simple is good: yeast models of neurodegeneration. FEMS Yeast Res 2010; 10: 970-9.
80. Tenreiro S, Reimao-Pinto MM, Antas P, Rino J, Wawrzycka D, Macedo D, et al. Phosphorylation modulates clearance of alphasynuclein inclusions in a yeast model of Parkinson's disease. PLoS Genet 2014b; 10: e1004302.
81. Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 1999; 344 (Pt 1): 109-16.
82. Tiscornia G, Singer O, Verma IM. Production and purification of lentiviral vectors. Nat Protoc 2006; 1: 241-5.
83. Vagelatos NT, Eslick GD. Type 2 diabetes as a risk factor for Alzheimer's disease: the confounders, interactions, and neuropathology associated with this relationship. Epidemiol Rev 2013; 35: 152-60.
84. Vander Jagt DL, Robinson B, Taylor KK, Hunsaker LA. Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J Biol Chem 1992; 267: 4364-9.
85. Vicente Miranda H, El-Agnaf OM, Outeiro TF. Glycation in Parkinson's disease and Alzheimer's disease. Mov Disord 2016a; 31: 782-90.
86. Vicente Miranda H, Gomes MA, Branco-Santos J, Breda C, Lazaro DF, Lopes LV, et al. Glycation potentiates neurodegeneration in models of Huntington's disease. Sci Rep 2016b; 6: 36798.
87. Vicente Miranda H, Outeiro TF. The sour side of neurodegenerative disorders: the effects of protein glycation. J Pathol 2010; 221: 13-25.
88. Vicente Miranda H, Xiang W, de Oliveira RM, Simoes T, Pimentel J, Klucken J, et al. Heat-mediated enrichment of alpha-synuclein from cells and tissue for assessing post-translational modifications. J Neurochem 2013; 126: 673-84.
89. Wales P, Pinho R, Lazaro DF, Outeiro TF. Limelight on alpha-synuclein: pathological and mechanistic implications in neurodegeneration. J Parkinsons Dis 2013; 3: 415-59.
90. Wang Y, Shi M, Chung KA, Zabetian CP, Leverenz JB, Berg D, et al. Phosphorylated alpha-synuclein in Parkinson's disease. Sci Transl Med 2012; 4: 121ra20.
91. Webster J, Urban C, Berbaum K, Loske C, Alpar A, Gartner U, et al. The carbonyl scavengers aminoguanidine and tenilsetam protect against the neurotoxic effects of methylglyoxal. Neurotox Res 2005; 7: 95-101.
92. Willingham S, Outeiro TF, DeVit MJ, Lindquist SL, Muchowski PJ. Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 2003; 302: 1769-72.
93. Yao D, Brownlee M. Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands. Diabetes 2010; 59: 249-55.
94. Zondler L, Miller-Fleming L, Repici M, Goncalves S, Tenreiro S, Rosado-Ramos R, et al. DJ-1 interactions with alpha-synuclein attenuate aggregation and cellular toxicity in models of Parkinson's disease. Cell Death Dis 2014; 5: e1350.